Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 21:38, 15 December 2007 (UTC)
[edit]Proteins without matches (18)
[edit]Proteins with a High Potential Match (2)
[edit]Redirected Proteins (5)
[edit]Manual Inspection (Page not found) (20)
[edit]
Protein Status Grid - Date: 21:38, 15 December 2007 (UTC)
[edit]Vebose Log - Date: 21:38, 15 December 2007 (UTC)
[edit]- INFO: Beginning work on ACTC1... {December 15, 2007 1:15:44 PM PST}
- REDIRECT: Page directory gave bad page (ACTC1). Continuing with search.. Please correct entry: <70,ACTC1>. {December 15, 2007 1:16:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:16:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atn.
| PDB = {{PDB2|1atn}}, {{PDB2|1c0g}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1hlu}}, {{PDB2|1ijj}}, {{PDB2|1j6z}}, {{PDB2|1kxp}}, {{PDB2|1lcu}}, {{PDB2|1lot}}, {{PDB2|1m8q}}, {{PDB2|1ma9}}, {{PDB2|1mdu}}, {{PDB2|1mvw}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nwk}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}, {{PDB2|1p8z}}, {{PDB2|1qz5}}, {{PDB2|1qz6}}, {{PDB2|1rdw}}, {{PDB2|1rfq}}, {{PDB2|1rgi}}, {{PDB2|1s22}}, {{PDB2|1sqk}}, {{PDB2|1t44}}, {{PDB2|1wua}}, {{PDB2|1y64}}, {{PDB2|1yxq}}, {{PDB2|2a3z}}, {{PDB2|2a40}}, {{PDB2|2a41}}, {{PDB2|2a42}}, {{PDB2|2a5x}}, {{PDB2|2asm}}, {{PDB2|2aso}}, {{PDB2|2asp}}, {{PDB2|2btf}}, {{PDB2|2d1k}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fxu}}, {{PDB2|2gwj}}, {{PDB2|2gwk}}, {{PDB2|2hf3}}, {{PDB2|2hf4}}, {{PDB2|2hmp}}, {{PDB2|2oan}}, {{PDB2|2q1n}}, {{PDB2|2q31}}, {{PDB2|2q36}}
| Name = Actin, alpha, cardiac muscle 1
| HGNCid = 143
| Symbol = ACTC1
| AltSymbols =; ACTC; CMD1R
| OMIM = 102540
| ECnumber =
| Homologene = 68446
| MGIid = 87905
| GeneAtlas_image1 = PBB_GE_ACTC1_205132_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005884 |text = actin filament}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 70
| Hs_Ensembl = ENSG00000159251
| Hs_RefseqProtein = NP_005150
| Hs_RefseqmRNA = NM_005159
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 32869724
| Hs_GenLoc_end = 32875181
| Hs_Uniprot = P68032
| Mm_EntrezGene = 11464
| Mm_Ensembl = ENSMUSG00000068614
| Mm_RefseqmRNA = XM_001002645
| Mm_RefseqProtein = XP_001002645
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 113738727
| Mm_GenLoc_end = 113744252
| Mm_Uniprot = Q3TG92
}}
}}
'''Actin, alpha, cardiac muscle 1''', also known as '''ACTC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTC1 actin, alpha, cardiac muscle 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=70| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Actins are highly conserved proteins that are involved in various types of cell motility. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to four others. The protein encoded by this gene belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in this gene have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).<ref name="entrez">{{cite web | title = Entrez Gene: ACTC1 actin, alpha, cardiac muscle 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=70| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Bearer EL, Prakash JM, Li Z |title=Actin dynamics in platelets. |journal=Int. Rev. Cytol. |volume=217 |issue= |pages= 137-82 |year= 2002 |pmid= 12019562 |doi= }}
*{{cite journal | author=Elzinga M, Maron BJ, Adelstein RS |title=Human heart and platelet actins are products of different genes. |journal=Science |volume=191 |issue= 4222 |pages= 94-5 |year= 1976 |pmid= 1246600 |doi= }}
*{{cite journal | author=Adams LD, Tomasselli AG, Robbins P, ''et al.'' |title=HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 2 |pages= 291-5 |year= 1992 |pmid= 1540415 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Kramer PL, Luty JA, Litt M |title=Regional localization of the gene for cardiac muscle actin (ACTC) on chromosome 15q. |journal=Genomics |volume=13 |issue= 3 |pages= 904-5 |year= 1992 |pmid= 1639426 |doi= }}
*{{cite journal | author=Watkins C, Bodfish P, Warne D, ''et al.'' |title=Dinucleotide repeat polymorphism in the human alpha-cardiac actin gene, intron IV (ACTC), detected using the polymerase chain reaction. |journal=Nucleic Acids Res. |volume=19 |issue= 24 |pages= 6980 |year= 1992 |pmid= 1762945 |doi= }}
*{{cite journal | author=Tomasselli AG, Hui JO, Adams L, ''et al.'' |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548-53 |year= 1991 |pmid= 1907279 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Buckingham M, Alonso S, Barton P, ''et al.'' |title=Actin and myosin multigene families: their expression during the formation and maturation of striated muscle. |journal=Am. J. Med. Genet. |volume=25 |issue= 4 |pages= 623-34 |year= 1987 |pmid= 3789022 |doi= 10.1002/ajmg.1320250405 }}
*{{cite journal | author=Engel JN, Gunning PW, Kedes L |title=Isolation and characterization of human actin genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 8 |pages= 4674-8 |year= 1982 |pmid= 6272269 |doi= }}
*{{cite journal | author=Humphries SE, Whittall R, Minty A, ''et al.'' |title=There are approximately 20 actin gene in the human genome. |journal=Nucleic Acids Res. |volume=9 |issue= 19 |pages= 4895-908 |year= 1982 |pmid= 6273789 |doi= }}
*{{cite journal | author=Hamada H, Petrino MG, Kakunaga T |title=Molecular structure and evolutionary origin of human cardiac muscle actin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 19 |pages= 5901-5 |year= 1983 |pmid= 6310553 |doi= }}
*{{cite journal | author=Gunning P, Ponte P, Kedes L, ''et al.'' |title=Chromosomal location of the co-expressed human skeletal and cardiac actin genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 6 |pages= 1813-7 |year= 1984 |pmid= 6584914 |doi= }}
*{{cite journal | author=Gunning P, Ponte P, Blau H, Kedes L |title=alpha-skeletal and alpha-cardiac actin genes are coexpressed in adult human skeletal muscle and heart. |journal=Mol. Cell. Biol. |volume=3 |issue= 11 |pages= 1985-95 |year= 1984 |pmid= 6689196 |doi= }}
*{{cite journal | author=Ueyama H, Inazawa J, Ariyama T, ''et al.'' |title=Reexamination of chromosomal loci of human muscle actin genes by fluorescence in situ hybridization. |journal=Jpn. J. Hum. Genet. |volume=40 |issue= 1 |pages= 145-8 |year= 1995 |pmid= 7780165 |doi= }}
*{{cite journal | author=Moroianu J, Riordan JF |title=Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 5 |pages= 1677-81 |year= 1994 |pmid= 8127865 |doi= }}
*{{cite journal | author=Dunwoodie SL, Joya JE, Arkell RM, Hardeman EC |title=Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 12212-9 |year= 1994 |pmid= 8163527 |doi= }}
*{{cite journal | author=Shuster CB, Lin AY, Nayak R, Herman IM |title=Beta cap73: a novel beta actin-specific binding protein. |journal=Cell Motil. Cytoskeleton |volume=35 |issue= 3 |pages= 175-87 |year= 1997 |pmid= 8913639 |doi= 10.1002/(SICI)1097-0169(1996)35:3<175::AID-CM1>3.0.CO;2-8 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AMBP... {December 15, 2007 1:16:31 PM PST}
- REDIRECT: Page directory gave bad page (AMBP). Continuing with search.. Please correct entry: <259,AMBP>. {December 15, 2007 1:17:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:17:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AMBP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bik.
| PDB = {{PDB2|1bik}}
| Name = Alpha-1-microglobulin/bikunin precursor
| HGNCid = 453
| Symbol = AMBP
| AltSymbols =; HCP; ITI; ITIL; UTI
| OMIM = 176870
| ECnumber =
| Homologene = 1234
| MGIid = 88002
| GeneAtlas_image1 = PBB_GE_AMBP_205477_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0019855 |text = calcium channel inhibitor activity}} {{GNF_GO|id=GO:0019862 |text = IgA binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0030304 |text = trypsin inhibitor activity}} {{GNF_GO|id=GO:0030568 |text = plasmin inhibitor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046904 |text = calcium oxalate binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0018298 |text = protein-chromophore linkage}} {{GNF_GO|id=GO:0042167 |text = heme catabolic process}} {{GNF_GO|id=GO:0046329 |text = negative regulation of JNK cascade}} {{GNF_GO|id=GO:0050777 |text = negative regulation of immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 259
| Hs_Ensembl = ENSG00000106927
| Hs_RefseqProtein = NP_001624
| Hs_RefseqmRNA = NM_001633
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 115862231
| Hs_GenLoc_end = 115880536
| Hs_Uniprot = P02760
| Mm_EntrezGene = 11699
| Mm_Ensembl = ENSMUSG00000028356
| Mm_RefseqmRNA = NM_007443
| Mm_RefseqProtein = NP_031469
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 62629637
| Mm_GenLoc_end = 62640516
| Mm_Uniprot = Q925W1
}}
}}
'''Alpha-1-microglobulin/bikunin precursor''', also known as '''AMBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMBP alpha-1-microglobulin/bikunin precursor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=259| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Akerström B, Lögdberg L, Berggård T, ''et al.'' |title=alpha(1)-Microglobulin: a yellow-brown lipocalin. |journal=Biochim. Biophys. Acta |volume=1482 |issue= 1-2 |pages= 172-84 |year= 2000 |pmid= 11058759 |doi= }}
*{{cite journal | author=Kobayashi H, Suzuki M, Hirashima Y, Terao T |title=The protease inhibitor bikunin, a novel anti-metastatic agent. |journal=Biol. Chem. |volume=384 |issue= 5 |pages= 749-54 |year= 2004 |pmid= 12817471 |doi= }}
*{{cite journal | author=Ekström B, Berggård I |title=Human alpha1-microglobulin. Purification procedure, chemical and physiochemical properties. |journal=J. Biol. Chem. |volume=252 |issue= 22 |pages= 8048-57 |year= 1977 |pmid= 72071 |doi= }}
*{{cite journal | author=Salier JP, Simon D, Rouet P, ''et al.'' |title=Homologous chromosomal locations of the four genes for inter-alpha-inhibitor and pre-alpha-inhibitor family in human and mouse: assignment of the ancestral gene for the lipocalin superfamily. |journal=Genomics |volume=14 |issue= 1 |pages= 83-8 |year= 1992 |pmid= 1385302 |doi= }}
*{{cite journal | author=Escribano J, Lopex-Otin C, Hjerpe A, ''et al.'' |title=Location and characterization of the three carbohydrate prosthetic groups of human protein HC. |journal=FEBS Lett. |volume=266 |issue= 1-2 |pages= 167-70 |year= 1990 |pmid= 1694784 |doi= }}
*{{cite journal | author=Diarra-Mehrpour M, Bourguignon J, Sesboüé R, ''et al.'' |title=Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene. |journal=Eur. J. Biochem. |volume=191 |issue= 1 |pages= 131-9 |year= 1990 |pmid= 1696200 |doi= }}
*{{cite journal | author=Gebhard W, Schreitmüller T, Vetr H, ''et al.'' |title=Complementary DNA and deduced amino acid sequences of procine alpha 1-microglobulin and bikunin. |journal=FEBS Lett. |volume=269 |issue= 1 |pages= 32-6 |year= 1990 |pmid= 1696914 |doi= }}
*{{cite journal | author=Falkenberg C, Grubb A, Akerström B |title=Isolation of rat serum alpha 1-microglobulin. Identification of a complex with alpha 1-inhibitor-3, a rat alpha 2-macroglobulin homologue. |journal=J. Biol. Chem. |volume=265 |issue= 27 |pages= 16150-7 |year= 1990 |pmid= 1697852 |doi= }}
*{{cite journal | author=Nazimova SV, Akulenko IV, Zaĭtseva IV, ''et al.'' |title=[Immunoenzyme analysis of placenta-specific alpha(1)-microglobulin in the blood serum in normal and pathological pregnancy] |journal=Akusherstvo i ginekologiia |volume= |issue= 7 |pages= 70-2 |year= 1990 |pmid= 1700638 |doi= }}
*{{cite journal | author=Vetr H, Gebhard W |title=Structure of the human alpha 1-microglobulin-bikunin gene. |journal=Biol. Chem. Hoppe-Seyler |volume=371 |issue= 12 |pages= 1185-96 |year= 1991 |pmid= 1708673 |doi= }}
*{{cite journal | author=Escribano J, Grubb A, Calero M, Méndez E |title=The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC. |journal=J. Biol. Chem. |volume=266 |issue= 24 |pages= 15758-63 |year= 1991 |pmid= 1714898 |doi= }}
*{{cite journal | author=Enghild JJ, Salvesen G, Hefta SA, ''et al.'' |title=Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor. |journal=J. Biol. Chem. |volume=266 |issue= 2 |pages= 747-51 |year= 1991 |pmid= 1898736 |doi= }}
*{{cite journal | author=Reisinger P, Hochstrasser K, Albrecht GJ, ''et al.'' |title=Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase. |journal=Biol. Chem. Hoppe-Seyler |volume=366 |issue= 5 |pages= 479-83 |year= 1985 |pmid= 2408638 |doi= }}
*{{cite journal | author=Bourguignon J, Diarra-Mehrpour M, Sesboüé R, ''et al.'' |title=Human inter-alpha-trypsin-inhibitor: characterization and partial nucleotide sequencing of a light chain-encoding cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 3 |pages= 1146-53 |year= 1985 |pmid= 2413856 |doi= }}
*{{cite journal | author=Méndez E, Fernández-Luna JL, Grubb A, Leyva-Cobián F |title=Human protein HC and its IgA complex are inhibitors of neutrophil chemotaxis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 5 |pages= 1472-5 |year= 1986 |pmid= 2419908 |doi= }}
*{{cite journal | author=Traboni C, Cortese R |title=Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin). |journal=Nucleic Acids Res. |volume=14 |issue= 15 |pages= 6340 |year= 1986 |pmid= 2428011 |doi= }}
*{{cite journal | author=Kaumeyer JF, Polazzi JO, Kotick MP |title=The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC). |journal=Nucleic Acids Res. |volume=14 |issue= 20 |pages= 7839-50 |year= 1986 |pmid= 2430261 |doi= }}
*{{cite journal | author=Zaraĭskiĭ EI, Nazimova SV, Olefirenko GA, ''et al.'' |title=[Immunoenzyme analysis of placenta-specific alpha 1-microglobulin in the serum of blood donors] |journal=Vopr. Med. Khim. |volume=35 |issue= 5 |pages= 130-2 |year= 1990 |pmid= 2482577 |doi= }}
*{{cite journal | author=Schreitmüller T, Hochstrasser K, Reisinger PW, ''et al.'' |title=cDNA cloning of human inter-alpha-trypsin inhibitor discloses three different proteins. |journal=Biol. Chem. Hoppe-Seyler |volume=368 |issue= 8 |pages= 963-70 |year= 1987 |pmid= 3663330 |doi= }}
*{{cite journal | author=Morii M, Travis J |title=The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein. |journal=Biol. Chem. Hoppe-Seyler |volume=366 |issue= 1 |pages= 19-21 |year= 1985 |pmid= 3890890 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATXN3... {December 15, 2007 1:24:09 PM PST}
- REDIRECT: Page directory gave bad page (ATXN3 (gene)). Continuing with search.. Please correct entry: <4287,ATXN3 (gene)>. {December 15, 2007 1:24:38 PM PST}
- SEARCH REDIRECT: Control Box Found: Ataxin 3 {December 15, 2007 1:25:00 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:25:01 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:25:01 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:25:01 PM PST}
- UPDATED: Updated protein page: Ataxin 3 {December 15, 2007 1:25:10 PM PST}
- INFO: Beginning work on BTRC... {December 15, 2007 1:31:58 PM PST}
- REDIRECT: Page directory gave bad page (BTRC (gene)). Continuing with search.. Please correct entry: <8945,BTRC (gene)>. {December 15, 2007 1:32:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:32:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BTRC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p22.
| PDB = {{PDB2|1p22}}
| Name = Beta-transducin repeat containing
| HGNCid = 1144
| Symbol = BTRC
| AltSymbols =; BETA-TRCP; FBW1A; FBXW1A; FWD1; MGC4643; bTrCP; bTrCP1; betaTrCP
| OMIM = 603482
| ECnumber =
| Homologene = 39330
| MGIid = 1338871
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8945
| Hs_Ensembl = ENSG00000166167
| Hs_RefseqProtein = NP_003930
| Hs_RefseqmRNA = NM_003939
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 103103810
| Hs_GenLoc_end = 103307068
| Hs_Uniprot = Q9Y297
| Mm_EntrezGene = 12234
| Mm_Ensembl = ENSMUSG00000025217
| Mm_RefseqmRNA = NM_001037758
| Mm_RefseqProtein = NP_001032847
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 45417062
| Mm_GenLoc_end = 45583324
| Mm_Uniprot =
}}
}}
'''Beta-transducin repeat containing''', also known as '''BTRC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BTRC beta-transducin repeat containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8945| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbws class; in addition to an F-box, this protein contains multiple WD-40 repeats. This protein is homologous to Xenopus bTrCP1, yeast Met30, Neurospora Scon2 and Drosophila Slimb proteins. It interacts with HIV-1 Vpu and connects CD4 to the proteolytic machinery. It also associates specifically with phosphorylated IkappaBalpha and beta-catenin destruction motifs, probably functioning in multiple transcriptional programs by activating the NF-kappaB pathway and inhibiting the beta-catenin pathway.<ref name="entrez">{{cite web | title = Entrez Gene: BTRC beta-transducin repeat containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8945| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Maniatis T |title=A ubiquitin ligase complex essential for the NF-kappaB, Wnt/Wingless, and Hedgehog signaling pathways. |journal=Genes Dev. |volume=13 |issue= 5 |pages= 505-10 |year= 1999 |pmid= 10072378 |doi= }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Margottin F, Bour SP, Durand H, ''et al.'' |title=A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. |journal=Mol. Cell |volume=1 |issue= 4 |pages= 565-74 |year= 1998 |pmid= 9660940 |doi= }}
*{{cite journal | author=Yaron A, Hatzubai A, Davis M, ''et al.'' |title=Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. |journal=Nature |volume=396 |issue= 6711 |pages= 590-4 |year= 1999 |pmid= 9859996 |doi= 10.1038/25159 }}
*{{cite journal | author=Winston JT, Strack P, Beer-Romero P, ''et al.'' |title=The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. |journal=Genes Dev. |volume=13 |issue= 3 |pages= 270-83 |year= 1999 |pmid= 9990852 |doi= }}
*{{cite journal | author=Spencer E, Jiang J, Chen ZJ |title=Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. |journal=Genes Dev. |volume=13 |issue= 3 |pages= 284-94 |year= 1999 |pmid= 9990853 |doi= }}
*{{cite journal | author=Kitagawa M, Hatakeyama S, Shirane M, ''et al.'' |title=An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of beta-catenin. |journal=EMBO J. |volume=18 |issue= 9 |pages= 2401-10 |year= 1999 |pmid= 10228155 |doi= 10.1093/emboj/18.9.2401 }}
*{{cite journal | author=Fujiwara T, Suzuki M, Tanigami A, ''et al.'' |title=The BTRC gene, encoding a human F-box/WD40-repeat protein, maps to chromosome 10q24-q25. |journal=Genomics |volume=58 |issue= 1 |pages= 104-5 |year= 1999 |pmid= 10331953 |doi= 10.1006/geno.1999.5792 }}
*{{cite journal | author=Wu C, Ghosh S |title=beta-TrCP mediates the signal-induced ubiquitination of IkappaBbeta. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 29591-4 |year= 1999 |pmid= 10514424 |doi= }}
*{{cite journal | author=Cenciarelli C, Chiaur DS, Guardavaccaro D, ''et al.'' |title=Identification of a family of human F-box proteins. |journal=Curr. Biol. |volume=9 |issue= 20 |pages= 1177-9 |year= 1999 |pmid= 10531035 |doi= 10.1016/S0960-9822(00)80020-2 }}
*{{cite journal | author=Stone DM, Murone M, Luoh S, ''et al.'' |title=Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli. |journal=J. Cell. Sci. |volume=112 ( Pt 23) |issue= |pages= 4437-48 |year= 2000 |pmid= 10564661 |doi= }}
*{{cite journal | author=Suzuki H, Chiba T, Suzuki T, ''et al.'' |title=Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2877-84 |year= 2000 |pmid= 10644755 |doi= }}
*{{cite journal | author=Read MA, Brownell JE, Gladysheva TB, ''et al.'' |title=Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2326-33 |year= 2000 |pmid= 10713156 |doi= }}
*{{cite journal | author=Sadot E, Simcha I, Iwai K, ''et al.'' |title=Differential interaction of plakoglobin and beta-catenin with the ubiquitin-proteasome system. |journal=Oncogene |volume=19 |issue= 16 |pages= 1992-2001 |year= 2000 |pmid= 10803460 |doi= 10.1038/sj.onc.1203519 }}
*{{cite journal | author=Chiaur DS, Murthy S, Cenciarelli C, ''et al.'' |title=Five human genes encoding F-box proteins: chromosome mapping and analysis in human tumors. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 3-4 |pages= 255-8 |year= 2000 |pmid= 10828603 |doi= }}
*{{cite journal | author=Orian A, Gonen H, Bercovich B, ''et al.'' |title=SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-kappaB p105 requires phosphorylation of its C-terminus by IkappaB kinase. |journal=EMBO J. |volume=19 |issue= 11 |pages= 2580-91 |year= 2000 |pmid= 10835356 |doi= 10.1093/emboj/19.11.2580 }}
*{{cite journal | author=Strack P, Caligiuri M, Pelletier M, ''et al.'' |title=SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4. |journal=Oncogene |volume=19 |issue= 31 |pages= 3529-36 |year= 2000 |pmid= 10918611 |doi= 10.1038/sj.onc.1203647 }}
*{{cite journal | author=Kleijnen MF, Shih AH, Zhou P, ''et al.'' |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409-19 |year= 2000 |pmid= 10983987 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD63... {December 15, 2007 1:17:21 PM PST}
- REDIRECT: Page directory gave bad page (CD63 (gene)). Continuing with search.. Please correct entry: <967,CD63 (gene)>. {December 15, 2007 1:17:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:18:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD63 molecule
| HGNCid = 1692
| Symbol = CD63
| AltSymbols =; LAMP-3; ME491; MLA1; OMA81H; TSPAN30
| OMIM = 155740
| ECnumber =
| Homologene = 37526
| MGIid =
| GeneAtlas_image1 = PBB_GE_CD63_200663_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 967
| Hs_Ensembl = ENSG00000135404
| Hs_RefseqProtein = NP_001035123
| Hs_RefseqmRNA = NM_001040034
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 54405533
| Hs_GenLoc_end = 54409711
| Hs_Uniprot = P08962
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CD63 molecule''', also known as '''CD63''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD63 CD63 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=967| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. It may function as a blood platelet activation marker. Deficiency of this protein is associated with Hermansky-Pudlak syndrome. Also this gene has been associated with tumor progression. The use of alternate polyadenylation sites has been found for this gene. Alternative splicing results in multiple transcript variants encoding different proteins.<ref name="entrez">{{cite web | title = Entrez Gene: CD63 CD63 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=967| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horejsí V, Vlcek C |title=Novel structurally distinct family of leucocyte surface glycoproteins including CD9, CD37, CD53 and CD63. |journal=FEBS Lett. |volume=288 |issue= 1-2 |pages= 1-4 |year= 1991 |pmid= 1879540 |doi= }}
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Wang MX, Earley JJ, Shields JA, Donoso LA |title=An ocular melanoma-associated antigen. Molecular characterization. |journal=Arch. Ophthalmol. |volume=110 |issue= 3 |pages= 399-404 |year= 1992 |pmid= 1339263 |doi= }}
*{{cite journal | author=Hotta H, Miyamoto H, Hara I, ''et al.'' |title=Genomic structure of the ME491/CD63 antigen gene and functional analysis of the 5'-flanking regulatory sequences. |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 1 |pages= 436-42 |year= 1992 |pmid= 1599482 |doi= }}
*{{cite journal | author=Metzelaar MJ, Wijngaard PL, Peters PJ, ''et al.'' |title=CD63 antigen. A novel lysosomal membrane glycoprotein, cloned by a screening procedure for intracellular antigens in eukaryotic cells. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 3239-45 |year= 1991 |pmid= 1993697 |doi= }}
*{{cite journal | author=Rapp G, Freudenstein J, Klaudiny J, ''et al.'' |title=Characterization of three abundant mRNAs from human ovarian granulosa cells. |journal=DNA Cell Biol. |volume=9 |issue= 7 |pages= 479-85 |year= 1990 |pmid= 2171551 |doi= }}
*{{cite journal | author=Hotta H, Takahashi N, Homma M |title=Transcriptional enhancement of the human gene encoding for a melanoma-associated antigen (ME491) in association with malignant transformation. |journal=Jpn. J. Cancer Res. |volume=80 |issue= 12 |pages= 1186-91 |year= 1990 |pmid= 2516848 |doi= }}
*{{cite journal | author=Hotta H, Ross AH, Huebner K, ''et al.'' |title=Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression. |journal=Cancer Res. |volume=48 |issue= 11 |pages= 2955-62 |year= 1988 |pmid= 3365686 |doi= }}
*{{cite journal | author=Ross AH, Dietzschold B, Jackson DM, ''et al.'' |title=Isolation and amino terminal sequencing of a novel melanoma-associated antigen. |journal=Arch. Biochem. Biophys. |volume=242 |issue= 2 |pages= 540-8 |year= 1985 |pmid= 4062294 |doi= }}
*{{cite journal | author=Berditchevski F, Bazzoni G, Hemler ME |title=Specific association of CD63 with the VLA-3 and VLA-6 integrins. |journal=J. Biol. Chem. |volume=270 |issue= 30 |pages= 17784-90 |year= 1995 |pmid= 7629079 |doi= }}
*{{cite journal | author=Nishibori M, Cham B, McNicol A, ''et al.'' |title=The protein CD63 is in platelet dense granules, is deficient in a patient with Hermansky-Pudlak syndrome, and appears identical to granulophysin. |journal=J. Clin. Invest. |volume=91 |issue= 4 |pages= 1775-82 |year= 1993 |pmid= 7682577 |doi= }}
*{{cite journal | author=Radford KJ, Thorne RF, Hersey P |title=CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 13-8 |year= 1996 |pmid= 8630057 |doi= 10.1006/bbrc.1996.0690 }}
*{{cite journal | author=Gwynn B, Eicher EM, Peters LL |title=Genetic localization of Cd63, a member of the transmembrane 4 superfamily, reveals two distinct loci in the mouse genome. |journal=Genomics |volume=35 |issue= 2 |pages= 389-91 |year= 1996 |pmid= 8661157 |doi= 10.1006/geno.1996.0375 }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi= }}
*{{cite journal | author=Skubitz KM, Campbell KD, Iida J, Skubitz AP |title=CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils. |journal=J. Immunol. |volume=157 |issue= 8 |pages= 3617-26 |year= 1996 |pmid= 8871662 |doi= }}
*{{cite journal | author=Berditchevski F, Tolias KF, Wong K, ''et al.'' |title=A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2595-8 |year= 1997 |pmid= 9006891 |doi= }}
*{{cite journal | author=Sincock PM, Mayrhofer G, Ashman LK |title=Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. |journal=J. Histochem. Cytochem. |volume=45 |issue= 4 |pages= 515-25 |year= 1997 |pmid= 9111230 |doi= }}
*{{cite journal | author=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174-80 |year= 1997 |pmid= 9360995 |doi= }}
*{{cite journal | author=Tachibana I, Bodorova J, Berditchevski F, ''et al.'' |title=NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29181-9 |year= 1997 |pmid= 9360996 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COPS5... {December 15, 2007 1:33:44 PM PST}
- REDIRECT: Page directory gave bad page (COPS5). Continuing with search.. Please correct entry: <10987,COPS5>. {December 15, 2007 1:34:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:34:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)
| HGNCid = 2240
| Symbol = COPS5
| AltSymbols =; CSN5; JAB1; MGC3149; MOV-34; SGN5
| OMIM = 604850
| ECnumber =
| Homologene = 55992
| MGIid = 1349415
| GeneAtlas_image1 = PBB_GE_COPS5_201652_at_tn.png
| GeneAtlas_image2 = PBB_GE_COPS5_gnf1h08492_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0003743 |text = translation initiation factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005852 |text = eukaryotic translation initiation factor 3 complex}} {{GNF_GO|id=GO:0008180 |text = signalosome}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006412 |text = translation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10987
| Hs_Ensembl = ENSG00000121022
| Hs_RefseqProtein = NP_006828
| Hs_RefseqmRNA = NM_006837
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 68117871
| Hs_GenLoc_end = 68136785
| Hs_Uniprot = Q92905
| Mm_EntrezGene = 26754
| Mm_Ensembl = ENSMUSG00000025917
| Mm_RefseqmRNA = NM_013715
| Mm_RefseqProtein = NP_038743
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 10009816
| Mm_GenLoc_end = 10023160
| Mm_Uniprot = Q3V0K7
}}
}}
'''COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)''', also known as '''COPS5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COPS5 COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10987| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is one of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein is reported to be involved in the degradation of cyclin-dependent kinase inhibitor CDKN1B/p27Kip1. It is also known to be an coactivator that increases the specificity of JUN/AP1 transcription factors.<ref name="entrez">{{cite web | title = Entrez Gene: COPS5 COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10987| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wolf DA, Zhou C, Wee S |title=The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? |journal=Nat. Cell Biol. |volume=5 |issue= 12 |pages= 1029-33 |year= 2004 |pmid= 14647295 |doi= 10.1038/ncb1203-1029 }}
*{{cite journal | author=Claret FX, Hibi M, Dhut S, ''et al.'' |title=A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. |journal=Nature |volume=383 |issue= 6599 |pages= 453-7 |year= 1996 |pmid= 8837781 |doi= 10.1038/383453a0 }}
*{{cite journal | author=Asano K, Vornlocher HP, Richter-Cook NJ, ''et al.'' |title=Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27042-52 |year= 1997 |pmid= 9341143 |doi= }}
*{{cite journal | author=Seeger M, Kraft R, Ferrell K, ''et al.'' |title=A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. |journal=FASEB J. |volume=12 |issue= 6 |pages= 469-78 |year= 1998 |pmid= 9535219 |doi= }}
*{{cite journal | author=Wei N, Tsuge T, Serino G, ''et al.'' |title=The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. |journal=Curr. Biol. |volume=8 |issue= 16 |pages= 919-22 |year= 1998 |pmid= 9707402 |doi= }}
*{{cite journal | author=Tomoda K, Kubota Y, Kato J |title=Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1. |journal=Nature |volume=398 |issue= 6723 |pages= 160-5 |year= 1999 |pmid= 10086358 |doi= 10.1038/18230 }}
*{{cite journal | author=Dechend R, Hirano F, Lehmann K, ''et al.'' |title=The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. |journal=Oncogene |volume=18 |issue= 22 |pages= 3316-23 |year= 1999 |pmid= 10362352 |doi= 10.1038/sj.onc.1202717 }}
*{{cite journal | author=Chauchereau A, Georgiakaki M, Perrin-Wolff M, ''et al.'' |title=JAB1 interacts with both the progesterone receptor and SRC-1. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8540-8 |year= 2000 |pmid= 10722692 |doi= }}
*{{cite journal | author=Bianchi E, Denti S, Granata A, ''et al.'' |title=Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. |journal=Nature |volume=404 |issue= 6778 |pages= 617-21 |year= 2000 |pmid= 10766246 |doi= 10.1038/35007098 }}
*{{cite journal | author=Kleemann R, Hausser A, Geiger G, ''et al.'' |title=Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1. |journal=Nature |volume=408 |issue= 6809 |pages= 211-6 |year= 2000 |pmid= 11089976 |doi= 10.1038/35041591 }}
*{{cite journal | author=Bech-Otschir D, Kraft R, Huang X, ''et al.'' |title=COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. |journal=EMBO J. |volume=20 |issue= 7 |pages= 1630-9 |year= 2001 |pmid= 11285227 |doi= 10.1093/emboj/20.7.1630 }}
*{{cite journal | author=Lyapina S, Cope G, Shevchenko A, ''et al.'' |title=Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. |journal=Science |volume=292 |issue= 5520 |pages= 1382-5 |year= 2001 |pmid= 11337588 |doi= 10.1126/science.1059780 }}
*{{cite journal | author=Tomoda K, Kubota Y, Arata Y, ''et al.'' |title=The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. |journal=J. Biol. Chem. |volume=277 |issue= 3 |pages= 2302-10 |year= 2002 |pmid= 11704659 |doi= 10.1074/jbc.M104431200 }}
*{{cite journal | author=Bae MK, Ahn MY, Jeong JW, ''et al.'' |title=Jab1 interacts directly with HIF-1alpha and regulates its stability. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 9-12 |year= 2002 |pmid= 11707426 |doi= 10.1074/jbc.C100442200 }}
*{{cite journal | author=Lu C, Li Y, Zhao Y, ''et al.'' |title=Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway. |journal=FASEB J. |volume=16 |issue= 1 |pages= 90-2 |year= 2002 |pmid= 11709497 |doi= 10.1096/fj.01-0506fje }}
*{{cite journal | author=Dai YS, Cserjesi P |title=The basic helix-loop-helix factor, HAND2, functions as a transcriptional activator by binding to E-boxes as a heterodimer. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12604-12 |year= 2002 |pmid= 11812799 |doi= 10.1074/jbc.M200283200 }}
*{{cite journal | author=Wan M, Cao X, Wu Y, ''et al.'' |title=Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation. |journal=EMBO Rep. |volume=3 |issue= 2 |pages= 171-6 |year= 2002 |pmid= 11818334 |doi= 10.1093/embo-reports/kvf024 }}
*{{cite journal | author=Gemmill RM, Bemis LT, Lee JP, ''et al.'' |title=The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway. |journal=Oncogene |volume=21 |issue= 22 |pages= 3507-16 |year= 2002 |pmid= 12032852 |doi= 10.1038/sj.onc.1205437 }}
*{{cite journal | author=Caballero OL, Resto V, Patturajan M, ''et al.'' |title=Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1). |journal=Oncogene |volume=21 |issue= 19 |pages= 3003-10 |year= 2002 |pmid= 12082530 |doi= 10.1038/sj.onc.1205390 }}
*{{cite journal | author=Chopra S, Fernandez De Mattos S, Lam EW, Mann DJ |title=Jab1 co-activation of c-Jun is abrogated by the serine 10-phosphorylated form of p27Kip1. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32413-6 |year= 2002 |pmid= 12119282 |doi= 10.1074/jbc.C200311200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COX2... {December 15, 2007 1:25:51 PM PST}
- REDIRECT: Page directory gave bad page (COX2 (gene)). Continuing with search.. Please correct entry: <4513,COX2 (gene)>. {December 15, 2007 1:26:18 PM PST}
- SEARCH REDIRECT: Control Box Found: COX2 {December 15, 2007 1:26:25 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:26:28 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:26:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:26:28 PM PST}
- UPDATED: Updated protein page: COX2 {December 15, 2007 1:26:35 PM PST}
- INFO: Beginning work on CSF1R... {December 15, 2007 1:18:06 PM PST}
- REDIRECT: Page directory gave bad page (CSF1R). Continuing with search.. Please correct entry: <1436,CSF1R>. {December 15, 2007 1:18:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:18:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog
| HGNCid = 2433
| Symbol = CSF1R
| AltSymbols =; C-FMS; CD115; CSFR; FIM2; FMS
| OMIM = 164770
| ECnumber =
| Homologene = 3817
| MGIid = 1339758
| GeneAtlas_image1 = PBB_GE_CSF1R_203104_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005011 |text = macrophage colony stimulating factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1436
| Hs_Ensembl = ENSG00000182578
| Hs_RefseqProtein = NP_005202
| Hs_RefseqmRNA = NM_005211
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 149413051
| Hs_GenLoc_end = 149473128
| Hs_Uniprot = P07333
| Mm_EntrezGene = 12978
| Mm_Ensembl = ENSMUSG00000024621
| Mm_RefseqmRNA = NM_001037859
| Mm_RefseqProtein = NP_001032948
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 61230941
| Mm_GenLoc_end = 61256506
| Mm_Uniprot = Q0P635
}}
}}
'''Colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog''', also known as '''CSF1R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSF1R colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1436| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is the receptor for colony stimulating factor 1, a cytokine which controls the production, differentiation, and function of macrophages. This receptor mediates most if not all of the biological effects of this cytokine. Ligand binding activates the receptor kinase through a process of oligomerization and transphosphorylation. The encoded protein is a tyrosine kinase transmembrane receptor and member of the CSF1/PDGF receptor family of tyrosine-protein kinases. Mutations in this gene have been associated with a predisposition to myeloid malignancy. The first intron of this gene contains a transcriptionally inactive ribosomal protein L7 processed pseudogene oriented in the opposite direction.<ref name="entrez">{{cite web | title = Entrez Gene: CSF1R colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1436| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rettenmier CW, Roussel MF, Sherr CJ |title=The colony-stimulating factor 1 (CSF-1) receptor (c-fms proto-oncogene product) and its ligand. |journal=J. Cell Sci. Suppl. |volume=9 |issue= |pages= 27-44 |year= 1989 |pmid= 2978516 |doi= }}
*{{cite journal | author=Stanley ER, Berg KL, Einstein DB, ''et al.'' |title=Biology and action of colony--stimulating factor-1. |journal=Mol. Reprod. Dev. |volume=46 |issue= 1 |pages= 4-10 |year= 1997 |pmid= 8981357 |doi= 10.1002/(SICI)1098-2795(199701)46:1<4::AID-MRD2>3.0.CO;2-V }}
*{{cite journal | author=Gout I, Dhand R, Panayotou G, ''et al.'' |title=Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression system. |journal=Biochem. J. |volume=288 ( Pt 2) |issue= |pages= 395-405 |year= 1993 |pmid= 1334406 |doi= }}
*{{cite journal | author=Galland F, Stefanova M, Lafage M, Birnbaum D |title=Localization of the 5' end of the MCF2 oncogene to human chromosome 15q15----q23. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 2 |pages= 114-6 |year= 1992 |pmid= 1611909 |doi= }}
*{{cite journal | author=Boultwood J, Rack K, Kelly S, ''et al.'' |title=Loss of both CSF1R (FMS) alleles in patients with myelodysplasia and a chromosome 5 deletion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 14 |pages= 6176-80 |year= 1991 |pmid= 1829836 |doi= }}
*{{cite journal | author=Roussel MF, Cleveland JL, Shurtleff SA, Sherr CJ |title=Myc rescue of a mutant CSF-1 receptor impaired in mitogenic signalling. |journal=Nature |volume=353 |issue= 6342 |pages= 361-3 |year= 1991 |pmid= 1833648 |doi= 10.1038/353361a0 }}
*{{cite journal | author=Reedijk M, Liu XQ, Pawson T |title=Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor. |journal=Mol. Cell. Biol. |volume=10 |issue= 11 |pages= 5601-8 |year= 1990 |pmid= 2172781 |doi= }}
*{{cite journal | author=Ridge SA, Worwood M, Oscier D, ''et al.'' |title=FMS mutations in myelodysplastic, leukemic, and normal subjects. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1377-80 |year= 1990 |pmid= 2406720 |doi= }}
*{{cite journal | author=Sherr CJ, Rettenmier CW, Sacca R, ''et al.'' |title=The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. |journal=Cell |volume=41 |issue= 3 |pages= 665-76 |year= 1985 |pmid= 2408759 |doi= }}
*{{cite journal | author=Coussens L, Van Beveren C, Smith D, ''et al.'' |title=Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminus. |journal=Nature |volume=320 |issue= 6059 |pages= 277-80 |year= 1986 |pmid= 2421165 |doi= 10.1038/320277a0 }}
*{{cite journal | author=Hampe A, Shamoon BM, Gobet M, ''et al.'' |title=Nucleotide sequence and structural organization of the human FMS proto-oncogene. |journal=Oncogene Res. |volume=4 |issue= 1 |pages= 9-17 |year= 1989 |pmid= 2524025 |doi= }}
*{{cite journal | author=Visvader J, Verma IM |title=Differential transcription of exon 1 of the human c-fms gene in placental trophoblasts and monocytes. |journal=Mol. Cell. Biol. |volume=9 |issue= 3 |pages= 1336-41 |year= 1989 |pmid= 2524648 |doi= }}
*{{cite journal | author=Roberts WM, Look AT, Roussel MF, Sherr CJ |title=Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes. |journal=Cell |volume=55 |issue= 4 |pages= 655-61 |year= 1988 |pmid= 2846185 |doi= }}
*{{cite journal | author=Xu DQ, Guilhot S, Galibert F |title=Restriction fragment length polymorphism of the human c-fms gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2862-5 |year= 1985 |pmid= 2986142 |doi= }}
*{{cite journal | author=Sherr CJ, Rettenmier CW |title=The fms gene and the CSF-1 receptor. |journal=Cancer Surv. |volume=5 |issue= 2 |pages= 221-32 |year= 1987 |pmid= 3022923 |doi= }}
*{{cite journal | author=Le Beau MM, Westbrook CA, Diaz MO, ''et al.'' |title=Evidence for the involvement of GM-CSF and FMS in the deletion (5q) in myeloid disorders. |journal=Science |volume=231 |issue= 4741 |pages= 984-7 |year= 1986 |pmid= 3484837 |doi= }}
*{{cite journal | author=Wheeler EF, Roussel MF, Hampe A, ''et al.'' |title=The amino-terminal domain of the v-fms oncogene product includes a functional signal peptide that directs synthesis of a transforming glycoprotein in the absence of feline leukemia virus gag sequences. |journal=J. Virol. |volume=59 |issue= 2 |pages= 224-33 |year= 1986 |pmid= 3525854 |doi= }}
*{{cite journal | author=Browning PJ, Bunn HF, Cline A, ''et al.'' |title="Replacement" of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 20 |pages= 7800-4 |year= 1986 |pmid= 3532121 |doi= }}
*{{cite journal | author=Verbeek JS, Roebroek AJ, van den Ouweland AM, ''et al.'' |title=Human c-fms proto-oncogene: comparative analysis with an abnormal allele. |journal=Mol. Cell. Biol. |volume=5 |issue= 2 |pages= 422-6 |year= 1985 |pmid= 3974576 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYCS... {December 15, 2007 1:36:03 PM PST}
- REDIRECT: Page directory gave bad page (CYCS (gene)). Continuing with search.. Please correct entry: <54205,CYCS (gene)>. {December 15, 2007 1:36:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:36:47 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYCS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j3s.
| PDB = {{PDB2|1j3s}}, {{PDB2|2b4z}}
| Name = Cytochrome c, somatic
| HGNCid = 19986
| Symbol = CYCS
| AltSymbols =; HCS; CYC
| OMIM = 123970
| ECnumber =
| Homologene = 68675
| MGIid = 88578
| GeneAtlas_image1 = PBB_GE_CYCS_208905_at_tn.png
| Function = {{GNF_GO|id=GO:0000158 |text = protein phosphatase type 2A activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0045155 |text = electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000159 |text = protein phosphatase type 2A complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005746 |text = mitochondrial respiratory chain}} {{GNF_GO|id=GO:0005758 |text = mitochondrial intermembrane space}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}} {{GNF_GO|id=GO:0045333 |text = cellular respiration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 54205
| Hs_Ensembl = ENSG00000172115
| Hs_RefseqProtein = NP_061820
| Hs_RefseqmRNA = NM_018947
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 25124802
| Hs_GenLoc_end = 25131480
| Hs_Uniprot = P99999
| Mm_EntrezGene = 13063
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_975140
| Mm_RefseqProtein = XP_980234
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cytochrome c, somatic''', also known as '''CYCS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYCS cytochrome c, somatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54205| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes cytochrome c, a component of the electron transport chain in mitochondria. The heme group of cytochrome c accepts electrons from the b-c1 complex and transfers electrons to the cytochrome oxidase complex. Cytochrome c is also involved in initiation of apoptosis. Upon release of cytochrome c to the cytoplasm, the protein binds apoptotic protease activating factor which activates the apoptotic initiator procaspase 9. Many cytochrome c pseudogenes exist, scattered throughout the human genome.<ref name="entrez">{{cite web | title = Entrez Gene: CYCS cytochrome c, somatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54205| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Skulachev VP |title=Cytochrome c in the apoptotic and antioxidant cascades. |journal=FEBS Lett. |volume=423 |issue= 3 |pages= 275-80 |year= 1998 |pmid= 9515723 |doi= }}
*{{cite journal | author=Mannella CA |title=Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. |journal=J. Struct. Biol. |volume=121 |issue= 2 |pages= 207-18 |year= 1998 |pmid= 9615439 |doi= 10.1006/jsbi.1997.3954 }}
*{{cite journal | author=Ferri KF, Jacotot E, Blanco J, ''et al.'' |title=Mitochondrial control of cell death induced by HIV-1-encoded proteins. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 149-64 |year= 2001 |pmid= 11193032 |doi= }}
*{{cite journal | author=Britton RS, Leicester KL, Bacon BR |title=Iron toxicity and chelation therapy. |journal=Int. J. Hematol. |volume=76 |issue= 3 |pages= 219-28 |year= 2002 |pmid= 12416732 |doi= }}
*{{cite journal | author=Haider N, Narula N, Narula J |title=Apoptosis in heart failure represents programmed cell survival, not death, of cardiomyocytes and likelihood of reverse remodeling. |journal=J. Card. Fail. |volume=8 |issue= 6 Suppl |pages= S512-7 |year= 2003 |pmid= 12555167 |doi= 10.1054/jcaf.2002.130034 }}
*{{cite journal | author=Castedo M, Perfettini JL, Andreau K, ''et al.'' |title=Mitochondrial apoptosis induced by the HIV-1 envelope. |journal=Ann. N. Y. Acad. Sci. |volume=1010 |issue= |pages= 19-28 |year= 2004 |pmid= 15033690 |doi= }}
*{{cite journal | author=Ng S, Smith MB, Smith HT, Millett F |title=Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. |journal=Biochemistry |volume=16 |issue= 23 |pages= 4975-8 |year= 1977 |pmid= 199233 |doi= }}
*{{cite journal | author=Lynch SR, Sherman D, Copeland RA |title=Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 298-302 |year= 1992 |pmid= 1309738 |doi= }}
*{{cite journal | author=Garber EA, Margoliash E |title=Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition. |journal=Biochim. Biophys. Acta |volume=1015 |issue= 2 |pages= 279-87 |year= 1990 |pmid= 2153405 |doi= }}
*{{cite journal | author=Bedetti CD |title=Immunocytochemical demonstration of cytochrome c oxidase with an immunoperoxidase method: a specific stain for mitochondria in formalin-fixed and paraffin-embedded human tissues. |journal=J. Histochem. Cytochem. |volume=33 |issue= 5 |pages= 446-52 |year= 1985 |pmid= 2580882 |doi= }}
*{{cite journal | author=Tanaka Y, Ashikari T, Shibano Y, ''et al.'' |title=Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. |journal=J. Biochem. |volume=103 |issue= 6 |pages= 954-61 |year= 1988 |pmid= 2844747 |doi= }}
*{{cite journal | author=Evans MJ, Scarpulla RC |title=The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 24 |pages= 9625-9 |year= 1989 |pmid= 2849112 |doi= }}
*{{cite journal | author=Passon PG, Hultquist DE |title=Soluble cytochrome b 5 reductase from human erythrocytes. |journal=Biochim. Biophys. Acta |volume=275 |issue= 1 |pages= 62-73 |year= 1972 |pmid= 4403130 |doi= }}
*{{cite journal | author=Dowe RJ, Vitello LB, Erman JE |title=Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase. |journal=Arch. Biochem. Biophys. |volume=232 |issue= 2 |pages= 566-73 |year= 1984 |pmid= 6087732 |doi= }}
*{{cite journal | author=Michel B, Bosshard HR |title=Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. |journal=J. Biol. Chem. |volume=259 |issue= 16 |pages= 10085-91 |year= 1984 |pmid= 6088481 |doi= }}
*{{cite journal | author=Broger C, Nałecz MJ, Azzi A |title=Interaction of cytochrome c with cytochrome bc1 complex of the mitochondrial respiratory chain. |journal=Biochim. Biophys. Acta |volume=592 |issue= 3 |pages= 519-27 |year= 1980 |pmid= 6251869 |doi= }}
*{{cite journal | author=Smith HT, Ahmed AJ, Millett F |title=Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase. |journal=J. Biol. Chem. |volume=256 |issue= 10 |pages= 4984-90 |year= 1981 |pmid= 6262312 |doi= }}
*{{cite journal | author=Geren LM, Millett F |title=Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c. |journal=J. Biol. Chem. |volume=256 |issue= 20 |pages= 10485-9 |year= 1981 |pmid= 6270113 |doi= }}
*{{cite journal | author=Favre B, Zolnierowicz S, Turowski P, Hemmings BA |title=The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. |journal=J. Biol. Chem. |volume=269 |issue= 23 |pages= 16311-7 |year= 1994 |pmid= 8206937 |doi= }}
*{{cite journal | author=Gao B, Eisenberg E, Greene L |title=Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16792-7 |year= 1996 |pmid= 8663341 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DDIT3... {December 15, 2007 1:19:53 PM PST}
- REDIRECT: Page directory gave bad page (DDIT3). Continuing with search.. Please correct entry: <1649,DDIT3>. {December 15, 2007 1:20:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:20:37 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = DNA-damage-inducible transcript 3
| HGNCid = 2726
| Symbol = DDIT3
| AltSymbols =; CEBPZ; CHOP; CHOP10; GADD153; MGC4154
| OMIM = 126337
| ECnumber =
| Homologene = 3012
| MGIid = 109247
| GeneAtlas_image1 = PBB_GE_DDIT3_209383_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0006983 |text = ER overload response}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0030503 |text = regulation of cell redox homeostasis}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0042789 |text = mRNA transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1649
| Hs_Ensembl = ENSG00000175197
| Hs_RefseqProtein = NP_004074
| Hs_RefseqmRNA = NM_004083
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 56196640
| Hs_GenLoc_end = 56200567
| Hs_Uniprot = P35638
| Mm_EntrezGene = 13198
| Mm_Ensembl = ENSMUSG00000025408
| Mm_RefseqmRNA = NM_007837
| Mm_RefseqProtein = NP_031863
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 126693757
| Mm_GenLoc_end = 126699237
| Mm_Uniprot = Q3V405
}}
}}
'''DNA-damage-inducible transcript 3''', also known as '''DDIT3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDIT3 DNA-damage-inducible transcript 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1649| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ramji DP, Foka P |title=CCAAT/enhancer-binding proteins: structure, function and regulation. |journal=Biochem. J. |volume=365 |issue= Pt 3 |pages= 561-75 |year= 2002 |pmid= 12006103 |doi= 10.1042/BJ20020508 }}
*{{cite journal | author=Oyadomari S, Mori M |title=Roles of CHOP/GADD153 in endoplasmic reticulum stress. |journal=Cell Death Differ. |volume=11 |issue= 4 |pages= 381-9 |year= 2004 |pmid= 14685163 |doi= 10.1038/sj.cdd.4401373 }}
*{{cite journal | author=Aman P, Ron D, Mandahl N, ''et al.'' |title=Rearrangement of the transcription factor gene CHOP in myxoid liposarcomas with t(12;16)(q13;p11). |journal=Genes Chromosomes Cancer |volume=5 |issue= 4 |pages= 278-85 |year= 1993 |pmid= 1283316 |doi= }}
*{{cite journal | author=Park JS, Luethy JD, Wang MG, ''et al.'' |title=Isolation, characterization and chromosomal localization of the human GADD153 gene. |journal=Gene |volume=116 |issue= 2 |pages= 259-67 |year= 1992 |pmid= 1339368 |doi= }}
*{{cite journal | author=Ron D, Habener JF |title=CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. |journal=Genes Dev. |volume=6 |issue= 3 |pages= 439-53 |year= 1992 |pmid= 1547942 |doi= }}
*{{cite journal | author=Papathanasiou MA, Kerr NC, Robbins JH, ''et al.'' |title=Induction by ionizing radiation of the gadd45 gene in cultured human cells: lack of mediation by protein kinase C. |journal=Mol. Cell. Biol. |volume=11 |issue= 2 |pages= 1009-16 |year= 1991 |pmid= 1990262 |doi= }}
*{{cite journal | author=Eneroth M, Mandahl N, Heim S, ''et al.'' |title=Localization of the chromosomal breakpoints of the t(12;16) in liposarcoma to subbands 12q13.3 and 16p11.2. |journal=Cancer Genet. Cytogenet. |volume=48 |issue= 1 |pages= 101-7 |year= 1990 |pmid= 2372777 |doi= }}
*{{cite journal | author=Rabbitts TH, Forster A, Larson R, Nathan P |title=Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma. |journal=Nat. Genet. |volume=4 |issue= 2 |pages= 175-80 |year= 1993 |pmid= 7503811 |doi= 10.1038/ng0693-175 }}
*{{cite journal | author=Crozat A, Aman P, Mandahl N, Ron D |title=Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. |journal=Nature |volume=363 |issue= 6430 |pages= 640-4 |year= 1993 |pmid= 8510758 |doi= 10.1038/363640a0 }}
*{{cite journal | author=Chen BP, Wolfgang CD, Hai T |title=Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10. |journal=Mol. Cell. Biol. |volume=16 |issue= 3 |pages= 1157-68 |year= 1996 |pmid= 8622660 |doi= }}
*{{cite journal | author=Panagopoulos I, Höglund M, Mertens F, ''et al.'' |title=Fusion of the EWS and CHOP genes in myxoid liposarcoma. |journal=Oncogene |volume=12 |issue= 3 |pages= 489-94 |year= 1996 |pmid= 8637704 |doi= }}
*{{cite journal | author=Wang XZ, Ron D |title=Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. |journal=Science |volume=272 |issue= 5266 |pages= 1347-9 |year= 1996 |pmid= 8650547 |doi= }}
*{{cite journal | author=Fawcett TW, Eastman HB, Martindale JL, Holbrook NJ |title=Physical and functional association between GADD153 and CCAAT/enhancer-binding protein beta during cellular stress. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 14285-9 |year= 1996 |pmid= 8662954 |doi= }}
*{{cite journal | author=Ubeda M, Vallejo M, Habener JF |title=CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7589-99 |year= 1999 |pmid= 10523647 |doi= }}
*{{cite journal | author=Cui K, Coutts M, Stahl J, Sytkowski AJ |title=Novel interaction between the transcription factor CHOP (GADD153) and the ribosomal protein FTE/S3a modulates erythropoiesis. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 7591-6 |year= 2000 |pmid= 10713066 |doi= }}
*{{cite journal | author=Gotoh T, Oyadomari S, Mori K, Mori M |title=Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12343-50 |year= 2002 |pmid= 11805088 |doi= 10.1074/jbc.M107988200 }}
*{{cite journal | author=Satoh T, Toyoda M, Hoshino H, ''et al.'' |title=Activation of peroxisome proliferator-activated receptor-gamma stimulates the growth arrest and DNA-damage inducible 153 gene in non-small cell lung carcinoma cells. |journal=Oncogene |volume=21 |issue= 14 |pages= 2171-80 |year= 2002 |pmid= 11948400 |doi= 10.1038/sj.onc.1205279 }}
*{{cite journal | author=Qiao D, Im E, Qi W, Martinez JD |title=Activator protein-1 and CCAAT/enhancer-binding protein mediated GADD153 expression is involved in deoxycholic acid-induced apoptosis. |journal=Biochim. Biophys. Acta |volume=1583 |issue= 1 |pages= 108-16 |year= 2002 |pmid= 12069855 |doi= }}
*{{cite journal | author=Talukder AH, Wang RA, Kumar R |title=Expression and transactivating functions of the bZIP transcription factor GADD153 in mammary epithelial cells. |journal=Oncogene |volume=21 |issue= 27 |pages= 4289-300 |year= 2002 |pmid= 12082616 |doi= 10.1038/sj.onc.1205529 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EIF2S1... {December 15, 2007 1:20:37 PM PST}
- REDIRECT: Page directory gave bad page (EIF2S1). Continuing with search.. Please correct entry: <1965,EIF2S1>. {December 15, 2007 1:21:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:21:24 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EIF2S1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1kl9.
| PDB = {{PDB2|1kl9}}, {{PDB2|1q8k}}
| Name = Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa
| HGNCid = 3265
| Symbol = EIF2S1
| AltSymbols =; EIF-2; EIF-2A; EIF-2alpha; EIF2; EIF2A
| OMIM = 603907
| ECnumber =
| Homologene = 3020
| MGIid = 95299
| GeneAtlas_image1 = PBB_GE_EIF2S1_201142_at_tn.png
| GeneAtlas_image2 = PBB_GE_EIF2S1_201143_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_EIF2S1_201144_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003743 |text = translation initiation factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005844 |text = polysome}} {{GNF_GO|id=GO:0005850 |text = eukaryotic translation initiation factor 2 complex}} {{GNF_GO|id=GO:0005851 |text = eukaryotic translation initiation factor 2B complex}}
| Process = {{GNF_GO|id=GO:0006417 |text = regulation of translation}} {{GNF_GO|id=GO:0043558 |text = regulation of translation initiation in response to stress}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1965
| Hs_Ensembl = ENSG00000134001
| Hs_RefseqProtein = NP_004085
| Hs_RefseqmRNA = NM_004094
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 66896787
| Hs_GenLoc_end = 66922986
| Hs_Uniprot = P05198
| Mm_EntrezGene = 13665
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_026114
| Mm_RefseqProtein = NP_080390
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa''', also known as '''EIF2S1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EIF2S1 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1965| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The translation initiation factor eIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, eIF2, and GTP. eIF2 is composed of 3 nonidentical subunits, alpha (36 kD), beta (38 kD, MIM 603908), and gamma (52 kD, MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of eIF2-alpha (Ernst et al., 1987).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: EIF2S1 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1965| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hershey JW |title=Translational control in mammalian cells. |journal=Annu. Rev. Biochem. |volume=60 |issue= |pages= 717-55 |year= 1991 |pmid= 1883206 |doi= 10.1146/annurev.bi.60.070191.003441 }}
*{{cite journal | author=Mao X, Green JM, Safer B, ''et al.'' |title=Regulation of translation initiation factor gene expression during human T cell activation. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20444-50 |year= 1992 |pmid= 1400363 |doi= }}
*{{cite journal | author=Mellor H, Proud CG |title=A synthetic peptide substrate for initiation factor-2 kinases. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 430-7 |year= 1991 |pmid= 1677563 |doi= }}
*{{cite journal | author=Green SR, Spalding A, Ashford T, ''et al.'' |title=Synthesis of human initiation factor-2 alpha in Saccharomyces cerevisiae. |journal=Gene |volume=108 |issue= 2 |pages= 253-8 |year= 1992 |pmid= 1748310 |doi= }}
*{{cite journal | author=Kramer G |title=Two phosphorylation sites on eIF-2 alpha. |journal=FEBS Lett. |volume=267 |issue= 2 |pages= 181-2 |year= 1990 |pmid= 2116318 |doi= }}
*{{cite journal | author=Ernst H, Duncan RF, Hershey JW |title=Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA. |journal=J. Biol. Chem. |volume=262 |issue= 3 |pages= 1206-12 |year= 1987 |pmid= 2948954 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
*{{cite journal | author=Ray MK, Chakraborty A, Datta B, ''et al.'' |title=Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide. |journal=Biochemistry |volume=32 |issue= 19 |pages= 5151-9 |year= 1993 |pmid= 8098621 |doi= }}
*{{cite journal | author=Dever TE, Chen JJ, Barber GN, ''et al.'' |title=Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4616-20 |year= 1993 |pmid= 8099443 |doi= }}
*{{cite journal | author=Barber GN, Wambach M, Wong ML, ''et al.'' |title=Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4621-5 |year= 1993 |pmid= 8099444 |doi= }}
*{{cite journal | author=Miyamoto S, Chiorini JA, Urcelay E, Safer B |title=Regulation of gene expression for translation initiation factor eIF-2 alpha: importance of the 3' untranslated region. |journal=Biochem. J. |volume=315 ( Pt 3) |issue= |pages= 791-8 |year= 1996 |pmid= 8645159 |doi= }}
*{{cite journal | author=Yang W, Hinnebusch AG |title=Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6603-16 |year= 1996 |pmid= 8887689 |doi= }}
*{{cite journal | author=Brand SR, Kobayashi R, Mathews MB |title=The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8388-95 |year= 1997 |pmid= 9079663 |doi= }}
*{{cite journal | author=Ting NS, Kao PN, Chan DW, ''et al.'' |title=DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2136-45 |year= 1998 |pmid= 9442054 |doi= }}
*{{cite journal | author=Kimball SR, Heinzinger NK, Horetsky RL, Jefferson LS |title=Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B. |journal=J. Biol. Chem. |volume=273 |issue= 5 |pages= 3039-44 |year= 1998 |pmid= 9446619 |doi= }}
*{{cite journal | author=Shi Y, Vattem KM, Sood R, ''et al.'' |title=Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7499-509 |year= 1998 |pmid= 9819435 |doi= }}
*{{cite journal | author=Satoh S, Hijikata M, Handa H, Shimotohno K |title=Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha. |journal=Biochem. J. |volume=342 ( Pt 1) |issue= |pages= 65-70 |year= 1999 |pmid= 10432301 |doi= }}
*{{cite journal | author=Berlanga JJ, Santoyo J, De Haro C |title=Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase. |journal=Eur. J. Biochem. |volume=265 |issue= 2 |pages= 754-62 |year= 1999 |pmid= 10504407 |doi= }}
*{{cite journal | author=Lu J, O'Hara EB, Trieselmann BA, ''et al.'' |title=The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2alpha. |journal=J. Biol. Chem. |volume=274 |issue= 45 |pages= 32198-203 |year= 1999 |pmid= 10542257 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPHA2... {December 15, 2007 1:21:24 PM PST}
- REDIRECT: Page directory gave bad page (EPHA2 (gene)). Continuing with search.. Please correct entry: <1969,EPHA2 (gene)>. {December 15, 2007 1:21:58 PM PST}
- SEARCH REDIRECT: Control Box Found: EPH receptor A2 {December 15, 2007 1:22:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:22:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:22:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:22:09 PM PST}
- UPDATED: Updated protein page: EPH receptor A2 {December 15, 2007 1:22:16 PM PST}
- INFO: Beginning work on EWSR1... {December 15, 2007 1:22:16 PM PST}
- REDIRECT: Page directory gave bad page (EWSR1). Continuing with search.. Please correct entry: <2130,EWSR1>. {December 15, 2007 1:22:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:22:42 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EWSR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2cpe.
| PDB = {{PDB2|2cpe}}
| Name = Ewing sarcoma breakpoint region 1
| HGNCid = 3508
| Symbol = EWSR1
| AltSymbols =; EWS
| OMIM = 133450
| ECnumber =
| Homologene = 22438
| MGIid = 99960
| GeneAtlas_image1 = PBB_GE_EWSR1_210012_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2130
| Hs_Ensembl = ENSG00000182944
| Hs_RefseqProtein = NP_005234
| Hs_RefseqmRNA = NM_005243
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 27994283
| Hs_GenLoc_end = 28026504
| Hs_Uniprot = Q01844
| Mm_EntrezGene = 14030
| Mm_Ensembl = ENSMUSG00000009079
| Mm_RefseqmRNA = XM_988357
| Mm_RefseqProtein = XP_993451
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 4969692
| Mm_GenLoc_end = 4999269
| Mm_Uniprot = Q9CRS5
}}
}}
'''Ewing sarcoma breakpoint region 1''', also known as '''EWSR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EWSR1 Ewing sarcoma breakpoint region 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2130| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a putative RNA binding protein. Mutations in this gene, specifically a t(11;22)(q24;q12) translocation, are known to cause Ewing sarcoma as well as neuroectodermal and various other tumors. Alternative splicing of this gene results in two products.<ref name="entrez">{{cite web | title = Entrez Gene: EWSR1 Ewing sarcoma breakpoint region 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2130| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ban J, Siligan C, Kreppel M, ''et al.'' |title=EWS-FLI1 in Ewing's sarcoma: real targets and collateral damage. |journal=Adv. Exp. Med. Biol. |volume=587 |issue= |pages= 41-52 |year= 2007 |pmid= 17163154 |doi= }}
*{{cite journal | author=Meister HP |title=[Morphological findings of chronic constipation in childhood] |journal=Monatsschrift für Kinderheilkunde |volume=124 |issue= 5 |pages= 354-6 |year= 1976 |pmid= 934118 |doi= }}
*{{cite journal | author=Guthrie GM, Verstraete A, Deines MM, Stern RM |title=Symptoms of stress in four societies. |journal=The Journal of social psychology |volume=95 |issue= Second half |pages= 165-72 |year= 1975 |pmid= 1127890 |doi= }}
*{{cite journal | author=Delattre O, Zucman J, Plougastel B, ''et al.'' |title=Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours. |journal=Nature |volume=359 |issue= 6391 |pages= 162-5 |year= 1992 |pmid= 1522903 |doi= 10.1038/359162a0 }}
*{{cite journal | author=Bhagirath T, Abe S, Nojima T, Yoshida MC |title=Molecular analysis of a t(11;22) translocation junction in a case of Ewing's sarcoma. |journal=Genes Chromosomes Cancer |volume=13 |issue= 2 |pages= 126-32 |year= 1995 |pmid= 7542907 |doi= }}
*{{cite journal | author=Ohno T, Ouchida M, Lee L, ''et al.'' |title=The EWS gene, involved in Ewing family of tumors, malignant melanoma of soft parts and desmoplastic small round cell tumors, codes for an RNA binding protein with novel regulatory domains. |journal=Oncogene |volume=9 |issue= 10 |pages= 3087-97 |year= 1994 |pmid= 8084618 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Plougastel B, Zucman J, Peter M, ''et al.'' |title=Genomic structure of the EWS gene and its relationship to EWSR1, a site of tumor-associated chromosome translocation. |journal=Genomics |volume=18 |issue= 3 |pages= 609-15 |year= 1994 |pmid= 8307570 |doi= }}
*{{cite journal | author=Zucman J, Delattre O, Desmaze C, ''et al.'' |title=EWS and ATF-1 gene fusion induced by t(12;22) translocation in malignant melanoma of soft parts. |journal=Nat. Genet. |volume=4 |issue= 4 |pages= 341-5 |year= 1993 |pmid= 8401579 |doi= 10.1038/ng0893-341 }}
*{{cite journal | author=Brodie SG, Stocker SJ, Wardlaw JC, ''et al.'' |title=EWS and WT-1 gene fusion in desmoplastic small round cell tumor of the abdomen. |journal=Hum. Pathol. |volume=26 |issue= 12 |pages= 1370-4 |year= 1996 |pmid= 8522311 |doi= }}
*{{cite journal | author=Fujimura Y, Ohno T, Siddique H, ''et al.'' |title=The EWS-ATF-1 gene involved in malignant melanoma of soft parts with t(12;22) chromosome translocation, encodes a constitutive transcriptional activator. |journal=Oncogene |volume=12 |issue= 1 |pages= 159-67 |year= 1996 |pmid= 8552387 |doi= }}
*{{cite journal | author=Clark J, Benjamin H, Gill S, ''et al.'' |title=Fusion of the EWS gene to CHN, a member of the steroid/thyroid receptor gene superfamily, in a human myxoid chondrosarcoma. |journal=Oncogene |volume=12 |issue= 2 |pages= 229-35 |year= 1996 |pmid= 8570200 |doi= }}
*{{cite journal | author=Magnaghi-Jaulin L, Masutani H, Robin P, ''et al.'' |title=SRE elements are binding sites for the fusion protein EWS-FLI-1. |journal=Nucleic Acids Res. |volume=24 |issue= 6 |pages= 1052-8 |year= 1996 |pmid= 8604338 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Aman P, Panagopoulos I, Lassen C, ''et al.'' |title=Expression patterns of the human sarcoma-associated genes FUS and EWS and the genomic structure of FUS. |journal=Genomics |volume=37 |issue= 1 |pages= 1-8 |year= 1997 |pmid= 8921363 |doi= 10.1006/geno.1996.0513 }}
*{{cite journal | author=Morohoshi F, Arai K, Takahashi EI, ''et al.'' |title=Cloning and mapping of a human RBP56 gene encoding a putative RNA binding protein similar to FUS/TLS and EWS proteins. |journal=Genomics |volume=38 |issue= 1 |pages= 51-7 |year= 1997 |pmid= 8954779 |doi= 10.1006/geno.1996.0591 }}
*{{cite journal | author=Zucman-Rossi J, Legoix P, Thomas G |title=Identification of new members of the Gas2 and Ras families in the 22q12 chromosome region. |journal=Genomics |volume=38 |issue= 3 |pages= 247-54 |year= 1997 |pmid= 8975699 |doi= 10.1006/geno.1996.0625 }}
*{{cite journal | author=Guinamard R, Fougereau M, Seckinger P |title=The SH3 domain of Bruton's tyrosine kinase interacts with Vav, Sam68 and EWS. |journal=Scand. J. Immunol. |volume=45 |issue= 6 |pages= 587-95 |year= 1997 |pmid= 9201297 |doi= }}
*{{cite journal | author=Deloulme JC, Prichard L, Delattre O, Storm DR |title=The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27369-77 |year= 1997 |pmid= 9341188 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGF7... {December 15, 2007 1:22:42 PM PST}
- REDIRECT: Page directory gave bad page (FGF7). Continuing with search.. Please correct entry: <2252,FGF7>. {December 15, 2007 1:23:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:23:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FGF7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qqk.
| PDB = {{PDB2|1qqk}}
| Name = Fibroblast growth factor 7 (keratinocyte growth factor)
| HGNCid = 3685
| Symbol = FGF7
| AltSymbols =; HBGF-7; KGF
| OMIM = 148180
| ECnumber =
| Homologene = 7316
| MGIid = 95521
| GeneAtlas_image1 = PBB_GE_FGF7_205782_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0009611 |text = response to wounding}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2252
| Hs_Ensembl = ENSG00000140285
| Hs_RefseqProtein = NP_002000
| Hs_RefseqmRNA = NM_002009
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 47502751
| Hs_GenLoc_end = 47566815
| Hs_Uniprot = P21781
| Mm_EntrezGene = 14178
| Mm_Ensembl = ENSMUSG00000027208
| Mm_RefseqmRNA = NM_008008
| Mm_RefseqProtein = NP_032034
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 125726225
| Mm_GenLoc_end = 125781969
| Mm_Uniprot = Q544I6
}}
}}
'''Fibroblast growth factor 7 (keratinocyte growth factor)''', also known as '''FGF7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FGF7 fibroblast growth factor 7 (keratinocyte growth factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2252| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.<ref name="entrez">{{cite web | title = Entrez Gene: FGF7 fibroblast growth factor 7 (keratinocyte growth factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2252| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Beer HD, Gassmann MG, Munz B, ''et al.'' |title=Expression and function of keratinocyte growth factor and activin in skin morphogenesis and cutaneous wound repair. |journal=J. Investig. Dermatol. Symp. Proc. |volume=5 |issue= 1 |pages= 34-9 |year= 2001 |pmid= 11147673 |doi= 10.1046/j.1087-0024.2000.00009.x }}
*{{cite journal | author=Ware LB, Matthay MA |title=Keratinocyte and hepatocyte growth factors in the lung: roles in lung development, inflammation, and repair. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=282 |issue= 5 |pages= L924-40 |year= 2002 |pmid= 11943656 |doi= 10.1152/ajplung.00439.2001 }}
*{{cite journal | author=Finch PW, Rubin JS |title=Keratinocyte growth factor/fibroblast growth factor 7, a homeostatic factor with therapeutic potential for epithelial protection and repair. |journal=Adv. Cancer Res. |volume=91 |issue= |pages= 69-136 |year= 2004 |pmid= 15327889 |doi= 10.1016/S0065-230X(04)91003-2 }}
*{{cite journal | author=Ishibashi T, Bottaro DP, Chan A, ''et al.'' |title=Expression cloning of a human dual-specificity phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 24 |pages= 12170-4 |year= 1993 |pmid= 1281549 |doi= }}
*{{cite journal | author=Kelley MJ, Pech M, Seuanez HN, ''et al.'' |title=Emergence of the keratinocyte growth factor multigene family during the great ape radiation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 19 |pages= 9287-91 |year= 1992 |pmid= 1409637 |doi= }}
*{{cite journal | author=Aaronson SA, Bottaro DP, Miki T, ''et al.'' |title=Keratinocyte growth factor. A fibroblast growth factor family member with unusual target cell specificity. |journal=Ann. N. Y. Acad. Sci. |volume=638 |issue= |pages= 62-77 |year= 1992 |pmid= 1664700 |doi= }}
*{{cite journal | author=Finch PW, Rubin JS, Miki T, ''et al.'' |title=Human KGF is FGF-related with properties of a paracrine effector of epithelial cell growth. |journal=Science |volume=245 |issue= 4919 |pages= 752-5 |year= 1989 |pmid= 2475908 |doi= }}
*{{cite journal | author=Rubin JS, Osada H, Finch PW, ''et al.'' |title=Purification and characterization of a newly identified growth factor specific for epithelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 802-6 |year= 1989 |pmid= 2915979 |doi= }}
*{{cite journal | author=Ron D, Reich R, Chedid M, ''et al.'' |title=Fibroblast growth factor receptor 4 is a high affinity receptor for both acidic and basic fibroblast growth factor but not for keratinocyte growth factor. |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 5388-94 |year= 1993 |pmid= 7680645 |doi= }}
*{{cite journal | author=Yan G, Fukabori Y, McBride G, ''et al.'' |title=Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy. |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4513-22 |year= 1993 |pmid= 7687739 |doi= }}
*{{cite journal | author=Mattei MG, deLapeyrière O, Bresnick J, ''et al.'' |title=Mouse Fgf7 (fibroblast growth factor 7) and Fgf8 (fibroblast growth factor 8) genes map to chromosomes 2 and 19 respectively. |journal=Mamm. Genome |volume=6 |issue= 3 |pages= 196-7 |year= 1995 |pmid= 7749227 |doi= }}
*{{cite journal | author=Werner S, Smola H, Liao X, ''et al.'' |title=The function of KGF in morphogenesis of epithelium and reepithelialization of wounds. |journal=Science |volume=266 |issue= 5186 |pages= 819-22 |year= 1994 |pmid= 7973639 |doi= }}
*{{cite journal | author=Wilson SE, Walker JW, Chwang EL, He YG |title=Hepatocyte growth factor, keratinocyte growth factor, their receptors, fibroblast growth factor receptor-2, and the cells of the cornea. |journal=Invest. Ophthalmol. Vis. Sci. |volume=34 |issue= 8 |pages= 2544-61 |year= 1993 |pmid= 8392040 |doi= }}
*{{cite journal | author=Guo L, Degenstein L, Fuchs E |title=Keratinocyte growth factor is required for hair development but not for wound healing. |journal=Genes Dev. |volume=10 |issue= 2 |pages= 165-75 |year= 1996 |pmid= 8566750 |doi= }}
*{{cite journal | author=Ornitz DM, Xu J, Colvin JS, ''et al.'' |title=Receptor specificity of the fibroblast growth factor family. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15292-7 |year= 1996 |pmid= 8663044 |doi= }}
*{{cite journal | author=Post M, Souza P, Liu J, ''et al.'' |title=Keratinocyte growth factor and its receptor are involved in regulating early lung branching. |journal=Development |volume=122 |issue= 10 |pages= 3107-15 |year= 1996 |pmid= 8898224 |doi= }}
*{{cite journal | author=Zimonjic DB, Kelley MJ, Rubin JS, ''et al.'' |title=Fluorescence in situ hybridization analysis of keratinocyte growth factor gene amplification and dispersion in evolution of great apes and humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 21 |pages= 11461-5 |year= 1997 |pmid= 9326632 |doi= }}
*{{cite journal | author=Winkles JA, Alberts GF, Chedid M, ''et al.'' |title=Differential expression of the keratinocyte growth factor (KGF) and KGF receptor genes in human vascular smooth muscle cells and arteries. |journal=J. Cell. Physiol. |volume=173 |issue= 3 |pages= 380-6 |year= 1997 |pmid= 9369951 |doi= 10.1002/(SICI)1097-4652(199712)173:3<380::AID-JCP10>3.0.CO;2-G }}
*{{cite journal | author=Ishibashi T, Tanaka T, Nibu K, ''et al.'' |title=Keratinocyte growth factor and its receptor messenger RNA expression in nasal mucosa and nasal polyps. |journal=Ann. Otol. Rhinol. Laryngol. |volume=107 |issue= 10 Pt 1 |pages= 885-90 |year= 1998 |pmid= 9794620 |doi= }}
*{{cite journal | author=Mongiat M, Taylor K, Otto J, ''et al.'' |title=The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7. |journal=J. Biol. Chem. |volume=275 |issue= 10 |pages= 7095-100 |year= 2000 |pmid= 10702276 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DRB5... {December 15, 2007 1:23:36 PM PST}
- REDIRECT: Page directory gave bad page (HLA-DRB5 (gene)). Continuing with search.. Please correct entry: <3127,HLA-DRB5 (gene)>. {December 15, 2007 1:23:54 PM PST}
- SEARCH REDIRECT: Control Box Found: HLA-DRB5 {December 15, 2007 1:23:59 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:24:01 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:24:01 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:24:01 PM PST}
- UPDATED: Updated protein page: HLA-DRB5 {December 15, 2007 1:24:09 PM PST}
- INFO: Beginning work on HTATIP... {December 15, 2007 1:32:52 PM PST}
- REDIRECT: Page directory gave bad page (HTATIP). Continuing with search.. Please correct entry: <10524,HTATIP>. {December 15, 2007 1:33:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:33:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HTATIP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ou2.
| PDB = {{PDB2|2ou2}}
| Name = HIV-1 Tat interacting protein, 60kDa
| HGNCid = 5275
| Symbol = HTATIP
| AltSymbols =; ESA1; HTATIP1; PLIP; TIP; TIP60; cPLA2
| OMIM = 601409
| ECnumber =
| Homologene = 4657
| MGIid = 1932051
| GeneAtlas_image1 = PBB_GE_HTATIP_206689_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HTATIP_209192_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_HTATIP_214258_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0035267 |text = NuA4 histone acetyltransferase complex}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0016573 |text = histone acetylation}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10524
| Hs_Ensembl = ENSG00000172977
| Hs_RefseqProtein = NP_006379
| Hs_RefseqmRNA = NM_006388
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 65236315
| Hs_GenLoc_end = 65243650
| Hs_Uniprot = Q92993
| Mm_EntrezGene = 81601
| Mm_Ensembl = ENSMUSG00000024926
| Mm_RefseqmRNA = NM_178637
| Mm_RefseqProtein = NP_848752
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 5603418
| Mm_GenLoc_end = 5610029
| Mm_Uniprot = Q3UJQ1
}}
}}
'''HIV-1 Tat interacting protein, 60kDa''', also known as '''HTATIP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Doyon Y, Côté J |title=The highly conserved and multifunctional NuA4 HAT complex. |journal=Curr. Opin. Genet. Dev. |volume=14 |issue= 2 |pages= 147-54 |year= 2004 |pmid= 15196461 |doi= 10.1016/j.gde.2004.02.009 }}
*{{cite journal | author=Sapountzi V, Logan IR, Robson CN |title=Cellular functions of TIP60. |journal=Int. J. Biochem. Cell Biol. |volume=38 |issue= 9 |pages= 1496-509 |year= 2006 |pmid= 16698308 |doi= 10.1016/j.biocel.2006.03.003 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Kamine J, Elangovan B, Subramanian T, ''et al.'' |title=Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. |journal=Virology |volume=216 |issue= 2 |pages= 357-66 |year= 1996 |pmid= 8607265 |doi= 10.1006/viro.1996.0071 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Yamamoto T, Horikoshi M |title=Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30595-8 |year= 1998 |pmid= 9388189 |doi= }}
*{{cite journal | author=Kimura A, Horikoshi M |title=Tip60 acetylates six lysines of a specific class in core histones in vitro. |journal=Genes Cells |volume=3 |issue= 12 |pages= 789-800 |year= 1999 |pmid= 10096020 |doi= }}
*{{cite journal | author=Dechend R, Hirano F, Lehmann K, ''et al.'' |title=The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. |journal=Oncogene |volume=18 |issue= 22 |pages= 3316-23 |year= 1999 |pmid= 10362352 |doi= 10.1038/sj.onc.1202717 }}
*{{cite journal | author=Brady ME, Ozanne DM, Gaughan L, ''et al.'' |title=Tip60 is a nuclear hormone receptor coactivator. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17599-604 |year= 1999 |pmid= 10364196 |doi= }}
*{{cite journal | author=Creaven M, Hans F, Mutskov V, ''et al.'' |title=Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat. |journal=Biochemistry |volume=38 |issue= 27 |pages= 8826-30 |year= 1999 |pmid= 10393559 |doi= 10.1021/bi9907274 }}
*{{cite journal | author=Sliva D, Zhu YX, Tsai S, ''et al.'' |title=Tip60 interacts with human interleukin-9 receptor alpha-chain. |journal=Biochem. Biophys. Res. Commun. |volume=263 |issue= 1 |pages= 149-55 |year= 1999 |pmid= 10486269 |doi= 10.1006/bbrc.1999.1083 }}
*{{cite journal | author=Gavaravarapu S, Kamine J |title=Tip60 inhibits activation of CREB protein by protein kinase A. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 3 |pages= 758-66 |year= 2000 |pmid= 10720489 |doi= 10.1006/bbrc.2000.2358 }}
*{{cite journal | author=Husi H, Ward MA, Choudhary JS, ''et al.'' |title=Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. |journal=Nat. Neurosci. |volume=3 |issue= 7 |pages= 661-9 |year= 2000 |pmid= 10862698 |doi= 10.1038/76615 }}
*{{cite journal | author=Ikura T, Ogryzko VV, Grigoriev M, ''et al.'' |title=Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. |journal=Cell |volume=102 |issue= 4 |pages= 463-73 |year= 2000 |pmid= 10966108 |doi= }}
*{{cite journal | author=Ran Q, Pereira-Smith OM |title=Identification of an alternatively spliced form of the Tat interactive protein (Tip60), Tip60(beta). |journal=Gene |volume=258 |issue= 1-2 |pages= 141-6 |year= 2001 |pmid= 11111051 |doi= }}
*{{cite journal | author=Lee HJ, Chun M, Kandror KV |title=Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 16597-600 |year= 2001 |pmid= 11262386 |doi= 10.1074/jbc.C000909200 }}
*{{cite journal | author=Hlubek F, Löhberg C, Meiler J, ''et al.'' |title=Tip60 is a cell-type-specific transcriptional regulator. |journal=J. Biochem. |volume=129 |issue= 4 |pages= 635-41 |year= 2001 |pmid= 11275565 |doi= }}
*{{cite journal | author=Sheridan AM, Force T, Yoon HJ, ''et al.'' |title=PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. |journal=Mol. Cell. Biol. |volume=21 |issue= 14 |pages= 4470-81 |year= 2001 |pmid= 11416127 |doi= 10.1128/MCB.21.14.4470-4481.2001 }}
*{{cite journal | author=Cao X, Südhof TC |title=A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. |journal=Science |volume=293 |issue= 5527 |pages= 115-20 |year= 2001 |pmid= 11441186 |doi= 10.1126/science.1058783 }}
*{{cite journal | author=Legube G, Linares LK, Lemercier C, ''et al.'' |title=Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. |journal=EMBO J. |volume=21 |issue= 7 |pages= 1704-12 |year= 2002 |pmid= 11927554 |doi= 10.1093/emboj/21.7.1704 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MMP13... {December 15, 2007 1:25:10 PM PST}
- REDIRECT: Page directory gave bad page (MMP13). Continuing with search.. Please correct entry: <4322,MMP13>. {December 15, 2007 1:25:33 PM PST}
- SEARCH REDIRECT: Control Box Found: Matrix metallopeptidase 13 {December 15, 2007 1:25:42 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:25:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:25:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:25:45 PM PST}
- UPDATED: Updated protein page: Matrix metallopeptidase 13 {December 15, 2007 1:25:51 PM PST}
- INFO: Beginning work on P4HB... {December 15, 2007 1:26:35 PM PST}
- REDIRECT: Page directory gave bad page (P4HB). Continuing with search.. Please correct entry: <5034,P4HB>. {December 15, 2007 1:27:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:27:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_P4HB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bjx.
| PDB = {{PDB2|1bjx}}, {{PDB2|1mek}}, {{PDB2|1x5c}}, {{PDB2|2bjx}}
| Name = Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
| HGNCid = 8548
| Symbol = P4HB
| AltSymbols =; DSI; ERBA2L; GIT; PDI; PDIA1; PHDB; PO4DB; PO4HB; PROHB
| OMIM = 176790
| ECnumber =
| Homologene = 55495
| MGIid = 97464
| GeneAtlas_image1 = PBB_GE_P4HB_200656_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_P4HB_200654_at_tn.png
| Function = {{GNF_GO|id=GO:0003756 |text = protein disulfide isomerase activity}} {{GNF_GO|id=GO:0004656 |text = procollagen-proline 4-dioxygenase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0015035 |text = protein disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005793 |text = ER-Golgi intermediate compartment}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0018401 |text = peptidyl-proline hydroxylation to 4-hydroxy-L-proline}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5034
| Hs_Ensembl = ENSG00000185624
| Hs_RefseqProtein = NP_000909
| Hs_RefseqmRNA = NM_000918
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 77394326
| Hs_GenLoc_end = 77411680
| Hs_Uniprot = P07237
| Mm_EntrezGene = 18453
| Mm_Ensembl = ENSMUSG00000025130
| Mm_RefseqmRNA = NM_011032
| Mm_RefseqProtein = NP_035162
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 120376394
| Mm_GenLoc_end = 120389026
| Mm_Uniprot = Q3TF72
}}
}}
'''Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide''', also known as '''P4HB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: P4HB procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5034| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.<ref name="entrez">{{cite web | title = Entrez Gene: P4HB procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5034| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pihlajaniemi T, Myllylä R, Kivirikko KI |title=Prolyl 4-hydroxylase and its role in collagen synthesis. |journal=J. Hepatol. |volume=13 Suppl 3 |issue= |pages= S2-7 |year= 1992 |pmid= 1667665 |doi= }}
*{{cite journal | author=Wilkinson B, Gilbert HF |title=Protein disulfide isomerase. |journal=Biochim. Biophys. Acta |volume=1699 |issue= 1-2 |pages= 35-44 |year= 2004 |pmid= 15158710 |doi= 10.1016/j.bbapap.2004.02.017 }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
*{{cite journal | author=Chessler SD, Byers PH |title=Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7751-7 |year= 1992 |pmid= 1339453 |doi= }}
*{{cite journal | author=Vuori K, Myllylä R, Pihlajaniemi T, Kivirikko KI |title=Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7211-4 |year= 1992 |pmid= 1559965 |doi= }}
*{{cite journal | author=Tasanen K, Oikarinen J, Kivirikko KI, Pihlajaniemi T |title=Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements. |journal=J. Biol. Chem. |volume=267 |issue= 16 |pages= 11513-9 |year= 1992 |pmid= 1597478 |doi= }}
*{{cite journal | author=Bauw G, Rasmussen HH, van den Bulcke M, ''et al.'' |title=Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes. |journal=Electrophoresis |volume=11 |issue= 7 |pages= 528-36 |year= 1990 |pmid= 1699755 |doi= 10.1002/elps.1150110703 }}
*{{cite journal | author=Ward LD, Hong J, Whitehead RH, Simpson RJ |title=Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis. |journal=Electrophoresis |volume=11 |issue= 10 |pages= 883-91 |year= 1991 |pmid= 2079031 |doi= 10.1002/elps.1150111019 }}
*{{cite journal | author=Tasanen K, Parkkonen T, Chow LT, ''et al.'' |title=Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16218-24 |year= 1988 |pmid= 2846539 |doi= }}
*{{cite journal | author=Koivu J, Myllylä R, Helaakoski T, ''et al.'' |title=A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. |journal=J. Biol. Chem. |volume=262 |issue= 14 |pages= 6447-9 |year= 1987 |pmid= 3032969 |doi= }}
*{{cite journal | author=Pihlajaniemi T, Helaakoski T, Tasanen K, ''et al.'' |title=Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. |journal=EMBO J. |volume=6 |issue= 3 |pages= 643-9 |year= 1987 |pmid= 3034602 |doi= }}
*{{cite journal | author=Morris JI, Varandani PT |title=Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase). |journal=Biochim. Biophys. Acta |volume=949 |issue= 2 |pages= 169-80 |year= 1988 |pmid= 3342239 |doi= }}
*{{cite journal | author=Gosden JR, Middleton PG, Rout D, De Angelis C |title=Chromosomal localization of the human oncogene ERBA2. |journal=Cytogenet. Cell Genet. |volume=43 |issue= 3-4 |pages= 150-3 |year= 1987 |pmid= 3467900 |doi= }}
*{{cite journal | author=Cheng SY, Gong QH, Parkison C, ''et al.'' |title=The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. |journal=J. Biol. Chem. |volume=262 |issue= 23 |pages= 11221-7 |year= 1987 |pmid= 3611107 |doi= }}
*{{cite journal | author=Helaakoski T, Annunen P, Vuori K, ''et al.'' |title=Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 10 |pages= 4427-31 |year= 1995 |pmid= 7753822 |doi= }}
*{{cite journal | author=Shoulders CC, Brett DJ, Bayliss JD, ''et al.'' |title=Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein. |journal=Hum. Mol. Genet. |volume=2 |issue= 12 |pages= 2109-16 |year= 1994 |pmid= 8111381 |doi= }}
*{{cite journal | author=Kemmink J, Darby NJ, Dijkstra K, ''et al.'' |title=Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. |journal=Protein Sci. |volume=4 |issue= 12 |pages= 2587-93 |year= 1996 |pmid= 8580850 |doi= }}
*{{cite journal | author=Kemmink J, Darby NJ, Dijkstra K, ''et al.'' |title=Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. |journal=Biochemistry |volume=35 |issue= 24 |pages= 7684-91 |year= 1996 |pmid= 8672469 |doi= 10.1021/bi960335m }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLA2G4A... {December 15, 2007 1:27:40 PM PST}
- REDIRECT: Page directory gave bad page (PLA2G4A). Continuing with search.. Please correct entry: <5321,PLA2G4A>. {December 15, 2007 1:28:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:28:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PLA2G4A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bci.
| PDB = {{PDB2|1bci}}, {{PDB2|1cjy}}, {{PDB2|1rlw}}
| Name = Phospholipase A2, group IVA (cytosolic, calcium-dependent)
| HGNCid = 9035
| Symbol = PLA2G4A
| AltSymbols =; MGC126350; PLA2G4; cPLA2-alpha
| OMIM = 600522
| ECnumber =
| Homologene = 32059
| MGIid = 1195256
| GeneAtlas_image1 = PBB_GE_PLA2G4A_210145_at_tn.png
| Function = {{GNF_GO|id=GO:0004622 |text = lysophospholipase activity}} {{GNF_GO|id=GO:0004623 |text = phospholipase A2 activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006663 |text = platelet activating factor biosynthetic process}} {{GNF_GO|id=GO:0006690 |text = icosanoid metabolic process}} {{GNF_GO|id=GO:0009395 |text = phospholipid catabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5321
| Hs_Ensembl = ENSG00000116711
| Hs_RefseqProtein = NP_077734
| Hs_RefseqmRNA = NM_024420
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 185064708
| Hs_GenLoc_end = 185224736
| Hs_Uniprot = P47712
| Mm_EntrezGene = 18783
| Mm_Ensembl = ENSMUSG00000056220
| Mm_RefseqmRNA = NM_008869
| Mm_RefseqProtein = NP_032895
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 151591836
| Mm_GenLoc_end = 151723502
| Mm_Uniprot = Q3UMQ1
}}
}}
'''Phospholipase A2, group IVA (cytosolic, calcium-dependent)''', also known as '''PLA2G4A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G4A phospholipase A2, group IVA (cytosolic, calcium-dependent)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5321| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytosolic phospholipase A2 group IV family. The enzyme catalyzes the hydrolysis of membrane phospholipids to release arachidonic acid which is subsequently metabolized into eicosanoids. Eicosanoids, including prostaglandins and leukotrienes, are lipid-based cellular hormones that regulate hemodynamics, inflammatory responses, and other intracellular pathways. The hydrolysis reaction also produces lysophospholipids that are converted into platelet-activating factor. The enzyme is activated by increased intracellular Ca(2+) levels and phosphorylation, resulting in its translocation from the cytosol and nucleus to perinuclear membrane vesicles.<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G4A phospholipase A2, group IVA (cytosolic, calcium-dependent)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5321| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dennis EA |title=Diversity of group types, regulation, and function of phospholipase A2. |journal=J. Biol. Chem. |volume=269 |issue= 18 |pages= 13057-60 |year= 1994 |pmid= 8175726 |doi= }}
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Hirabayashi T, Murayama T, Shimizu T |title=Regulatory mechanism and physiological role of cytosolic phospholipase A2. |journal=Biol. Pharm. Bull. |volume=27 |issue= 8 |pages= 1168-73 |year= 2005 |pmid= 15305015 |doi= }}
*{{cite journal | author=Law MH, Cotton RG, Berger GE |title=The role of phospholipases A2 in schizophrenia. |journal=Mol. Psychiatry |volume=11 |issue= 6 |pages= 547-56 |year= 2006 |pmid= 16585943 |doi= 10.1038/sj.mp.4001819 }}
*{{cite journal | author=Shimizu T, Ohto T, Kita Y |title=Cytosolic phospholipase A2: biochemical properties and physiological roles. |journal=IUBMB Life |volume=58 |issue= 5-6 |pages= 328-33 |year= 2006 |pmid= 16754327 |doi= 10.1080/15216540600702289 }}
*{{cite journal | author=Sharp JD, White DL, Chiou XG, ''et al.'' |title=Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 14850-3 |year= 1991 |pmid= 1869522 |doi= }}
*{{cite journal | author=Clark JD, Lin LL, Kriz RW, ''et al.'' |title=A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. |journal=Cell |volume=65 |issue= 6 |pages= 1043-51 |year= 1991 |pmid= 1904318 |doi= }}
*{{cite journal | author=Tay A, Simon JS, Squire J, ''et al.'' |title=Cytosolic phospholipase A2 gene in human and rat: chromosomal localization and polymorphic markers. |journal=Genomics |volume=26 |issue= 1 |pages= 138-41 |year= 1995 |pmid= 7782073 |doi= }}
*{{cite journal | author=Wu T, Ikezono T, Angus CW, Shelhamer JH |title=Characterization of the promoter for the human 85 kDa cytosolic phospholipase A2 gene. |journal=Nucleic Acids Res. |volume=22 |issue= 23 |pages= 5093-8 |year= 1995 |pmid= 7800505 |doi= }}
*{{cite journal | author=Miyashita A, Crystal RG, Hay JG |title=Identification of a 27 bp 5'-flanking region element responsible for the low level constitutive expression of the human cytosolic phospholipase A2 gene. |journal=Nucleic Acids Res. |volume=23 |issue= 2 |pages= 293-301 |year= 1995 |pmid= 7862535 |doi= }}
*{{cite journal | author=Morri H, Ozaki M, Watanabe Y |title=5'-flanking region surrounding a human cytosolic phospholipase A2 gene. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 6-11 |year= 1995 |pmid= 7999086 |doi= }}
*{{cite journal | author=Sharp JD, Pickard RT, Chiou XG, ''et al.'' |title=Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23250-4 |year= 1994 |pmid= 8083230 |doi= }}
*{{cite journal | author=Lin LL, Wartmann M, Lin AY, ''et al.'' |title=cPLA2 is phosphorylated and activated by MAP kinase. |journal=Cell |volume=72 |issue= 2 |pages= 269-78 |year= 1993 |pmid= 8381049 |doi= }}
*{{cite journal | author=Flati V, Haque SJ, Williams BR |title=Interferon-alpha-induced phosphorylation and activation of cytosolic phospholipase A2 is required for the formation of interferon-stimulated gene factor three. |journal=EMBO J. |volume=15 |issue= 7 |pages= 1566-71 |year= 1996 |pmid= 8612580 |doi= }}
*{{cite journal | author=de Carvalho MG, McCormack AL, Olson E, ''et al.'' |title=Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 6987-97 |year= 1996 |pmid= 8636128 |doi= }}
*{{cite journal | author=Freed KA, Moses EK, Brennecke SP, Rice GE |title=Differential expression of type II, IV and cytosolic PLA2 messenger RNA in human intrauterine tissues at term. |journal=Mol. Hum. Reprod. |volume=3 |issue= 6 |pages= 493-9 |year= 1997 |pmid= 9239738 |doi= }}
*{{cite journal | author=Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, ''et al.'' |title=HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=16 |issue= 1 |pages= 1-9 |year= 1997 |pmid= 9377118 |doi= }}
*{{cite journal | author=Perisic O, Fong S, Lynch DE, ''et al.'' |title=Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1596-604 |year= 1998 |pmid= 9430701 |doi= }}
*{{cite journal | author=Börsch-Haubold AG, Bartoli F, Asselin J, ''et al.'' |title=Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4449-58 |year= 1998 |pmid= 9468497 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKCI... {December 15, 2007 1:28:27 PM PST}
- REDIRECT: Page directory gave bad page (PRKCI). Continuing with search.. Please correct entry: <5584,PRKCI>. {December 15, 2007 1:28:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:29:17 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRKCI_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1vd2.
| PDB = {{PDB2|1vd2}}, {{PDB2|1wmh}}, {{PDB2|1zrz}}
| Name = Protein kinase C, iota
| HGNCid = 9404
| Symbol = PRKCI
| AltSymbols =; DXS1179E; MGC26534; PKCI; nPKC-iota
| OMIM = 600539
| ECnumber =
| Homologene = 37667
| MGIid = 99260
| GeneAtlas_image1 = PBB_GE_PRKCI_1603_g_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKCI_209678_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PRKCI_209677_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000133 |text = polarisome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0045177 |text = apical part of cell}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006612 |text = protein targeting to membrane}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016044 |text = membrane organization and biogenesis}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} {{GNF_GO|id=GO:0035089 |text = establishment of apical/basal cell polarity}} {{GNF_GO|id=GO:0042462 |text = eye photoreceptor cell development}} {{GNF_GO|id=GO:0045197 |text = establishment and/or maintenance of epithelial cell polarity}} {{GNF_GO|id=GO:0045216 |text = intercellular junction assembly and maintenance}} {{GNF_GO|id=GO:0046903 |text = secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5584
| Hs_Ensembl = ENSG00000163558
| Hs_RefseqProtein = NP_002731
| Hs_RefseqmRNA = NM_002740
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 171422919
| Hs_GenLoc_end = 171506458
| Hs_Uniprot = P41743
| Mm_EntrezGene = 18759
| Mm_Ensembl = ENSMUSG00000037643
| Mm_RefseqmRNA = NM_008857
| Mm_RefseqProtein = NP_032883
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 31186625
| Mm_GenLoc_end = 31243615
| Mm_Uniprot = Q3TJJ5
}}
}}
'''Protein kinase C, iota''', also known as '''PRKCI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKCI protein kinase C, iota| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5584| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.<ref name="entrez">{{cite web | title = Entrez Gene: PRKCI protein kinase C, iota| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5584| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Suzuki A, Akimoto K, Ohno S |title=Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms. |journal=J. Biochem. |volume=133 |issue= 1 |pages= 9-16 |year= 2003 |pmid= 12761193 |doi= }}
*{{cite journal | author=Fields AP, Regala RP |title=Protein kinase C iota: human oncogene, prognostic marker and therapeutic target. |journal=Pharmacol. Res. |volume=55 |issue= 6 |pages= 487-97 |year= 2007 |pmid= 17570678 |doi= 10.1016/j.phrs.2007.04.015 }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
*{{cite journal | author=Chowdhury IH, Koyanagi Y, Kobayashi S, ''et al.'' |title=The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. |journal=Virology |volume=176 |issue= 1 |pages= 126-32 |year= 1990 |pmid= 1970444 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41. |journal=J. Immunol. |volume=144 |issue= 10 |pages= 3928-35 |year= 1990 |pmid= 2139676 |doi= }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal | author=Fields AP, Bednarik DP, Hess A, May WS |title=Human immunodeficiency virus induces phosphorylation of its cell surface receptor. |journal=Nature |volume=333 |issue= 6170 |pages= 278-80 |year= 1988 |pmid= 3259291 |doi= 10.1038/333278a0 }}
*{{cite journal | author=Mazzarella R, Ciccodicola A, Esposito T, ''et al.'' |title=Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3. |journal=Genomics |volume=26 |issue= 3 |pages= 629-31 |year= 1995 |pmid= 7607695 |doi= }}
*{{cite journal | author=Chirmule N, Goonewardena H, Pahwa S, ''et al.'' |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364-9 |year= 1995 |pmid= 7642615 |doi= }}
*{{cite journal | author=Ward NE, Gravitt KR, O'Brian CA |title=Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein. |journal=Cancer Lett. |volume=88 |issue= 1 |pages= 37-40 |year= 1995 |pmid= 7850771 |doi= }}
*{{cite journal | author=Gupta S, Aggarwal S, Kim C, Gollapudi S |title=Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report. |journal=Int. J. Immunopharmacol. |volume=16 |issue= 3 |pages= 197-204 |year= 1994 |pmid= 8206685 |doi= }}
*{{cite journal | author=Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ |title=Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24296-302 |year= 1993 |pmid= 8226978 |doi= }}
*{{cite journal | author=Diaz-Meco MT, Municio MM, Sanchez P, ''et al.'' |title=Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. |journal=Mol. Cell. Biol. |volume=16 |issue= 1 |pages= 105-14 |year= 1996 |pmid= 8524286 |doi= }}
*{{cite journal | author=Parada NA, Cruikshank WW, Danis HL, ''et al.'' |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100-6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi= }}
*{{cite journal | author=Díaz-Meco MT, Municio MM, Frutos S, ''et al.'' |title=The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C. |journal=Cell |volume=86 |issue= 5 |pages= 777-86 |year= 1996 |pmid= 8797824 |doi= }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal | author=Murray NR, Fields AP |title=Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27521-4 |year= 1997 |pmid= 9346882 |doi= }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Sanchez P, De Carcer G, Sandoval IV, ''et al.'' |title=Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 3069-80 |year= 1998 |pmid= 9566925 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKD1... {December 15, 2007 1:29:17 PM PST}
- REDIRECT: Page directory gave bad page (PRKD1). Continuing with search.. Please correct entry: <5587,PRKD1>. {December 15, 2007 1:29:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:30:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein kinase D1
| HGNCid = 9407
| Symbol = PRKD1
| AltSymbols =; PKC-MU; PKCM; PKD; PRKCM
| OMIM = 605435
| ECnumber =
| Homologene = 55680
| MGIid = 99879
| GeneAtlas_image1 = PBB_GE_PRKD1_205880_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5587
| Hs_Ensembl = ENSG00000184304
| Hs_RefseqProtein = NP_002733
| Hs_RefseqmRNA = NM_002742
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 29116195
| Hs_GenLoc_end = 29466469
| Hs_Uniprot = Q15139
| Mm_EntrezGene = 18760
| Mm_Ensembl = ENSMUSG00000002688
| Mm_RefseqmRNA = NM_008858
| Mm_RefseqProtein = NP_032884
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 51217854
| Mm_GenLoc_end = 51571105
| Mm_Uniprot = Q62101
}}
}}
'''Protein kinase D1''', also known as '''PRKD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Van Lint J, Rykx A, Maeda Y, ''et al.'' |title=Protein kinase D: an intracellular traffic regulator on the move. |journal=Trends Cell Biol. |volume=12 |issue= 4 |pages= 193-200 |year= 2002 |pmid= 11978539 |doi= }}
*{{cite journal | author=Busch H, Eisenhart-Rothe BV |title=[Old and new dangers of blood transfusion (author's transl)] |journal=MMW, Münchener medizinische Wochenschrift |volume=118 |issue= 22 |pages= 713-8 |year= 1976 |pmid= 5668 |doi= }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal | author=Davis RJ, Czech MP |title=Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 1974-8 |year= 1985 |pmid= 2984676 |doi= }}
*{{cite journal | author=Davis RJ, Czech MP |title=Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4080-4 |year= 1985 |pmid= 2987962 |doi= }}
*{{cite journal | author=Johannes FJ, Prestle J, Eis S, ''et al.'' |title=PKCu is a novel, atypical member of the protein kinase C family. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 6140-8 |year= 1994 |pmid= 8119958 |doi= }}
*{{cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi= }}
*{{cite journal | author=Sidorenko SP, Law CL, Klaus SJ, ''et al.'' |title=Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling. |journal=Immunity |volume=5 |issue= 4 |pages= 353-63 |year= 1996 |pmid= 8885868 |doi= }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi= }}
*{{cite journal | author=Waldron RT, Iglesias T, Rozengurt E |title=The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9224-30 |year= 1999 |pmid= 10092595 |doi= }}
*{{cite journal | author=Hausser A, Storz P, Link G, ''et al.'' |title=Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9258-64 |year= 1999 |pmid= 10092600 |doi= }}
*{{cite journal | author=Jamora C, Yamanouye N, Van Lint J, ''et al.'' |title=Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. |journal=Cell |volume=98 |issue= 1 |pages= 59-68 |year= 1999 |pmid= 10412981 |doi= 10.1016/S0092-8674(00)80606-6 }}
*{{cite journal | author=Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A |title=Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. |journal=EMBO J. |volume=18 |issue= 20 |pages= 5567-76 |year= 1999 |pmid= 10523301 |doi= 10.1093/emboj/18.20.5567 }}
*{{cite journal | author=Johannes FJ, Hausser A, Storz P, ''et al.'' |title=Bruton's tyrosine kinase (Btk) associates with protein kinase C mu. |journal=FEBS Lett. |volume=461 |issue= 1-2 |pages= 68-72 |year= 1999 |pmid= 10561498 |doi= }}
*{{cite journal | author=Storz P, Hausser A, Link G, ''et al.'' |title=Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24601-7 |year= 2000 |pmid= 10831594 |doi= 10.1074/jbc.M002964200 }}
*{{cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538-42 |year= 2000 |pmid= 10843712 |doi= }}
*{{cite journal | author=Matthews SA, Iglesias T, Rozengurt E, Cantrell D |title=Spatial and temporal regulation of protein kinase D (PKD). |journal=EMBO J. |volume=19 |issue= 12 |pages= 2935-45 |year= 2000 |pmid= 10856238 |doi= 10.1093/emboj/19.12.2935 }}
*{{cite journal | author=Vertommen D, Rider M, Ni Y, ''et al.'' |title=Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19567-76 |year= 2000 |pmid= 10867018 |doi= 10.1074/jbc.M001357200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMB8... {December 15, 2007 1:30:12 PM PST}
- REDIRECT: Page directory gave bad page (PSMB8). Continuing with search.. Please correct entry: <5696,PSMB8>. {December 15, 2007 1:30:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:31:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)
| HGNCid = 9545
| Symbol = PSMB8
| AltSymbols =; D6S216; D6S216E; LMP7; MGC1491; RING10
| OMIM = 177046
| ECnumber =
| Homologene = 56499
| MGIid = 1346527
| GeneAtlas_image1 = PBB_GE_PSMB8_209040_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5696
| Hs_Ensembl = ENSG00000204264
| Hs_RefseqProtein = NP_004150
| Hs_RefseqmRNA = NM_004159
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 32916471
| Hs_GenLoc_end = 32920690
| Hs_Uniprot = P28062
| Mm_EntrezGene = 16913
| Mm_Ensembl = ENSMUSG00000024338
| Mm_RefseqmRNA = NM_010724
| Mm_RefseqProtein = NP_034854
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 33808583
| Mm_GenLoc_end = 33811657
| Mm_Uniprot = P28063
}}
}}
'''Proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)''', also known as '''PSMB8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMB8 proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5696| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 3 (proteasome beta 5 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. Two alternative transcripts encoding two isoforms have been identified; both isoforms are processed to yield the same mature subunit.<ref name="entrez">{{cite web | title = Entrez Gene: PSMB8 proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5696| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Früh K, Yang Y, Arnold D, ''et al.'' |title=Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. |journal=J. Biol. Chem. |volume=267 |issue= 31 |pages= 22131-40 |year= 1992 |pmid= 1429565 |doi= }}
*{{cite journal | author=Beck S, Kelly A, Radley E, ''et al.'' |title=DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing. |journal=J. Mol. Biol. |volume=228 |issue= 2 |pages= 433-41 |year= 1992 |pmid= 1453454 |doi= }}
*{{cite journal | author=Bodmer JG, Marsh SG, Albert ED, ''et al.'' |title=Nomenclature for factors of the HLA system, 1991. WHO Nomenclature Committee for factors of the HLA system. |journal=Tissue Antigens |volume=39 |issue= 4 |pages= 161-73 |year= 1992 |pmid= 1529427 |doi= }}
*{{cite journal | author=Glynne R, Powis SH, Beck S, ''et al.'' |title=A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC. |journal=Nature |volume=353 |issue= 6342 |pages= 357-60 |year= 1991 |pmid= 1922342 |doi= 10.1038/353357a0 }}
*{{cite journal | author=Ustrell V, Realini C, Pratt G, Rechsteiner M |title=Human lymphoblast and erythrocyte multicatalytic proteases: differential peptidase activities and responses to the 11S regulator. |journal=FEBS Lett. |volume=376 |issue= 3 |pages= 155-8 |year= 1996 |pmid= 7498531 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Meinhardt T, Gräf U, Hämmerling GJ |title=Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes. |journal=Immunogenetics |volume=38 |issue= 5 |pages= 373-9 |year= 1993 |pmid= 8344725 |doi= }}
*{{cite journal | author=Glynne R, Kerr LA, Mockridge I, ''et al.'' |title=The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing. |journal=Eur. J. Immunol. |volume=23 |issue= 4 |pages= 860-6 |year= 1993 |pmid= 8458375 |doi= }}
*{{cite journal | author=Roby KF, Yang Y, Gershon D, Hunt JS |title=Cellular distribution of proteasome subunit Lmp7 mRNA and protein in human placentas. |journal=Immunology |volume=86 |issue= 3 |pages= 469-74 |year= 1996 |pmid= 8550087 |doi= }}
*{{cite journal | author=Beck S, Abdulla S, Alderton RP, ''et al.'' |title=Evolutionary dynamics of non-coding sequences within the class II region of the human MHC. |journal=J. Mol. Biol. |volume=255 |issue= 1 |pages= 1-13 |year= 1996 |pmid= 8568858 |doi= 10.1006/jmbi.1996.0001 }}
*{{cite journal | author=Hisamatsu H, Shimbara N, Saito Y, ''et al.'' |title=Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1807-16 |year= 1996 |pmid= 8666937 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Kim TG, Lee YH, Choi HB, Han H |title=Two newly discovered alleles of major histocompatibility complex-encoded LMP7 in Korean populations. |journal=Hum. Immunol. |volume=46 |issue= 1 |pages= 61-4 |year= 1997 |pmid= 9157092 |doi= }}
*{{cite journal | author=Vives-Pi M, Vargas F, James RF, ''et al.'' |title=Proteasome subunits, low-molecular-mass polypeptides 2 and 7 are hyperexpressed by target cells in autoimmune thyroid disease but not in insulin-dependent diabetes mellitus: implications for autoimmunity. |journal=Tissue Antigens |volume=50 |issue= 2 |pages= 153-63 |year= 1997 |pmid= 9271825 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Sewell AK, Price DA, Teisserenc H, ''et al.'' |title=IFN-gamma exposes a cryptic cytotoxic T lymphocyte epitope in HIV-1 reverse transcriptase. |journal=J. Immunol. |volume=162 |issue= 12 |pages= 7075-9 |year= 1999 |pmid= 10358150 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTCH1... {December 15, 2007 1:31:03 PM PST}
- REDIRECT: Page directory gave bad page (PTCH1). Continuing with search.. Please correct entry: <5727,PTCH1>. {December 15, 2007 1:31:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:31:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Patched homolog 1 (Drosophila)
| HGNCid = 9585
| Symbol = PTCH1
| AltSymbols =; PTC; BCNS; FLJ42602; HPE7; NBCCS; PTC1; PTCH
| OMIM = 601309
| ECnumber =
| Homologene = 223
| MGIid = 105373
| GeneAtlas_image1 = PBB_GE_PTCH1_209815_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTCH1_208522_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTCH1_209816_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005113 |text = patched binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008158 |text = hedgehog receptor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001841 |text = neural tube formation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007224 |text = smoothened signaling pathway}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0009953 |text = dorsal/ventral pattern formation}} {{GNF_GO|id=GO:0016485 |text = protein processing}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} {{GNF_GO|id=GO:0040015 |text = negative regulation of body size}} {{GNF_GO|id=GO:0043109 |text = regulation of smoothened activity}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5727
| Hs_Ensembl = ENSG00000185920
| Hs_RefseqProtein = NP_000255
| Hs_RefseqmRNA = NM_000264
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 97245083
| Hs_GenLoc_end = 97318923
| Hs_Uniprot = Q13635
| Mm_EntrezGene = 19206
| Mm_Ensembl = ENSMUSG00000021466
| Mm_RefseqmRNA = NM_008957
| Mm_RefseqProtein = NP_032983
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 63520755
| Mm_GenLoc_end = 63574742
| Mm_Uniprot = Q3LG17
}}
}}
'''Patched homolog 1 (Drosophila)''', also known as '''PTCH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTCH1 patched homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5727| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the patched gene family. The encoded protein is the receptor for sonic hedgehog, a secreted molecule implicated in the formation of embryonic structures and in tumorigenesis. This gene functions as a tumor suppressor. Mutations of this gene have been associated with nevoid basal cell carcinoma syndrome, esophageal squamous cell carcinoma, trichoepitheliomas, transitional cell carcinomas of the bladder, as well as holoprosencephaly. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences and biological validity cannot be determined currently.<ref name="entrez">{{cite web | title = Entrez Gene: PTCH1 patched homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5727| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Villavicencio EH, Walterhouse DO, Iannaccone PM |title=The sonic hedgehog-patched-gli pathway in human development and disease. |journal=Am. J. Hum. Genet. |volume=67 |issue= 5 |pages= 1047-54 |year= 2000 |pmid= 11001584 |doi= }}
*{{cite journal | author=Corcoran RB, Scott MP |title=A mouse model for medulloblastoma and basal cell nevus syndrome. |journal=J. Neurooncol. |volume=53 |issue= 3 |pages= 307-18 |year= 2002 |pmid= 11718263 |doi= }}
*{{cite journal | author=Lindström E, Shimokawa T, Toftgård R, Zaphiropoulos PG |title=PTCH mutations: distribution and analyses. |journal=Hum. Mutat. |volume=27 |issue= 3 |pages= 215-9 |year= 2006 |pmid= 16419085 |doi= 10.1002/humu.20296 }}
*{{cite journal | author=Gailani MR, Bale SJ, Leffell DJ, ''et al.'' |title=Developmental defects in Gorlin syndrome related to a putative tumor suppressor gene on chromosome 9. |journal=Cell |volume=69 |issue= 1 |pages= 111-7 |year= 1992 |pmid= 1348213 |doi= }}
*{{cite journal | author=Hahn H, Christiansen J, Wicking C, ''et al.'' |title=A mammalian patched homolog is expressed in target tissues of sonic hedgehog and maps to a region associated with developmental abnormalities. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12125-8 |year= 1996 |pmid= 8647801 |doi= }}
*{{cite journal | author=Johnson RL, Rothman AL, Xie J, ''et al.'' |title=Human homolog of patched, a candidate gene for the basal cell nevus syndrome. |journal=Science |volume=272 |issue= 5268 |pages= 1668-71 |year= 1996 |pmid= 8658145 |doi= }}
*{{cite journal | author=Hahn H, Wicking C, Zaphiropoulous PG, ''et al.'' |title=Mutations of the human homolog of Drosophila patched in the nevoid basal cell carcinoma syndrome. |journal=Cell |volume=85 |issue= 6 |pages= 841-51 |year= 1996 |pmid= 8681379 |doi= }}
*{{cite journal | author=Gailani MR, Ståhle-Bäckdahl M, Leffell DJ, ''et al.'' |title=The role of the human homologue of Drosophila patched in sporadic basal cell carcinomas. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 78-81 |year= 1996 |pmid= 8782823 |doi= 10.1038/ng0996-78 }}
*{{cite journal | author=Chidambaram A, Goldstein AM, Gailani MR, ''et al.'' |title=Mutations in the human homologue of the Drosophila patched gene in Caucasian and African-American nevoid basal cell carcinoma syndrome patients. |journal=Cancer Res. |volume=56 |issue= 20 |pages= 4599-601 |year= 1996 |pmid= 8840969 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Stone DM, Hynes M, Armanini M, ''et al.'' |title=The tumour-suppressor gene patched encodes a candidate receptor for Sonic hedgehog. |journal=Nature |volume=384 |issue= 6605 |pages= 129-34 |year= 1996 |pmid= 8906787 |doi= 10.1038/384129a0 }}
*{{cite journal | author=Wicking C, Shanley S, Smyth I, ''et al.'' |title=Most germ-line mutations in the nevoid basal cell carcinoma syndrome lead to a premature termination of the PATCHED protein, and no genotype-phenotype correlations are evident. |journal=Am. J. Hum. Genet. |volume=60 |issue= 1 |pages= 21-6 |year= 1997 |pmid= 8981943 |doi= }}
*{{cite journal | author=Lench NJ, Telford EA, High AS, ''et al.'' |title=Characterisation of human patched germ line mutations in naevoid basal cell carcinoma syndrome. |journal=Hum. Genet. |volume=100 |issue= 5-6 |pages= 497-502 |year= 1997 |pmid= 9341860 |doi= }}
*{{cite journal | author=Aszterbaum M, Rothman A, Johnson RL, ''et al.'' |title=Identification of mutations in the human PATCHED gene in sporadic basal cell carcinomas and in patients with the basal cell nevus syndrome. |journal=J. Invest. Dermatol. |volume=110 |issue= 6 |pages= 885-8 |year= 1998 |pmid= 9620294 |doi= 10.1046/j.1523-1747.1998.00222.x }}
*{{cite journal | author=Carpenter D, Stone DM, Brush J, ''et al.'' |title=Characterization of two patched receptors for the vertebrate hedgehog protein family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 23 |pages= 13630-4 |year= 1998 |pmid= 9811851 |doi= }}
*{{cite journal | author=Liu JH, Wei S, Burnette PK, ''et al.'' |title=Functional association of TGF-beta receptor II with cyclin B. |journal=Oncogene |volume=18 |issue= 1 |pages= 269-75 |year= 1999 |pmid= 9926943 |doi= 10.1038/sj.onc.1202263 }}
*{{cite journal | author=Hasenpusch-Theil K, Bataille V, Laehdetie J, ''et al.'' |title=Gorlin syndrome: identification of 4 novel germ-line mutations of the human patched (PTCH) gene. Mutations in brief no. 137. Online. |journal=Hum. Mutat. |volume=11 |issue= 6 |pages= 480 |year= 1999 |pmid= 10200051 |doi= 10.1002/(SICI)1098-1004(1998)11:6<480::AID-HUMU9>3.0.CO;2-4 }}
*{{cite journal | author=Dong J, Gailani MR, Pomeroy SL, ''et al.'' |title=Identification of PATCHED mutations in medulloblastomas by direct sequencing. |journal=Hum. Mutat. |volume=16 |issue= 1 |pages= 89-90 |year= 2000 |pmid= 10874314 |doi= 10.1002/1098-1004(200007)16:1<89::AID-HUMU18>3.0.CO;2-7 }}
*{{cite journal | author=Reifenberger J, Arnold N, Kiechle M, ''et al.'' |title=Coincident PTCH and BRCA1 germline mutations in a patient with nevoid basal cell carcinoma syndrome and familial breast cancer. |journal=J. Invest. Dermatol. |volume=116 |issue= 3 |pages= 472-4 |year= 2001 |pmid= 11231326 |doi= 10.1046/j.1523-1747.2001.01279-2.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTPN22... {December 15, 2007 1:34:23 PM PST}
- REDIRECT: Page directory gave bad page (PTPN22). Continuing with search.. Please correct entry: <26191,PTPN22>. {December 15, 2007 1:34:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:36:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PTPN22_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2p6x.
| PDB = {{PDB2|2p6x}}
| Name = Protein tyrosine phosphatase, non-receptor type 22 (lymphoid)
| HGNCid = 9652
| Symbol = PTPN22
| AltSymbols =; LYP; PEP; Lyp1; Lyp2; PTPN8
| OMIM = 600716
| ECnumber =
| Homologene = 7498
| MGIid = 107170
| GeneAtlas_image1 = PBB_GE_PTPN22_206060_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPN22_208010_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTPN22_208011_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030217 |text = T cell differentiation}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 26191
| Hs_Ensembl = ENSG00000134242
| Hs_RefseqProtein = NP_036543
| Hs_RefseqmRNA = NM_012411
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 114092981
| Hs_GenLoc_end = 114215904
| Hs_Uniprot = Q9Y2R2
| Mm_EntrezGene = 19260
| Mm_Ensembl = ENSMUSG00000027843
| Mm_RefseqmRNA = NM_008979
| Mm_RefseqProtein = NP_033005
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 103989353
| Mm_GenLoc_end = 104041308
| Mm_Uniprot = Q3TEL9
}}
}}
'''Protein tyrosine phosphatase, non-receptor type 22 (lymphoid)''', also known as '''PTPN22''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN22 protein tyrosine phosphatase, non-receptor type 22 (lymphoid)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26191| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein tyrosine phosphatase which is expressed primarily in lymphoid tissues. This enzyme associates with the molecular adapter protein CBL and may be involved in regulating CBL function in the T-cell receptor signaling pathway. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN22 protein tyrosine phosphatase, non-receptor type 22 (lymphoid)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26191| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gregersen PK |title=Pathways to gene identification in rheumatoid arthritis: PTPN22 and beyond. |journal=Immunol. Rev. |volume=204 |issue= |pages= 74-86 |year= 2005 |pmid= 15790351 |doi= 10.1111/j.0105-2896.2005.00243.x }}
*{{cite journal | author=Brand O, Gough S, Heward J |title=HLA , CTLA-4 and PTPN22 : the shared genetic master-key to autoimmunity? |journal=Expert reviews in molecular medicine |volume=7 |issue= 23 |pages= 1-15 |year= 2007 |pmid= 16229750 |doi= 10.1017/S1462399405009981 }}
*{{cite journal | author=Bottini N, Vang T, Cucca F, Mustelin T |title=Role of PTPN22 in type 1 diabetes and other autoimmune diseases. |journal=Semin. Immunol. |volume=18 |issue= 4 |pages= 207-13 |year= 2007 |pmid= 16697661 |doi= 10.1016/j.smim.2006.03.008 }}
*{{cite journal | author=Matthews RJ, Bowne DB, Flores E, Thomas ML |title=Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. |journal=Mol. Cell. Biol. |volume=12 |issue= 5 |pages= 2396-405 |year= 1992 |pmid= 1373816 |doi= }}
*{{cite journal | author=Gregorieff A, Cloutier JF, Veillette A |title=Sequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk). |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 13217-22 |year= 1998 |pmid= 9582365 |doi= }}
*{{cite journal | author=Cohen S, Dadi H, Shaoul E, ''et al.'' |title=Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp. |journal=Blood |volume=93 |issue= 6 |pages= 2013-24 |year= 1999 |pmid= 10068674 |doi= }}
*{{cite journal | author=Gjörloff-Wingren A, Saxena M, Han S, ''et al.'' |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells. |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412-21 |year= 2000 |pmid= 10940933 |doi= }}
*{{cite journal | author=Hill RJ, Zozulya S, Lu YL, ''et al.'' |title=The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation. |journal=Exp. Hematol. |volume=30 |issue= 3 |pages= 237-44 |year= 2002 |pmid= 11882361 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Chien W, Tidow N, Williamson EA, ''et al.'' |title=Characterization of a myeloid tyrosine phosphatase, Lyp, and its role in the Bcr-Abl signal transduction pathway. |journal=J. Biol. Chem. |volume=278 |issue= 30 |pages= 27413-20 |year= 2003 |pmid= 12764153 |doi= 10.1074/jbc.M304575200 }}
*{{cite journal | author=Bottini N, Musumeci L, Alonso A, ''et al.'' |title=A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes. |journal=Nat. Genet. |volume=36 |issue= 4 |pages= 337-8 |year= 2004 |pmid= 15004560 |doi= 10.1038/ng1323 }}
*{{cite journal | author=Begovich AB, Carlton VE, Honigberg LA, ''et al.'' |title=A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. |journal=Am. J. Hum. Genet. |volume=75 |issue= 2 |pages= 330-7 |year= 2004 |pmid= 15208781 |doi= 10.1086/422827 }}
*{{cite journal | author=Kyogoku C, Langefeld CD, Ortmann WA, ''et al.'' |title=Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE. |journal=Am. J. Hum. Genet. |volume=75 |issue= 3 |pages= 504-7 |year= 2004 |pmid= 15273934 |doi= 10.1086/423790 }}
*{{cite journal | author=Smyth D, Cooper JD, Collins JE, ''et al.'' |title=Replication of an association between the lymphoid tyrosine phosphatase locus (LYP/PTPN22) with type 1 diabetes, and evidence for its role as a general autoimmunity locus. |journal=Diabetes |volume=53 |issue= 11 |pages= 3020-3 |year= 2005 |pmid= 15504986 |doi= }}
*{{cite journal | author=Ladner MB, Bottini N, Valdes AM, Noble JA |title=Association of the single nucleotide polymorphism C1858T of the PTPN22 gene with type 1 diabetes. |journal=Hum. Immunol. |volume=66 |issue= 1 |pages= 60-4 |year= 2005 |pmid= 15620463 |doi= 10.1016/j.humimm.2004.09.016 }}
*{{cite journal | author=Orozco G, Sánchez E, González-Gay MA, ''et al.'' |title=Association of a functional single-nucleotide polymorphism of PTPN22, encoding lymphoid protein phosphatase, with rheumatoid arthritis and systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=52 |issue= 1 |pages= 219-24 |year= 2005 |pmid= 15641066 |doi= 10.1002/art.20771 }}
*{{cite journal | author=Steer S, Lad B, Grumley JA, ''et al.'' |title=Association of R602W in a protein tyrosine phosphatase gene with a high risk of rheumatoid arthritis in a British population: evidence for an early onset/disease severity effect. |journal=Arthritis Rheum. |volume=52 |issue= 1 |pages= 358-60 |year= 2005 |pmid= 15641088 |doi= 10.1002/art.20737 }}
*{{cite journal | author=Zheng W, She JX |title=Genetic association between a lymphoid tyrosine phosphatase (PTPN22) and type 1 diabetes. |journal=Diabetes |volume=54 |issue= 3 |pages= 906-8 |year= 2005 |pmid= 15734872 |doi= }}
*{{cite journal | author=Zhernakova A, Eerligh P, Wijmenga C, ''et al.'' |title=Differential association of the PTPN22 coding variant with autoimmune diseases in a Dutch population. |journal=Genes Immun. |volume=6 |issue= 6 |pages= 459-61 |year= 2005 |pmid= 15875058 |doi= 10.1038/sj.gene.6364220 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VCAN... {December 15, 2007 1:18:52 PM PST}
- REDIRECT: Page directory gave bad page (VCAN). Continuing with search.. Please correct entry: <1462,VCAN>. {December 15, 2007 1:19:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:19:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Versican
| HGNCid = 2464
| Symbol = VCAN
| AltSymbols =; CSPG2; DKFZp686K06110; ERVR; PG-M; WGN; WGN1
| OMIM = 118661
| ECnumber =
| Homologene = 3228
| MGIid = 102889
| GeneAtlas_image1 = PBB_GE_VCAN_204620_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_VCAN_204619_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_VCAN_211571_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0005540 |text = hyaluronic acid binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008037 |text = cell recognition}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1462
| Hs_Ensembl = ENSG00000038427
| Hs_RefseqProtein = NP_004376
| Hs_RefseqmRNA = NM_004385
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 82803339
| Hs_GenLoc_end = 82912737
| Hs_Uniprot = P13611
| Mm_EntrezGene = 13003
| Mm_Ensembl = ENSMUSG00000021614
| Mm_RefseqmRNA = XM_488510
| Mm_RefseqProtein = XP_488510
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 90131260
| Mm_GenLoc_end = 90216522
| Mm_Uniprot = P70267
}}
}}
'''Versican''', also known as '''VCAN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VCAN versican| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1462| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wight TN, Merrilees MJ |title=Proteoglycans in atherosclerosis and restenosis: key roles for versican. |journal=Circ. Res. |volume=94 |issue= 9 |pages= 1158-67 |year= 2004 |pmid= 15142969 |doi= 10.1161/01.RES.0000126921.29919.51 }}
*{{cite journal | author=Kenagy RD, Plaas AH, Wight TN |title=Versican degradation and vascular disease. |journal=Trends Cardiovasc. Med. |volume=16 |issue= 6 |pages= 209-15 |year= 2006 |pmid= 16839865 |doi= 10.1016/j.tcm.2006.03.011 }}
*{{cite journal | author=Perides G, Rahemtulla F, Lane WS, ''et al.'' |title=Isolation of a large aggregating proteoglycan from human brain. |journal=J. Biol. Chem. |volume=267 |issue= 33 |pages= 23883-7 |year= 1992 |pmid= 1429726 |doi= }}
*{{cite journal | author=Iozzo RV, Naso MF, Cannizzaro LA, ''et al.'' |title=Mapping of the versican proteoglycan gene (CSPG2) to the long arm of human chromosome 5 (5q12-5q14). |journal=Genomics |volume=14 |issue= 4 |pages= 845-51 |year= 1993 |pmid= 1478664 |doi= }}
*{{cite journal | author=Perides G, Lane WS, Andrews D, ''et al.'' |title=Isolation and partial characterization of a glial hyaluronate-binding protein. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5981-7 |year= 1989 |pmid= 2466833 |doi= }}
*{{cite journal | author=Bignami A, Lane WS, Andrews D, Dahl D |title=Structural similarity of hyaluronate binding proteins in brain and cartilage. |journal=Brain Res. Bull. |volume=22 |issue= 1 |pages= 67-70 |year= 1989 |pmid= 2469524 |doi= }}
*{{cite journal | author=Zimmermann DR, Ruoslahti E |title=Multiple domains of the large fibroblast proteoglycan, versican. |journal=EMBO J. |volume=8 |issue= 10 |pages= 2975-81 |year= 1990 |pmid= 2583089 |doi= }}
*{{cite journal | author=Krusius T, Gehlsen KR, Ruoslahti E |title=A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and growth factor-like sequences. |journal=J. Biol. Chem. |volume=262 |issue= 27 |pages= 13120-5 |year= 1987 |pmid= 2820964 |doi= }}
*{{cite journal | author=Naso MF, Zimmermann DR, Iozzo RV |title=Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32999-3008 |year= 1995 |pmid= 7528742 |doi= }}
*{{cite journal | author=Brown DM, Graemiger RA, Hergersberg M, ''et al.'' |title=Genetic linkage of Wagner disease and erosive vitreoretinopathy to chromosome 5q13-14. |journal=Arch. Ophthalmol. |volume=113 |issue= 5 |pages= 671-5 |year= 1995 |pmid= 7748141 |doi= }}
*{{cite journal | author=Dours-Zimmermann MT, Zimmermann DR |title=A novel glycosaminoglycan attachment domain identified in two alternative splice variants of human versican. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32992-8 |year= 1995 |pmid= 7806529 |doi= }}
*{{cite journal | author=Zako M, Shinomura T, Ujita M, ''et al.'' |title=Expression of PG-M(V3), an alternatively spliced form of PG-M without a chondroitin sulfate attachment in region in mouse and human tissues. |journal=J. Biol. Chem. |volume=270 |issue= 8 |pages= 3914-8 |year= 1995 |pmid= 7876137 |doi= }}
*{{cite journal | author=Yao LY, Moody C, Schönherr E, ''et al.'' |title=Identification of the proteoglycan versican in aorta and smooth muscle cells by DNA sequence analysis, in situ hybridization and immunohistochemistry. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 213-25 |year= 1994 |pmid= 7921538 |doi= }}
*{{cite journal | author=Bode-Lesniewska B, Dours-Zimmermann MT, Odermatt BF, ''et al.'' |title=Distribution of the large aggregating proteoglycan versican in adult human tissues. |journal=J. Histochem. Cytochem. |volume=44 |issue= 4 |pages= 303-12 |year= 1996 |pmid= 8601689 |doi= }}
*{{cite journal | author=Paulus W, Baur I, Dours-Zimmermann MT, Zimmermann DR |title=Differential expression of versican isoforms in brain tumors. |journal=J. Neuropathol. Exp. Neurol. |volume=55 |issue= 5 |pages= 528-33 |year= 1996 |pmid= 8627343 |doi= }}
*{{cite journal | author=Sartipy P, Johansen B, Camejo G, ''et al.'' |title=Binding of human phospholipase A2 type II to proteoglycans. Differential effect of glycosaminoglycans on enzyme activity. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26307-14 |year= 1996 |pmid= 8824283 |doi= }}
*{{cite journal | author=Aspberg A, Miura R, Bourdoulous S, ''et al.'' |title=The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 19 |pages= 10116-21 |year= 1997 |pmid= 9294172 |doi= }}
*{{cite journal | author=Sartipy P, Bondjers G, Hurt-Camejo E |title=Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=18 |issue= 12 |pages= 1934-41 |year= 1999 |pmid= 9848887 |doi= }}
*{{cite journal | author=Perveen R, Hart-Holden N, Dixon MJ, ''et al.'' |title=Refined genetic and physical localization of the Wagner disease (WGN1) locus and the genes CRTL1 and CSPG2 to a 2- to 2.5-cM region of chromosome 5q14.3. |journal=Genomics |volume=57 |issue= 2 |pages= 219-26 |year= 1999 |pmid= 10198161 |doi= 10.1006/geno.1999.5766 }}
*{{cite journal | author=Lemire JM, Braun KR, Maurel P, ''et al.'' |title=Versican/PG-M isoforms in vascular smooth muscle cells. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=19 |issue= 7 |pages= 1630-9 |year= 1999 |pmid= 10397680 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
