AKAP10

AKAP10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3IM4, 3TMH
Identifiers
Aliases	AKAP10, AKAP-10, D-AKAP-2, D-AKAP2, PRKA10, A-kinase anchoring protein 10
External IDs	OMIM: 604694; MGI: 1890218; HomoloGene: 32452; GeneCards: AKAP10; OMA:AKAP10 - orthologs
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B2 Start 61,762,133 bp End 61,821,078 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve Achilles tendon trabecular bone monocyte nipple blood optic nerve bone marrow cells visceral pleura pancreatic ductal cell Top expressed in spermatid endocardial cushion zygote secondary oocyte renal corpuscle medullary collecting duct Rostral migratory stream seminiferous tubule spermatocyte primary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding protein kinase A binding Cellular component plasma membrane membrane mitochondrion cytoplasm cytosol protein-containing complex Biological process blood coagulation signal transduction protein localization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11216 56697 Ensembl n/a ENSMUSG00000047804 UniProt O43572 O88845 RefSeq (mRNA) NM_007202 NM_001330152 NM_019921 RefSeq (protein) NP_001317081 NP_009133 NP_064305 Location (UCSC) n/a Chr 11: 61.76 – 61.82 Mb PubMed search
Wikidata
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A kinase anchor protein 10, mitochondrial is an enzyme that in humans is encoded by the AKAP10 gene.

Function

The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein interacts with both the type I and type II regulatory subunits of PKA; therefore, it is a dual-specific AKAP. This protein is highly enriched in mitochondria. It contains RGS (regulator of G protein signalling) domains, in addition to a PKA-RII subunit-binding domain. The mitochondrial localization and the presence of RGS domains may have important implications for the function of this protein in PKA and G protein signal transduction.

Interactions

AKAP10 has been shown to interact with PDZK1 and PRKAR1A.

External links

• Human AKAP10 genome location and AKAP10 gene details page in the UCSC Genome Browser.

Further reading

• Lester LB, Scott JD (1997). "Anchoring and scaffold proteins for kinases and phosphatases". Recent Prog. Horm. Res. 52: 409–29, discussion 429–30. PMID 9238861.
• Michel JJ, Scott JD (2002). "AKAP mediated signal transduction". Annu. Rev. Pharmacol. Toxicol. 42: 235–57. doi:10.1146/annurev.pharmtox.42.083101.135801. PMID 11807172.
• Epplen C, Epplen JT (1994). "Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes". Hum. Genet. 93 (1): 35–41. doi:10.1007/BF00218910. PMID 7505766. S2CID 22998633.
• Wang L, Sunahara RK, Krumins A, Perkins G, Crochiere ML, Mackey M, Bell S, Ellisman MH, Taylor SS (2001). "Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3220–5. Bibcode:2001PNAS...98.3220W. doi:10.1073/pnas.051633398. PMC 30634. PMID 11248059.
• Hamuro Y, Burns L, Canaves J, Hoffman R, Taylor S, Woods V (2002). "Domain organization of D-AKAP2 revealed by enhanced deuterium exchange-mass spectrometry (DXMS)". J. Mol. Biol. 321 (4): 703–14. CiteSeerX 10.1.1.477.4850. doi:10.1016/S0022-2836(02)00419-9. PMID 12206784.
• Kammerer S, Burns-Hamuro LL, Ma Y, Hamon SC, Canaves JM, Shi MM, Nelson MR, Sing CF, Cantor CR, Taylor SS, Braun A (2003). "Amino acid variant in the kinase binding domain of dual-specific A kinase-anchoring protein 2: a disease susceptibility polymorphism". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 4066–71. Bibcode:2003PNAS..100.4066K. doi:10.1073/pnas.2628028100. PMC 153049. PMID 12646697.
• Gisler SM, Pribanic S, Bacic D, Forrer P, Gantenbein A, Sabourin LA, Tsuji A, Zhao ZS, Manser E, Biber J, Murer H (2003). "PDZK1: I. a major scaffolder in brush borders of proximal tubular cells". Kidney Int. 64 (5): 1733–45. doi:10.1046/j.1523-1755.2003.00266.x. PMID 14531806.
• Burns-Hamuro LL, Barraclough DM, Taylor SS (2004). "Identification and Functional Analysis of Dual-Specific a Kinase-Anchoring Protein-2". Regulators of G-Protein Signaling, Part B. Methods in Enzymology. Vol. 390. Academic Press. pp. 354–74. doi:10.1016/S0076-6879(04)90022-5. ISBN 978-0-12-182795-3. PMID 15488188.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Tingley WG, Pawlikowska L, Zaroff JG, Kim T, Nguyen T, Young SG, Vranizan K, Kwok PY, Whooley MA, Conklin BR (2007). "Gene-trapped mouse embryonic stem cell-derived cardiac myocytes and human genetics implicate AKAP10 in heart rhythm regulation". Proc. Natl. Acad. Sci. U.S.A. 104 (20): 8461–6. Bibcode:2007PNAS..104.8461T. doi:10.1073/pnas.0610393104. PMC 1866184. PMID 17485678.