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Ankyrin-1

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ANK1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesANK1, ANK, SPH1, SPH2, ankyrin 1
External IDsOMIM: 612641; MGI: 88024; HomoloGene: 55427; GeneCards: ANK1; OMA:ANK1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

286

11733

Ensembl

ENSG00000029534

ENSMUSG00000031543

UniProt

P16157

Q02357

RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 8: 41.65 – 41.9 MbChr 8: 23.46 – 23.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ankyrin 1, also known as ANK-1, and erythrocyte ankyrin, is a protein that in humans is encoded by the ANK1 gene.[5][6]

Tissue distribution

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The protein encoded by this gene, Ankyrin 1, is the prototype of the ankyrin family, was first discovered in erythrocytes, but since has also been found in brain and muscles.[6]

Genetics

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Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known. Alternative polyadenylation accounting for the different sized erythrocytic ankyrin 1 mRNAs, has also been reported. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.[6]

Disease linkage

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Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis.[6]

ANK1 shows altered methylation and expression in Alzheimer's disease.[7][8] A gene expression study of postmortem brains has suggested ANK1 interacts with interferon-γ signalling.[9]

Function

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The ANK1 protein belongs to the ankyrin family that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact, and maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin-binding domain; and a carboxy-terminal regulatory domain, which is the least conserved and subject to variation.[6]

The small ANK1 (sAnk1) protein splice variants makes contacts with obscurin, a giant protein surrounding the contractile apparatus in striated muscle.[10]

Interactions

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ANK1 has been shown to interact with T-cell lymphoma invasion and metastasis-inducing protein 1,[11] Titin,[12] RHAG[13] and OBSCN.[14]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000029534 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031543 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lambert S, Yu H, Prchal JT, Lawler J, Ruff P, Speicher D, et al. (March 1990). "cDNA sequence for human erythrocyte ankyrin". Proceedings of the National Academy of Sciences of the United States of America. 87 (5): 1730–1734. Bibcode:1990PNAS...87.1730L. doi:10.1073/pnas.87.5.1730. PMC 53556. PMID 1689849.
  6. ^ a b c d e "Entrez Gene: ANK1 ankyrin 1, erythrocytic".
  7. ^ De Jager PL, Srivastava G, Lunnon K, Burgess J, Schalkwyk LC, Yu L, et al. (September 2014). "Alzheimer's disease: early alterations in brain DNA methylation at ANK1, BIN1, RHBDF2 and other loci". Nature Neuroscience. 17 (9): 1156–1163. doi:10.1038/nn.3786. PMC 4292795. PMID 25129075.
  8. ^ Lunnon K, Smith R, Hannon E, De Jager PL, Srivastava G, Volta M, et al. (September 2014). "Methylomic profiling implicates cortical deregulation of ANK1 in Alzheimer's disease". Nature Neuroscience. 17 (9): 1164–1170. doi:10.1038/nn.3782. PMC 4410018. PMID 25129077.
  9. ^ Liscovitch N, French L (2014). "Differential Co-Expression between α-Synuclein and IFN-γ Signaling Genes across Development and in Parkinson's Disease". PLOS ONE. 9 (12): e115029. Bibcode:2014PLoSO...9k5029L. doi:10.1371/journal.pone.0115029. PMC 4262449. PMID 25493648.
  10. ^ Borzok MA, Catino DH, Nicholson JD, Kontrogianni-Konstantopoulos A, Bloch RJ (November 2007). "Mapping the binding site on small ankyrin 1 for obscurin". The Journal of Biological Chemistry. 282 (44): 32384–32396. doi:10.1074/jbc.M704089200. PMID 17720975.
  11. ^ Bourguignon LY, Zhu H, Shao L, Chen YW (July 2000). "Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration". The Journal of Cell Biology. 150 (1): 177–191. doi:10.1083/jcb.150.1.177. PMC 2185563. PMID 10893266.
  12. ^ Kontrogianni-Konstantopoulos A, Bloch RJ (February 2003). "The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin". The Journal of Biological Chemistry. 278 (6): 3985–3991. doi:10.1074/jbc.M209012200. PMID 12444090.
  13. ^ Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, et al. (July 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". The Journal of Biological Chemistry. 278 (28): 25526–25533. doi:10.1074/jbc.M302816200. PMID 12719424.
  14. ^ Kontrogianni-Konstantopoulos A, Jones EM, Van Rossum DB, Bloch RJ (March 2003). "Obscurin is a ligand for small ankyrin 1 in skeletal muscle". Molecular Biology of the Cell. 14 (3): 1138–1148. doi:10.1091/mbc.E02-07-0411. PMC 151585. PMID 12631729.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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