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PTPRA

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PTPRA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPTPRA, HEPTP, HLPR, HPTPA, HPTPalpha, LRP, PTPA, PTPRL2, R-PTP-alpha, RPTPA, protein tyrosine phosphatase, receptor type A, protein tyrosine phosphatase receptor type A
External IDsOMIM: 176884; MGI: 97808; HomoloGene: 20621; GeneCards: PTPRA; OMA:PTPRA - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_080841
NM_002836
NM_080840

NM_001163688
NM_008980
NM_001355161

RefSeq (protein)

NP_002827
NP_543030
NP_543031

NP_001157160
NP_033006
NP_001342090

Location (UCSC)Chr 20: 2.86 – 3.04 MbChr 2: 130.29 – 130.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.[5][6][7]

Function

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The protein encoded by this gene is a member of the receptor tyrosine phosphatases (RTP), a family of protein tyrosine phosphatases. RTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This RTP contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type RTP. This RTP has been shown to dephosphorylate and activate Src family tyrosine kinases,[8] and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported.[7]

Interactions

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PTPRA has been shown to interact with Grb2[9][10][11] and KCNA2.[12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000132670Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027303Ensembl, 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. ^ Jirik FR, Janzen NM, Melhado IG, Harder KW (December 1990). "Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase". FEBS Lett. 273 (1–2): 239–42. Bibcode:1990FEBSL.273..239J. doi:10.1016/0014-5793(90)81094-5. PMID 2172030. S2CID 31501542.
  6. ^ Kaplan R, Morse B, Huebner K, Croce C, Howk R, Ravera M, Ricca G, Jaye M, Schlessinger J (October 1990). "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain". Proc Natl Acad Sci U S A. 87 (18): 7000–4. Bibcode:1990PNAS...87.7000K. doi:10.1073/pnas.87.18.7000. PMC 54670. PMID 2169617.
  7. ^ a b "Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A".
  8. ^ den Hertog J, Pals CE, Peppelenbosch MP, Tertoolen LG, de Laat SW, Kruijer W (1993). "Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation". EMBO Journal. 12 (10): 3789–98. doi:10.1002/j.1460-2075.1993.tb06057.x. PMC 413662. PMID 7691597.
  9. ^ den Hertog J, Hunter T (June 1996). "Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains". EMBO J. 15 (12): 3016–27. doi:10.1002/j.1460-2075.1996.tb00665.x. PMC 450243. PMID 8670803.
  10. ^ den Hertog J, Tracy S, Hunter T (July 1994). "Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo". EMBO J. 13 (13): 3020–32. doi:10.1002/j.1460-2075.1994.tb06601.x. PMC 395191. PMID 7518772.
  11. ^ Zheng XM, Resnick RJ, Shalloway D (June 2002). "Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation". J. Biol. Chem. 277 (24): 21922–9. doi:10.1074/jbc.M201394200. PMC 5641391. PMID 11923305.
  12. ^ Tsai W, Morielli AD, Cachero TG, Peralta EG (January 1999). "Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity". EMBO J. 18 (1): 109–18. doi:10.1093/emboj/18.1.109. PMC 1171107. PMID 9878055.

Further reading

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