PTPRA

PTPRA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1P15, 1YFO
Identifiers
Aliases	PTPRA , HEPTP, HLPR, HPTPA, HPTPalpha, LRP, PTPA, PTPRL2, R-PTP-alpha, RPTPA, protein tyrosine phosphatase, receptor type A, protein tyrosine phosphatase receptor type A
External IDs	OMIM: 176884; MGI: 97808; HomoloGene: 20621; GeneCards: PTPRA; OMA:PTPRA - orthologs
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20p13 Start 2,864,184 bp [1] End 3,039,076 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 F1|2 63.23 cM Start 130,292,198 bp [2] End 130,398,044 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon ventricular zone ganglionic eminence right frontal lobe prefrontal cortex nucleus accumbens right hemisphere of cerebellum amygdala cingulate gyrus anterior cingulate cortex Top expressed in dentate gyrus of hippocampal formation granule cell stroma of bone marrow epithelium of lens superior frontal gyrus ventricular zone subiculum right kidney primary visual cortex cerebellar cortex nucleus accumbens More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding phosphatase activity protein tyrosine phosphatase activity phosphoprotein phosphatase activity transmembrane receptor protein tyrosine phosphatase activity hydrolase activity Cellular component receptor complex integral component of plasma membrane integral component of membrane membrane extracellular exosome plasma membrane intracellular anatomical structure Schaffer collateral - CA1 synapse integral component of synaptic membrane Biological process dephosphorylation axon guidance protein phosphorylation protein dephosphorylation MAPK cascade peptidyl-tyrosine dephosphorylation insulin receptor signaling pathway regulation of molecular function modulation of chemical synaptic transmission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5786 19262 Ensembl ENSG00000132670 ENSMUSG00000027303 UniProt P18433 Q5JWG0 P18052 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 Mb Chr 2: 130.29 – 130.4 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Function

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

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

References

1. GRCh38: Ensembl release 89: ENSG00000132670 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027303 – 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. 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. "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

• Mustelin T, Hunter T (2002). "Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha". Sci. STKE. 2002 (115): PE3. doi:10.1126/stke.2002.115.pe3. PMID   11796915. S2CID   1111167.
• Zheng XM, Wang Y, Pallen CJ (1992). "Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase". Nature. 359 (6393): 336–9. Bibcode:1992Natur.359..336Z. doi:10.1038/359336a0. PMID   1383828. S2CID   1283722.
• Jirik FR, Anderson LL, Duncan AM (1992). "The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is assigned to chromosome 20p13". Cytogenet. Cell Genet. 60 (2): 117–8. doi:10.1159/000133317. PMID   1611910.
• Rao VV, Löffler C, Sap J, Schlessinger J, Hansmann I (1992). "The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH)". Genomics. 13 (3): 906–7. doi:10.1016/0888-7543(92)90186-V. PMID   1639427.
• Sap J, D'Eustachio P, Givol D, Schlessinger J (1990). "Cloning and expression of a widely expressed receptor tyrosine phosphatase". Proc. Natl. Acad. Sci. U.S.A. 87 (16): 6112–6. Bibcode:1990PNAS...87.6112S. doi: 10.1073/pnas.87.16.6112 . PMC   54482 . PMID   2166945.
• Krueger NX, Streuli M, Saito H (1990). "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases". EMBO J. 9 (10): 3241–52. doi:10.1002/j.1460-2075.1990.tb07523.x. PMC   552056 . PMID   2170109.
• Ohagi S, Nishi M, Steiner DF (1991). "Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide)". Nucleic Acids Res. 18 (23): 7159. doi:10.1093/nar/18.23.7159. PMC   332805 . PMID   2175890.
• den Hertog J, Tracy S, Hunter T (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.
• 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 J. 12 (10): 3789–98. doi:10.1002/j.1460-2075.1993.tb06057.x. PMC   413662 . PMID   7691597.
• Stover DR, Furet P, Lydon NB (1996). "Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain". J. Biol. Chem. 271 (21): 12481–7. doi: 10.1074/jbc.271.21.12481 . PMID   8647855.
• den Hertog J, Hunter T (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.
• Shimizu Y, Sugiyama H, Fujii Y, Sasaki K, Inoue K, Ogawa H, Tamaki H, Miyake S, Oji Y, Soma T, Yamagami T, Hirata M, Ikeda K, Monden T, Kishimoto T (1997). "Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells". Am. J. Hematol. 54 (1): 1–11. doi:10.1002/(SICI)1096-8652(199701)54:1<1::AID-AJH1>3.0.CO;2-1. PMID   8980254. S2CID   36581335.
• Lim KL, Lai DS, Kalousek MB, Wang Y, Pallen CJ (1997). "Kinetic analysis of two closely related receptor-like protein-tyrosine-phosphatases, PTP alpha and PTP epsilon". Eur. J. Biochem. 245 (3): 693–700. doi: 10.1111/j.1432-1033.1997.00693.x . PMID   9183007.
• Somani AK, Bignon JS, Mills GB, Siminovitch KA, Branch DR (1997). "Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase". J. Biol. Chem. 272 (34): 21113–9. doi: 10.1074/jbc.272.34.21113 . PMID   9261115.
• Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U (1997). "gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules". Int. Immunol. 9 (8): 1141–7. doi: 10.1093/intimm/9.8.1141 . PMID   9263011.
• Norris K, Norris F, Kono DH, Vestergaard H, Pedersen O, Theofilopoulos AN, Møller NP (1997). "Expression of protein-tyrosine phosphatases in the major insulin target tissues". FEBS Lett. 415 (3): 243–8. Bibcode:1997FEBSL.415..243N. doi:10.1016/S0014-5793(97)01133-2. PMID   9357975. S2CID   9414519.
• Bhandari V, Lim KL, Pallen CJ (1998). "Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn". J. Biol. Chem. 273 (15): 8691–8. doi: 10.1074/jbc.273.15.8691 . PMID   9535845.
• Harder KW, Moller NP, Peacock JW, Jirik FR (1998). "Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion". J. Biol. Chem. 273 (48): 31890–900. doi: 10.1074/jbc.273.48.31890 . PMID   9822658.