PTPN6

From Wikipedia, the free encyclopedia

Protein tyrosine phosphatase, non-receptor type 6

PDB rendering based on 1fpr.

Available structures: 1fpr, 1gwz, 1x6c, 2b3o

Identifiers

Symbol(s)

PTPN6; HCP; HCPH; HPTP1C; PTP-1C; SH-PTP1; SHP-1; SHP-1L; SHP1

External IDs

OMIM: 176883 MGI: 96055 HomoloGene: 56589

Gene ontology
Molecular Function:	• phosphotyrosine binding • molecular_function • protein tyrosine phosphatase activity • protein binding • hydrolase activity
Cellular Component:	• cellular_component • cytoskeleton • membrane
Biological Process:	• protein amino acid dephosphorylation • apoptosis • G-protein coupled receptor protein signaling pathway • intracellular signaling cascade • negative regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002831 (mRNA)
NP_002822 (protein)

NM_001077705 (mRNA)
NP_001071173 (protein)

Location

Chr 12: 6.93 - 6.94 Mb

Chr 6: 124.69 - 124.7 Mb

Pubmed search

[1]

[2]

Protein tyrosine phosphatase, non-receptor type 6, also known as PTPN6, is a human gene.

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.^[1]

[edit] References

^ Entrez Gene: PTPN6 protein tyrosine phosphatase, non-receptor type 6.

[edit] Further reading

Blasioli J, Goodnow CC (2002). "Lyn/CD22/SHP-1 and their importance in autoimmunity.". Curr. Dir. Autoimmun. 5: 151–60. PMID 11826756.
Tortorella C, Simone O, Piazzolla G, et al. (2007). "Age-related impairment of GM-CSF-induced signalling in neutrophils: role of SHP-1 and SOCS proteins.". Ageing Res. Rev. 6 (2): 81–93. doi:10.1016/j.arr.2006.10.001. PMID 17142110.
Plutzky J, Neel BG, Rosenberg RD, et al. (1992). "Chromosomal localization of an SH2-containing tyrosine phosphatase (PTPN6).". Genomics 13 (3): 869–72. PMID 1639416.
Shen SH, Bastien L, Posner BI, Chrétien P (1991). "A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases.". Nature 352 (6337): 736–9. doi:10.1038/352736a0. PMID 1652101.
Yi TL, Cleveland JL, Ihle JN (1992). "Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13.". Mol. Cell. Biol. 12 (2): 836–46. PMID 1732748.
Plutzky J, Neel BG, Rosenberg RD (1992). "Isolation of a src homology 2-containing tyrosine phosphatase.". Proc. Natl. Acad. Sci. U.S.A. 89 (3): 1123–7. PMID 1736296.
Uchida T, Matozaki T, Noguchi T, et al. (1994). "Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains.". J. Biol. Chem. 269 (16): 12220–8. PMID 7512963.
Bouchard P, Zhao Z, Banville D, et al. (1994). "Phosphorylation and identification of a major tyrosine phosphorylation site in protein tyrosine phosphatase 1C.". J. Biol. Chem. 269 (30): 19585–9. PMID 7518460.
Pani G, Kozlowski M, Cambier JC, et al. (1995). "Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling.". J. Exp. Med. 181 (6): 2077–84. PMID 7539038.
Arnold SF, Obourn JD, Jaffe H, Notides AC (1995). "Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro.". Mol. Endocrinol. 9 (1): 24–33. PMID 7539106.
Doody GM, Justement LB, Delibrias CC, et al. (1995). "A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP.". Science 269 (5221): 242–4. PMID 7618087.
Yetter A, Uddin S, Krolewski JJ, et al. (1995). "Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase.". J. Biol. Chem. 270 (31): 18179–82. PMID 7629131.
Banville D, Stocco R, Shen SH (1995). "Human protein tyrosine phosphatase 1C (PTPN6) gene structure: alternate promoter usage and exon skipping generate multiple transcripts.". Genomics 27 (1): 165–73. doi:10.1006/geno.1995.1020. PMID 7665165.
Yi T, Ihle JN (1993). "Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand.". Mol. Cell. Biol. 13 (6): 3350–8. PMID 7684496.
D'Ambrosio D, Hippen KL, Minskoff SA, et al. (1995). "Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1.". Science 268 (5208): 293–7. PMID 7716523.
Li RY, Gaits F, Ragab A, et al. (1995). "Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertussis toxin-sensitive heterotrimeric G-protein.". EMBO J. 14 (11): 2519–26. PMID 7781604.
Klingmüller U, Lorenz U, Cantley LC, et al. (1995). "Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals.". Cell 80 (5): 729–38. PMID 7889566.
Lorenz U, Ravichandran KS, Pei D, et al. (1994). "Lck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTP1 in murine T cells.". Mol. Cell. Biol. 14 (3): 1824–34. PMID 8114715.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Yi T, Mui AL, Krystal G, Ihle JN (1994). "Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis.". Mol. Cell. Biol. 13 (12): 7577–86. PMID 8246974.