Protein tyrosine phosphatase, non-receptor type 1
PDB rendering based on 1a5y.
Available structures
1a5y, 1aax, 1bzc, 1bzh, 1bzj, 1c83, 1c84, 1c85, 1c86, 1c87, 1c88, 1ecv, 1een, 1eeo, 1g1f, 1g1g, 1g1h, 1g7f, 1g7g, 1gfy, 1i57, 1jf7, 1kak, 1kav, 1l8g, 1lqf, 1nl9, 1nny, 1no6, 1nwe, 1nwl, 1nz7, 1oem, 1oeo, 1oes, 1oet, 1oeu, 1oev, 1ony, 1onz, 1pa1, 1ph0, 1ptt, 1ptu, 1ptv, 1pty, 1pxh, 1pyn, 1q1m, 1q6j, 1q6m, 1q6n, 1q6p, 1q6s, 1q6t, 1qxk, 1sug, 1t48, 1t49, 1t4j, 1wax, 1xbo, 2azr, 2b07, 2b4s, 2bgd, 2bge, 2cm2, 2cm3, 2cm7, 2cm8, 2cma, 2cmb, 2cmc, 2cne, 2cnf, 2cng, 2cnh, 2cni, 2f6f, 2f6t, 2f6v, 2f6w, 2f6y, 2f6z, 2f70, 2f71, 2fjm, 2fjn, 2h4g, 2h4k, 2hb1, 2hnp, 2hnq, 2nt7, 2nta
Identifiers
Symbols	PTPN1; PTP1B
External IDs	OMIM: 176885 MGI: 97805 HomoloGene: 2119
Gene ontology Molecular function • protein tyrosine phosphatase activity • protein binding • hydrolase activity Cellular component • soluble fraction • cytoplasm • endoplasmic reticulum Biological process • protein amino acid dephosphorylation • signal transduction • insulin receptor signaling pathway
Orthologs
Species	Human	Mouse
Entrez	5770	19246
Ensembl	ENSG00000196396	ENSMUSG00000027540
UniProt	P18031	Q3T9Y9
RefSeq	NM_002827 (mRNA)	NM_011201 (mRNA)
	NP_002818 (protein)	NP_035331 (protein)
Location	Chr 20: 48.56 - 48.63 Mb	Chr 2: 167.62 - 167.67 Mb
PubMed search	[1]	[2]

Tyrosine-protein phosphatase non-receptor type 1 is an enzyme that in humans is encoded by the PTPN1 gene.^[1]

The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation.^[2]

[edit] See also

• Protein tyrosine phosphatase

[edit] Interactions

PTPN1 has been shown to interact with BCAR1,^[3] Epidermal growth factor receptor,^[4][5] Grb2^[6][3] and IRS1.^[6][7]

[edit] References

v • d • e PDB Gallery 1a5y: PROTEIN TYROSINE PHOSPHATASE 1B CYSTEINYL-PHOSPHATE INTERMEDIATE   1aax: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO BIS(PARA-PHOSPHOPHENYL)METHANE (BPPM) MOLECULES   1bzc: HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI   1bzh: CYCLIC PEPTIDE INHIBITOR OF HUMAN PTP1B   1bzj: Human ptp1b complexed with tpicooh   1c83: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 6-(OXALYL-AMINO)-1H-INDOLE-5-CARBOXYLIC ACID   1c84: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 3-(OXALYL-AMINO)-NAPHTHALENE-2-CARBOXLIC ACID   1c85: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO)-BENZOIC ACID   1c86: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B (R47V,D48N) COMPLEXED WITH 2-(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID   1c87: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID   1c88: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDINE-3-CARBOXYLIC ACID   1ecv: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 5-IODO-2-(OXALYL-AMINO)-BENZOIC ACID   1een: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-D-A-D-BPA-PTYR-L-I-P-Q-Q-G   1eeo: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-E-L-E-F-PTYR-M-D-Y-E-NH2   1g1f: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE   1g1g: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A MONO-PHOSPHORYLATED PEPTIDE (ETDY(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE   1g1h: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE   1g7f: HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177496   1g7g: HUMAN PTP1B CATALYTIC DOMAIN COMPLEXES WITH PNU179326   1gfy: RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA   1i57: CRYSTAL STRUCTURE OF APO HUMAN PTP1B (C215S) MUTANT   1jf7: HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177836   1kak: Human Tyrosine Phosphatase 1B Complexed with an Inhibitor   1kav: Human Tyrosine Phosphatase 1B Complexed with an Inhibitor   1l8g: Crystal structure of PTP1B complexed with 7-(1,1-Dioxo-1H-benzo[d]isothiazol-3-yloxymethyl)-2-(oxalyl-amino)-4,7-dihydro-5H-thieno[2,3-c]pyran-3-carboxylic acid   1lqf: Structure of PTP1b in Complex with a Peptidic Bisphosphonate Inhibitor   1nl9: Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 12 Using a Linked-Fragment Strategy   1nny: Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 23 Using a Linked-Fragment Strategy   1no6: Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 5 Using a Linked-Fragment Strategy   1nwe: Ptp1B R47C Modified at C47 with N-[4-(2-{2-[3-(2-Bromo-acetylamino)-propionylamino]-3-hydroxy-propionylamino}-ethyl)-phenyl]-oxalamic acid   The maximum number of images (30) is exceeded !

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