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UniProtKB/Swiss-Prot entry P18031


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTN1_HUMAN
Primary accession number P18031
Secondary accession numbers Q5TGD8 Q9BQV9 Q9NQQ4
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1990 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 128)
Name and origin of the protein
Protein name Tyrosine-protein phosphatase non-receptor type 1
Synonyms EC 3.1.3.48
Protein-tyrosine phosphatase 1B
PTP-1B
Gene name
Name: PTPN1
Synonyms: PTP1B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1073/pnas.87.7.2735; PubMed=2157211 [NCBI, ExPASy, EBI, Israel, Japan]
Chernoff J., Schievella A.R., Jost C.A., Erikson R.L., Neel B.G.;
"Cloning of a cDNA for a major human protein-tyrosine-phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 87:2735-2739(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Placenta;
DOI=10.1073/pnas.87.13.5148; PubMed=2164224 [NCBI, ExPASy, EBI, Israel, Japan]
Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A., Green N.R., Hill D.E.;
"Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B.";
Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-321.
TISSUE=Placenta;
DOI=10.1073/pnas.86.14.5252; PubMed=2546149 [NCBI, ExPASy, EBI, Israel, Japan]
Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.;
"Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins.";
Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989).
[7]
PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.
PubMed=8491187 [NCBI, ExPASy, EBI, Israel, Japan]
Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.;
"Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation.";
EMBO J. 12:1937-1946(1993).
[8]
SUBCELLULAR LOCATION.
DOI=10.1016/0092-8674(92)90190-N; PubMed=1739967 [NCBI, ExPASy, EBI, Israel, Japan]
Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.;
"The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence.";
Cell 68:545-560(1992).
[9]
PHOSPHORYLATION AT SER-50, AND MUTAGENESIS OF SER-50.
DOI=10.1210/me.15.10.1768; PubMed=11579209 [NCBI, ExPASy, EBI, Israel, Japan]
Ravichandran L.V., Chen H., Li Y., Quon M.J.;
"Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor.";
Mol. Endocrinol. 15:1768-1780(2001).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-295, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-352, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-321.
DOI=10.1126/science.8128219; PubMed=8128219 [NCBI, ExPASy, EBI, Israel, Japan]
Barford D., Flint A.J., Tonks N.K.;
"Crystal structure of human protein tyrosine phosphatase 1B.";
Science 263:1397-1404(1994).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-298 OF MUTANT SER-215.
DOI=10.1073/pnas.94.25.13420; PubMed=9391040 [NCBI, ExPASy, EBI, Israel, Japan]
Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.;
"Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design.";
Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-285.
DOI=10.1074/jbc.273.17.10454; PubMed=9553104 [NCBI, ExPASy, EBI, Israel, Japan]
Pannifer A.D., Flint A.J., Tonks N.K., Barford D.;
"Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography.";
J. Biol. Chem. 273:10454-10462(1998).
[17]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-298.
DOI=10.1021/bi9816958; PubMed=9922143 [NCBI, ExPASy, EBI, Israel, Japan]
Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.;
"Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics.";
Biochemistry 37:17773-17783(1998).
[18]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, AND CROSS-LINK 215-CYS-SER-216.
DOI=10.1038/nature01680; PubMed=12802338 [NCBI, ExPASy, EBI, Israel, Japan]
Salmeen A., Andersen J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K., Barford D.;
"Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate.";
Nature 423:769-773(2003).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, AND CROSS-LINK 215-CYS-SER-216.
DOI=10.1038/nature01681; PubMed=12802339 [NCBI, ExPASy, EBI, Israel, Japan]
Van Montfort R.L.M., Congreve M., Tisi D., Carr R., Jhoti H.;
"Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B.";
Nature 423:773-777(2003).
[20]
ASSOCIATION OF VARIANT LEU-387 WITH LOW GLUCOSE TOLERANCE.
DOI=10.1038/oby.2005.95; PubMed=15919835 [NCBI, ExPASy, EBI, Israel, Japan]
Ukkola O., Rankinen T., Lakka T., Leon A.S., Skinner J.S., Wilmore J.H., Rao D.C., Kesaeniemi Y.A., Bouchard C.;
"Protein tyrosine phosphatase 1B variant associated with fat distribution and insulin metabolism.";
Obes. Res. 13:829-834(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31724; AAA60223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33689; AAA60157.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33684; AAA60158.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33688; AAA60158.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33687; AAA60158.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33686; AAA60158.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33685; AAA60158.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006752; AAP35398.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133230; CAC00618.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL034429; CAC00618.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL034429; CAI23215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133230; CAI23215.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015660; AAH15660.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018164; AAH18164.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00297261; -.
PIR A35992; TPHUN1.
RefSeq NP_002818.1; -.
UniGene Hs.417549
3D structure databases
PDB
1A5Y; X-ray; 2.50 A; A=1-330.[ExPASy / RCSB / EBI]
1AAX; X-ray; 1.90 A; A=1-321.[ExPASy / RCSB / EBI]
1BZC; X-ray; 2.35 A; A=1-321.[ExPASy / RCSB / EBI]
1BZH; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1BZJ; X-ray; 2.25 A; A=2-298.[ExPASy / RCSB / EBI]
1C83; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
1C84; X-ray; 2.35 A; A=1-298.[ExPASy / RCSB / EBI]
1C85; X-ray; 2.72 A; A=1-298.[ExPASy / RCSB / EBI]
1C86; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
1C87; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1C88; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
1ECV; X-ray; 1.95 A; A=1-298.[ExPASy / RCSB / EBI]
1EEN; X-ray; 1.90 A; A=1-321.[ExPASy / RCSB / EBI]
1EEO; X-ray; 1.80 A; A=1-321.[ExPASy / RCSB / EBI]
1G1F; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1G1G; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1G1H; X-ray; 2.40 A; A=1-298.[ExPASy / RCSB / EBI]
1G7F; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
1G7G; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1GFY; X-ray; 2.13 A; A=1-298.[ExPASy / RCSB / EBI]
1I57; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1JF7; X-ray; 2.20 A; A/B=1-298.[ExPASy / RCSB / EBI]
1KAK; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1KAV; X-ray; 2.35 A; A=1-298.[ExPASy / RCSB / EBI]
1L8G; X-ray; 2.50 A; A=1-321.[ExPASy / RCSB / EBI]
1LQF; X-ray; 2.50 A; A/B/C/D=1-283.[ExPASy / RCSB / EBI]
1NL9; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
1NNY; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
1NO6; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
1NWE; X-ray; 3.10 A; A=1-298.[ExPASy / RCSB / EBI]
1NWL; X-ray; 2.40 A; A=1-298.[ExPASy / RCSB / EBI]
1NZ7; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
1OEM; X-ray; 1.80 A; X=1-321.[ExPASy / RCSB / EBI]
1OEO; X-ray; 2.15 A; X=1-321.[ExPASy / RCSB / EBI]
1OES; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
1OET; X-ray; 2.30 A; A=1-321.[ExPASy / RCSB / EBI]
1OEU; X-ray; 2.50 A; A=1-321.[ExPASy / RCSB / EBI]
1OEV; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
1ONY; X-ray; 2.15 A; A=1-321.[ExPASy / RCSB / EBI]
1ONZ; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
1PA1; X-ray; 1.60 A; A=1-298.[ExPASy / RCSB / EBI]
1PH0; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
1PTT; X-ray; 2.90 A; A=1-321.[ExPASy / RCSB / EBI]
1PTU; X-ray; 2.60 A; A=1-321.[ExPASy / RCSB / EBI]
1PTV; X-ray; 2.30 A; A=1-321.[ExPASy / RCSB / EBI]
1PTY; X-ray; 1.85 A; A=1-321.[ExPASy / RCSB / EBI]
1PXH; X-ray; 2.15 A; A=1-321.[ExPASy / RCSB / EBI]
1PYN; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
1Q1M; X-ray; 2.60 A; A=1-321.[ExPASy / RCSB / EBI]
1Q6J; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1Q6M; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1Q6N; X-ray; 2.10 A; A/B=1-298.[ExPASy / RCSB / EBI]
1Q6P; X-ray; 2.30 A; A/B=1-298.[ExPASy / RCSB / EBI]
1Q6S; X-ray; 2.20 A; A/B=1-298.[ExPASy / RCSB / EBI]
1Q6T; X-ray; 2.30 A; A/B=1-298.[ExPASy / RCSB / EBI]
1QXK; X-ray; 2.30 A; A=1-321.[ExPASy / RCSB / EBI]
1SUG; X-ray; 1.95 A; A=1-321.[ExPASy / RCSB / EBI]
1T48; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1T49; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1T4J; X-ray; 2.70 A; A=1-298.[ExPASy / RCSB / EBI]
1WAX; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
1XBO; X-ray; 2.50 A; A=1-321.[ExPASy / RCSB / EBI]
2AZR; X-ray; 2.00 A; A=1-299.[ExPASy / RCSB / EBI]
2B07; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2B4S; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
2BGD; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
2BGE; X-ray; 1.80 A; A=1-321.[ExPASy / RCSB / EBI]
2CM2; X-ray; 1.50 A; A=2-298.[ExPASy / RCSB / EBI]
2CM3; X-ray; 2.10 A; A/B=1-298.[ExPASy / RCSB / EBI]
2CM7; X-ray; 2.10 A; A=1-321.[ExPASy / RCSB / EBI]
2CM8; X-ray; 2.10 A; A=1-321.[ExPASy / RCSB / EBI]
2CMA; X-ray; 2.30 A; A=1-321.[ExPASy / RCSB / EBI]
2CMB; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2CMC; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2CNE; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2CNF; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
2CNG; X-ray; 1.90 A; A=1-321.[ExPASy / RCSB / EBI]
2CNH; X-ray; 1.80 A; A=1-321.[ExPASy / RCSB / EBI]
2CNI; X-ray; 2.00 A; A=1-321.[ExPASy / RCSB / EBI]
2F6F; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2F6T; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2F6V; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2F6W; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2F6Y; X-ray; 2.15 A; A=1-298.[ExPASy / RCSB / EBI]
2F6Z; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2F70; X-ray; 2.12 A; A=1-298.[ExPASy / RCSB / EBI]
2F71; X-ray; 1.55 A; A=1-298.[ExPASy / RCSB / EBI]
2FJM; X-ray; 2.10 A; A/B=1-298.[ExPASy / RCSB / EBI]
2FJN; X-ray; 2.20 A; A/B=1-298.[ExPASy / RCSB / EBI]
2H4G; X-ray; 2.50 A; A=1-299.[ExPASy / RCSB / EBI]
2H4K; X-ray; 2.30 A; A=1-299.[ExPASy / RCSB / EBI]
2HB1; X-ray; 2.00 A; A=1-299.[ExPASy / RCSB / EBI]
2HNP; X-ray; 2.85 A; A=1-321.[ExPASy / RCSB / EBI]
2HNQ; X-ray; 2.85 A; A=1-321.[ExPASy / RCSB / EBI]
2NT7; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2NTA; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2QBP; X-ray; 2.50 A; A=1-299.[ExPASy / RCSB / EBI]
2QBQ; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2QBR; X-ray; 2.30 A; A=1-299.[ExPASy / RCSB / EBI]
2QBS; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2VEU; X-ray; 2.40 A; A=1-321.[ExPASy / RCSB / EBI]
2VEV; X-ray; 1.80 A; A=1-321.[ExPASy / RCSB / EBI]
2VEW; X-ray; 2.00 A; A=1-321.[ExPASy / RCSB / EBI]
2VEX; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
2VEY; X-ray; 2.20 A; A=1-321.[ExPASy / RCSB / EBI]
2ZMM; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
2ZN7; X-ray; 2.10 A; A=1-299.[ExPASy / RCSB / EBI]
3CWE; X-ray; 1.60 A; A=1-283.[ExPASy / RCSB / EBI]
3D9C; X-ray; 2.30 A; A=1-321.[ExPASy / RCSB / EBI]
3EU0; X-ray; 2.70 A; A=1-321.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 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; -.
2QBP; -.
2QBQ; -.
2QBR; -.
2QBS; -.
2VEU; -.
2VEV; -.
2VEW; -.
2VEX; -.
2VEY; -.
2ZMM; -.
2ZN7; -.
3CWE; -.
3D9C; -.
3EU0; -.
ModBase P18031.
Protein-protein interaction databases
IntAct P18031; 11.
PTM databases
PhosphoSite P18031; -.
Enzyme and pathway databases
BRENDA 3.1.3.48; 247.
Pathway_Interaction_DB nfat_tfpathway; Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
igf1_pathway; IGF1 pathway.
insulin_pathway; Insulin Pathway.
pdgfrbpathway; PDGFR-beta signaling pathway.
ptp1bpathway; Signaling events mediated by PTP1B.
2D gel databases
OGP P18031; -.
Organism-specific databases
GeneCards GC20P048560; -.
H-InvDB HIX0015910; -.
HIX0027718; -.
HGNC HGNC:9642; PTPN1.
GenAtlas PTPN1.
HPA CAB009329; -.
CAB015217; -.
HPA012542; -.
MIM 176885; gene. [NCBI / EBI]
PharmGKB PA33985; -.
Gene expression databases
ArrayExpress P18031; -.
Bgee P18031; -.
CleanEx HS_PTPN1; -.
GermOnline ENSG00000196396; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0046627; Biological process: negative regulation of insulin receptor signaling pathway (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR012265; Tyr_Pase_non-rcpt_typ-1/2.
IPR000242; Tyr_Pase_rcpt/non-rcpt.
Graphical view of domain structure.
PANTHER PTHR19134:SF57; Tyr_Phos_no_rcpt; 1.
Pfam PF00102; Y_phosphatase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000926; Tyr-Ptase_nr1; 1.
PRINTS PR00700; PRTYPHPHTASE.
SMART SM00194; PTPc; 1.
SMART graphical view of domain structure.
PROSITE PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PS50055; TYR_PHOSPHATASE_PTP; 1.
PROSITE graphical view of domain structure (profiles).
Other
SWISS-3DIMAGE P18031.
Proteomic databases
PeptideAtlas P18031; -.
PRIDE P18031; -.
Genome annotation databases
Ensembl ENSG00000196396; Homo sapiens. [Contig view]
GeneID 5770; -.
KEGG hsa:5770; -.
Phylogenomic databases
HOGENOM P18031; -.
HOVERGEN P18031; -.
OMA P18031; AYLCYRV.
Other
DrugBank DB00720; Clodronate.
DB01133; Tiludronate.
NextBio 22442; -.
PMAP-CutDB P18031; -.
SOURCE PTPN1; Homo sapiens.
ProtoNet P18031.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Endoplasmic reticulum; Hydrolase; Membrane; Oxidation; Phosphoprotein; Polymorphism; Protein phosphatase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   435  435     Tyrosine-protein phosphatase non-receptor type 1. PRO_0000094748
DOMAIN   3   277  275     Tyrosine-protein phosphatase. 
ACT_SITE   215   215        Phosphocysteine intermediate. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   20    20        Phosphotyrosine. 
MOD_RES   50    50        Phosphoserine; by PKB/AKT1. 
MOD_RES   295   295        Phosphoserine. 
MOD_RES   352   352        Phosphoserine. 
MOD_RES   378   378        Phosphoserine; by PKC. 
MOD_RES   386   386        Phosphoserine; by CDC2. 
MOD_RES   393   393        Phosphoserine (By similarity). 
CROSSLNK   215   216        4-amino-3-isothiazolidinone serine (Cys-Ser); in inhibited form. 
VARIANT   381   381  1     G -> S (in dbSNP:rs16995304 [NCBI]). VAR_022013 
VARIANT   387   387  1     P -> L (associated with low glucose tolerance; dbSNP:rs16995309 [NCBI]). VAR_022014 
MUTAGEN   50    50        S->A,D: No phosphorylation. 
HELIX   3    13  11      
HELIX   16    26  11      
TURN   33    36  4      
HELIX   38    43  6      
TURN   53    55  3      
STRAND   56    58  3      
STRAND   66    74  9      
TURN   75    78  4      
STRAND   79    84  6      
TURN   89    91  3      
HELIX   92   101  10      
STRAND   106   109  4      
STRAND   113   115  3      
STRAND   133   135  3      
TURN   136   139  4      
STRAND   140   149  10      
STRAND   151   162  12      
TURN   163   165  3      
STRAND   168   176  9      
HELIX   188   200  13      
TURN   201   204  4      
STRAND   211   214  4      
STRAND   216   219  4      
HELIX   220   238  19      
HELIX   241   243  3      
HELIX   246   253  8      
TURN   254   256  3      
HELIX   264   281  18      
HELIX   287   295  9      
Sequence information
Length: 435 AA [This is the length of the unprocessed precursor] Molecular weight: 49967 Da [This is the MW of the unprocessed precursor] CRC64: 802377DCD33F41FD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLH 

        70         80         90        100        110        120 
QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLK 

       130        140        150        160        170        180 
CAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP 

       190        200        210        220        230        240 
DFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD 

       250        260        270        280        290        300 
PSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE 

       310        320        330        340        350        360 
PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK GSPLNAAPYG 

       370        380        390        400        410        420 
IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED HALSYWKPFL VNMCVATVLT 

       430 
AGAYLCYRFL FNSNT 

P18031 in FASTA format

View entry in raw text format (no links)
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