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P18031 (PTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 1

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 1B
Short name=PTP-1B
Gene names
Name:PTPN1
Synonyms:PTP1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. Ref.13 Ref.15 Ref.18

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET. Ref.13 Ref.15

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note: Interacts with EPHA3 at the cell membrane. Ref.8 Ref.15

Post-translational modification

Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.

Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.

S-nitrosylation of Cys-215 inactivates the enzyme activity.

Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Oxidation
Phosphoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.15. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Inferred from direct assay Ref.18. Source: UniProtKB

insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of insulin receptor signaling pathway

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.15. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet-derived growth factor receptor-beta signaling pathway

Inferred from mutant phenotype PubMed 14966296. Source: UniProtKB

regulation of endocytosis

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of hepatocyte growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of signal transduction

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

early endosome

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.18. Source: UniProtKB

ephrin receptor binding

Inferred from physical interaction Ref.15. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10660596PubMed 10889023PubMed 11007774PubMed 11106648PubMed 11163213PubMed 11506178Ref.11PubMed 11694501PubMed 11970898PubMed 12023880PubMed 12176037PubMed 12237455PubMed 12614164PubMed 12634852PubMed 12857726PubMed 12907755PubMed 14527337PubMed 14722096PubMed 15588987PubMed 15821101PubMed 15866871PubMed 15894168PubMed 15976035PubMed 16115959PubMed 16271887PubMed 16388599PubMed 16537444PubMed 16582879PubMed 16644720PubMed 16926280PubMed 17092689PubMed 17128263PubMed 17159996PubMed 17197020PubMed 17416557PubMed 17481567PubMed 17974954PubMed 18387954PubMed 18515860PubMed 18579758PubMed 19029027PubMed 19167335PubMed 19712109PubMed 21806020PubMed 22789536PubMed 8702689PubMed 8940134PubMed 8999839PubMed 9050838Ref.9PubMed 9407132PubMed 9418872PubMed 9566916PubMed 9600099. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 18074158Ref.18. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.13. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 18074158. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Tyrosine-protein phosphatase non-receptor type 1
PRO_0000094748

Regions

Domain3 – 277275Tyrosine-protein phosphatase
Region215 – 2217Substrate binding By similarity

Sites

Active site2151Phosphocysteine intermediate
Binding site1811Substrate
Binding site2621Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6
Modified residue201Phosphotyrosine Ref.12
Modified residue501Phosphoserine; by PKB/AKT1, CLK1 and CLK2 Ref.10 Ref.11
Modified residue661Phosphotyrosine; by EGFR Ref.9
Modified residue2151Cysteine persulfide Ref.18
Modified residue2151S-nitrosocysteine; in reversibly inhibited form Ref.18
Modified residue2421Phosphoserine; by CLK1 and CLK2 Ref.10
Modified residue2431Phosphoserine; by CLK1 and CLK2 Ref.10
Modified residue3521Phosphoserine Ref.7 Ref.14 Ref.16
Modified residue3781Phosphoserine; by PKC Ref.7 Ref.19
Modified residue3861Phosphoserine; by CDK1 Ref.7
Cross-link215 ↔ 216N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form

Natural variations

Natural variant3811G → S.
Corresponds to variant rs16995304 [ dbSNP | Ensembl ].
VAR_022013
Natural variant3871P → L Associated with low glucose tolerance. Ref.26
Corresponds to variant rs16995309 [ dbSNP | Ensembl ].
VAR_022014

Experimental info

Mutagenesis501S → A or D: No phosphorylation. Ref.10 Ref.11
Mutagenesis1811D → A: Substrate-trapping mutant. Ref.18
Mutagenesis2151C → S: Catalytically inactive mutant; abolishes sulfhydration. Ref.18

Secondary structure

............................................................ 435
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18031 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 802377DCD33F41FD

FASTA43549,967
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a cDNA for a major human protein-tyrosine-phosphatase."
Chernoff J., Schievella A.R., Jost C.A., Erikson R.L., Neel B.G.
Proc. Natl. Acad. Sci. U.S.A. 87:2735-2739(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B."
Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A., Green N.R., Hill D.E.
Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Placenta.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Lymph.
[6]"Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins."
Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.
Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-321, ACETYLATION AT MET-1.
Tissue: Placenta.
[7]"Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation."
Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.
EMBO J. 12:1937-1946(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.
[8]"The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence."
Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.
Cell 68:545-560(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor."
Liu F., Chernoff J.
Biochem. J. 327:139-145(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-66.
[10]"The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
Moeslein F.M., Myers M.P., Landreth G.E.
J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-50; SER-242 AND SER-243, MUTAGENESIS OF SER-50.
[11]"Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor."
Ravichandran L.V., Chen H., Li Y., Quon M.J.
Mol. Endocrinol. 15:1768-1780(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-50, MUTAGENESIS OF SER-50.
[12]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF MET, INTERACTION WITH MET.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"PTP1B regulates Eph receptor function and trafficking."
Nievergall E., Janes P.W., Stegmayer C., Vail M.E., Haj F.G., Teng S.W., Neel B.G., Bastiaens P.I., Lackmann M.
J. Cell Biol. 191:1189-1203(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA3, FUNCTION IN EPHA3 DEPHOSPHORYLATION, SUBCELLULAR LOCATION.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
Krishnan N., Fu C., Pappin D.J., Tonks N.K.
Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SULFHYDRATION AT CYS-215, S-NITROSYLATION AT CYS-215, MUTAGENESIS OF CYS-215, MUTAGENESIS OF ASP-181 AND CYS-215.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of human protein tyrosine phosphatase 1B."
Barford D., Flint A.J., Tonks N.K.
Science 263:1397-1404(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-321.
[21]"Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design."
Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.
Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-298 OF MUTANT SER-215.
[22]"Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography."
Pannifer A.D., Flint A.J., Tonks N.K., Barford D.
J. Biol. Chem. 273:10454-10462(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-285.
[23]"Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics."
Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.
Biochemistry 37:17773-17783(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-298.
[24]"Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate."
Salmeen A., Andersen J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K., Barford D.
Nature 423:769-773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
[25]"Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B."
Van Montfort R.L.M., Congreve M., Tisi D., Carr R., Jhoti H.
Nature 423:773-777(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
[26]"Protein tyrosine phosphatase 1B variant associated with fat distribution and insulin metabolism."
Ukkola O., Rankinen T., Lakka T., Leon A.S., Skinner J.S., Wilmore J.H., Rao D.C., Kesaeniemi Y.A., Bouchard C.
Obes. Res. 13:829-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT LEU-387 WITH LOW GLUCOSE TOLERANCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31724 mRNA. Translation: AAA60223.1.
M33689 mRNA. Translation: AAA60157.1.
M33684 expand/collapse EMBL AC list , M33688, M33687, M33686, M33685 Genomic DNA. Translation: AAA60158.1.
BT006752 mRNA. Translation: AAP35398.1.
AL133230, AL034429 Genomic DNA. Translation: CAC00618.2.
AL034429, AL133230 Genomic DNA. Translation: CAI23215.1.
BC015660 mRNA. Translation: AAH15660.1.
BC018164 mRNA. Translation: AAH18164.1.
CCDSCCDS13430.1.
PIRTPHUN1. A35992.
RefSeqNP_001265547.1. NM_001278618.1.
NP_002818.1. NM_002827.3.
UniGeneHs.417549.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5YX-ray2.50A1-330[»]
1AAXX-ray1.90A1-321[»]
1BZCX-ray2.35A1-321[»]
1BZHX-ray2.10A1-298[»]
1BZJX-ray2.25A2-298[»]
1C83X-ray1.80A1-298[»]
1C84X-ray2.35A1-298[»]
1C85X-ray2.72A1-298[»]
1C86X-ray2.30A1-298[»]
1C87X-ray2.10A1-298[»]
1C88X-ray1.80A1-298[»]
1ECVX-ray1.95A1-298[»]
1EENX-ray1.90A1-321[»]
1EEOX-ray1.80A1-321[»]
1G1FX-ray2.00A1-298[»]
1G1GX-ray2.20A1-298[»]
1G1HX-ray2.40A1-298[»]
1G7FX-ray1.80A1-298[»]
1G7GX-ray2.20A1-298[»]
1GFYX-ray2.13A1-298[»]
1I57X-ray2.10A1-298[»]
1JF7X-ray2.20A/B1-298[»]
1KAKX-ray2.50A1-298[»]
1KAVX-ray2.35A1-298[»]
1L8GX-ray2.50A1-321[»]
1LQFX-ray2.50A/B/C/D1-283[»]
1NL9X-ray2.40A1-321[»]
1NNYX-ray2.40A1-321[»]
1NO6X-ray2.40A1-321[»]
1NWEX-ray3.10A1-298[»]
1NWLX-ray2.40A1-298[»]
1NZ7X-ray2.40A1-321[»]
1OEMX-ray1.80X1-321[»]
1OEOX-ray2.15X1-321[»]
1OESX-ray2.20A1-321[»]
1OETX-ray2.30A1-321[»]
1OEUX-ray2.50A1-321[»]
1OEVX-ray2.20A1-321[»]
1ONYX-ray2.15A1-321[»]
1ONZX-ray2.40A1-321[»]
1PA1X-ray1.60A1-298[»]
1PH0X-ray2.20A1-321[»]
1PTTX-ray2.90A1-321[»]
1PTUX-ray2.60A1-321[»]
1PTVX-ray2.30A1-321[»]
1PTYX-ray1.85A1-321[»]
1PXHX-ray2.15A1-321[»]
1PYNX-ray2.20A1-321[»]
1Q1MX-ray2.60A1-321[»]
1Q6JX-ray2.20A1-298[»]
1Q6MX-ray2.20A1-298[»]
1Q6NX-ray2.10A/B1-298[»]
1Q6PX-ray2.30A/B1-298[»]
1Q6SX-ray2.20A/B1-298[»]
1Q6TX-ray2.30A/B1-298[»]
1QXKX-ray2.30A1-321[»]
1SUGX-ray1.95A1-321[»]
1T48X-ray2.20A1-298[»]
1T49X-ray1.90A1-298[»]
1T4JX-ray2.70A1-298[»]
1WAXX-ray2.20A1-321[»]
1XBOX-ray2.50A1-321[»]
2AZRX-ray2.00A1-299[»]
2B07X-ray2.10A1-299[»]
2B4SX-ray2.30A/C1-298[»]
2BGDX-ray2.40A1-321[»]
2BGEX-ray1.80A1-321[»]
2CM2X-ray1.50A2-298[»]
2CM3X-ray2.10A/B1-298[»]
2CM7X-ray2.10A1-321[»]
2CM8X-ray2.10A1-321[»]
2CMAX-ray2.30A1-321[»]
2CMBX-ray1.70A1-298[»]
2CMCX-ray2.20A1-298[»]
2CNEX-ray1.80A1-298[»]
2CNFX-ray2.20A1-321[»]
2CNGX-ray1.90A1-321[»]
2CNHX-ray1.80A1-321[»]
2CNIX-ray2.00A1-321[»]
2F6FX-ray2.00A1-298[»]
2F6TX-ray1.70A1-298[»]
2F6VX-ray1.70A1-298[»]
2F6WX-ray2.20A1-298[»]
2F6YX-ray2.15A1-298[»]
2F6ZX-ray1.70A1-298[»]
2F70X-ray2.12A1-298[»]
2F71X-ray1.55A1-298[»]
2FJMX-ray2.10A/B1-298[»]
2FJNX-ray2.20A/B1-298[»]
2H4GX-ray2.50A1-299[»]
2H4KX-ray2.30A1-299[»]
2HB1X-ray2.00A1-299[»]
2HNPX-ray2.85A1-321[»]
2HNQX-ray2.85A1-321[»]
2NT7X-ray2.10A1-299[»]
2NTAX-ray2.10A1-299[»]
2QBPX-ray2.50A1-299[»]
2QBQX-ray2.10A1-299[»]
2QBRX-ray2.30A1-299[»]
2QBSX-ray2.10A1-299[»]
2VEUX-ray2.40A1-321[»]
2VEVX-ray1.80A1-321[»]
2VEWX-ray2.00A1-321[»]
2VEXX-ray2.20A1-321[»]
2VEYX-ray2.20A1-321[»]
2ZMMX-ray2.10A1-299[»]
2ZN7X-ray2.10A1-299[»]
3A5JX-ray1.70A2-321[»]
3A5KX-ray1.85A2-298[»]
3CWEX-ray1.60A1-283[»]
3D9CX-ray2.30A1-321[»]
3EAXX-ray1.90A1-321[»]
3EB1X-ray2.40A1-321[»]
3EU0X-ray2.70A1-282[»]
3I7ZX-ray2.30A1-321[»]
3I80X-ray2.25A1-321[»]
3QKPX-ray2.05A1-321[»]
3QKQX-ray2.20A1-321[»]
3SMEX-ray1.70A1-298[»]
3ZMPX-ray2.62A/B1-321[»]
3ZMQX-ray3.30A1-321[»]
3ZV2X-ray2.80A1-320[»]
4BJOX-ray2.06A/B2-321[»]
4I8NX-ray2.50A1-320[»]
ProteinModelPortalP18031.
SMRP18031. Positions 2-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111736. 35 interactions.
DIPDIP-38014N.
IntActP18031. 78 interactions.
MINTMINT-441655.
STRING9606.ENSP00000360683.

Chemistry

BindingDBP18031.
ChEMBLCHEMBL335.
DrugBankDB00720. Clodronate.
DB01133. Tiludronate.

PTM databases

PhosphoSiteP18031.

Polymorphism databases

DMDM131467.

2D gel databases

OGPP18031.

Proteomic databases

MaxQBP18031.
PaxDbP18031.
PeptideAtlasP18031.
PRIDEP18031.

Protocols and materials databases

DNASU5770.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371621; ENSP00000360683; ENSG00000196396.
GeneID5770.
KEGGhsa:5770.
UCSCuc002xvl.3. human.

Organism-specific databases

CTD5770.
GeneCardsGC20P049126.
H-InvDBHIX0027718.
HGNCHGNC:9642. PTPN1.
HPACAB009329.
CAB015217.
HPA012542.
MIM176885. gene.
neXtProtNX_P18031.
PharmGKBPA33985.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000273908.
HOVERGENHBG008321.
InParanoidP18031.
KOK05696.
OMAMCMATVL.
OrthoDBEOG7RV9G4.
PhylomeDBP18031.
TreeFamTF315897.

Enzyme and pathway databases

BRENDA3.1.3.48. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SABIO-RKP18031.
SignaLinkP18031.

Gene expression databases

ArrayExpressP18031.
BgeeP18031.
CleanExHS_PTPN1.
GenevestigatorP18031.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN1. human.
EvolutionaryTraceP18031.
GeneWikiPTPN1.
GenomeRNAi5770.
NextBio22442.
PMAP-CutDBP18031.
PROP18031.
SOURCESearch...

Entry information

Entry namePTN1_HUMAN
AccessionPrimary (citable) accession number: P18031
Secondary accession number(s): Q5TGD8, Q9BQV9, Q9NQQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM