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UniProtKB/Swiss-Prot entry P29350


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

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Entry information
Entry name PTN6_HUMAN
Primary accession number P29350
Secondary accession number Q969V8
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 110)
Name and origin of the protein
Protein name Tyrosine-protein phosphatase non-receptor type 6
Synonyms EC 3.1.3.48
Protein-tyrosine phosphatase 1C
PTP-1C
Hematopoietic cell protein-tyrosine phosphatase
SH-PTP1
Protein-tyrosine phosphatase SHP-1
Gene name
Name: PTPN6
Synonyms: HCP, PTP1C
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] (ISOFORM 1).
PubMed=1732748 [NCBI, ExPASy, EBI, Israel, Japan]
Yi T., Cleveland J.L., Ihle J.N.;
"Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13.";
Mol. Cell. Biol. 12:836-846(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Mammary gland;
DOI=10.1038/352736a0; PubMed=1652101 [NCBI, ExPASy, EBI, Israel, Japan]
Shen S.H., Bastien L., Posner B.I., Chretien P.;
"A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases.";
Nature 352:736-739(1991).
[3]
ERRATUM, AND SEQUENCE REVISION.
Shen S.H., Bastien L., Posner B.I., Chretien P.;
Nature 353:868-868(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1736296 [NCBI, ExPASy, EBI, Israel, Japan]
Plutzky J., Neel B.G., Rosenberg R.D.;
"Isolation of a src homology 2-containing tyrosine phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 89:1123-1127(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
DOI=10.1006/geno.1995.1020; PubMed=7665165 [NCBI, ExPASy, EBI, Israel, Japan]
Banville D., Stocco R., Shen S.H.;
"Human protein tyrosine phosphatase 1C (PTPN6) gene structure: alternate promoter usage and exon skipping generate multiple transcripts.";
Genomics 27:165-173(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9074930 [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination.";
Genome Res. 7:268-280(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
Oka T., Ouchida M.;
"Gene silencing of SHP-1 gene in leukemias/lymphomas by aberrant methylation.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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).
[9]
PHOSPHORYLATION.
PubMed=7781604 [NCBI, ExPASy, EBI, Israel, Japan]
Li R.Y., Gaits F., Ragab A., Ragab-Thomas J.M.F., Chap H.;
"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. 14:2519-2526(1995).
[10]
INTERACTION WITH LILRB1.
DOI=10.1016/S1074-7613(00)80529-4; PubMed=9285411 [NCBI, ExPASy, EBI, Israel, Japan]
Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L., Hsu M.-L.;
"A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules.";
Immunity 7:273-282(1997).
[11]
INTERACTION WITH LILRB2.
DOI=10.1002/(SICI)1521-4141(199811)28:11<3423::AID-IMMU3423>3.0.CO;2-2; PubMed=9842885 [NCBI, ExPASy, EBI, Israel, Japan]
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R., Borges L.;
"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes.";
Eur. J. Immunol. 28:3423-3434(1998).
[12]
INTERACTION WITH PTPNS1.
DOI=10.1074/jbc.273.35.22719; PubMed=9712903 [NCBI, ExPASy, EBI, Israel, Japan]
Veillette A., Thibaudeau E., Latour S.;
"High expression of inhibitory receptor SHPS-1 and its association with protein tyrosine phosphatase SHP-1 in macrophages.";
J. Biol. Chem. 273:22719-22728(1998).
[13]
INTERACTION WITH FCRL2 AND FCRL3.
DOI=10.1006/bbrc.2000.4213; PubMed=11162587 [NCBI, ExPASy, EBI, Israel, Japan]
Xu M.-J., Zhao R., Zhao Z.J.;
"Molecular cloning and characterization of SPAP1, an inhibitory receptor.";
Biochem. Biophys. Res. Commun. 280:768-775(2001).
[14]
INTERACTION WITH CD84.
DOI=10.1006/clim.2001.5035; PubMed=11414741 [NCBI, ExPASy, EBI, Israel, Japan]
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D., Notarangelo L.D., Duckett C.S.;
"Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family.";
Clin. Immunol. 100:15-23(2001).
[15]
INTERACTION WITH FCRL4.
DOI=10.1073/pnas.1935944100; PubMed=14597715 [NCBI, ExPASy, EBI, Israel, Japan]
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A., Cooper M.D.;
"The inhibitory potential of Fc receptor homolog 4 on memory B cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003).
[16]
INTERACTION WITH CD300LF.
DOI=10.1016/j.bbrc.2004.05.065; PubMed=15184070 [NCBI, ExPASy, EBI, Israel, Japan]
Sui L., Li N., Liu Q., Zhang W., Wan T., Wang B., Luo K., Sun H., Cao X.;
"IgSF13, a novel human inhibitory receptor of the immunoglobulin superfamily, is preferentially expressed in dendritic cells and monocytes.";
Biochem. Biophys. Res. Commun. 319:920-928(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-536 AND TYR-564, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-509, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 248-399.
DOI=10.1074/jbc.273.43.28199; PubMed=9774441 [NCBI, ExPASy, EBI, Israel, Japan]
Yang J., Liang X., Niu T., Meng W., Zhao Z., Zhou G.W.;
"Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1.";
J. Biol. Chem. 273:28199-28207(1998).
[20]
STRUCTURE BY NMR OF 110-214.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the SH2 domain of human protein-tyrosine phosphatase SHP-1.";
Submitted (NOV-2005) to the PDB data bank.
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
M74903; AAA35963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X62055; CAA43982.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77273; AAA36610.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15528; AAA82880.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15536; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15535; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15534; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15533; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15532; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15531; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15530; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15529; AAA82880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15528; AAA82879.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15537; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15535; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15534; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15533; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15532; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15531; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15530; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U15529; AAA82879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47924; AAB51322.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47924; AAB51323.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB079851; BAC81774.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB079851; BAC81775.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002523; AAH02523.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007667; AAH07667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B42031; S20825.
RefSeq NP_002822.2; -.
NP_536858.1; -.
NP_536859.1; -.
UniGene Hs.63489
3D structure databases
PDB
1FPR; X-ray; 2.50 A; A=243-526.[ExPASy / RCSB / EBI]
1GWZ; X-ray; 2.50 A; A=243-541.[ExPASy / RCSB / EBI]
1X6C; NMR; -; A=110-214.[ExPASy / RCSB / EBI]
2B3O; X-ray; 2.80 A; A=1-532.[ExPASy / RCSB / EBI]
2YU7; NMR; -; A=107-215.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FPR; -.
1GWZ; -.
1X6C; -.
2B3O; -.
2YU7; -.
ModBase P29350.
Protein-protein interaction databases
IntAct P29350; -.
PTM databases
PhosphoSite P29350; -.
2D gel databases
OGP P29350; -.
Organism-specific databases
H-InvDB HIX0010381; -.
HGNC HGNC:9658; PTPN6.
GenAtlas PTPN6.
HPA CAB004572; -.
MIM 176883; gene. [NCBI / EBI]
PharmGKB PA34002; -.
GeneCards P29350.
Gene expression databases
ArrayExpress P29350; -.
CleanEx HS_PTPN6; -.
GermOnline ENSG00000111679; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0016020; Cellular component: membrane (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (traceable author statement from ProtInc).
GO:0006915; Biological process: apoptosis (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0006470; Biological process: protein amino acid dephosphorylation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000980; SH2.
IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
IPR000242; Tyr_Pase_rcpt/non-rcpt.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 2.
Pfam PF00017; SH2; 2.
PF00102; Y_phosphatase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000929; Tyr-Ptase_nr_6; 1.
PRINTS PR00700; PRTYPHPHTASE.
PR00401; SH2DOMAIN.
ProDom PD000093; SH2; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00194; PTPc; 1.
SM00252; SH2; 2.
SMART graphical view of domain structure.
PROSITE PS50001; SH2; 2.
PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PS50055; TYR_PHOSPHATASE_PTP; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29350.
ProtoNet P29350.
Genome annotation databases
Ensembl ENSG00000111679; Homo sapiens. [Contig view]
GeneID 5777; -.
KEGG hsa:5777; -.
Phylogenomic databases
HOVERGEN P29350; -.
Other
NextBio 22466; -.
SOURCE PTPN6; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase; Repeat; SH2 domain.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   595  595     Tyrosine-protein phosphatase non-receptor type 6. PRO_0000094758
DOMAIN   4   100  97     SH2 1. 
DOMAIN   110   213  104     SH2 2. 
DOMAIN   244   515  272     Tyrosine-protein phosphatase. 
ACT_SITE   453   453        Phosphocysteine intermediate. 
MOD_RES   377   377        Phosphotyrosine (By similarity). 
MOD_RES   509   509        Phosphotyrosine. 
MOD_RES   536   536        Phosphotyrosine. 
MOD_RES   564   564        Phosphotyrosine. 
VAR_SEQ   1    39        Missing (in isoform 3). VSP_005129
VAR_SEQ   1     3        MVR -> MLSRG (in isoform 2). VSP_007775
VAR_SEQ   40    44        SLSVR -> MLSRG (in isoform 3). VSP_005130
CONFLICT   6     6        H -> L (in Ref. 5; AAA82880). 
CONFLICT   86    86        L -> V (in Ref. 4; AAA36610). 
CONFLICT   146   146        V -> E (in Ref. 5; AAA82880/AAA82879). 
HELIX   11    21  11      
STRAND   26    31  6      
STRAND   33    45  13      
STRAND   48    55  8      
STRAND   57    59  3      
STRAND   61    63  3      
STRAND   68    70  3      
HELIX   72    80  9      
STRAND   89    91  3      
HELIX   105   107  3      
HELIX   117   127  11      
STRAND   132   137  6      
STRAND   139   141  3      
STRAND   145   154  10      
STRAND   162   170  9      
STRAND   175   181  7      
STRAND   184   186  3      
HELIX   187   197  11      
STRAND   202   204  3      
HELIX   221   223  3      
HELIX   244   251  8      
TURN   257   259  3      
TURN   263   266  4      
STRAND   283   288  6      
STRAND   296   305  10      
HELIX   314   316  3      
STRAND   320   322  3      
HELIX   329   331  3      
HELIX   332   341  10      
STRAND   346   349  4      
STRAND   356   358  3      
STRAND   370   374  5      
STRAND   377   384  8      
STRAND   388   390  3      
STRAND   393   401  9      
STRAND   403   405  3      
STRAND   407   411  5      
HELIX   427   440  14      
STRAND   449   457  9      
HELIX   458   476  19      
HELIX   484   492  9      
HELIX   503   523  21      
Sequence information
Length: 595 AA [This is the length of the unprocessed precursor] Molecular weight: 67561 Da [This is the MW of the unprocessed precursor] CRC64: 4D7736C21D3542D2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVRWFHRDLS GLDAETLLKG RGVHGSFLAR PSRKNQGDFS LSVRVGDQVT HIRIQNSGDF 

        70         80         90        100        110        120 
YDLYGGEKFA TLTELVEYYT QQQGVLQDRD GTIIHLKYPL NCSDPTSERW YHGHMSGGQA 

       130        140        150        160        170        180 
ETLLQAKGEP WTFLVRESLS QPGDFVLSVL SDQPKAGPGS PLRVTHIKVM CEGGRYTVGG 

       190        200        210        220        230        240 
LETFDSLTDL VEHFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA 

       250        260        270        280        290        300 
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD 

       310        320        330        340        350        360 
YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNK 

       370        380        390        400        410        420 
CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH 

       430        440        450        460        470        480 
GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDC 

       490        500        510        520        530        540 
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNIT 

       550        560        570        580        590 
YPPAMKNAHA KASRTSSKHK EDVYENLHTK NKREEKVKKQ RSADKEKSKG SLKRK 

P29350 in FASTA format

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View entry in raw text format (no links)
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