CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005768
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein phosphatase non-receptor type 6 
Protein Synonyms/Alias
 70Z-SHP; Hematopoietic cell protein-tyrosine phosphatase; PTPTY-42; Protein-tyrosine phosphatase 1C; PTP-1C; SH-PTP1; SHP-1 
Gene Name
 Ptpn6 
Gene Synonyms/Alias
 Hcp; Hcph; Ptp1C 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
391EHDTAEYKLRTLQISubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. 
Sequence Annotation
 DOMAIN 4 100 SH2 1.
 DOMAIN 110 213 SH2 2.
 DOMAIN 244 515 Tyrosine-protein phosphatase.
 REGION 453 459 Substrate binding (By similarity).
 ACT_SITE 453 453 Phosphocysteine intermediate (By
 BINDING 419 419 Substrate (By similarity).
 BINDING 500 500 Substrate (By similarity).
 MOD_RES 64 64 Phosphotyrosine (By similarity).
 MOD_RES 377 377 Phosphotyrosine.
 MOD_RES 536 536 Phosphotyrosine.
 MOD_RES 564 564 Phosphotyrosine; by LYN (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; SH2 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 595 AA 
Protein Sequence
MVRWFHRDLS GPDAETLLKG RGVPGSFLAR PSRKNQGDFS LSVRVDDQVT HIRIQNSGDF 60
YDLYGGEKFA TLTELVEYYT QQQGILQDRD GTIIHLKYPL NCSDPTSERW YHGHISGGQA 120
ESLLQAKGEP WTFLVRESLS QPGDFVLSVL NDQPKAGPGS PLRVTHIKVM CEGGRYTVGG 180
SETFDSLTDL VEHFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA 240
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KSKNRYKNIL PFDHSRVILQ GRDSNIPGSD 300
YINANYVKNQ LLGPDENSKT YIASQGCLDA TVNDFWQMAW QENTRVIVMT TREVEKGRNK 360
CVPYWPEVGT QRVYGLYSVT NSREHDTAEY KLRTLQISPL DNGDLVREIW HYQYLSWPDH 420
GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ESISTKGLDC 480
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEIIQSQK GQESEYGNIT 540
YPPAVRSAHA KASRTSSKHK EEVYENVHSK SKKEEKVKKQ RSADKEKNKG SLKRK 595 
Gene Ontology
 GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0042169; F:SH2 domain binding; IDA:MGI.
 GO:0017124; F:SH3 domain binding; IDA:MGI.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:UniProtKB.
 GO:0050853; P:B cell receptor signaling pathway; IMP:MGI.
 GO:0030154; P:cell differentiation; ISS:UniProtKB.
 GO:0008283; P:cell proliferation; ISS:UniProtKB.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:MGI.
 GO:0035556; P:intracellular signal transduction; IDA:MGI.
 GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
 GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
 GO:0043407; P:negative regulation of MAP kinase activity; IMP:MGI.
 GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
 GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
 GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:MGI.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IEA:Compara.
 GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
 GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
 GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Compara. 
Interpro
 IPR000980; SH2.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00017; SH2
 PF00102; Y_phosphatase 
SMART
 SM00194; PTPc
 SM00252; SH2 
PROSITE
 PS50001; SH2
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.
 PR00401; SH2DOMAIN.