Ptpn6
entrez
15170
canonical
uniprot
P29351
canonical
ensembl
ENSMUSG00000004266
resolver
ensp
ENSMUSP00000108103
resolver
ensp
ENSMUSP00000129124
resolver
genesymbol
Ptpn6
resolver
genesymbol_syn
Hcp
resolver
genesymbol_syn
Hcph
resolver
genesymbol_syn
Ptp1C
resolver
uniprot
O35128
resolver
uniprot
Q3UB72
resolver
uniprot
Q3UCJ0
resolver
uniprot
Q63872
resolver
uniprot
Q63873
resolver
uniprot
Q63874
resolver
uniprot
Q921G3
resolver
uniprot
Q9QVA6
resolver
uniprot
Q9QVA7
resolver
uniprot
Q9QVA8
resolver
uniprot
Q9R0V6
resolver
uniprot_entry
PTN6_MOUSE
resolver
uniprot_entry
Q3UB72_MOUSE
resolver
uniprot_entry
Q3UCJ0_MOUSE
resolver
uniprot_sec
O35128
resolver
uniprot_sec
Q63872
resolver
uniprot_sec
Q63873
resolver
uniprot_sec
Q63874
resolver
uniprot_sec
Q921G3
resolver
uniprot_sec
Q9QVA6
resolver
uniprot_sec
Q9QVA7
resolver
uniprot_sec
Q9QVA8
resolver
uniprot_sec
Q9R0V6
resolver
amino_acid_sequence
MVRWFHRDLSGPDAETLLKGRGVPGSFLARPSRKNQGDFSLSVRVDDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGILQDRDGTIIHLKYPLNCSDPTSERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENSKTYIASQGCLDATVNDFWQMAWQENTRVIVMTTREVEKGRNKCVPYWPEVGTQRVYGLYSVTNSREHDTAEYKLRTLQISPLDNGDLVREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEIIQSQKGQESEYGNITYPPAVRSAHAKASRTSSKHKEEVYENVHSKSKKEEKVKKQRSADKEKNKGSLKRK
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Ptpn6 are the cause of the motheaten (me) or viable motheaten (mev) phenotypes. Mice homozygous for the recessive allelic mutations develop severe defects in hematopoiesis.
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis. Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:9528781). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:10026201, PubMed:33990399). Modulates the signaling of several cytokine receptors including IL-4 receptor. Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling. Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Also acts as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A. {ECO:0000250|UniProtKB:P29350, ECO:0000269|PubMed:10026201, ECO:0000269|PubMed:33990399, ECO:0000269|PubMed:9528781}.
uniprot
proteins
mass_dalton
67559
uniprot
proteins
mutagenesis
MUTAGEN 30..33; /note="RPSR->KPSE: Slight reduction in binding to phosphorylated Lilrb4a."; /evidence="ECO:0000269|PubMed:9973385"; MUTAGEN 136; /note="R->K: Abolishes binding to phosphorylated Lilrb4a."; /evidence="ECO:0000269|PubMed:9973385"; MUTAGEN 482; /note="I->F: Mice display a low bone mass density and are associated with osteopenia and elevated inflammatory cytokines."; /evidence="ECO:0000269|PubMed:19419305
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (PubMed:1385421, PubMed:9528781). Phosphorylation at Tyr-564 by LYN enhances phosphatase activity. Phosphorylation at Thr-394 by TAOK3 leads to polyubiquitination and subsequent proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P29350, ECO:0000269|PubMed:1385421, ECO:0000269|PubMed:9528781}.; PTM: Ubiquitinated after phosphorylation by TAOK3. Ubiquitinated by a cooperation between ITCH and WWP2 via 'Lys-27'-mediated polyubiquitin chains resulting in the reduction of its association with LCK. {ECO:0000250|UniProtKB:P29350}.
uniprot
proteins
protein_family
Non-receptor class 2 subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10026201
uniprot
proteins
pubmed
10327049
uniprot
proteins
pubmed
10419485
uniprot
proteins
pubmed
1373816
uniprot
proteins
pubmed
1385421
uniprot
proteins
pubmed
14662855
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1732748
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
1932742
uniprot
proteins
pubmed
19419305
uniprot
proteins
pubmed
19948503
uniprot
proteins
pubmed
20526344
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23112346
uniprot
proteins
pubmed
29247647
uniprot
proteins
pubmed
33990399
uniprot
proteins
pubmed
8324828
uniprot
proteins
pubmed
9445485
uniprot
proteins
pubmed
9528781
uniprot
proteins
pubmed
9712903
uniprot
proteins
pubmed
9867848
uniprot
proteins
pubmed
9973385
uniprot
proteins
sequence_length
595
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity). {ECO:0000250}.
uniprot
proteins