PTPN7
entrez
5778
canonical
uniprot
P35236
canonical
ensembl
ENSG00000143851
resolver
ensp
ENSP00000309116
resolver
ensp
ENSP00000356248
resolver
ensp
ENSP00000418416
resolver
ensp
ENSP00000509436
resolver
genesymbol
PTPN7
resolver
hgnc
HGNC:9659
resolver
uniprot
B3KXE1
resolver
uniprot
B4DZD9
resolver
uniprot
Q53XK4
resolver
uniprot
Q5SXQ0
resolver
uniprot
Q5SXQ1
resolver
uniprot
Q9BV05
resolver
uniprot_entry
B4DZD9_HUMAN
resolver
uniprot_entry
PTN7_HUMAN
resolver
uniprot_sec
B3KXE1
resolver
uniprot_sec
Q53XK4
resolver
uniprot_sec
Q5SXQ0
resolver
uniprot_sec
Q5SXQ1
resolver
uniprot_sec
Q9BV05
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited in cells after FCER1A triggering. {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MVQAHGGRSRAQPLTLSLGAAMTQPPPEKTPAKKHVRLQERRGSNVALMLDVRSLGAVEPICSVNTPREVTLHFLRTAGHPLTRWALQRQPPSPKQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAGQLPEEPSP
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}.
uniprot
proteins
mass_dalton
40529
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="S->A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation."; /evidence="ECO:0000269|PubMed:14613483"; MUTAGEN 44; /note="S->D: Reduces binding of MAP kinase."; /evidence="ECO:0000269|PubMed:14613483"; MUTAGEN 66; /note="T->A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93."; /evidence="ECO:0000269|PubMed:10206983"; MUTAGEN 93; /note="S->A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66."; /evidence="ECO:0000269|PubMed:10206983"; MUTAGEN 125; /note="Y->A: Strongly reduced catalytic activity."; /evidence="ECO:0000269|PubMed:15466470"; MUTAGEN 257; /note="D->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:15466470"; MUTAGEN 291; /note="C->S: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:9624114"; MUTAGEN 335; /note="Q->A: Reduced catalytic activity."; /evidence="ECO:0000269|PubMed:15466470
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:14613483}.; PTM: Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H(2)O(2)) or with antigen enhanced oxidation of active site cysteine (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Non-receptor class subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10206983
uniprot
proteins
pubmed
10559944
uniprot
proteins
pubmed
10702794
uniprot
proteins
pubmed
14613483
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1510684
uniprot
proteins
pubmed
1530918
uniprot
proteins
pubmed
15466470
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16226275
uniprot
proteins
pubmed
16441242
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16765894
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
9624114
uniprot
proteins
sequence_length
360
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14613483}. Cytoplasm, cytoskeleton {ECO:0000250}.
uniprot
proteins