PTP4A1
entrez
7803
canonical
uniprot
Q93096
canonical
ensembl
ENSG00000112245
resolver
ensp
ENSP00000485687
resolver
ensp
ENSP00000497588
resolver
ensp
ENSP00000500859
resolver
ensp
ENSP00000500952
resolver
enst
ENST00000626021
resolver
enst
ENST00000648894
resolver
enst
ENST00000672924
resolver
enst
ENST00000673199
resolver
genesymbol
PTP4A1
resolver
genesymbol_syn
PRL1
resolver
genesymbol_syn
PTPCAAX1
resolver
hgnc
HGNC:9634
resolver
uniprot
B2R6C8
resolver
uniprot
O00648
resolver
uniprot
Q49A54
resolver
uniprot_entry
TP4A1_HUMAN
resolver
uniprot_sec
B2R6C8
resolver
uniprot_sec
O00648
resolver
uniprot_sec
Q49A54
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine. {ECO:0000269|PubMed:12516958}.
uniprot
proteins
amino_acid_sequence
MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. {ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:12782572, ECO:0000269|PubMed:14643450}.
uniprot
proteins
mass_dalton
19815
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="T->F: Reduces trimerization."; /evidence="ECO:0000269|PubMed:15571731"; MUTAGEN 71; /note="D->A: No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:12235145"; MUTAGEN 72; /note="D->A: 80% loss of catalytic activity; delay in progression through G2/M."; /evidence="ECO:0000269|PubMed:12235145"; MUTAGEN 104; /note="C->S: Abolishes enzymatic activity."; /evidence="ECO:0000269|PubMed:12235145"; MUTAGEN 131; /note="Q->A: Reduces trimerization."; /evidence="ECO:0000269|PubMed:15571731"; MUTAGEN 170; /note="C->S: Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis."; /evidence="ECO:0000269|PubMed:12235145"; MUTAGEN 171; /note="C->S: No effect on subcellular location."; /evidence="ECO:0000269|PubMed:12235145
uniprot
proteins
post_translational_modification
PTM: Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10940933
uniprot
proteins
pubmed
12235145
uniprot
proteins
pubmed
12516958
uniprot
proteins
pubmed
12782572
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14643450
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15501285
uniprot
proteins
pubmed
15571731
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
9018080
uniprot
proteins
pubmed
9633825
uniprot
proteins
pubmed
9642300
uniprot
proteins
sequence_length
173
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:15571731}; Lipid-anchor {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:15571731}. Early endosome {ECO:0000269|PubMed:12235145}. Endoplasmic reticulum {ECO:0000269|PubMed:12235145}. Cytoplasm {ECO:0000269|PubMed:12235145}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12235145}. Nucleus {ECO:0000250|UniProtKB:Q78EG7}. Note=And mitotic spindle. {ECO:0000269|PubMed:12235145}.
uniprot
proteins