Q93096 · TP4A1_HUMAN
- ProteinProtein tyrosine phosphatase type IVA 1
- GenePTP4A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids173 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Activity regulation
Inhibited by sodium orthovanadate and pentamidine.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | early endosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | nucleus | |
Cellular Component | spindle | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | positive regulation of cell migration |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein tyrosine phosphatase type IVA 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ93096
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: And mitotic spindle.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 13 | Reduces trimerization. | ||||
Sequence: T → F | ||||||
Mutagenesis | 71 | No effect on catalytic activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 72 | 80% loss of catalytic activity; delay in progression through G2/M. | ||||
Sequence: D → A | ||||||
Mutagenesis | 104 | Abolishes enzymatic activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 131 | Reduces trimerization. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 170 | Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis. | ||||
Sequence: C → S | ||||||
Mutagenesis | 171 | No effect on subcellular location. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 150 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), disulfide bond, modified residue, lipidation, propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000094780 | 1-170 | UniProt | Protein tyrosine phosphatase type IVA 1 | |||
Sequence: MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNC | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Disulfide bond | 49↔104 | UniProt | |||||
Sequence: CEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHC | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 170 | UniProt | Cysteine methyl ester | ||||
Sequence: C | |||||||
Lipidation | 170 | UniProt | S-farnesyl cysteine | ||||
Sequence: C | |||||||
Propeptide | PRO_0000396726 | 171-173 | UniProt | Removed in mature form | |||
Sequence: CIQ |
Post-translational modification
Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in bone marrow, lymph nodes, T lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor cell lines.
Induction
Strongly down-regulated upon tetrodotoxin treatment.
Developmental stage
Expressed in fetal liver.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotrimer. Interacts with ATF5 (By similarity).
Interacts with tubulin
Interacts with tubulin
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q93096 | CNNM1 Q9NRU3 | 7 | EBI-1058467, EBI-11986439 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-161 | Tyrosine-protein phosphatase | ||||
Sequence: APVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFK | ||||||
Region | 97-132 | Interaction with ATF5 | ||||
Sequence: GCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQF |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length173
- Mass (Da)19,815
- Last updated2005-07-05 v2
- Checksum702008013D3F3835
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B3ISR8 | A0A3B3ISR8_HUMAN | PTP4A1 | 35 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U48296 EMBL· GenBank· DDBJ | AAB40597.1 EMBL· GenBank· DDBJ | mRNA | ||
AF051160 EMBL· GenBank· DDBJ | AAC39836.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK312526 EMBL· GenBank· DDBJ | BAG35425.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749458 EMBL· GenBank· DDBJ | CAH18292.1 EMBL· GenBank· DDBJ | mRNA | ||
AL135905 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471143 EMBL· GenBank· DDBJ | EAW88494.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC023975 EMBL· GenBank· DDBJ | AAH23975.1 EMBL· GenBank· DDBJ | mRNA | ||
BC045571 EMBL· GenBank· DDBJ | AAH45571.1 EMBL· GenBank· DDBJ | mRNA | ||
U69701 EMBL· GenBank· DDBJ | AAB09080.1 EMBL· GenBank· DDBJ | mRNA |