P35831 · PTN12_MOUSE
- ProteinTyrosine-protein phosphatase non-receptor type 12
- GenePtpn12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids775 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:17070019).
Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (By similarity).
Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (By similarity).
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 199 | substrate | ||||
Sequence: D | ||||||
Active site | 231 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 231-237 | substrate | ||||
Sequence: CSAGCGR | ||||||
Binding site | 278 | substrate | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | nucleus | |
Cellular Component | podosome | |
Molecular Function | non-membrane spanning protein tyrosine phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | SH3 domain binding | |
Biological Process | cellular response to epidermal growth factor stimulus | |
Biological Process | peptidyl-tyrosine dephosphorylation | |
Biological Process | regulation of epidermal growth factor receptor signaling pathway | |
Biological Process | tissue regeneration |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein phosphatase non-receptor type 12
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP35831
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Complete embryonic lethality at 9.5 to 10.5 dpc. Heterozygous mice have no obvious phenotype.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 58 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000094772 | 1-775 | Tyrosine-protein phosphatase non-receptor type 12 | |||
Sequence: MEQVEILRRFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGNEITTGTMVSSIDSEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDSDRYHPKPVLHMASPEQHPADLNRSYDKSADPMGKSESAIEHIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASSSVVDRTSKPQELSAGALKVDDVSQNSCADCSAAHSHRAAESSEESQSNSHTPPRPDCLPLDKKGHVTWSLHGPENATPVPDSPDGKSPDNHSQTLKTVSSTPNSTAEEEAHDLTEHHNSSPLLKAPLSFTNPLHSDDSDSDGGSSDGAVTRNKTSISTASATVSPASSAESACTRRVLPMSIARQEVAGTPHSGAEKDADVSEESPPPLPERTPESFVLADMPVRPEWHELPNQEWSEQRESEGLTTSGNEKHDAGGIHTEASADSPPAFSDKKDQITKSPAEVTDIGFGNRCGKPKGPREPPSEWT | ||||||
Modified residue | 19 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 331 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 434 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 448 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 467 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 519 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 550 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 567 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 569 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 596 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 598 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 603 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 606 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 608 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 613 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 673 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 748 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by STK24/MST3 and this results in inhibition of its activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with PSTPIP1 and TGFB1I1 (PubMed:10092676, PubMed:11711533).
Interacts with PTK2B/PYK2 (PubMed:12674328).
Interacts with LPXN (PubMed:12674328, PubMed:15786712).
Interacts with SORBS2; this interaction greatly enhances WASF1 dephosphorylation and might mediate partial translocation to focal adhesion sites (By similarity).
Interacts with PTK2B/PYK2 (PubMed:12674328).
Interacts with LPXN (PubMed:12674328, PubMed:15786712).
Interacts with SORBS2; this interaction greatly enhances WASF1 dephosphorylation and might mediate partial translocation to focal adhesion sites (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35831 | Pstpip1 P97814 | 5 | EBI-2642957, EBI-7484574 | |
BINARY | P35831 | Shc1 P98083 | 2 | EBI-2642957, EBI-300201 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-293 | Tyrosine-protein phosphatase | ||||
Sequence: FARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQL | ||||||
Region | 322-341 | Disordered | ||||
Sequence: SSIDSEKQDSPPPKPPRTRS | ||||||
Region | 344-437 | Interaction with TGFB1I1 | ||||
Sequence: VEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDSDRYHPKPVLHMASPEQHPADLNRSYDKSADPMGKSESAIEHIDKKLERNLSFEI | ||||||
Region | 462-775 | Disordered | ||||
Sequence: KIKSASSSVVDRTSKPQELSAGALKVDDVSQNSCADCSAAHSHRAAESSEESQSNSHTPPRPDCLPLDKKGHVTWSLHGPENATPVPDSPDGKSPDNHSQTLKTVSSTPNSTAEEEAHDLTEHHNSSPLLKAPLSFTNPLHSDDSDSDGGSSDGAVTRNKTSISTASATVSPASSAESACTRRVLPMSIARQEVAGTPHSGAEKDADVSEESPPPLPERTPESFVLADMPVRPEWHELPNQEWSEQRESEGLTTSGNEKHDAGGIHTEASADSPPAFSDKKDQITKSPAEVTDIGFGNRCGKPKGPREPPSEWT | ||||||
Compositional bias | 554-575 | Polar residues | ||||
Sequence: KSPDNHSQTLKTVSSTPNSTAE | ||||||
Compositional bias | 589-639 | Polar residues | ||||
Sequence: PLLKAPLSFTNPLHSDDSDSDGGSSDGAVTRNKTSISTASATVSPASSAES | ||||||
Compositional bias | 659-673 | Basic and acidic residues | ||||
Sequence: PHSGAEKDADVSEES |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length775
- Mass (Da)86,526
- Last updated2011-07-27 v3
- ChecksumED1A7A577CE4352C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 110-111 | in Ref. 3; CAA60477 | ||||
Sequence: LA → FR | ||||||
Sequence conflict | 128 | in Ref. 3; CAA60477 | ||||
Sequence: I → M | ||||||
Sequence conflict | 296 | in Ref. 1; CAA45037 | ||||
Sequence: K → N | ||||||
Sequence conflict | 310 | in Ref. 3; CAA60477 | ||||
Sequence: A → R | ||||||
Sequence conflict | 328-332 | in Ref. 1; CAA45037 | ||||
Sequence: KQDSP → DETS | ||||||
Sequence conflict | 380 | in Ref. 1; CAA45037 | ||||
Sequence: W → V | ||||||
Sequence conflict | 414-415 | in Ref. 3; CAA60477 | ||||
Sequence: PM → QW | ||||||
Compositional bias | 554-575 | Polar residues | ||||
Sequence: KSPDNHSQTLKTVSSTPNSTAE | ||||||
Compositional bias | 589-639 | Polar residues | ||||
Sequence: PLLKAPLSFTNPLHSDDSDSDGGSSDGAVTRNKTSISTASATVSPASSAES | ||||||
Sequence conflict | 606-607 | in Ref. 3; CAA60477 | ||||
Sequence: SD → WH | ||||||
Sequence conflict | 642 | in Ref. 3; CAA60477 | ||||
Sequence: T → H | ||||||
Compositional bias | 659-673 | Basic and acidic residues | ||||
Sequence: PHSGAEKDADVSEES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X63440 EMBL· GenBank· DDBJ | CAA45037.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
X86781 EMBL· GenBank· DDBJ | CAA60477.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK154107 EMBL· GenBank· DDBJ | BAE32381.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466586 EMBL· GenBank· DDBJ | EDL03216.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC051980 EMBL· GenBank· DDBJ | AAH51980.1 EMBL· GenBank· DDBJ | mRNA |