B1AUH1 · PTPRU_MOUSE
- ProteinReceptor-type tyrosine-protein phosphatase U
- GenePtpru
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1446 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (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 | 1053 | substrate | ||||
Sequence: E | ||||||
Active site | 1085 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 1085-1091 | substrate | ||||
Sequence: CSAGTGR | ||||||
Binding site | 1129 | substrate | ||||
Sequence: Q | ||||||
Active site | 1380 | Phosphocysteine intermediate | ||||
Sequence: C |
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-cell junction | |
Cellular Component | plasma membrane | |
Molecular Function | beta-catenin binding | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | animal organ regeneration | |
Biological Process | cell differentiation | |
Biological Process | homotypic cell-cell adhesion | |
Biological Process | negative regulation of canonical Wnt signaling pathway | |
Biological Process | negative regulation of cell migration | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of cell-cell adhesion mediated by cadherin | |
Biological Process | protein localization to cell surface | |
Biological Process | response to glucocorticoid |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReceptor-type tyrosine-protein phosphatase U
- EC number
- Short namesR-PTP-U
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionB1AUH1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-749 | Extracellular | ||||
Sequence: ETETPAAGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPTRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCYRYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLILTNPEGRKEGKEVTFQTDEDVPGGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVVVEEERPRRLRREPGAQDCFSVPLTFETALARGLVHYFGAELAASSLLEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLIL | ||||||
Transmembrane | 750-770 | Helical | ||||
Sequence: GICAGGLAVLILLLGAIIVII | ||||||
Topological domain | 771-1446 | Cytoplasmic | ||||
Sequence: RKGRDRYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDAPGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALELR |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MARAQALVLALTFQFCAP | ||||||
Chain | PRO_0000371659 | 19-1446 | Receptor-type tyrosine-protein phosphatase U | |||
Sequence: ETETPAAGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPTRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCYRYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLILTNPEGRKEGKEVTFQTDEDVPGGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVVVEEERPRRLRREPGAQDCFSVPLTFETALARGLVHYFGAELAASSLLEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLILGICAGGLAVLILLLGAIIVIIRKGRDRYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDAPGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALELR | ||||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 210↔264 | |||||
Sequence: CMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRC | ||||||
Glycosylation | 410 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 685 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 848 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 853 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 863 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 865 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed (By similarity).
N-glycosylated.
Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Transcripts of different sizes are differentially expressed in a subset of tissues. Detected in brain, lung, skeletal muscle, heart, kidney and placenta. In brain; expressed in olfactory bulb, cerebral cortex, hippocampus and cerebellum.
Developmental stage
Expressed throughout embryonic development. First detected at 7 dpc.
Gene expression databases
Interaction
Subunit
Forms homooligomeric complexes which mediate cell homotypic adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT (By similarity).
May interact with AP3B1 (By similarity).
May interact with AP3B1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-188 | MAM | ||||
Sequence: AGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAK | ||||||
Domain | 190-275 | Ig-like C2-type | ||||
Sequence: PHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVS | ||||||
Domain | 288-383 | Fibronectin type-III 1 | ||||
Sequence: PIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEP | ||||||
Domain | 386-484 | Fibronectin type-III 2 | ||||
Sequence: APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCYRYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLILTNPEGRKEGKEVTFQTDED | ||||||
Domain | 485-591 | Fibronectin type-III 3 | ||||
Sequence: VPGGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGFGQAALTEITTNISAPS | ||||||
Domain | 592-668 | Fibronectin type-III 4 | ||||
Sequence: FDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVVVEEERPRRLRREPGAQDCFSVPLTFETALARGLVHYFGAE | ||||||
Region | 771-887 | Mediates interaction with CTNNB1 | ||||
Sequence: RKGRDRYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDAPGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMK | ||||||
Region | 830-867 | Disordered | ||||
Sequence: PGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHT | ||||||
Domain | 888-1144 | Tyrosine-protein phosphatase 1 | ||||
Sequence: TAEGYGFKQEYESFFEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA | ||||||
Domain | 1176-1439 | Tyrosine-protein phosphatase 2 | ||||
Sequence: LREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEY |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
B1AUH1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,446
- Mass (Da)162,494
- Last updated2008-04-08 v1
- ChecksumCBF639D8150D0D0B
B1AUH1-2
- Name2
- Differences from canonical
- 774-783: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q3V360 | Q3V360_MOUSE | Ptpru | 907 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 80 | in Ref. 2; AAB17895 | ||||
Sequence: A → T | ||||||
Sequence conflict | 158 | in Ref. 2; AAB17895 | ||||
Sequence: Y → F | ||||||
Sequence conflict | 265 | in Ref. 6; AAH80736 | ||||
Sequence: V → A | ||||||
Sequence conflict | 387 | in Ref. 6; AAH80736 | ||||
Sequence: P → S | ||||||
Sequence conflict | 506 | in Ref. 6; AAH80736 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_037086 | 774-783 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1158 | in Ref. 2; AAB17895 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D88187 EMBL· GenBank· DDBJ | BAA23475.1 EMBL· GenBank· DDBJ | mRNA | ||
U55057 EMBL· GenBank· DDBJ | AAB17895.1 EMBL· GenBank· DDBJ | mRNA | ||
AL670959 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466552 EMBL· GenBank· DDBJ | EDL30128.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK052720 EMBL· GenBank· DDBJ | BAE43351.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC080736 EMBL· GenBank· DDBJ | AAH80736.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |