Q8TF42 · UBS3B_HUMAN
- ProteinUbiquitin-associated and SH3 domain-containing protein B
- GeneUBASH3B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids649 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 390 | |||||
Sequence: R | ||||||
Active site | 391 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Active site | 576 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | phosphoprotein binding | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | collagen-activated tyrosine kinase receptor signaling pathway | |
Biological Process | negative regulation of bone resorption | |
Biological Process | negative regulation of osteoclast differentiation | |
Biological Process | negative regulation of platelet aggregation | |
Biological Process | negative regulation of signal transduction | |
Biological Process | platelet aggregation | |
Biological Process | regulation of osteoclast differentiation | |
Biological Process | regulation of release of sequestered calcium ion into cytosol |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin-associated and SH3 domain-containing protein B
- 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 accessionQ8TF42
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052676 | 68 | in dbSNP:rs12790613 | |||
Sequence: A → T | ||||||
Natural variant | VAR_061923 | 569 | in dbSNP:rs35343548 | |||
Sequence: N → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 620 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000245508 | 1-649 | UniProt | Ubiquitin-associated and SH3 domain-containing protein B | |||
Sequence: MAQYGHPSPLGMAAREELYSKVTPRRNRQQRPGTIKHGSALDVLLSMGFPRARAQKALASTGGRSVQAACDWLFSHVGDPFLDDPLPREYVLYLRPTGPLAQKLSDFWQQSKQICGKNKAHNIFPHITLCQFFMCEDSKVDALGEALQTTVSRWKCKFSAPLPLELYTSSNFIGLFVKEDSAEVLKKFAADFAAEAASKTEVHVEPHKKQLHVTLAYHFQASHLPTLEKLAQNIDVKLGCDWVATIFSRDIRFANHETLQVIYPYTPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADECSTWIFHGSYSILNTSSSNSLTFGDGVLERRPYEDQGLGETTPLTIICQPMQPLRVNSQPGPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGGFRDYEKDAPITVFGCMQARLVGEALLESNTIIDHVYCSPSLRCVQTAHNILKGLQQENHLKIRVEPGLFEWTKWVAGSTLPAWIPPSELAAANLSVDTTYRPHIPISKLVVSESYDTYISRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 20 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 23 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Interacts with JAK2 (in vitro) (By similarity).
Interacts with CBL (PubMed:15159412).
Part of a complex containing CBL and activated EGFR (PubMed:15159412).
Interacts with ubiquitin and with mono-ubiquitinated proteins (PubMed:15159412).
Interacts with ZAP70 (ubiquitinated form) (PubMed:26903241).
Interacts with CBL (PubMed:15159412).
Part of a complex containing CBL and activated EGFR (PubMed:15159412).
Interacts with ubiquitin and with mono-ubiquitinated proteins (PubMed:15159412).
Interacts with ZAP70 (ubiquitinated form) (PubMed:26903241).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-76 | UBA | ||||
Sequence: NRQQRPGTIKHGSALDVLLSMGFPRARAQKALASTGGRSVQAACDWLFSH | ||||||
Domain | 254-319 | SH3 | ||||
Sequence: ANHETLQVIYPYTPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADE | ||||||
Region | 380-649 | Protein tyrosine phosphatase | ||||
Sequence: GPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGGFRDYEKDAPITVFGCMQARLVGEALLESNTIIDHVYCSPSLRCVQTAHNILKGLQQENHLKIRVEPGLFEWTKWVAGSTLPAWIPPSELAAANLSVDTTYRPHIPISKLVVSESYDTYISRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length649
- Mass (Da)72,696
- Last updated2006-07-11 v2
- Checksum70ED9F50EA20BF43
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 465 | in Ref. 3; BAD96563/BAD96566 | ||||
Sequence: H → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB075839 EMBL· GenBank· DDBJ | BAB85545.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK075203 EMBL· GenBank· DDBJ | BAC11468.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222843 EMBL· GenBank· DDBJ | BAD96563.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222846 EMBL· GenBank· DDBJ | BAD96566.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007541 EMBL· GenBank· DDBJ | AAH07541.2 EMBL· GenBank· DDBJ | mRNA | ||
AF425252 EMBL· GenBank· DDBJ | AAL16953.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |