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STS-1
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. Note: This description may include information from UniProtKB.
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| Protein type: EC 3.1.3.48; Protein phosphatase, tyrosine (non-receptor) |
| Chromosomal Location of human Ortholog: 11q24.1 |
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Cellular Component:
cytoplasm; nucleus
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Molecular Function:
identical protein binding; phosphoprotein binding; protein binding; protein tyrosine phosphatase activity; ubiquitin protein ligase binding
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Biological Process:
collagen-activated tyrosine kinase receptor signaling pathway; negative regulation of bone resorption; negative regulation of osteoclast differentiation; negative regulation of platelet aggregation; negative regulation of protein kinase activity; negative regulation of signal transduction; peptidyl-tyrosine dephosphorylation; platelet aggregation; regulation of osteoclast differentiation; regulation of protein binding; regulation of release of sequestered calcium ion into cytosol
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Reference #:
Q8TF42
(UniProtKB)
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Alt. Names/Synonyms: Cbl-interacting protein p70; Cbl-interacting protein Sts-1; KIAA1959; MGC15437; nm23-phosphorylated unknown substrate; p70; SH3 domain-containing 70 kDa protein, suppressor of T-cell receptor signaling 1, nm23-phosphorylated unknown substrate; STS-1; STS1; Suppressor of T-cell receptor signaling 1; T-cell ubiquitin ligand 2; TULA-2; TULA2; Tyrosine-protein phosphatase STS1/TULA2; UBASH3B; ubiquitin associated and SH3 domain containing B; ubiquitin associated and SH3 domain containing, B; Ubiquitin-associated and SH3 domain-containing protein B; UBS3B
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Gene Symbols: UBASH3B
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Molecular weight:
72,696 Da
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Basal Isoelectric point:
6.48
Predict pI for various phosphorylation states
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