| Tag | Content |
|---|
| CPLM ID | CPLM-016397 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin-associated and SH3 domain-containing protein B |
Protein Synonyms/Alias | Cbl-interacting protein p70; Suppressor of T-cell receptor signaling 1; STS-1; T-cell ubiquitin ligand 2; TULA-2; Tyrosine-protein phosphatase STS1/TULA2 |
Gene Name | Ubash3b |
Gene Synonyms/Alias | Sts1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 400 | LSQCFDAKGRYIRTN | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 23 65 UBA.
DOMAIN 243 308 SH3.
REGION 369 638 Protein tyrosine phosphatase.
ACT_SITE 379 379
ACT_SITE 380 380 Tele-phosphohistidine intermediate.
ACT_SITE 565 565
MOD_RES 9 9 Phosphoserine (By similarity).
MOD_RES 12 12 Phosphothreonine (By similarity). |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; SH3 domain. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 638 AA |
Protein Sequence | MAAREELYSK VTPRRDRLQR PGTVKHGSAL DVLLSMGFPR ARAQKALAST GGRSVQAACD 60
WLFSHVGDPF LDDPLPREYV LYLRPTGPLA QKLSDFWQQS KQICGKNKAH NIFPHITLCQ 120
FFMCEDSKVD ALGEALQTTV SRWKCKFSAP LPLELYTSSN FIGLFVKEDS AEVLKKFAAD 180
FAAEAASKTE VHVEPHKKQL HVTLAYHFQA SHLPTLEKLA QNIDVKLGCD WVATIFSRDI 240
RFANHETLQV IYPYSPQNDD ELELVPGDFI FMSPMEQTST SEGWIYGTSL TTGCSGLLPE 300
NYITKADECS TWIFHGSYSI LNTVSSSSLA FGDGALERRQ YEDQGLGETT PLTIICQPMQ 360
PLRVNSQPGP QKRCLFVCRH GERMDVVFGK YWLSQCFDAK GRYIRTNLNM PHSLPQRSGG 420
FRDYEKDAPI TVFGCMQARL VGEALLESNT VIDHVYCSPS LRCVQTAHNI LKGLQQDNHL 480
KIRVEPGLFE WTKWVAGSTL PAWIPPSELA AANLSVDTTY RPHIPVSKLA ISESYDTYIN 540
RSFQVTKEII SECKSKGNNI LIVAHASSLE ACTCQLQGLS PQNSKDFVQM VRKIPYLGFC 600
SCEELGETGI WQLTDPPILP LTHGPTGGFN WRETLLQE 638 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC. GO:0090331; P:negative regulation of platelet aggregation; IMP:MGI. GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI. GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:MGI. GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |