| Tag | Content |
|---|
| CPLM ID | CPLM-012029 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase CBL-B |
Protein Synonyms/Alias | Casitas B-lineage lymphoma proto-oncogene b; RING finger protein 56; SH3-binding protein CBL-B; Signal transduction protein CBL-B |
Gene Name | CBLB |
Gene Synonyms/Alias | RNF56; Nbla00127 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 64 | VRLCQNPKLQLKNSP | ubiquitination | [1] | | 516 | PRLDLIQKGIVRSPC | ubiquitination | [1, 2] | | 531 | GSPTGSPKSSPCMVR | ubiquitination | [1] | | 616 | LLGEGSPKPGITASS | ubiquitination | [1] | | 881 | RLPGENVKTNRTSQD | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA. Mol Cell Proteomics. 2012 May;11(5):148-59. [ PMID: 22505724] |
Functional Description | E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B- cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T- cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization. |
Sequence Annotation | DOMAIN 35 343 Cbl-PTB.
DOMAIN 931 970 UBA.
ZN_FING 373 412 RING-type.
REGION 35 167 4H.
REGION 168 240 EF-hand-like.
REGION 241 343 SH2-like.
REGION 344 372 Linker.
REGION 543 568 Interaction with VAV1.
REGION 891 927 Interaction with SH3KBP1.
BINDING 286 286 Phosphotyrosine (By similarity).
MOD_RES 282 282 Phosphoserine; by PKC/PRKCQ.
MOD_RES 521 521 Phosphoserine.
MOD_RES 525 525 Phosphoserine.
MOD_RES 529 529 Phosphoserine.
MOD_RES 634 634 Phosphoserine (By similarity).
MOD_RES 665 665 Phosphotyrosine.
MOD_RES 709 709 Phosphotyrosine.
MOD_RES 889 889 Phosphotyrosine. |
Keyword | 3D-structure; Alternative splicing; Calcium; Complete proteome; Cytoplasm; Ligase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 982 AA |
Protein Sequence | MANSMNGRNP GGRGGNPRKG RILGIIDAIQ DAVGPPKQAA ADRRTVEKTW KLMDKVVRLC 60
QNPKLQLKNS PPYILDILPD TYQHLRLILS KYDDNQKLAQ LSENEYFKIY IDSLMKKSKR 120
AIRLFKEGKE RMYEEQSQDR RNLTKLSLIF SHMLAEIKAI FPNGQFQGDN FRITKADAAE 180
FWRKFFGDKT IVPWKVFRQC LHEVHQISSG LEAMALKSTI DLTCNDYISV FEFDIFTRLF 240
QPWGSILRNW NFLAVTHPGY MAFLTYDEVK ARLQKYSTKP GSYIFRLSCT RLGQWAIGYV 300
TGDGNILQTI PHNKPLFQAL IDGSREGFYL YPDGRSYNPD LTGLCEPTPH DHIKVTQEQY 360
ELYCEMGSTF QLCKICAEND KDVKIEPCGH LMCTSCLTAW QESDGQGCPF CRCEIKGTEP 420
IIVDPFDPRD EGSRCCSIID PFGMPMLDLD DDDDREESLM MNRLANVRKC TDRQNSPVTS 480
PGSSPLAQRR KPQPDPLQIP HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ 540
DKPLPAPPPP LRDPPPPPPE RPPPIPPDNR LSRHIHHVES VPSRDPPMPL EAWCPRDVFG 600
TNQLVGCRLL GEGSPKPGIT ASSNVNGRHS RVGSDPVLMR KHRRHDLPLE GAKVFSNGHL 660
GSEEYDVPPR LSPPPPVTTL LPSIKCTGPL ANSLSEKTRD PVEEDDDEYK IPSSHPVSLN 720
SQPSHCHNVK PPVRSCDNGH CMLNGTHGPS SEKKSNIPDL SIYLKGDVFD SASDPVPLPP 780
ARPPTRDNPK HGSSLNRTPS DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG 840
SSSRPSSGQD LFLLPSDPFV DLASGQVPLP PARRLPGENV KTNRTSQDYD QLPSCSDGSQ 900
APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK RALEIAQNNV 960
EVARSILREF AFPPPVSPRL NL 982 |
Gene Ontology | GO:0005829; C:cytosol; TAS:Reactome. GO:0005634; C:nucleus; IDA:HPA. GO:0005886; C:plasma membrane; TAS:Reactome. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0004871; F:signal transducer activity; IEA:InterPro. GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; TAS:ProtInc. GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. GO:0006955; P:immune response; IEA:Compara. GO:0035556; P:intracellular signal transduction; IEA:Compara. GO:0046642; P:negative regulation of alpha-beta T cell proliferation; IEA:Compara. GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Compara. GO:0006607; P:NLS-bearing substrate import into nucleus; TAS:ProtInc. GO:0045732; P:positive regulation of protein catabolic process; IEA:Compara. GO:0002669; P:positive regulation of T cell anergy; IEA:Compara. GO:0007165; P:signal transduction; TAS:ProtInc. GO:0042110; P:T cell activation; IEA:Compara. |
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Pfam | |
SMART | |
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PRINTS | |