Tag | Content |
---|
CPLM ID | CPLM-024654 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | OTU domain-containing protein 7B |
Protein Synonyms/Alias | Cellular zinc finger anti-NF-kappa-B protein; Zinc finger A20 domain-containing protein 1; Zinc finger protein Cezanne |
Gene Name | Otud7b |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
---|
93 | QDDVIQEKRLSRGIS | ubiquitination | [1] | 263 | KEWNELIKLASSEPR | ubiquitination | [1] | 511 | NKLGSFGKTLGSKLK | 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 | Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF- kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Mediates deubiquitination of EGFR. Has deubiquitinating activity toward 'Lys-11', 'Lys-48' or 'Lys-63'- linked polyubiquitin chains. In vitro, has preference for 'Lys- 11'-linked polyubiquitin chains; however such data are unsure in vivo. Hydrolyzes both linear and branched forms of polyubiquitin. |
Sequence Annotation | DOMAIN 183 365 OTU. ZN_FING 793 828 A20-type. REGION 152 401 TRAF-binding (By similarity). REGION 167 440 Catalytic (By similarity). MOTIF 483 498 Nuclear localization signal (Potential). ACT_SITE 194 194 Nucleophile (Probable). ACT_SITE 358 358 Proton acceptor (Probable). MOD_RES 100 100 Phosphoserine (By similarity). MOD_RES 471 471 Phosphoserine. |
Keyword | Complete proteome; Cytoplasm; Hydrolase; Immunity; Metal-binding; Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 840 AA |
Protein Sequence | MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVSAALSD FEQLRQVHAG NLSPPFSGGS 60 TCPKTPEKGG SDREPTRPSR PILQRQDDVI QEKRLSRGIS HASSSIVSLA RSHVSSNGGG 120 GGSSEHPLEM PICAFQLPDL TVYKEDFRSF IERDLIEQSM LVALEQAGRL NWWVSMDSTC 180 QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LVLRKALYAL MEKGVEKEAL RRRWRWQQTQ 240 QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGSNGASG GGVESSEEPV YESLEEFHVF 300 VLAHVLKRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS 360 ALVSMEQKES AKEQAVIPLT DSEHKLLPLH FAVDPGKGWE WGKDDNDNVR LASIILSLEV 420 KLHLLHSYMN VKWIPLSSDS QAPLAQPESP TASAGDEPRS TPESGESDKE SVGSSSLGNE 480 GSRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGP KPGGLGSGSG 540 ISSGTETLEK KKKNNTLKSW KGGKEEAAGD GPVSEKPPSE SVGNGGSKYS QEVMQSLSTM 600 RIAMQGEGKY IFVGTLKMGH RHQYQEEMIQ RYLADAEERF LAEQKQKEVE RKIMNGGLVS 660 GPPPAKKPEP DGGEDQPSDS PAEPKAMAFS TAYPGGFTIP RPSGGGVHCQ EPRRQLAGGP 720 CVGGLPSYAT FPRQYPGRPY PHQDNIPALE PGKDGVHRGA LLPPQFRVAD SYSNGYREPP 780 EPDGWAGAPR GLPPTQTKCK QPNCSFYGHP ETNNLCSCCY REELRRRERE PGGELLAHRF 840 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:MGI. GO:0015630; C:microtubule cytoskeleton; IEA:Compara. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB. GO:0003677; F:DNA binding; IEA:InterPro. GO:0070530; F:K63-linked polyubiquitin binding; IDA:BHF-UCL. GO:0004221; F:ubiquitin thiolesterase activity; IMP:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0002385; P:mucosal immune response; IMP:UniProtKB. GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB. GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB. GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB. GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |