CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014915
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
 ZA20D1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93QDDIVQEKRLSRGISubiquitination[1, 2]
223ALYALMEKGVEKEALubiquitination[1]
243WQQTQQNKESGLVYTubiquitination[1]
263KEWNELIKLASSEPRubiquitination[1, 3, 4]
511NKLGSFGKTLGSKLKubiquitination[5]
644ERFLAEQKQKEAERKubiquitination[1]
651KQKEAERKIMNGGIGubiquitination[1]
665GGGPPPAKKPEPDARubiquitination[1]
666GGPPPAKKPEPDAREubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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 796 831 A20-type.
 REGION 152 401 TRAF-binding.
 REGION 167 440 Catalytic.
 MOTIF 483 498 Nuclear localization signal (Potential).
 ACT_SITE 194 194 Nucleophile (Probable).
 ACT_SITE 358 358 Proton acceptor (By similarity).
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 471 471 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; 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
 843 AA 
Protein Sequence
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG NLPPSFSEGS 60
GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS HASSSIVSLA RSHVSSNGGG 120
GGSNEHPLEM PICAFQLPDL TVYNEDFRSF IERDLIEQSM LVALEQAGRL NWWVSVDPTS 180
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ 240
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGTNGANC GGVESSEEPV YESLEEFHVF 300
VLAHVLRRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS 360
ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE WGKDDSDNVR LASVILSLEV 420
KLHLLHSYMN VKWIPLSSDA QAPLAQPESP TASAGDEPRS TPESGDSDKE SVGSSSTSNE 480
GGRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG 540
GSSGTETLEK KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR 600
TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER KIMNGGIGGG 660
PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR PSGGGVHCQE PRRQLAGGPC 720
VGGLPPYATF PRQCPPGRPY PHQDSIPSLE PGSHSKDGLH RGALLPPPYR VADSYSNGYR 780
EPPEPDGWAG GLRGLPPTQT KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV 840
HRF 843 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HGNC.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HGNC.
 GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0002385; P:mucosal immune response; ISS:UniProtKB.
 GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; IDA:HGNC.
 GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
 GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
 GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR003323; OTU.
 IPR009060; UBA-like.
 IPR002653; Znf_A20. 
Pfam
 PF02338; OTU 
SMART
  
PROSITE
 PS50802; OTU
 PS51036; ZF_A20 
PRINTS