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B2RUR8 (OTU7B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
OTU domain-containing protein 7B

EC=3.4.19.12
Alternative name(s):
Cellular zinc finger anti-NF-kappa-B protein
Zinc finger A20 domain-containing protein 1
Zinc finger protein Cezanne
Gene names
Name:Otud7b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length840 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Enzyme regulation

Deubiquitinase activity is inhibited following interactin with PARK7 By similarity.

Subunit structure

Interacts with TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4 By similarity. Interacts with TRAF3. Ref.5

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner.

Post-translational modification

Phosphorylated by EGFR By similarity.

Disruption phenotype

Mice do not show obvious defects in survival, except a moderately reduced body weight. They however display hyperactivation of non-canonical NF-kappa-B without affecting canonical NF-kappa-B activation. Mice show B-cell hyper-responsiveness to antigens, lymphoid follicular hyperplasia in the intestinal mucosa and elevated host-defense ability against an intestinal bacterial pathogen, Citrobacter rodentium. Ref.5

Sequence similarities

Belongs to the peptidase C64 family.

Contains 1 A20-type zinc finger.

Contains 1 OTU domain.

Sequence caution

The sequence AAH37040.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processImmunity
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmucosal immune response

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.5. Source: UniProtKB

protein K11-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked deubiquitination

Inferred from mutant phenotype Ref.5. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from direct assay PubMed 12682062. Source: MGI

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12682062. Source: MGI

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

K63-linked polyubiquitin binding

Inferred from direct assay PubMed 18281465. Source: BHF-UCL

cysteine-type peptidase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 840840OTU domain-containing protein 7B
PRO_0000421819

Regions

Domain183 – 365183OTU
Zinc finger793 – 82836A20-type
Region152 – 401250TRAF-binding By similarity
Region167 – 440274Catalytic By similarity
Motif483 – 49816Nuclear localization signal Potential

Sites

Active site1911 By similarity
Active site1941Nucleophile Probable
Active site3581Proton acceptor Probable

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Experimental info

Mutagenesis1941C → S: Loss of deubiquitinating activity; when associated with R-358. Ref.5
Mutagenesis3581H → R: Loss of deubiquitinating activity; when associated with S-194. Ref.5

Sequences

Sequence LengthMass (Da)Tools
B2RUR8 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: B63C06B656CC02EE

FASTA84091,983
        10         20         30         40         50         60 
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVSAALSD FEQLRQVHAG NLSPPFSGGS 

        70         80         90        100        110        120 
TCPKTPEKGG SDREPTRPSR PILQRQDDVI QEKRLSRGIS HASSSIVSLA RSHVSSNGGG 

       130        140        150        160        170        180 
GGSSEHPLEM PICAFQLPDL TVYKEDFRSF IERDLIEQSM LVALEQAGRL NWWVSMDSTC 

       190        200        210        220        230        240 
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LVLRKALYAL MEKGVEKEAL RRRWRWQQTQ 

       250        260        270        280        290        300 
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGSNGASG GGVESSEEPV YESLEEFHVF 

       310        320        330        340        350        360 
VLAHVLKRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS 

       370        380        390        400        410        420 
ALVSMEQKES AKEQAVIPLT DSEHKLLPLH FAVDPGKGWE WGKDDNDNVR LASIILSLEV 

       430        440        450        460        470        480 
KLHLLHSYMN VKWIPLSSDS QAPLAQPESP TASAGDEPRS TPESGESDKE SVGSSSLGNE 

       490        500        510        520        530        540 
GSRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGP KPGGLGSGSG 

       550        560        570        580        590        600 
ISSGTETLEK KKKNNTLKSW KGGKEEAAGD GPVSEKPPSE SVGNGGSKYS QEVMQSLSTM 

       610        620        630        640        650        660 
RIAMQGEGKY IFVGTLKMGH RHQYQEEMIQ RYLADAEERF LAEQKQKEVE RKIMNGGLVS 

       670        680        690        700        710        720 
GPPPAKKPEP DGGEDQPSDS PAEPKAMAFS TAYPGGFTIP RPSGGGVHCQ EPRRQLAGGP 

       730        740        750        760        770        780 
CVGGLPSYAT FPRQYPGRPY PHQDNIPALE PGKDGVHRGA LLPPQFRVAD SYSNGYREPP 

       790        800        810        820        830        840 
EPDGWAGAPR GLPPTQTKCK QPNCSFYGHP ETNNLCSCCY REELRRRERE PGGELLAHRF 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Eye.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"OTUD7B controls non-canonical NF-kappaB activation through deubiquitination of TRAF3."
Hu H., Brittain G.C., Chang J.H., Puebla-Osorio N., Jin J., Zal A., Xiao Y., Cheng X., Chang M., Fu Y.X., Zal T., Zhu C., Sun S.C.
Nature 494:371-374(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TRAF3, MUTAGENESIS OF CYS-194 AND HIS-358.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC092094 Genomic DNA. No translation available.
CH466620 Genomic DNA. Translation: EDL38862.1.
BC141397 mRNA. Translation: AAI41398.1.
BC037040 mRNA. Translation: AAH37040.1. Sequence problems.
BC141398 mRNA. Translation: AAI41399.1.
RefSeqNP_001020784.1. NM_001025613.1.
NP_001020785.1. NM_001025614.1.
XP_006501447.1. XM_006501384.1.
XP_006501448.1. XM_006501385.1.
XP_006501449.1. XM_006501386.1.
XP_006501450.1. XM_006501387.1.
XP_006501451.1. XM_006501388.1.
XP_006501452.1. XM_006501389.1.
UniGeneMm.272336.
Mm.487453.

3D structure databases

ProteinModelPortalB2RUR8.
SMRB2RUR8. Positions 1-59, 107-438, 798-829.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60128N.
IntActB2RUR8. 1 interaction.
STRING10090.ENSMUSP00000088291.

Protein family/group databases

MEROPSC64.001.

Proteomic databases

PaxDbB2RUR8.
PRIDEB2RUR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035519; ENSMUSP00000046413; ENSMUSG00000038495.
ENSMUST00000090785; ENSMUSP00000088291; ENSMUSG00000038495.
ENSMUST00000098849; ENSMUSP00000096449; ENSMUSG00000038495.
GeneID229603.
KEGGmmu:229603.
UCSCuc008qma.1. mouse.

Organism-specific databases

CTD56957.
MGIMGI:2654703. Otud7b.

Phylogenomic databases

eggNOGNOG282016.
GeneTreeENSGT00530000062989.
HOGENOMHOG000048103.
HOVERGENHBG050904.
InParanoidB2RUR8.
KOK11860.
OMAYATFPRQ.
OrthoDBEOG7JHM57.
PhylomeDBB2RUR8.
TreeFamTF323312.

Gene expression databases

ArrayExpressB2RUR8.
GenevestigatorB2RUR8.

Family and domain databases

InterProIPR003323. OTU.
IPR002653. Znf_A20.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379553.
PROB2RUR8.
SOURCESearch...

Entry information

Entry nameOTU7B_MOUSE
AccessionPrimary (citable) accession number: B2RUR8
Secondary accession number(s): Q8CFS0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot