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Q6GQQ9 (OTU7B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
Synonyms:ZA20D1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length843 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.1 Ref.7 Ref.10 Ref.14 Ref.20 Ref.21

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). Ref.21

Enzyme regulation

Deubiquitinase activity is inhibited following interactin with PARK7. Ref.17

Subunit structure

Interacts with TRAF3 and TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4. Ref.1 Ref.17 Ref.20

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. Ref.1 Ref.19

Tissue specificity

Widely expressed. Abundant in kidney, heart and fetal liver. Expressed differentially among B-cells at distinct developmental stages. Higher expression seen in primary immature B-cells as compared to the mature cells. Ref.1 Ref.7

Induction

By TNF-alpha. Ref.10 Ref.17

Post-translational modification

Phosphorylated by EGFR. Ref.20

Sequence similarities

Belongs to the peptidase C64 family.

Contains 1 A20-type zinc finger.

Contains 1 OTU domain.

Sequence caution

The sequence CAB97494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processImmunity
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   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 sequence or structural similarity. Source: UniProtKB

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

Inferred from direct assay Ref.1. Source: HGNC

protein K11-linked deubiquitination

Inferred from direct assay Ref.14Ref.21. Source: UniProtKB

protein K48-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: HGNC

nucleus

Inferred from direct assay Ref.1. Source: HGNC

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

cysteine-type peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18029035Ref.17. Source: IntAct

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.21. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCDC50Q8IVM05EBI-527784,EBI-723996
PARK7Q994973EBI-527784,EBI-1164361

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6GQQ9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6GQQ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     805-833: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843OTU domain-containing protein 7B
PRO_0000188788

Regions

Domain183 – 365183OTU
Zinc finger796 – 83136A20-type
Region152 – 401250TRAF-binding
Region167 – 440274Catalytic
Motif483 – 49816Nuclear localization signal Potential

Sites

Active site1911 By similarity
Active site1941Nucleophile Probable
Active site3581Proton acceptor By similarity

Amino acid modifications

Modified residue1001Phosphoserine Ref.11 Ref.12

Natural variations

Alternative sequence805 – 83329Missing in isoform 2.
VSP_046015

Experimental info

Mutagenesis1941C → A: Increased ability to interact with polyubiquitin. Ref.7 Ref.8 Ref.20
Mutagenesis1941C → S: Loss of deubiquitinating activity. Ref.7 Ref.8 Ref.20
Mutagenesis8091F → A: Does not affect interaction with EGFR. Ref.20
Mutagenesis8101Y → A: Impairs interaction with EGFR. Ref.20
Sequence conflict2431K → E in AAH20622. Ref.5
Sequence conflict4211K → R in AAH20622. Ref.5
Sequence conflict7911G → S in BAH13129. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 6D386C864B12EE57

FASTA84392,526
        10         20         30         40         50         60 
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG NLPPSFSEGS 

        70         80         90        100        110        120 
GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS HASSSIVSLA RSHVSSNGGG 

       130        140        150        160        170        180 
GGSNEHPLEM PICAFQLPDL TVYNEDFRSF IERDLIEQSM LVALEQAGRL NWWVSVDPTS 

       190        200        210        220        230        240 
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ 

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

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

       370        380        390        400        410        420 
ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE WGKDDSDNVR LASVILSLEV 

       430        440        450        460        470        480 
KLHLLHSYMN VKWIPLSSDA QAPLAQPESP TASAGDEPRS TPESGDSDKE SVGSSSTSNE 

       490        500        510        520        530        540 
GGRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG 

       550        560        570        580        590        600 
GSSGTETLEK KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR 

       610        620        630        640        650        660 
TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER KIMNGGIGGG 

       670        680        690        700        710        720 
PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR PSGGGVHCQE PRRQLAGGPC 

       730        740        750        760        770        780 
VGGLPPYATF PRQCPPGRPY PHQDSIPSLE PGSHSKDGLH RGALLPPPYR VADSYSNGYR 

       790        800        810        820        830        840 
EPPEPDGWAG GLRGLPPTQT KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV 


HRF 

« Hide

Isoform 2 [UniParc].

Checksum: 26C3BFE215BEC0D3
Show »

FASTA81488,947

References

« Hide 'large scale' references
[1]"Isolation and characterization of two novel A20-like proteins."
Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R., Kilshaw P.J.
Biochem. J. 357:617-623(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRAF6.
Tissue: Lymphocyte.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Eye and Prostate.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-843.
Tissue: Testis.
[7]"A novel type of deubiquitinating enzyme."
Evans P.C., Smith T.S., Lai M.-J., Williams M.G., Burke D.F., Heyninck K., Kreike M.M., Beyaert R., Blundell T.L., Kilshaw P.J.
J. Biol. Chem. 278:23180-23186(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-194.
[8]"Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity."
Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S., Ploegh H.L., Smith T.S.
Biochem. J. 378:727-734(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-194.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling."
Enesa K., Zakkar M., Chaudhury H., Luong le A., Rawlinson L., Mason J.C., Haskard D.O., Dean J.L., Evans P.C.
J. Biol. Chem. 283:7036-7045(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
Bremm A., Freund S.M., Komander D.
Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH PARK7.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family."
Garcia-Santisteban I., Banuelos S., Rodriguez J.A.
Biochem. J. 441:209-217(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression."
Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y.
Oncogene 31:4599-4608(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EGFR; ITCH AND NEDD4, MUTAGENESIS OF CYS-194; PHE-809 AND TYR-810.
[21]"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293573 mRNA. Translation: CAB97494.1. Different initiation.
AK299790 mRNA. Translation: BAH13129.1.
AL590487 Genomic DNA. Translation: CAI12651.1.
CH471121 Genomic DNA. Translation: EAW53586.1.
CH471121 Genomic DNA. Translation: EAW53587.1.
BC020622 mRNA. Translation: AAH20622.1.
BC072681 mRNA. Translation: AAH72681.1.
AL122102 mRNA. Translation: CAB59268.1.
CCDSCCDS41389.1. [Q6GQQ9-1]
PIRT34535.
RefSeqNP_064590.2. NM_020205.3. [Q6GQQ9-1]
XP_006711524.1. XM_006711461.1. [Q6GQQ9-1]
XP_006711525.1. XM_006711462.1. [Q6GQQ9-1]
XP_006711526.1. XM_006711463.1. [Q6GQQ9-1]
UniGeneHs.98322.

3D structure databases

ProteinModelPortalQ6GQQ9.
SMRQ6GQQ9. Positions 1-61, 147-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121281. 12 interactions.
DIPDIP-33805N.
IntActQ6GQQ9. 13 interactions.
STRING9606.ENSP00000358131.

Protein family/group databases

MEROPSC64.001.

PTM databases

PhosphoSiteQ6GQQ9.

Polymorphism databases

DMDM51701318.

Proteomic databases

MaxQBQ6GQQ9.
PaxDbQ6GQQ9.
PRIDEQ6GQQ9.

Protocols and materials databases

DNASU56957.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369135; ENSP00000358131; ENSG00000163113. [Q6GQQ9-1]
GeneID56957.
KEGGhsa:56957.
UCSCuc001etn.3. human. [Q6GQQ9-1]

Organism-specific databases

CTD56957.
GeneCardsGC01M149912.
HGNCHGNC:16683. OTUD7B.
HPAHPA027045.
MIM611748. gene.
neXtProtNX_Q6GQQ9.
PharmGKBPA134873802.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282016.
HOGENOMHOG000048103.
HOVERGENHBG050904.
InParanoidQ6GQQ9.
KOK11860.
OMAYATFPRQ.
OrthoDBEOG7JHM57.
PhylomeDBQ6GQQ9.
TreeFamTF323312.

Enzyme and pathway databases

SignaLinkQ6GQQ9.

Gene expression databases

ArrayExpressQ6GQQ9.
BgeeQ6GQQ9.
CleanExHS_OTUD7B.
GenevestigatorQ6GQQ9.

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

ChiTaRSOTUD7B. human.
GeneWikiOTUD7B.
GenomeRNAi56957.
NextBio35479876.
PROQ6GQQ9.
SOURCESearch...

Entry information

Entry nameOTU7B_HUMAN
AccessionPrimary (citable) accession number: Q6GQQ9
Secondary accession number(s): B7Z643 expand/collapse secondary AC list , D3DUZ8, Q5SZ60, Q8WWA7, Q9NQ53, Q9UFF4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM