Q6GQQ9 (OTU7B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	843 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.19
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. Ref.16
Subunit structure	Interacts with TRAF3 and TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4. Ref.1 Ref.16 Ref.19
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. Ref.1 Ref.18
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.16
Post-translational modification	Phosphorylated by EGFR. Ref.19
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 process	Immunity Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mucosal immune response Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.1. Source: HGNC protein K11-linked deubiquitination Inferred from direct assay Ref.13. Source: UniProtKB protein K48-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K63-linked deubiquitination Inferred from direct assay Ref.13. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: HGNC microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.1. Source: HGNC
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro cysteine-type peptidase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCDC50	Q8IVM0	5	EBI-527784,EBI-723996
PARK7	Q99497	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 843	843	OTU domain-containing protein 7B		PRO_0000188788
Regions
	Domain	183 – 365	183	OTU
	Zinc finger	796 – 831	36	A20-type
	Region	152 – 401	250	TRAF-binding
	Region	167 – 440	274	Catalytic
	Motif	483 – 498	16	Nuclear localization signal Potential
Sites
	Active site	194	1	Nucleophile Probable
	Active site	358	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	100	1	Phosphoserine Ref.11 Ref.12
	Modified residue	471	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	805 – 833	29	Missing in isoform 2.		VSP_046015
Experimental info
	Mutagenesis	194	1	C → A: Increased ability to interact with polyubiquitin. Ref.7 Ref.8 Ref.19
	Mutagenesis	194	1	C → S: Loss of deubiquitinating activity. Ref.7 Ref.8 Ref.19
	Mutagenesis	809	1	F → A: Does not affect interaction with EGFR. Ref.19
	Mutagenesis	810	1	Y → A: Impairs interaction with EGFR. Ref.19
	Sequence conflict	243	1	K → E in AAH20622. Ref.5
	Sequence conflict	421	1	K → R in AAH20622. Ref.5
	Sequence conflict	791	1	G → S in BAH13129. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 6D386C864B12EE57	FASTA	843	92,526
	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
	Isoform 2 [UniParc]. Checksum: 26C3BFE215BEC0D3	FASTA	814	88,947
	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 EPPEPDGWAG GLRGLPPTQT KCKQPDGELL VHRF

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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.
[15]	"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].
[16]	"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.
[17]	"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].
[18]	"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.
[19]	"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.
+	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.
IPI	IPI00024658.
PIR	T34535.
RefSeq	NP_064590.2. NM_020205.2.
UniGene	Hs.98322.
3D structure databases
ProteinModelPortal	Q6GQQ9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6GQQ9. 12 interactions.
STRING	9606.ENSP00000358131.
Protein family/group databases
MEROPS	C64.001.
PTM databases
PhosphoSite	Q6GQQ9.
Polymorphism databases
DMDM	51701318.
Proteomic databases
PaxDb	Q6GQQ9.
PRIDE	Q6GQQ9.
Protocols and materials databases
DNASU	56957.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369135; ENSP00000358131; ENSG00000163113.
GeneID	56957.
KEGG	hsa:56957.
UCSC	uc001etn.3. human.
Organism-specific databases
CTD	56957.
GeneCards	GC01M149912.
HGNC	HGNC:16683. OTUD7B.
HPA	HPA027045.
MIM	611748. gene.
neXtProt	NX_Q6GQQ9.
PharmGKB	PA134873802.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG282016.
HOGENOM	HOG000048103.
HOVERGEN	HBG050904.
InParanoid	Q6GQQ9.
KO	K11860.
OMA	ATFPRQC.
OrthoDB	EOG4BRWK6.
Gene expression databases
ArrayExpress	Q6GQQ9.
Bgee	Q6GQQ9.
CleanEx	HS_OTUD7B.
Genevestigator	Q6GQQ9.
GermOnline	ENSG00000163113. Homo sapiens.
Family and domain databases
InterPro	IPR003323. OTU. IPR009060. UBA-like. IPR002653. Znf_A20. [Graphical view]
Pfam	PF02338. OTU. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit.
PROSITE	PS50802. OTU. 1 hit. PS51036. ZF_A20. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	OTUD7B. human.
GenomeRNAi	56957.
NextBio	35479876.
SOURCE	Search...

Entry information

Entry name

OTU7B_HUMAN

Accession

Primary (citable) accession number: Q6GQQ9
Secondary accession number(s): B7Z643 , D3DUZ8, Q5SZ60, Q8WWA7, Q9NQ53, Q9UFF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.