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OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Cezanne) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne)

 OTU7B_HUMAN             Reviewed;         843 AA.
Q6GQQ9; B7Z643; D3DUZ8; Q5SZ60; Q8WWA7; Q9NQ53; Q9UFF4;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
27-SEP-2017, entry version 143.
RecName: Full=OTU domain-containing protein 7B;
EC=3.4.19.12 {ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:27732584};
AltName: Full=Cellular zinc finger anti-NF-kappa-B protein {ECO:0000303|PubMed:11463333};
Short=Cezanne {ECO:0000303|PubMed:11463333, ECO:0000303|PubMed:18178551, ECO:0000303|PubMed:27732584};
AltName: Full=Zinc finger A20 domain-containing protein 1;
AltName: Full=Zinc finger protein Cezanne {ECO:0000305};
Name=OTUD7B; Synonyms=ZA20D1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TRAF6.
TISSUE=Lymphocyte;
PubMed=11463333; DOI=10.1042/0264-6021:3570617;
Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R.,
Kilshaw P.J.;
"Isolation and characterization of two novel A20-like proteins.";
Biochem. J. 357:617-623(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-843.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
CYS-194.
PubMed=12682062; DOI=10.1074/jbc.M301863200;
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.;
"A novel type of deubiquitinating enzyme.";
J. Biol. Chem. 278:23180-23186(2003).
[8]
MUTAGENESIS OF CYS-194, AND CATALYTIC ACTIVITY.
PubMed=14748687; DOI=10.1042/BJ20031377;
Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S.,
Ploegh H.L., Smith T.S.;
"Zinc-finger protein A20, a regulator of inflammation and cell
survival, has de-ubiquitinating activity.";
Biochem. J. 378:727-734(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
FUNCTION, AND INDUCTION.
PubMed=18178551; DOI=10.1074/jbc.M708690200;
Enesa K., Zakkar M., Chaudhury H., Luong le A., Rawlinson L.,
Mason J.C., Haskard D.O., Dean J.L., Evans P.C.;
"NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel
negative feedback loop in pro-inflammatory signaling.";
J. Biol. Chem. 283:7036-7045(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION.
PubMed=20622874; DOI=10.1038/nsmb.1873;
Bremm A., Freund S.M., Komander D.;
"Lys11-linked ubiquitin chains adopt compact conformations and are
preferentially hydrolyzed by the deubiquitinase Cezanne.";
Nat. Struct. Mol. Biol. 17:939-947(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ENZYME REGULATION, AND INTERACTION WITH PARK7.
PubMed=21097510; DOI=10.1074/jbc.M110.147371;
McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A.,
Mak T.W., Ting J.P.;
"DJ-1 enhances cell survival through the binding of cezanne, a
negative regulator of NF-{kappa}B.";
J. Biol. Chem. 286:4098-4106(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
SUBCELLULAR LOCATION.
PubMed=21888622; DOI=10.1042/BJ20111300;
Garcia-Santisteban I., Banuelos S., Rodriguez J.A.;
"A global survey of CRM1-dependent nuclear export sequences in the
human deubiquitinase family.";
Biochem. J. 441:209-217(2012).
[20]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, INTERACTION WITH EGFR;
ITCH AND NEDD4, AND MUTAGENESIS OF CYS-194; PHE-809 AND TYR-810.
PubMed=22179831; DOI=10.1038/onc.2011.587;
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.;
"Deubiquitination of EGFR by Cezanne-1 contributes to cancer
progression.";
Oncogene 31:4599-4608(2012).
[21]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
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.;
"OTU deubiquitinases reveal mechanisms of linkage specificity and
enable ubiquitin chain restriction analysis.";
Cell 154:169-184(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
FUNCTION, INTERACTION WITH ZAP70, MUTAGENESIS OF CYS-194 AND HIS-358,
AND CATALYTIC ACTIVITY.
PubMed=26903241; DOI=10.1084/jem.20151426;
Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
Sun S.C.;
"Otud7b facilitates T cell activation and inflammatory responses by
regulating Zap70 ubiquitination.";
J. Exp. Med. 213:399-414(2016).
[25] {ECO:0000244|PDB:5LRU, ECO:0000244|PDB:5LRV, ECO:0000244|PDB:5LRW}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 129-438 OF APOPROTEIN AND IN
COMPLEXES WITH UBIQUITIN, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
FUNCTION, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF 155-LEU-ILE-156;
GLU-157; ASN-193; CYS-194; HIS-197; ASP-210; GLU-295 AND HIS-358.
PubMed=27732584; DOI=10.1038/nature19836;
Mevissen T.E., Kulathu Y., Mulder M.P., Geurink P.P., Maslen S.L.,
Gersch M., Elliott P.R., Burke J.E., van Tol B.D., Akutsu M.,
El Oualid F., Kawasaki M., Freund S.M., Ovaa H., Komander D.;
"Molecular basis of Lys11-polyubiquitin specificity in the
deubiquitinase Cezanne.";
Nature 538:402-405(2016).
-!- 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 (By similarity). Deubiquitinates ZAP70, and
thereby regulates T cell receptor (TCR) signaling that leads to
the activation of NF-kappa-B (PubMed:26903241). Plays a role in T
cell homeostasis and is required for normal T cell responses,
including production of IFNG and IL2 (By similarity). Mediates
deubiquitination of EGFR (PubMed:22179831). Has deubiquitinating
activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked
polyubiquitin chains (PubMed:27732584). Has a much higher
catalytic rate with 'Lys-11'-linked polyubiquitin chains (in
vitro); however the physiological significance of these data are
unsure (PubMed:27732584). Hydrolyzes both linear and branched
forms of polyubiquitin. {ECO:0000250|UniProtKB:B2RUR8,
ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062,
ECO:0000269|PubMed:18178551, ECO:0000269|PubMed:20622874,
ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681,
ECO:0000269|PubMed:27732584}.
-!- 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).
{ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681,
ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:27732584}.
-!- ENZYME REGULATION: Deubiquitinase activity is inhibited following
interaction with PARK7. {ECO:0000269|PubMed:21097510}.
-!- SUBUNIT: Interacts with ZAP70 in activated T cells, but not in
resting T cells (PubMed:26903241). Interacts with TRAF3 (By
similarity). Interacts with TRAF6 (PubMed:11463333). Interacts
with PARK7, leading to inhibit deubiquitinase activity
(PubMed:21097510). Interacts with EGFR, ITCH and NEDD4
(PubMed:22179831). {ECO:0000250|UniProtKB:B2RUR8,
ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:21097510,
ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:26903241}.
-!- INTERACTION:
Q8IVM0:CCDC50; NbExp=5; IntAct=EBI-527784, EBI-723996;
Q99497:PARK7; NbExp=3; IntAct=EBI-527784, EBI-1164361;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-527784, EBI-79893;
Q7Z5V6-2:PPP1R32; NbExp=4; IntAct=EBI-527784, EBI-12000762;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11463333,
ECO:0000269|PubMed:21888622}. Nucleus
{ECO:0000269|PubMed:21888622}. Note=Shuttles be cytoplasm and the
nucleus in a XPO1/CRM1-dependent manner.
{ECO:0000269|PubMed:21888622}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6GQQ9-1; Sequence=Displayed;
Name=2;
IsoId=Q6GQQ9-2; Sequence=VSP_046015;
-!- 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.
{ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062}.
-!- INDUCTION: By TNF-alpha. {ECO:0000269|PubMed:18178551}.
-!- DOMAIN: The protein undergoes a significant conformation change
upon binding to ubiquitinated substrates. The loop that precedes
the active site is in an autoinhibitory conformation in the
apoprotein. Ubiquitin binding leads to a conformation change; the
loop is stabilized in a catalytically competent conformation with
the result that the active site Cys can form the reaction state
intermediate. {ECO:0000269|PubMed:27732584}.
-!- PTM: Phosphorylated by EGFR. {ECO:0000269|PubMed:22179831}.
-!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB97494.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ293573; CAB97494.1; ALT_INIT; mRNA.
EMBL; AK299790; BAH13129.1; -; mRNA.
EMBL; AL590487; CAI12651.1; -; Genomic_DNA.
EMBL; CH471121; EAW53586.1; -; Genomic_DNA.
EMBL; CH471121; EAW53587.1; -; Genomic_DNA.
EMBL; BC020622; AAH20622.1; -; mRNA.
EMBL; BC072681; AAH72681.1; -; mRNA.
EMBL; AL122102; CAB59268.1; -; mRNA.
CCDS; CCDS72903.1; -. [Q6GQQ9-1]
PIR; T34535; T34535.
RefSeq; NP_064590.2; NM_020205.3. [Q6GQQ9-1]
UniGene; Hs.98322; -.
PDB; 5LRU; X-ray; 2.20 A; A=129-438.
PDB; 5LRV; X-ray; 2.80 A; A=129-438.
PDB; 5LRW; X-ray; 2.00 A; A/C=129-266, A/C=292-438.
PDBsum; 5LRU; -.
PDBsum; 5LRV; -.
PDBsum; 5LRW; -.
ProteinModelPortal; Q6GQQ9; -.
SMR; Q6GQQ9; -.
BioGrid; 121281; 20.
DIP; DIP-33805N; -.
IntAct; Q6GQQ9; 22.
STRING; 9606.ENSP00000358131; -.
MEROPS; C64.001; -.
iPTMnet; Q6GQQ9; -.
PhosphoSitePlus; Q6GQQ9; -.
DMDM; 51701318; -.
EPD; Q6GQQ9; -.
MaxQB; Q6GQQ9; -.
PaxDb; Q6GQQ9; -.
PeptideAtlas; Q6GQQ9; -.
PRIDE; Q6GQQ9; -.
DNASU; 56957; -.
Ensembl; ENST00000581312; ENSP00000462729; ENSG00000264522. [Q6GQQ9-1]
GeneID; 56957; -.
KEGG; hsa:56957; -.
UCSC; uc001etn.5; human. [Q6GQQ9-1]
CTD; 56957; -.
DisGeNET; 56957; -.
EuPathDB; HostDB:ENSG00000264522.5; -.
GeneCards; OTUD7B; -.
HGNC; HGNC:16683; OTUD7B.
HPA; HPA027045; -.
MIM; 611748; gene.
neXtProt; NX_Q6GQQ9; -.
OpenTargets; ENSG00000264522; -.
PharmGKB; PA134873802; -.
eggNOG; KOG4345; Eukaryota.
eggNOG; ENOG410XT8E; LUCA.
GeneTree; ENSGT00530000062989; -.
HOGENOM; HOG000048103; -.
HOVERGEN; HBG050904; -.
InParanoid; Q6GQQ9; -.
KO; K11860; -.
OMA; YATFPRQ; -.
OrthoDB; EOG091G03R0; -.
PhylomeDB; Q6GQQ9; -.
TreeFam; TF323312; -.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
SignaLink; Q6GQQ9; -.
ChiTaRS; OTUD7B; human.
GeneWiki; OTUD7B; -.
GenomeRNAi; 56957; -.
PRO; PR:Q6GQQ9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000264522; -.
CleanEx; HS_OTUD7B; -.
ExpressionAtlas; Q6GQQ9; baseline and differential.
Genevisible; Q6GQQ9; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0002385; P:mucosal immune response; ISS:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:HGNC.
GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:ParkinsonsUK-UCL.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
InterPro; IPR003323; OTU_dom.
InterPro; IPR002653; Znf_A20.
Pfam; PF02338; OTU; 1.
Pfam; PF01754; zf-A20; 1.
SMART; SM00259; ZnF_A20; 1.
PROSITE; PS50802; OTU; 1.
PROSITE; PS51036; ZF_A20; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Cytoplasm; Hydrolase; Immunity; Metal-binding;
Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 843 OTU domain-containing protein 7B.
/FTId=PRO_0000188788.
DOMAIN 183 365 OTU. {ECO:0000255|PROSITE-
ProRule:PRU00139}.
ZN_FING 796 831 A20-type. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
REGION 152 401 TRAF-binding.
REGION 167 440 Catalytic.
REGION 187 193 Regulatory loop.
{ECO:0000269|PubMed:27732584}.
MOTIF 483 498 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 191 191 {ECO:0000250}.
ACT_SITE 194 194 Nucleophile.
{ECO:0000269|PubMed:12682062,
ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:22179831,
ECO:0000269|PubMed:27732584}.
ACT_SITE 358 358 Proton acceptor.
{ECO:0000269|PubMed:27732584}.
SITE 197 197 Stabilizes the conformation of the
regulatory loop.
{ECO:0000269|PubMed:27732584}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000250|UniProtKB:B2RUR8}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000250|UniProtKB:B2RUR8}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000250|UniProtKB:B2RUR8}.
VAR_SEQ 805 833 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046015.
MUTAGEN 155 156 LI->GG: Reduces deubiquitinating
activity. {ECO:0000269|PubMed:27732584}.
MUTAGEN 157 157 E->K: Reduces deubiquitinating activity
with 'Lys-11'-linked ubiquitin chains; no
effect on cleavage of 'Lys-48'-linked and
'Lys-63'-linked ubiquitin chains.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 193 193 N->L,M: Loss of deubiquitinating activity
due to stabilization of the autoinhibited
conformation.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 194 194 C->A: Loss of deubiquitinating activity.
Increased ability to interact with
polyubiquitin.
{ECO:0000269|PubMed:12682062,
ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:22179831,
ECO:0000269|PubMed:27732584}.
MUTAGEN 194 194 C->S: Loss of deubiquitinating activity.
{ECO:0000269|PubMed:12682062,
ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:22179831}.
MUTAGEN 194 194 C->S: Loss of deubiquitinating activity;
when associated with N-358.
{ECO:0000269|PubMed:26903241}.
MUTAGEN 197 197 H->A,E: Strongly reduces deubiquitinating
activity. {ECO:0000269|PubMed:27732584}.
MUTAGEN 197 197 H->D,N: Reduces deubiquitinating
activity. {ECO:0000269|PubMed:27732584}.
MUTAGEN 210 210 D->A: Reduces deubiquitinating activity.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 295 295 E->K: Loss of deubiquitinating activity.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 358 358 H->A: Loss of deubiquitinating activity.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 358 358 H->N: Loss of deubiquitinating activity;
when associated with S-194.
{ECO:0000269|PubMed:26903241}.
MUTAGEN 809 809 F->A: Does not affect interaction with
EGFR. {ECO:0000269|PubMed:22179831}.
MUTAGEN 810 810 Y->A: Impairs interaction with EGFR.
{ECO:0000269|PubMed:22179831}.
CONFLICT 243 243 K -> E (in Ref. 5; AAH20622).
{ECO:0000305}.
CONFLICT 421 421 K -> R (in Ref. 5; AAH20622).
{ECO:0000305}.
CONFLICT 791 791 G -> S (in Ref. 2; BAH13129).
{ECO:0000305}.
STRAND 129 135 {ECO:0000244|PDB:5LRW}.
STRAND 141 143 {ECO:0000244|PDB:5LRW}.
HELIX 144 152 {ECO:0000244|PDB:5LRW}.
HELIX 158 166 {ECO:0000244|PDB:5LRW}.
STRAND 169 171 {ECO:0000244|PDB:5LRU}.
HELIX 173 176 {ECO:0000244|PDB:5LRW}.
STRAND 177 179 {ECO:0000244|PDB:5LRV}.
STRAND 183 186 {ECO:0000244|PDB:5LRW}.
STRAND 190 192 {ECO:0000244|PDB:5LRW}.
HELIX 194 199 {ECO:0000244|PDB:5LRW}.
HELIX 200 203 {ECO:0000244|PDB:5LRW}.
TURN 206 208 {ECO:0000244|PDB:5LRV}.
HELIX 209 222 {ECO:0000244|PDB:5LRW}.
HELIX 227 243 {ECO:0000244|PDB:5LRW}.
TURN 244 246 {ECO:0000244|PDB:5LRW}.
HELIX 251 266 {ECO:0000244|PDB:5LRW}.
HELIX 294 304 {ECO:0000244|PDB:5LRW}.
STRAND 308 311 {ECO:0000244|PDB:5LRW}.
STRAND 314 317 {ECO:0000244|PDB:5LRW}.
STRAND 323 326 {ECO:0000244|PDB:5LRW}.
STRAND 331 333 {ECO:0000244|PDB:5LRW}.
HELIX 340 342 {ECO:0000244|PDB:5LRW}.
STRAND 348 353 {ECO:0000244|PDB:5LRW}.
STRAND 356 362 {ECO:0000244|PDB:5LRW}.
HELIX 363 366 {ECO:0000244|PDB:5LRW}.
STRAND 373 378 {ECO:0000244|PDB:5LRW}.
HELIX 393 395 {ECO:0000244|PDB:5LRW}.
HELIX 401 406 {ECO:0000244|PDB:5LRV}.
HELIX 410 426 {ECO:0000244|PDB:5LRW}.
STRAND 430 433 {ECO:0000244|PDB:5LRW}.
SEQUENCE 843 AA; 92526 MW; 6D386C864B12EE57 CRC64;
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG NLPPSFSEGS
GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS HASSSIVSLA RSHVSSNGGG
GGSNEHPLEM PICAFQLPDL TVYNEDFRSF IERDLIEQSM LVALEQAGRL NWWVSVDPTS
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGTNGANC GGVESSEEPV YESLEEFHVF
VLAHVLRRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS
ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE WGKDDSDNVR LASVILSLEV
KLHLLHSYMN VKWIPLSSDA QAPLAQPESP TASAGDEPRS TPESGDSDKE SVGSSSTSNE
GGRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG
GSSGTETLEK KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR
TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER KIMNGGIGGG
PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR PSGGGVHCQE PRRQLAGGPC
VGGLPPYATF PRQCPPGRPY PHQDSIPSLE PGSHSKDGLH RGALLPPPYR VADSYSNGYR
EPPEPDGWAG GLRGLPPTQT KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV
HRF


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