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Tumor necrosis factor alpha-induced protein 3 (TNF alpha-induced protein 3) (EC 3.4.19.12) (EC 6.3.2.-) (OTU domain-containing protein 7C) (Putative DNA-binding protein A20) (Zinc finger protein A20) [Cleaved into: A20p50; A20p37]

 TNAP3_HUMAN             Reviewed;         790 AA.
P21580; B2R767; E1P588; Q2HIX9; Q5VXQ7; Q9NSR6;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=Tumor necrosis factor alpha-induced protein 3;
Short=TNF alpha-induced protein 3;
EC=3.4.19.12 {ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:17961127, ECO:0000269|PubMed:18164316, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:27732584};
EC=6.3.2.-;
AltName: Full=OTU domain-containing protein 7C;
AltName: Full=Putative DNA-binding protein A20;
AltName: Full=Zinc finger protein A20;
Contains:
RecName: Full=A20p50;
Contains:
RecName: Full=A20p37;
Name=TNFAIP3; Synonyms=OTUD7C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2118515;
Opipari A.W. Jr., Boguski M.S., Dixit V.M.;
"The A20 cDNA induced by tumor necrosis factor alpha encodes a novel
type of zinc finger protein.";
J. Biol. Chem. 265:14705-14708(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
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 [GENOMIC DNA], AND VARIANTS VAL-125; CYS-127 AND
PRO-766.
SeattleSNPs variation discovery resource;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-790.
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).
[8]
FUNCTION, AND INTERACTION WITH TRAF1 AND TRAF2.
PubMed=8692885; DOI=10.1073/pnas.93.13.6721;
Song H.Y., Rothe M., Goeddel D.V.;
"The tumor necrosis factor-inducible zinc finger protein A20 interacts
with TRAF1/TRAF2 and inhibits NF-kappaB activation.";
Proc. Natl. Acad. Sci. U.S.A. 93:6721-6725(1996).
[9]
FUNCTION, INTERACTION WITH YWHAZ AND YWHAH, AND MUTAGENESIS OF ARG-562
AND SER-565.
PubMed=9299557; DOI=10.1006/bbrc.1997.7343;
De Valck D., Heyninck K., Van Criekinge W., Vandenabeele P., Fiers W.,
Beyaert R.;
"A20 inhibits NF-kappaB activation independently of binding to 14-3-3
proteins.";
Biochem. Biophys. Res. Commun. 238:590-594(1997).
[10]
FUNCTION, AND INTERACTION WITH TRAF2.
PubMed=9882303;
Eliopoulos A.G., Blake S.M., Floettmann J.E., Rowe M., Young L.S.;
"Epstein-Barr virus-encoded latent membrane protein 1 activates the
JNK pathway through its extreme C-terminus via a mechanism involving
TRADD and TRAF2.";
J. Virol. 73:1023-1035(1999).
[11]
INTERACTION WITH TAX1BP1.
PubMed=10435631; DOI=10.1038/sj.onc.1202787;
de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R.,
Fiers W., Jeang K.-T., Beyaert R.;
"The zinc finger protein A20 interacts with a novel anti-apoptotic
protein which is cleaved by specific caspases.";
Oncogene 18:4182-4190(1999).
[12]
SUBCELLULAR LOCATION.
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).
[13]
FUNCTION, MUTAGENESIS OF CYS-103, 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).
[14]
FUNCTION, DOMAIN OTU, DOMAIN A20-TYPE ZINC-FINGER, AND MUTAGENESIS OF
CYS-103; CYS-521; CYS-524; CYS-624 AND CYS-627.
PubMed=15258597; DOI=10.1038/nature02794;
Wertz I.E., O'Rourke K.M., Zhou H., Eby M., Aravind L., Seshagiri S.,
Wu P., Wiesmann C., Baker R., Boone D.L., Ma A., Koonin E.V.,
Dixit V.M.;
"De-ubiquitination and ubiquitin ligase domains of A20 downregulate
NF-kappaB signalling.";
Nature 430:694-699(2004).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
FUNCTION, AND INTERACTION WITH IKBKG AND TNIP1.
PubMed=16684768; DOI=10.1074/jbc.M601502200;
Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A.,
Acquaviva R., Formisano S., Vito P., Leonardi A.;
"ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting
NF-kappaB.";
J. Biol. Chem. 281:18482-18488(2006).
[17]
PROTEOLYTIC CLEAVAGE.
PubMed=18223652; DOI=10.1038/ni1561;
Coornaert B., Baens M., Heyninck K., Bekaert T., Haegman M., Staal J.,
Sun L., Chen Z.J., Marynen P., Beyaert R.;
"T cell antigen receptor stimulation induces MALT1 paracaspase-
mediated cleavage of the NF-kappaB inhibitor A20.";
Nat. Immunol. 9:263-271(2008).
[18]
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).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18952128; DOI=10.1016/j.bbamcr.2008.09.013;
Li L., Soetandyo N., Wang Q., Ye Y.;
"The zinc finger protein A20 targets TRAF2 to the lysosomes for
degradation.";
Biochim. Biophys. Acta 1793:346-353(2009).
[20]
INTERACTION WITH TAX1BP1; RNF11 AND RIPK1.
PubMed=19131965; DOI=10.1038/emboj.2008.285;
Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
"The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-
kappaB signalling.";
EMBO J. 28:513-522(2009).
[21]
FUNCTION.
PubMed=19494296; DOI=10.4049/jimmunol.0803313;
Duwel M., Welteke V., Oeckinghaus A., Baens M., Kloo B., Ferch U.,
Darnay B.G., Ruland J., Marynen P., Krappmann D.;
"A20 negatively regulates T cell receptor signaling to NF-kappaB by
cleaving Malt1 ubiquitin chains.";
J. Immunol. 182:7718-7728(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
PubMed=20804738; DOI=10.1016/j.bbrc.2010.08.091;
Malinverni C., Unterreiner A., Staal J., Demeyer A., Galaup M.,
Luyten M., Beyaert R., Bornancin F.;
"Cleavage by MALT1 induces cytosolic release of A20.";
Biochem. Biophys. Res. Commun. 400:543-547(2010).
[24]
FUNCTION, INTERACTION WITH IKBKG, AND MUTAGENESIS OF 770-PHE-GLY-771;
CYS-779 AND CYS-782.
PubMed=22099304; DOI=10.1016/j.molcel.2011.09.015;
Skaug B., Chen J., Du F., He J., Ma A., Chen Z.J.;
"Direct, noncatalytic mechanism of IKK inhibition by A20.";
Mol. Cell 44:559-571(2011).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND 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).
[29]
INVOLVEMENT IN AISBL.
PubMed=26642243; DOI=10.1038/ng.3459;
Zhou Q., Wang H., Schwartz D.M., Stoffels M., Park Y.H., Zhang Y.,
Yang D., Demirkaya E., Takeuchi M., Tsai W.L., Lyons J.J., Yu X.,
Ouyang C., Chen C., Chin D.T., Zaal K., Chandrasekharappa S.C.,
P Hanson E., Yu Z., Mullikin J.C., Hasni S.A., Wertz I.E.,
Ombrello A.K., Stone D.L., Hoffmann P., Jones A., Barham B.K.,
Leavis H.L., van Royen-Kerkof A., Sibley C., Batu E.D., Guel A.,
Siegel R.M., Boehm M., Milner J.D., Ozen S., Gadina M., Chae J.,
Laxer R.M., Kastner D.L., Aksentijevich I.;
"Loss-of-function mutations in TNFAIP3 leading to A20
haploinsufficiency cause an early-onset autoinflammatory disease.";
Nat. Genet. 48:67-73(2016).
[30]
STRUCTURE BY NMR OF 381-790.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the A20-type zinc finger domains from human
tumor necrosis factor, alpha-induced protein 3.";
Submitted (OCT-2007) to the PDB data bank.
[31]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-366, CATALYTIC ACTIVITY,
FUNCTION, AND MUTAGENESIS OF ASP-70; CYS-103 AND HIS-256.
PubMed=17961127; DOI=10.1042/BJ20071399;
Komander D., Barford D.;
"Structure of the A20 OTU domain and mechanistic insights into
deubiquitination.";
Biochem. J. 409:77-85(2008).
[32]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-370, ACTIVE SITE, CATALYTIC
ACTIVITY, FUNCTION, AND MUTAGENESIS OF ASP-70; THR-97; ASP-100;
CYS-103; LEU-157; TYR-159; SER-190; GLU-192; PHE-224 AND LEU-227.
PubMed=18164316; DOI=10.1016/j.jmb.2007.11.092;
Lin S.C., Chung J.Y., Lamothe B., Rajashankar K., Lu M., Lo Y.C.,
Lam A.Y., Darnay B.G., Wu H.;
"Molecular basis for the unique deubiquitinating activity of the NF-
kappaB inhibitor A20.";
J. Mol. Biol. 376:526-540(2008).
[33]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 592-635 IN COMPLEX WITH
UBIQUITIN, X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 592-635 IN COMPLEX
WITH UBIQUITIN AND UBE2D1, AND MUTAGENESIS OF TYR-614; PHE-615 AND
LEU-626.
PubMed=21095585; DOI=10.1016/j.molcel.2010.10.009;
Bosanac I., Wertz I.E., Pan B., Yu C., Kusam S., Lam C., Phu L.,
Phung Q., Maurer B., Arnott D., Kirkpatrick D.S., Dixit V.M.,
Hymowitz S.G.;
"Ubiquitin binding to A20 ZnF4 is required for modulation of NF-kappaB
signaling.";
Mol. Cell 40:548-557(2010).
[34] {ECO:0000244|PDB:5LRX}
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-366, CATALYTIC ACTIVITY,
AND MUTAGENESIS OF HIS-106 AND HIS-256.
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).
[35]
VARIANT AISBL TYR-243, AND CHARACTERIZATION OF VARIANT AISBL TYR-243.
PubMed=27175295; DOI=10.1136/rmdopen-2015-000223;
Shigemura T., Kaneko N., Kobayashi N., Kobayashi K., Takeuchi Y.,
Nakano N., Masumoto J., Agematsu K.;
"Novel heterozygous C243Y A20/TNFAIP3 gene mutation is responsible for
chronic inflammation in autosomal-dominant Behcet's disease.";
RMD Open 2:E000223-E000223(2016).
-!- FUNCTION: Ubiquitin-editing enzyme that contains both ubiquitin
ligase and deubiquitinase activities. Involved in immune and
inflammatory responses signaled by cytokines, such as TNF-alpha
and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through
terminating NF-kappa-B activity. Essential component of a
ubiquitin-editing protein complex, comprising also RNF11, ITCH and
TAX1BP1, that ensures the transient nature of inflammatory
signaling pathways. In cooperation with TAX1BP1 promotes
disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R
and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2
and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3.
In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and
proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation,
deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and
catalyzes the formation of 'Lys-48'-polyubiquitin chains. This
leads to RIPK1 proteasomal degradation and consequently
termination of the TNF- or LPS-mediated activation of NF-kappa-B.
Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked
polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell
activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1
thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1)
and IKK complexes and preventing sustained IKK activation.
Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1
and leads to inhibition of NF-kappa-B activation. Upon stimulation
by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can
also inhibit I-kappa-B-kinase (IKK) through a non-catalytic
mechanism which involves polyubiquitin; polyubiquitin promotes
association with IKBKG and prevents IKK MAP3K7-mediated
phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro
able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63'
polyubiquitin chains. Inhibitor of programmed cell death. Has a
role in the function of the lymphoid system. Required for LPS-
induced production of proinflammatory cytokines and IFN beta in
LPS-tolerized macrophages. {ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:15258597, ECO:0000269|PubMed:16684768,
ECO:0000269|PubMed:17961127, ECO:0000269|PubMed:18164316,
ECO:0000269|PubMed:18952128, ECO:0000269|PubMed:19494296,
ECO:0000269|PubMed:22099304, ECO:0000269|PubMed:23827681,
ECO:0000269|PubMed:8692885, ECO:0000269|PubMed:9299557,
ECO:0000269|PubMed:9882303}.
-!- 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:14748687, ECO:0000269|PubMed:17961127,
ECO:0000269|PubMed:18164316, ECO:0000269|PubMed:23827681,
ECO:0000269|PubMed:27732584}.
-!- SUBUNIT: Homodimer. Interacts with TNIP1, TAX1BP1 and TRAF2.
Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation;
these interaction are transient and they are lost after 1 hour of
stimulation with TNF (By similarity). Interacts with YWHAZ and
YWHAH. Interacts with IKBKG; the interaction is induced by TNF
stimulation and by polyubiquitin. Interacts with RIPK1. Interacts
with UBE2N; the interaction requires TAX1BP1. Interacts with
TRAF6; the interaction is inhibited by HTLV-1 protein Tax.
{ECO:0000250, ECO:0000269|PubMed:10435631,
ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:19131965,
ECO:0000269|PubMed:21095585, ECO:0000269|PubMed:22099304,
ECO:0000269|PubMed:8692885, ECO:0000269|PubMed:9299557,
ECO:0000269|PubMed:9882303}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-527670, EBI-527670;
Q96B67:ARRDC3; NbExp=5; IntAct=EBI-527670, EBI-2875665;
Q14790:CASP8; NbExp=3; IntAct=EBI-527670, EBI-78060;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-527670, EBI-81279;
Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-527670, EBI-396669;
Q15025:TNIP1; NbExp=6; IntAct=EBI-527670, EBI-357849;
Q96KP6:TNIP3; NbExp=3; IntAct=EBI-527670, EBI-2509913;
Q12933:TRAF2; NbExp=5; IntAct=EBI-527670, EBI-355744;
P36406:TRIM23; NbExp=5; IntAct=EBI-527670, EBI-740098;
P68510:Ywhah (xeno); NbExp=3; IntAct=EBI-527670, EBI-444641;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Lysosome.
-!- SUBCELLULAR LOCATION: A20p50: Cytoplasm.
-!- INDUCTION: By TNF.
-!- DOMAIN: The A20-type zinc fingers mediate the ubiquitin ligase
activity. The A20-type zinc finger 4 selectively recognizes 'Lys-
63'-linked polyubiquitin. The A20-type zinc finger 4-7 are
sufficient to bind polyubiquitin. {ECO:0000269|PubMed:15258597}.
-!- DOMAIN: The OTU domain mediates the deubiquitinase activity.
{ECO:0000269|PubMed:15258597}.
-!- PTM: Proteolytically cleaved by MALT1 upon TCR stimulation;
disrupts NF-kappa-B inhibitory function and results in increased
IL-2 production. It is proposed that only a fraction of TNFAIP3
colocalized with TCR and CBM complex is cleaved, leaving the main
TNFAIP3 pool intact. {ECO:0000269|PubMed:18223652,
ECO:0000269|PubMed:20804738}.
-!- DISEASE: Autoinflammatory syndrome, familial, Behcet-like (AISBL)
[MIM:616744]: An autosomal dominant, autoinflammatory disorder
with early onset, characterized by ulceration of mucosal surfaces,
particularly in the oral and genital areas. Additional variable
features include skin rash, uveitis, and polyarthritis.
{ECO:0000269|PubMed:26642243, ECO:0000269|PubMed:27175295}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tnfaip3/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TNFAIP3ID42600ch6q23.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M59465; AAA51550.1; -; mRNA.
EMBL; AK312862; BAG35714.1; -; mRNA.
EMBL; AY248754; AAO61093.1; -; Genomic_DNA.
EMBL; AL357060; CAH72937.1; -; Genomic_DNA.
EMBL; CH471051; EAW47925.1; -; Genomic_DNA.
EMBL; CH471051; EAW47926.1; -; Genomic_DNA.
EMBL; BC113871; AAI13872.1; -; mRNA.
EMBL; BC114480; AAI14481.1; -; mRNA.
EMBL; AL157444; CAB75664.1; -; mRNA.
CCDS; CCDS5187.1; -.
PIR; A35797; A35797.
RefSeq; NP_001257436.1; NM_001270507.1.
RefSeq; NP_001257437.1; NM_001270508.1.
RefSeq; NP_006281.1; NM_006290.3.
RefSeq; XP_005267176.1; XM_005267119.1.
RefSeq; XP_011534397.1; XM_011536095.1.
UniGene; Hs.211600; -.
PDB; 2EQE; NMR; -; A=597-631.
PDB; 2EQF; NMR; -; A=758-790.
PDB; 2EQG; NMR; -; A=381-416.
PDB; 2VFJ; X-ray; 3.20 A; A/B/C/D=1-366.
PDB; 3DKB; X-ray; 2.50 A; A/B/C/D/E/F=1-370.
PDB; 3OJ3; X-ray; 2.50 A; I/J/K/L/M/N/O/P=592-635.
PDB; 3OJ4; X-ray; 3.40 A; C/F=592-635.
PDB; 3VUW; X-ray; 1.95 A; E/F/G=757-789.
PDB; 3VUX; X-ray; 1.70 A; E/F/G=757-790.
PDB; 3VUY; X-ray; 1.98 A; D/E/F=757-790.
PDB; 3ZJD; X-ray; 1.87 A; A/B=1-366.
PDB; 3ZJE; X-ray; 1.84 A; A/B=1-366.
PDB; 3ZJF; X-ray; 2.20 A; A/B=1-366.
PDB; 3ZJG; X-ray; 1.92 A; A/B=1-366.
PDB; 4ZRH; X-ray; 2.70 A; A/B/C/D/E/F=1-366.
PDB; 4ZS5; X-ray; 3.20 A; A/B/C/D/E/F=1-366.
PDB; 5DOD; X-ray; 2.50 A; A/B/C/D/E/F=1-366.
PDB; 5LRX; X-ray; 2.85 A; A/C/E/F=1-366.
PDBsum; 2EQE; -.
PDBsum; 2EQF; -.
PDBsum; 2EQG; -.
PDBsum; 2VFJ; -.
PDBsum; 3DKB; -.
PDBsum; 3OJ3; -.
PDBsum; 3OJ4; -.
PDBsum; 3VUW; -.
PDBsum; 3VUX; -.
PDBsum; 3VUY; -.
PDBsum; 3ZJD; -.
PDBsum; 3ZJE; -.
PDBsum; 3ZJF; -.
PDBsum; 3ZJG; -.
PDBsum; 4ZRH; -.
PDBsum; 4ZS5; -.
PDBsum; 5DOD; -.
PDBsum; 5LRX; -.
ProteinModelPortal; P21580; -.
SMR; P21580; -.
BioGrid; 112983; 92.
DIP; DIP-33804N; -.
IntAct; P21580; 33.
MINT; MINT-97330; -.
STRING; 9606.ENSP00000237289; -.
MEROPS; C64.003; -.
iPTMnet; P21580; -.
PhosphoSitePlus; P21580; -.
BioMuta; TNFAIP3; -.
DMDM; 112894; -.
EPD; P21580; -.
MaxQB; P21580; -.
PaxDb; P21580; -.
PeptideAtlas; P21580; -.
PRIDE; P21580; -.
Ensembl; ENST00000237289; ENSP00000237289; ENSG00000118503.
Ensembl; ENST00000612899; ENSP00000481570; ENSG00000118503.
GeneID; 7128; -.
KEGG; hsa:7128; -.
UCSC; uc003qhr.5; human.
CTD; 7128; -.
DisGeNET; 7128; -.
EuPathDB; HostDB:ENSG00000118503.14; -.
GeneCards; TNFAIP3; -.
HGNC; HGNC:11896; TNFAIP3.
HPA; HPA002116; -.
MalaCards; TNFAIP3; -.
MIM; 191163; gene.
MIM; 616744; phenotype.
neXtProt; NX_P21580; -.
OpenTargets; ENSG00000118503; -.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA36593; -.
eggNOG; ENOG410IQZK; Eukaryota.
eggNOG; ENOG41117NJ; LUCA.
GeneTree; ENSGT00530000062989; -.
HOGENOM; HOG000133004; -.
HOVERGEN; HBG059260; -.
InParanoid; P21580; -.
KO; K11859; -.
OMA; IYLPLHW; -.
OrthoDB; EOG091G01QE; -.
PhylomeDB; P21580; -.
TreeFam; TF323312; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
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.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
SignaLink; P21580; -.
SIGNOR; P21580; -.
ChiTaRS; TNFAIP3; human.
EvolutionaryTrace; P21580; -.
GeneWiki; TNFAIP3; -.
GenomeRNAi; 7128; -.
PRO; PR:P21580; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118503; -.
CleanEx; HS_TNFAIP3; -.
ExpressionAtlas; P21580; baseline and differential.
Genevisible; P21580; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; EXP:Reactome.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0043621; F:protein self-association; IDA:BHF-UCL.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IMP:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IPI:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001922; P:B-1 B cell homeostasis; ISS:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0050869; P:negative regulation of B cell activation; ISS:BHF-UCL.
GO; GO:0045779; P:negative regulation of bone resorption; NAS:BHF-UCL.
GO; GO:2000349; P:negative regulation of CD40 signaling pathway; IMP:BHF-UCL.
GO; GO:0002677; P:negative regulation of chronic inflammatory response; IEA:Ensembl.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:BHF-UCL.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:BHF-UCL.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0070429; P:negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
GO; GO:0090291; P:negative regulation of osteoclast proliferation; NAS:BHF-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; NAS:BHF-UCL.
GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IDA:BHF-UCL.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; NAS:BHF-UCL.
GO; GO:0034148; P:negative regulation of toll-like receptor 5 signaling pathway; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IEA:Ensembl.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:BHF-UCL.
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:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; NAS:BHF-UCL.
GO; GO:0050691; P:regulation of defense response to virus by host; NAS:BHF-UCL.
GO; GO:0002634; P:regulation of germinal center formation; ISS:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0061043; P:regulation of vascular wound healing; NAS:BHF-UCL.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:BHF-UCL.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0072573; P:tolerance induction to lipopolysaccharide; IMP:BHF-UCL.
InterPro; IPR033478; A20.
InterPro; IPR003323; OTU_dom.
InterPro; IPR002653; Znf_A20.
PANTHER; PTHR13367:SF3; PTHR13367:SF3; 1.
Pfam; PF02338; OTU; 1.
Pfam; PF01754; zf-A20; 4.
SMART; SM00259; ZnF_A20; 7.
PROSITE; PS50802; OTU; 1.
PROSITE; PS51036; ZF_A20; 7.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Hydrolase; Inflammatory response;
Ligase; Lysosome; Metal-binding; Multifunctional enzyme; Nucleus;
Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat;
Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 790 Tumor necrosis factor alpha-induced
protein 3.
/FTId=PRO_0000188791.
CHAIN 2 439 A20p50.
/FTId=PRO_0000418127.
CHAIN 440 790 A20p37.
/FTId=PRO_0000418128.
DOMAIN 92 263 OTU. {ECO:0000255|PROSITE-
ProRule:PRU00139}.
REPEAT 286 317 1.
REPEAT 324 356 2.
ZN_FING 381 416 A20-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 472 507 A20-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 515 548 A20-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 601 636 A20-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 651 686 A20-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 710 745 A20-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
ZN_FING 756 790 A20-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
REGION 58 300 TRAF-binding.
REGION 157 159 Interaction with ubiquitin.
{ECO:0000305}.
REGION 190 192 Interaction with ubiquitin.
{ECO:0000305}.
REGION 224 227 Interaction with ubiquitin.
{ECO:0000305}.
REGION 286 356 2 X approximate repeats.
REGION 369 775 Interaction with TNIP1. {ECO:0000250}.
REGION 386 453 Interaction with RIPK1.
{ECO:0000269|PubMed:19131965}.
REGION 605 655 Required for proteosomal degradation of
UBE2N and UBE2D3, TRAF6 deubiquitination,
and TAX1BP1 interaction with UBE2N.
{ECO:0000250}.
REGION 606 790 Sufficient for inhibitory activity of
TNF-induced NF-kappa-B activity.
{ECO:0000250}.
REGION 697 790 Required for lysosomal localization and
for TRAF2 lysosomal degradation.
ACT_SITE 100 100 {ECO:0000250}.
ACT_SITE 103 103 Nucleophile.
{ECO:0000269|PubMed:18164316}.
ACT_SITE 256 256 Proton acceptor.
{ECO:0000305|PubMed:18164316}.
SITE 439 440 Cleavage; by MALT1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 125 125 A -> V (in dbSNP:rs5029941).
{ECO:0000269|Ref.3}.
/FTId=VAR_020447.
VARIANT 127 127 F -> C (in dbSNP:rs2230926).
{ECO:0000269|Ref.3}.
/FTId=VAR_022143.
VARIANT 243 243 C -> Y (in AISBL; increases inflammatory
cytokine secretion; increases NF-kappaB
signaling).
{ECO:0000269|PubMed:27175295}.
/FTId=VAR_076302.
VARIANT 766 766 A -> P (in dbSNP:rs5029957).
{ECO:0000269|Ref.3}.
/FTId=VAR_029319.
MUTAGEN 70 70 D->A: Minor effect on 'Lys-48'
deubiquitinase activity. Strongly reduced
'Lys-63' deubiquitinase activity.
{ECO:0000269|PubMed:17961127,
ECO:0000269|PubMed:18164316}.
MUTAGEN 97 97 T->A: Minor effect on 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 100 100 D->A: Strongly reduced deubiquitinase
activity. {ECO:0000269|PubMed:18164316}.
MUTAGEN 103 103 C->A: Loss of deubiquitinase activity.
{ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:15258597,
ECO:0000269|PubMed:17961127,
ECO:0000269|PubMed:18164316}.
MUTAGEN 103 103 C->S: Loss of 'Lys-63' deubiquitinating
activity. Down-regulation of TNF-induced
NF-kappa-B activity less effective.
{ECO:0000269|PubMed:14748687,
ECO:0000269|PubMed:15258597,
ECO:0000269|PubMed:17961127,
ECO:0000269|PubMed:18164316}.
MUTAGEN 106 106 H->A: Reduces deubiquitinase activity.
{ECO:0000269|PubMed:27732584}.
MUTAGEN 157 157 L->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 159 159 Y->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 190 190 S->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 192 192 E->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 224 224 F->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 227 227 L->A: Strongly reduced 'Lys-48'
deubiquitinase activity.
{ECO:0000269|PubMed:18164316}.
MUTAGEN 256 256 H->A: Loss of deubiquitinase activity.
{ECO:0000269|PubMed:17961127,
ECO:0000269|PubMed:27732584}.
MUTAGEN 521 521 C->A: No effect on ubiquitin ligase
activity; when associated with A-524.
{ECO:0000269|PubMed:15258597}.
MUTAGEN 524 524 C->A: No effect on ubiquitin ligase
activity; when associated with A-521.
{ECO:0000269|PubMed:15258597}.
MUTAGEN 562 562 R->A: Abolishes interactionj with YWHAZ
AND YWHAH; no effect on inhibitory
activity of TNF-induced NF-kappa-B
activation. {ECO:0000269|PubMed:9299557}.
MUTAGEN 565 565 S->A: Abolishes interactionj with YWHAZ
AND YWHAH; no effect on inhibitory
activity of TNF-induced NF-kappa-B
activation. {ECO:0000269|PubMed:9299557}.
MUTAGEN 614 614 Y->A: Impairs ubiquitination activity.
Loss of down-regulation of NF-kappa-B
activity; when associated with A-615 or
R-626. {ECO:0000269|PubMed:21095585}.
MUTAGEN 615 615 F->A: Impairs ubiquitination activity.
Loss of down-regulation of NF-kappa-B
activity; when associated with A-614.
{ECO:0000269|PubMed:21095585}.
MUTAGEN 624 624 C->A: Marked attenuation of ubiquitin
ligase activity and inhibition of RIPK1
degradation; when associated with A-627.
{ECO:0000269|PubMed:15258597}.
MUTAGEN 626 626 L->R: Impairs ubiquitination activity.
Loss of down-regulation of NF-kappa-B
activity; when associated with A-614.
{ECO:0000269|PubMed:21095585}.
MUTAGEN 627 627 C->A: Marked attenuation of ubiquitin
ligase activity and inhibition of RIPK1
degradation; when associated with A-624.
{ECO:0000269|PubMed:15258597}.
MUTAGEN 770 771 FG->AA: Impairs polyubiquitin binding,
abolishes inhibition of IKK activation.
{ECO:0000269|PubMed:22099304}.
MUTAGEN 779 779 C->A: Impairs polyubiquitin binding,
abolishes inhibition of IKK activation;
when associated with A-782.
{ECO:0000269|PubMed:22099304}.
MUTAGEN 782 782 C->A: Impairs polyubiquitin binding,
abolishes inhibition of IKK activation;
when associated with A-779.
{ECO:0000269|PubMed:22099304}.
HELIX 10 13 {ECO:0000244|PDB:3ZJE}.
HELIX 15 27 {ECO:0000244|PDB:3ZJE}.
STRAND 33 35 {ECO:0000244|PDB:3ZJE}.
STRAND 39 42 {ECO:0000244|PDB:3ZJE}.
HELIX 43 45 {ECO:0000244|PDB:3ZJE}.
STRAND 54 56 {ECO:0000244|PDB:3ZJG}.
HELIX 58 68 {ECO:0000244|PDB:3ZJE}.
HELIX 71 79 {ECO:0000244|PDB:3ZJE}.
STRAND 82 84 {ECO:0000244|PDB:3ZJG}.
STRAND 87 89 {ECO:0000244|PDB:3DKB}.
STRAND 92 95 {ECO:0000244|PDB:3ZJE}.
HELIX 103 113 {ECO:0000244|PDB:3ZJE}.
HELIX 121 132 {ECO:0000244|PDB:3ZJE}.
HELIX 136 147 {ECO:0000244|PDB:3ZJE}.
HELIX 152 155 {ECO:0000244|PDB:5LRX}.
HELIX 164 174 {ECO:0000244|PDB:3ZJE}.
STRAND 176 178 {ECO:0000244|PDB:5LRX}.
STRAND 181 185 {ECO:0000244|PDB:3DKB}.
HELIX 193 203 {ECO:0000244|PDB:3ZJE}.
STRAND 207 211 {ECO:0000244|PDB:3ZJE}.
STRAND 213 216 {ECO:0000244|PDB:5LRX}.
TURN 218 220 {ECO:0000244|PDB:5LRX}.
STRAND 221 226 {ECO:0000244|PDB:5LRX}.
STRAND 231 233 {ECO:0000244|PDB:3ZJE}.
HELIX 240 242 {ECO:0000244|PDB:3ZJE}.
STRAND 248 253 {ECO:0000244|PDB:3ZJE}.
STRAND 256 263 {ECO:0000244|PDB:3ZJE}.
STRAND 267 270 {ECO:0000244|PDB:3ZJG}.
STRAND 272 279 {ECO:0000244|PDB:3ZJE}.
STRAND 282 285 {ECO:0000244|PDB:3ZJE}.
HELIX 293 297 {ECO:0000244|PDB:3ZJE}.
HELIX 299 306 {ECO:0000244|PDB:3ZJE}.
STRAND 309 315 {ECO:0000244|PDB:3ZJE}.
STRAND 317 329 {ECO:0000244|PDB:3ZJE}.
HELIX 337 339 {ECO:0000244|PDB:3ZJE}.
HELIX 341 354 {ECO:0000244|PDB:3ZJE}.
HELIX 359 361 {ECO:0000244|PDB:3DKB}.
STRAND 384 386 {ECO:0000244|PDB:2EQG}.
TURN 398 402 {ECO:0000244|PDB:2EQG}.
HELIX 405 412 {ECO:0000244|PDB:2EQG}.
STRAND 604 606 {ECO:0000244|PDB:2EQE}.
STRAND 613 615 {ECO:0000244|PDB:3OJ3}.
HELIX 618 620 {ECO:0000244|PDB:3OJ3}.
HELIX 625 634 {ECO:0000244|PDB:3OJ3}.
HELIX 773 775 {ECO:0000244|PDB:3VUX}.
HELIX 780 788 {ECO:0000244|PDB:3VUX}.
SEQUENCE 790 AA; 89614 MW; 320AEA97F58D4491 CRC64;
MAEQVLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIHHF KTMHRYTLEM FRTCQFCPQF
REIIHKALID RNIQATLESQ KKLNWCREVR KLVALKTNGD GNCLMHATSQ YMWGVQDTDL
VLRKALFSTL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LIKMASTDTP
MARSGLQYNS LEEIHIFVLC NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA
QECYRYPIVL GYDSHHFVPL VTLKDSGPEI RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
KLLKEYLMVI EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENS
EQGRREGHAQ NPMEPSVPQL SLMDVKCETP NCPFFMSVNT QPLCHECSER RQKNQNKLPK
LNSKPGPEGL PGMALGASRG EAYEPLAWNP EESTGGPHSA PPTAPSPFLF SETTAMKCRS
PGCPFTLNVQ HNGFCERCHN ARQLHASHAP DHTRHLDPGK CQACLQDVTR TFNGICSTCF
KRTTAEASSS LSTSLPPSCH QRSKSDPSRL VRSPSPHSCH RAGNDAPAGC LSQAARTPGD
RTGTSKCRKA GCVYFGTPEN KGFCTLCFIE YRENKHFAAA SGKVSPTASR FQNTIPCLGR
ECGTLGSTMF EGYCQKCFIE AQNQRFHEAK RTEEQLRSSQ RRDVPRTTQS TSRPKCARAS
CKNILACRSE ELCMECQHPN QRMGPGAHRG EPAPEDPPKQ RCRAPACDHF GNAKCNGYCN
ECFQFKQMYG


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