ID TAXB1_HUMAN Reviewed; 789 AA.
AC Q86VP1; A4D196; B4DKU7; E7ENV2; O60398; O95770; Q13311; Q9BQG5; Q9UI88;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Tax1-binding protein 1;
DE AltName: Full=TRAF6-binding protein;
GN Name=TAX1BP1; Synonyms=T6BP; ORFNames=PRO0105;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TNFAIP3,
RP INTERACTION WITH HTLV-1 PROTEIN TAX (MICROBIAL INFECTION), AND ALTERNATIVE
RP SPLICING (ISOFORM 3).
RC TISSUE=Cervix carcinoma;
RX PubMed=10435631; DOI=10.1038/sj.onc.1202787;
RA de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R.,
RA Fiers W., Jeang K.-T., Beyaert R.;
RT "The zinc finger protein A20 interacts with a novel anti-apoptotic protein
RT which is cleaved by specific caspases.";
RL Oncogene 18:4182-4190(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TRAF6,
RP AND SUBUNIT.
RX PubMed=10920205; DOI=10.1073/pnas.170279097;
RA Ling L., Goeddel D.V.;
RT "T6BP, a TRAF6-interacting protein involved in IL-1 signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9567-9572(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 50 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Testis, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-307.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP INTERACTION WITH STARD13.
RX PubMed=14697242; DOI=10.1016/j.bbrc.2003.12.001;
RA Nagaraja G.M., Kandpal R.P.;
RT "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth
RT of breast carcinoma cells, and yeast two-hybrid screen shows its
RT interaction with several proteins.";
RL Biochem. Biophys. Res. Commun. 313:654-665(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HTLV-1 PROTEIN
RP TAX (MICROBIAL INFECTION).
RX PubMed=14530271; DOI=10.1074/jbc.m310069200;
RA Wu K., Bottazzi M.E., de la Fuente C., Deng L., Gitlin S.D., Maddukuri A.,
RA Dadgar S., Li H., Vertes A., Pumfery A., Kashanchi F.;
RT "Protein profile of tax-associated complexes.";
RL J. Biol. Chem. 279:495-508(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH RIPK1 AND TRAF6.
RX PubMed=17703191; DOI=10.1038/sj.emboj.7601823;
RA Shembade N., Harhaj N.S., Liebl D.J., Harhaj E.W.;
RT "Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and
RT LPS-mediated NF-kappaB and JNK signaling.";
RL EMBO J. 26:3910-3922(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP FUNCTION, AND INTERACTION WITH TNIP1.
RX PubMed=21885437; DOI=10.1074/jbc.m111.283762;
RA Gao L., Coope H., Grant S., Ma A., Ley S.C., Harhaj E.W.;
RT "ABIN1 protein cooperates with TAX1BP1 and A20 proteins to inhibit
RT antiviral signaling.";
RL J. Biol. Chem. 286:36592-36602(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP MUTAGENESIS OF GLN-771; GLU-774; ARG-775; VAL-777; GLN-778 AND PHE-781.
RX PubMed=27062441; DOI=10.1111/febs.13734;
RA Suzuki N., Rohaim A., Kato R., Dikic I., Wakatsuki S., Kawasaki M.;
RT "A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger
RT domain of WRNIP1.";
RL FEBS J. 283:2004-2017(2016).
RN [19]
RP FUNCTION, INTERACTION WITH MAVS, AND SUBCELLULAR LOCATION.
RX PubMed=27736772; DOI=10.1128/mcb.00422-16;
RA Choi Y.B., Shembade N., Parvatiyar K., Balachandran S., Harhaj E.W.;
RT "TAX1BP1 Restrains Virus-Induced Apoptosis by Facilitating Itch-Mediated
RT Degradation of the Mitochondrial Adaptor MAVS.";
RL Mol. Cell. Biol. 37:0-0(2017).
RN [20]
RP FUNCTION, AND INTERACTION WITH TICAM1 AND TRIM32.
RX PubMed=28898289; DOI=10.1371/journal.ppat.1006600;
RA Yang Q., Liu T.T., Lin H., Zhang M., Wei J., Luo W.W., Hu Y.H., Zhong B.,
RA Hu M.M., Shu H.B.;
RT "TRIM32-TAX1BP1-dependent selective autophagic degradation of TRIF
RT negatively regulates TLR3/4-mediated innate immune responses.";
RL PLoS Pathog. 13:e1006600-e1006600(2017).
RN [21]
RP FUNCTION, INTERACTION WITH LASSA VIRUS AND MOPEIA VIRUS PROTEIN Z
RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=30909570; DOI=10.3390/v11030293;
RA Baillet N., Krieger S., Journeaux A., Caro V., Tangy F., Vidalain P.O.,
RA Baize S.;
RT "Autophagy Promotes Infectious Particle Production of Mopeia and Lassa
RT Viruses.";
RL Viruses 11:0-0(2019).
RN [22]
RP FUNCTION, INTERACTION WITH NBR1; RB1CC1 AND TBK1, MUTAGENESIS OF ALA-114,
RP AND SUBCELLULAR LOCATION.
RX PubMed=33226137; DOI=10.15252/embj.2020104948;
RA Ohnstad A.E., Delgado J.M., North B.J., Nasa I., Kettenbach A.N.,
RA Schultz S.W., Shoemaker C.J.;
RT "Receptor-mediated clustering of FIP200 bypasses the role of LC3 lipidation
RT in autophagy.";
RL EMBO J. 39:e104948-e104948(2020).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NBR1; RB1CC1 AND
RP SQSTM1.
RX PubMed=34471133; DOI=10.1038/s41467-021-25572-w;
RA Turco E., Savova A., Gere F., Ferrari L., Romanov J., Schuschnig M.,
RA Martens S.;
RT "Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin
RT condensate formation and autophagy initiation.";
RL Nat. Commun. 12:5212-5212(2021).
RN [24]
RP INTERACTION WITH RESPIRATORY SYNCYTIAL VIRUS PROTEIN N (MICROBIAL
RP INFECTION).
RX PubMed=34431698; DOI=10.1128/jvi.00912-21;
RA Descamps D., Peres de Oliveira A., Gonnin L., Madrieres S., Fix J.,
RA Drajac C., Marquant Q., Bouguyon E., Pietralunga V., Iha H.,
RA Morais Ventura A., Tangy F., Vidalain P.O., Eleouet J.F., Galloux M.;
RT "Depletion of TAX1BP1 Amplifies Innate Immune Responses during Respiratory
RT Syncytial Virus Infection.";
RL J. Virol. 95:e0091221-e0091221(2021).
RN [25]
RP STRUCTURE BY NMR OF 725-789, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF
RP 725-789, AND UBZ-TYPE ZINC FINGERS.
RX PubMed=24239949; DOI=10.1016/j.jmb.2013.11.006;
RA Ceregido M.A., Spinola Amilibia M., Buts L., Rivera-Torres J.,
RA Garcia-Pino A., Bravo J., van Nuland N.A.;
RT "The structure of TAX1BP1 UBZ1+2 provides insight into target specificity
RT and adaptability.";
RL J. Mol. Biol. 426:674-690(2014).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-457.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [27]
RP PHOSPHORYLATION AT SER-593 AND SER-666 BY CHUK/IKKA.
RX PubMed=21765415; DOI=10.1038/ni.2066;
RA Shembade N., Pujari R., Harhaj N.S., Abbott D.W., Harhaj E.W.;
RT "The kinase IKKalpha inhibits activation of the transcription factor NF-
RT kappaB by phosphorylating the regulatory molecule TAX1BP1.";
RL Nat. Immunol. 12:834-843(2011).
RN [28]
RP INTERACTION WITH MYO6 AND TOM1.
RX PubMed=31371777; DOI=10.1038/s41467-019-11481-6;
RA Hu S., Guo Y., Wang Y., Li Y., Fu T., Zhou Z., Wang Y., Liu J., Pan L.;
RT "Structure of Myosin VI/Tom1 complex reveals a cargo recognition mode of
RT Myosin VI for tethering.";
RL Nat. Commun. 10:3459-3459(2019).
RN [29] {ECO:0007744|PDB:5AAS}
RP STRUCTURE BY NMR OF 722-784, FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH MAP1LC3B AND MAP1LC3C, AND MUTAGENESIS OF VAL-143.
RX PubMed=26451915; DOI=10.1371/journal.ppat.1005174;
RA Tumbarello D.A., Manna P.T., Allen M., Bycroft M., Arden S.D.,
RA Kendrick-Jones J., Buss F.;
RT "The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are
RT Required for Clearance of Salmonella Typhimurium by Autophagy.";
RL PLoS Pathog. 11:e1005174-E1005174(2015).
RN [30] {ECO:0007744|PDB:5YT6}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 754-787, AND FUNCTION.
RX PubMed=29940186; DOI=10.1016/j.jmb.2018.06.030;
RA Hu S., Wang Y., Gong Y., Liu J., Li Y., Pan L.;
RT "Mechanistic Insights into Recognitions of Ubiquitin and Myosin VI by
RT Autophagy Receptor TAX1BP1.";
RL J. Mol. Biol. 430:3283-3296(2018).
RN [31] {ECO:0007744|PDB:5Z7G}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-121, FUNCTION, AND INTERACTION
RP WITH AZI2.
RX PubMed=30459273; DOI=10.1073/pnas.1811421115;
RA Fu T., Liu J., Wang Y., Xie X., Hu S., Pan L.;
RT "Mechanistic insights into the interactions of NAP1 with the SKICH domains
RT of NDP52 and TAX1BP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E11651-E11660(2018).
CC -!- FUNCTION: Ubiquitin-binding adapter that participates in inflammatory,
CC antiviral and innate immune processes as well as selective autophagy
CC regulation (PubMed:30459273, PubMed:29940186, PubMed:30909570). Plays a
CC key role in the negative regulation of NF-kappa-B and IRF3 signalings
CC by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to
CC bind and inactivate its substrates (PubMed:17703191). Disrupts the
CC interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to
CC attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-
CC beta production (PubMed:21885437). Recruits also A20/TNFAIP3 to
CC ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their
CC deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B
CC signaling pathways (PubMed:17703191). Inhibits virus-induced apoptosis
CC by inducing the 'Lys-48'-linked polyubiquitination and degradation of
CC MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-
CC mediated apoptosis signaling (PubMed:27736772). As a
CC macroautophagy/autophagy receptor, facilitates the xenophagic clearance
CC of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium
CC tuberculosis (PubMed:26451915). Upon NBR1 recruitment to the SQSTM1-
CC ubiquitin condensates, acts as the major recruiter of RB1CC1 to these
CC ubiquitin condensates to promote their autophagic degradation
CC (PubMed:33226137, PubMed:34471133). Mediates the autophagic degradation
CC of other substrates including TICAM1 (PubMed:28898289).
CC {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205,
CC ECO:0000269|PubMed:17703191, ECO:0000269|PubMed:21885437,
CC ECO:0000269|PubMed:26451915, ECO:0000269|PubMed:27736772,
CC ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:29940186,
CC ECO:0000269|PubMed:30459273, ECO:0000269|PubMed:30909570,
CC ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133}.
CC -!- SUBUNIT: Homooligomer. Interacts with TNFAIP3. Interacts with STARD13.
CC Interacts with MYO6 (PubMed:31371777). Interacts with TOM1; the
CC interaction is indirect and is mediated by MYO6, which acts as a bridge
CC between TOM1 and TAX1BP1 (PubMed:31371777). Interacts with MAVS; this
CC interaction induces MAVS polyubiquitination (PubMed:27736772).
CC Interacts with TNIP1 (PubMed:21885437). Interacts with TRAF6; this
CC interaction mediates deubiquitination of TRAF6 and inhibition of NF-
CC kappa-B activation (PubMed:17703191). Interacts with RIPK1; this
CC interaction negatively regulates RIPK1 ubiquitination
CC (PubMed:17703191). Interacts with NBR1 (PubMed:33226137,
CC PubMed:34471133). Interacts with TBK1 (PubMed:33226137). Interacts with
CC RB1CC1 (PubMed:33226137, PubMed:34471133). Interacts with SQSTM1
CC (PubMed:34471133). Interacts with AZI2 (PubMed:30459273). Interacts
CC with TICAM1 and TRIM32; these interactions target TICAM1 to TAX1BP1-
CC mediated selective autophagic degradation (PubMed:28898289).
CC {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205,
CC ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:17703191,
CC ECO:0000269|PubMed:21885437, ECO:0000269|PubMed:27736772,
CC ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:30459273,
CC ECO:0000269|PubMed:31371777, ECO:0000269|PubMed:33226137,
CC ECO:0000269|PubMed:34471133}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the HTLV-1 protein Tax.
CC {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:14530271}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Respiratory syncytial
CC virus protein N; this interaction may promote viral growth by
CC inhibiting the innate immune response. {ECO:0000269|PubMed:34431698}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Lassa virus protein Z.
CC {ECO:0000269|PubMed:30909570}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Mopeia virus protein Z.
CC {ECO:0000269|PubMed:30909570}.
CC -!- INTERACTION:
CC Q86VP1; Q96B23: ARK2N; NbExp=3; IntAct=EBI-529518, EBI-742108;
CC Q86VP1; Q9HC52: CBX8; NbExp=3; IntAct=EBI-529518, EBI-712912;
CC Q86VP1; O15111: CHUK; NbExp=2; IntAct=EBI-529518, EBI-81249;
CC Q86VP1; P83436: COG7; NbExp=10; IntAct=EBI-529518, EBI-389534;
CC Q86VP1; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-529518, EBI-5453285;
CC Q86VP1; Q9P0U4: CXXC1; NbExp=3; IntAct=EBI-529518, EBI-949911;
CC Q86VP1; Q9P0U4-2: CXXC1; NbExp=3; IntAct=EBI-529518, EBI-12743307;
CC Q86VP1; Q9UER7: DAXX; NbExp=3; IntAct=EBI-529518, EBI-77321;
CC Q86VP1; Q15038: DAZAP2; NbExp=6; IntAct=EBI-529518, EBI-724310;
CC Q86VP1; P60981: DSTN; NbExp=6; IntAct=EBI-529518, EBI-745191;
CC Q86VP1; Q9Y6C2: EMILIN1; NbExp=3; IntAct=EBI-529518, EBI-744586;
CC Q86VP1; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-529518, EBI-11748557;
CC Q86VP1; Q3B820: FAM161A; NbExp=3; IntAct=EBI-529518, EBI-719941;
CC Q86VP1; Q92567: FAM168A; NbExp=3; IntAct=EBI-529518, EBI-7957930;
CC Q86VP1; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-529518, EBI-11978259;
CC Q86VP1; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-529518, EBI-6658203;
CC Q86VP1; Q99958: FOXC2; NbExp=3; IntAct=EBI-529518, EBI-3956892;
CC Q86VP1; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-529518, EBI-746969;
CC Q86VP1; P60520: GABARAPL2; NbExp=3; IntAct=EBI-529518, EBI-720116;
CC Q86VP1; P28799: GRN; NbExp=3; IntAct=EBI-529518, EBI-747754;
CC Q86VP1; V9HW29: HEL-S-61; NbExp=3; IntAct=EBI-529518, EBI-10330057;
CC Q86VP1; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-529518, EBI-11955401;
CC Q86VP1; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-529518, EBI-2556193;
CC Q86VP1; Q92993: KAT5; NbExp=3; IntAct=EBI-529518, EBI-399080;
CC Q86VP1; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-529518, EBI-739909;
CC Q86VP1; O00214: LGALS8; NbExp=4; IntAct=EBI-529518, EBI-740058;
CC Q86VP1; O00214-2: LGALS8; NbExp=3; IntAct=EBI-529518, EBI-12069522;
CC Q86VP1; Q99732: LITAF; NbExp=3; IntAct=EBI-529518, EBI-725647;
CC Q86VP1; Q8TAP4: LMO3; NbExp=3; IntAct=EBI-529518, EBI-742259;
CC Q86VP1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-529518, EBI-739832;
CC Q86VP1; Q96KN1: LRATD2; NbExp=3; IntAct=EBI-529518, EBI-9057780;
CC Q86VP1; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-529518, EBI-2603996;
CC Q86VP1; Q9Y3B7: MRPL11; NbExp=6; IntAct=EBI-529518, EBI-5453723;
CC Q86VP1; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-529518, EBI-2513715;
CC Q86VP1; Q9NWW6: NMRK1; NbExp=6; IntAct=EBI-529518, EBI-10315485;
CC Q86VP1; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-529518, EBI-741158;
CC Q86VP1; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-529518, EBI-14066006;
CC Q86VP1; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-529518, EBI-373552;
CC Q86VP1; Q494U1: PLEKHN1; NbExp=4; IntAct=EBI-529518, EBI-10241513;
CC Q86VP1; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-529518, EBI-12014286;
CC Q86VP1; O15160: POLR1C; NbExp=3; IntAct=EBI-529518, EBI-1055079;
CC Q86VP1; Q9NP72: RAB18; NbExp=3; IntAct=EBI-529518, EBI-722247;
CC Q86VP1; Q9NS91: RAD18; NbExp=6; IntAct=EBI-529518, EBI-2339393;
CC Q86VP1; P54727: RAD23B; NbExp=3; IntAct=EBI-529518, EBI-954531;
CC Q86VP1; Q15311: RALBP1; NbExp=3; IntAct=EBI-529518, EBI-749285;
CC Q86VP1; Q9Y3C5: RNF11; NbExp=2; IntAct=EBI-529518, EBI-396669;
CC Q86VP1; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-529518, EBI-748391;
CC Q86VP1; Q16385: SSX2B; NbExp=3; IntAct=EBI-529518, EBI-2210673;
CC Q86VP1; Q9Y3M8: STARD13; NbExp=2; IntAct=EBI-529518, EBI-465487;
CC Q86VP1; Q8TC07: TBC1D15; NbExp=3; IntAct=EBI-529518, EBI-1048247;
CC Q86VP1; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-529518, EBI-11974855;
CC Q86VP1; Q15560: TCEA2; NbExp=3; IntAct=EBI-529518, EBI-710310;
CC Q86VP1; P56279: TCL1A; NbExp=3; IntAct=EBI-529518, EBI-749995;
CC Q86VP1; P21580: TNFAIP3; NbExp=5; IntAct=EBI-529518, EBI-527670;
CC Q86VP1; Q15025: TNIP1; NbExp=8; IntAct=EBI-529518, EBI-357849;
CC Q86VP1; Q96KP6: TNIP3; NbExp=7; IntAct=EBI-529518, EBI-2509913;
CC Q86VP1; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-529518, EBI-3650647;
CC Q86VP1; Q9Y4K3: TRAF6; NbExp=8; IntAct=EBI-529518, EBI-359276;
CC Q86VP1; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-529518, EBI-8451480;
CC Q86VP1; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-529518, EBI-11993364;
CC Q86VP1; Q8NCE0: TSEN2; NbExp=3; IntAct=EBI-529518, EBI-2559818;
CC Q86VP1; Q99816: TSG101; NbExp=6; IntAct=EBI-529518, EBI-346882;
CC Q86VP1; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-529518, EBI-9053916;
CC Q86VP1; P62987: UBA52; NbExp=3; IntAct=EBI-529518, EBI-357304;
CC Q86VP1; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-529518, EBI-7353612;
CC Q86VP1; P0CG47: UBB; NbExp=3; IntAct=EBI-529518, EBI-413034;
CC Q86VP1; P0CG48: UBC; NbExp=8; IntAct=EBI-529518, EBI-3390054;
CC Q86VP1; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-529518, EBI-17208936;
CC Q86VP1; O75604: USP2; NbExp=3; IntAct=EBI-529518, EBI-743272;
CC Q86VP1; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-529518, EBI-740232;
CC Q86VP1; Q8WU02; NbExp=3; IntAct=EBI-529518, EBI-747182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30909570}.
CC Mitochondrion {ECO:0000269|PubMed:27736772}. Preautophagosomal
CC structure {ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:26451915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86VP1-1; Sequence=Displayed;
CC Name=2; Synonyms=TXBP151-L;
CC IsoId=Q86VP1-2; Sequence=VSP_018355;
CC Name=3; Synonyms=TXBP151-S;
CC IsoId=Q86VP1-3; Sequence=VSP_018354, VSP_018355;
CC Name=4;
CC IsoId=Q86VP1-4; Sequence=VSP_045921, VSP_018355;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC -!- DOMAIN: The C-terminal UBZ-type zinc fingers function as ubiquitin-
CC binding domains. {ECO:0000269|PubMed:24239949}.
CC -!- PTM: Phosphorylated in the C-terminal region by CHUK/IKKA leading to
CC NF-kappa-B signaling down-regulation. {ECO:0000269|PubMed:21765415}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13359.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U33821; AAA75595.2; -; mRNA.
DR EMBL; AF268075; AAG03025.1; -; mRNA.
DR EMBL; AL136586; CAB66521.1; -; mRNA.
DR EMBL; AF090891; AAF24016.1; -; mRNA.
DR EMBL; CR457056; CAG33337.1; -; mRNA.
DR EMBL; AK296720; BAG59309.1; -; mRNA.
DR EMBL; AK314292; BAG36949.1; -; mRNA.
DR EMBL; CR533556; CAG38587.1; -; mRNA.
DR EMBL; AC004549; AAC13359.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005091; AAD15412.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24213.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93901.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93904.1; -; Genomic_DNA.
DR EMBL; BC050358; AAH50358.1; -; mRNA.
DR CCDS; CCDS43561.1; -. [Q86VP1-2]
DR CCDS; CCDS5415.1; -. [Q86VP1-1]
DR CCDS; CCDS56471.1; -. [Q86VP1-4]
DR PIR; G02043; G02043.
DR RefSeq; NP_001073333.1; NM_001079864.2. [Q86VP1-2]
DR RefSeq; NP_001193830.1; NM_001206901.1. [Q86VP1-2]
DR RefSeq; NP_001193831.1; NM_001206902.1. [Q86VP1-4]
DR RefSeq; NP_006015.4; NM_006024.6. [Q86VP1-1]
DR PDB; 2M7Q; NMR; -; A=725-789.
DR PDB; 4BMJ; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J/K=725-789.
DR PDB; 4NLH; X-ray; 1.90 A; A/B=15-147.
DR PDB; 4Z4K; X-ray; 2.80 A; A/B=725-781.
DR PDB; 4Z4M; X-ray; 2.15 A; A/B=755-781.
DR PDB; 5AAS; NMR; -; A=722-784.
DR PDB; 5YT6; X-ray; 1.50 A; B/D/F/H=754-787.
DR PDB; 5Z7G; X-ray; 2.30 A; A/B=1-121.
DR PDBsum; 2M7Q; -.
DR PDBsum; 4BMJ; -.
DR PDBsum; 4NLH; -.
DR PDBsum; 4Z4K; -.
DR PDBsum; 4Z4M; -.
DR PDBsum; 5AAS; -.
DR PDBsum; 5YT6; -.
DR PDBsum; 5Z7G; -.
DR AlphaFoldDB; Q86VP1; -.
DR BMRB; Q86VP1; -.
DR SMR; Q86VP1; -.
DR BioGRID; 114405; 351.
DR DIP; DIP-33010N; -.
DR IntAct; Q86VP1; 121.
DR MINT; Q86VP1; -.
DR STRING; 9606.ENSP00000379612; -.
DR MoonDB; Q86VP1; Predicted.
DR GlyGen; Q86VP1; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q86VP1; -.
DR PhosphoSitePlus; Q86VP1; -.
DR BioMuta; TAX1BP1; -.
DR DMDM; 97202549; -.
DR EPD; Q86VP1; -.
DR jPOST; Q86VP1; -.
DR MassIVE; Q86VP1; -.
DR MaxQB; Q86VP1; -.
DR PaxDb; 9606-ENSP00000379612; -.
DR PeptideAtlas; Q86VP1; -.
DR ProteomicsDB; 17229; -.
DR ProteomicsDB; 70045; -. [Q86VP1-1]
DR ProteomicsDB; 70046; -. [Q86VP1-2]
DR ProteomicsDB; 70047; -. [Q86VP1-3]
DR Pumba; Q86VP1; -.
DR Antibodypedia; 12449; 280 antibodies from 29 providers.
DR DNASU; 8887; -.
DR Ensembl; ENST00000265393.10; ENSP00000265393.6; ENSG00000106052.14. [Q86VP1-2]
DR Ensembl; ENST00000396319.7; ENSP00000379612.2; ENSG00000106052.14. [Q86VP1-1]
DR Ensembl; ENST00000433216.6; ENSP00000391907.2; ENSG00000106052.14. [Q86VP1-4]
DR Ensembl; ENST00000543117.5; ENSP00000444811.1; ENSG00000106052.14. [Q86VP1-2]
DR GeneID; 8887; -.
DR KEGG; hsa:8887; -.
DR MANE-Select; ENST00000396319.7; ENSP00000379612.2; NM_006024.7; NP_006015.4.
DR UCSC; uc003szk.4; human. [Q86VP1-1]
DR AGR; HGNC:11575; -.
DR CTD; 8887; -.
DR DisGeNET; 8887; -.
DR GeneCards; TAX1BP1; -.
DR HGNC; HGNC:11575; TAX1BP1.
DR HPA; ENSG00000106052; Low tissue specificity.
DR MIM; 605326; gene.
DR neXtProt; NX_Q86VP1; -.
DR OpenTargets; ENSG00000106052; -.
DR PharmGKB; PA36339; -.
DR VEuPathDB; HostDB:ENSG00000106052; -.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_021315_1_0_1; -.
DR InParanoid; Q86VP1; -.
DR OrthoDB; 3062393at2759; -.
DR PhylomeDB; Q86VP1; -.
DR TreeFam; TF329501; -.
DR PathwayCommons; Q86VP1; -.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR SignaLink; Q86VP1; -.
DR SIGNOR; Q86VP1; -.
DR BioGRID-ORCS; 8887; 35 hits in 1161 CRISPR screens.
DR ChiTaRS; TAX1BP1; human.
DR GeneWiki; TAX1BP1; -.
DR GenomeRNAi; 8887; -.
DR Pharos; Q86VP1; Tbio.
DR PRO; PR:Q86VP1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86VP1; Protein.
DR Bgee; ENSG00000106052; Expressed in secondary oocyte and 213 other cell types or tissues.
DR ExpressionAtlas; Q86VP1; baseline and differential.
DR Genevisible; Q86VP1; HS.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProt.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0019900; F:kinase binding; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProt.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0039532; P:negative regulation of cytoplasmic pattern recognition receptor signaling pathway; IDA:UniProt.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IDA:UniProt.
DR GO; GO:1905161; P:protein localization to phagocytic vesicle; IDA:UniProt.
DR CDD; cd21969; Zn-C2H2_TAX1BP1_rpt1; 1.
DR CDD; cd21970; Zn-C2H2_TAX1BP1_rpt2; 1.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 6.20.250.40; -; 1.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
DR PANTHER; PTHR31915; SKICH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31915:SF8; TAX1-BINDING PROTEIN 1; 1.
DR Pfam; PF07888; CALCOCO1; 1.
DR Pfam; PF17751; SKICH; 1.
DR Pfam; PF18112; Zn-C2H2_12; 2.
DR PROSITE; PS51905; ZF_UBZ1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Autophagy; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Host-virus interaction; Immunity;
KW Innate immunity; Metal-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..789
FT /note="Tax1-binding protein 1"
FT /id="PRO_0000234554"
FT ZN_FING 727..753
FT /note="UBZ1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT ZN_FING 754..780
FT /note="UBZ1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 320..420
FT /note="Oligomerization"
FT REGION 478..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..599
FT /evidence="ECO:0000255"
FT COMPBIAS 478..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 730
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 776
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UKC1"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 593
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000269|PubMed:21765415"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UKC1"
FT MOD_RES 666
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000269|PubMed:21765415,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018354"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045921"
FT VAR_SEQ 604..645
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10435631,
FT ECO:0000303|PubMed:10920205, ECO:0000303|PubMed:14702039,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.6"
FT /id="VSP_018355"
FT VARIANT 58
FT /note="S -> N (in dbSNP:rs7809260)"
FT /id="VAR_051415"
FT VARIANT 307
FT /note="L -> I (in dbSNP:rs11540483)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026286"
FT VARIANT 457
FT /note="Q -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035665"
FT MUTAGEN 114
FT /note="A->Q: Complete loss of TBK1 and RB1CC1 binding."
FT /evidence="ECO:0000269|PubMed:33226137"
FT MUTAGEN 143
FT /note="V->S: Complete loss of MAP1LC3B binding."
FT /evidence="ECO:0000269|PubMed:26451915"
FT MUTAGEN 771
FT /note="Q->A: Normal affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT MUTAGEN 774
FT /note="E->A: Reduced affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT MUTAGEN 775
FT /note="R->A: Normal affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT MUTAGEN 777
FT /note="V->S: Reduced affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT MUTAGEN 778
FT /note="Q->A: Reduced affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT MUTAGEN 781
FT /note="F->A: Reduced affinity for ubiquitin."
FT /evidence="ECO:0000269|PubMed:27062441"
FT CONFLICT 199
FT /note="L -> P (in Ref. 5; BAG59309)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..234
FT /note="QL -> HV (in Ref. 1; AAA75595)"
FT /evidence="ECO:0000305"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5Z7G"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4NLH"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4NLH"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4NLH"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:4BMJ"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:4BMJ"
FT HELIX 743..751
FT /evidence="ECO:0007829|PDB:4BMJ"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:4BMJ"
FT TURN 758..760
FT /evidence="ECO:0007829|PDB:5YT6"
FT HELIX 770..779
FT /evidence="ECO:0007829|PDB:5YT6"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:5YT6"
SQ SEQUENCE 789 AA; 90877 MW; DE8460DAA6712125 CRC64;
MTSFQEVPLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHPKDWV GIFKVGWSTA
RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
RASSPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTMKE KEELLKLIAV LEKETAQLRE
QVGRMERELN HEKERCDQLQ AEQKGLTEVT QSLKMENEEF KKRFSDATSK AHQLEEDIVS
VTHKAIEKET ELDSLKDKLK KAQHEREQLE CQLKTEKDEK ELYKVHLKNT EIENTKLMSE
VQTLKNLDGN KESVITHFKE EIGRLQLCLA EKENLQRTFL LTTSSKEDTC FLKEQLRKAE
EQVQATRQEV VFLAKELSDA VNVRDRTMAD LHTARLENEK VKKQLADAVA ELKLNAMKKD
QDKTDTLEHE LRREVEDLKL RLQMAADHYK EKFKECQRLQ KQINKLSDQS ANNNNVFTKK
TGNQQKVNDA SVNTDPATSA STVDVKPSPS AAEADFDIVT KGQVCEMTKE IADKTEKYNK
CKQLLQDEKA KCNKYADELA KMELKWKEQV KIAENVKLEL AEVQDNYKEL KRSLENPAER
KMEGQNSQSP QCFKTCSEQN GYVLTLSNAQ PVLQYGNPYA SQETRDGADG AFYPDEIQRP
PVRVPSWGLE DNVVCSQPAR NFSRPDGLED SEDSKEDENV PTAPDPPSQH LRGHGTGFCF
DSSFDVHKKC PLCELMFPPN YDQSKFEEHV ESHWKVCPMC SEQFPPDYDQ QVFERHVQTH
FDQNVLNFD
//
