TAXB1_HUMAN
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 03-AUG-2022, entry version 158.
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 AND HTLV-1 PROTEIN TAX-1, AND ALTERNATIVE 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-1.
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 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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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).
CC -!- FUNCTION: Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-
CC apoptotic activity. Degraded by caspase-3-like family proteins upon
CC TNF-induced apoptosis. May also play a role in the pro-inflammatory
CC cytokine IL-1 signaling cascade. {ECO:0000269|PubMed:10435631,
CC ECO:0000269|PubMed:10920205}.
CC -!- SUBUNIT: Homooligomer. Interacts with TRAF6 in a IL-1-dependent manner.
CC Interacts with TNFAIP3. Interacts with STARD13. Interacts with the
CC HTLV-1 protein Tax-1. {ECO:0000269|PubMed:10435631,
CC ECO:0000269|PubMed:10920205, ECO:0000269|PubMed:14530271,
CC ECO:0000269|PubMed:14697242}.
CC -!- INTERACTION:
CC Q86VP1; Q96B23: C18orf25; 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 -!- 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; 333.
DR DIP; DIP-33010N; -.
DR IntAct; Q86VP1; 119.
DR MINT; Q86VP1; -.
DR STRING; 9606.ENSP00000379612; -.
DR MoonDB; Q86VP1; Predicted.
DR GlyGen; Q86VP1; 1 site, 1 O-linked glycan (1 site).
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; Q86VP1; -.
DR PeptideAtlas; Q86VP1; -.
DR PRIDE; Q86VP1; -.
DR ProteomicsDB; 17229; -.
DR ProteomicsDB; 70045; -. [Q86VP1-1]
DR ProteomicsDB; 70046; -. [Q86VP1-2]
DR ProteomicsDB; 70047; -. [Q86VP1-3]
DR Antibodypedia; 12449; 246 antibodies from 28 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 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; 179838at2759; -.
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 1085 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 211 other tissues.
DR ExpressionAtlas; Q86VP1; baseline and differential.
DR Genevisible; Q86VP1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
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; Coiled coil; Metal-binding;
KW Phosphoprotein; 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 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
