TAB3_HUMAN
ID TAB3_HUMAN Reviewed; 712 AA.
AC Q8N5C8; A6NDD9; Q6VQR0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 3;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 3;
DE AltName: Full=NF-kappa-B-activating protein 1;
DE AltName: Full=TAK1-binding protein 3 {ECO:0000303|PubMed:14633987};
DE Short=TAB-3 {ECO:0000303|PubMed:14633987};
DE AltName: Full=TGF-beta-activated kinase 1-binding protein 3 {ECO:0000303|PubMed:14633987};
GN Name=TAB3 {ECO:0000303|PubMed:14633987, ECO:0000312|HGNC:HGNC:30681};
GN Synonyms=MAP3K7IP3;
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 1), INTERACTION WITH MAP3K7; TRAF2 AND
RP TRAF6, UBIQUITINATION, PHOSPHORYLATION, AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=14633987; DOI=10.1093/emboj/cdg605;
RA Ishitani T., Takaesu G., Ninomiya-Tsuji J., Shibuya H., Gaynor R.B.,
RA Matsumoto K.;
RT "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling.";
RL EMBO J. 22:6277-6288(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND INTERACTION WITH TAB1; TAB2 AND MAP3K7.
RX PubMed=14670075; DOI=10.1042/bj20031794;
RA Cheung P.C., Nebreda A.R., Cohen P.;
RT "TAB3, a new binding partner of the protein kinase TAK1.";
RL Biochem. J. 378:27-34(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH MAP3K7 AND
RP TRAF6, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=14766965; DOI=10.1073/pnas.0307314101;
RA Jin G., Klika A., Callahan M., Faga B., Danzig J., Jiang Z., Li X.,
RA Stark G.R., Harrington J., Sherf B.;
RT "Identification of a human NF-kappaB-activating protein, TAB3.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2028-2033(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP FUNCTION.
RX PubMed=15327770; DOI=10.1016/j.molcel.2004.08.008;
RA Kanayama A., Seth R.B., Sun L., Ea C.K., Hong M., Shaito A., Chiu Y.H.,
RA Deng L., Chen Z.J.;
RT "TAB2 and TAB3 activate the NF-kappaB pathway through binding to
RT polyubiquitin chains.";
RL Mol. Cell 15:535-548(2004).
RN [7]
RP INTERACTION WITH RBCK1.
RX PubMed=17449468; DOI=10.1074/jbc.m701913200;
RA Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M.,
RA Chen D.Y., Zhai Z.H., Shu H.B.;
RT "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
RT triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
RL J. Biol. Chem. 282:16776-16782(2007).
RN [8]
RP PHOSPHORYLATION AT SER-506.
RX PubMed=18021073; DOI=10.1042/bj20071149;
RA Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H.,
RA Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P.;
RT "Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the
RT TAB3 regulatory subunit and activity of the TAK1 complex.";
RL Biochem. J. 409:711-722(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-404 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INTERACTION WITH DYNC2I2.
RX PubMed=19521662; DOI=10.1007/s00018-009-0059-6;
RA Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.;
RT "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced
RT NF-kappaB activation pathway.";
RL Cell. Mol. Life Sci. 66:2573-2584(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-60, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY 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 [12]
RP FUNCTION, DOMAIN, METHYLATION AT CYS-692 (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF CYS-689; CYS-692; CYS-703 AND CYS-706.
RX PubMed=22158122; DOI=10.1038/nature10690;
RA Zhang L., Ding X., Cui J., Xu H., Chen J., Gong Y.N., Hu L., Zhou Y.,
RA Ge J., Lu Q., Liu L., Chen S., Shao F.;
RT "Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB
RT activation.";
RL Nature 481:204-208(2011).
RN [13]
RP INTERACTION WITH TRIM5.
RX PubMed=21512573; DOI=10.1038/nature09976;
RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L.,
RA Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-385; THR-404 AND
RP SER-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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-101, 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 SUBCELLULAR LOCATION, DEGRADATION, AND INTERACTION WITH TRIM38.
RX PubMed=24434549; DOI=10.1073/pnas.1318227111;
RA Hu M.M., Yang Q., Zhang J., Liu S.M., Zhang Y., Lin H., Huang Z.F.,
RA Wang Y.Y., Zhang X.D., Zhong B., Shu H.B.;
RT "TRIM38 inhibits TNFalpha- and IL-1beta-triggered NF-kappaB activation by
RT mediating lysosome-dependent degradation of TAB2/3.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1509-1514(2014).
RN [17]
RP INTERACTION WITH MYCOBACTERIUM TUBERCULOSIS PTPA (MICROBIAL INFECTION).
RX PubMed=25642820; DOI=10.1038/ni.3096;
RA Wang J., Li B.X., Ge P.P., Li J., Wang Q., Gao G.F., Qiu X.B., Liu C.H.;
RT "Mycobacterium tuberculosis suppresses innate immunity by coopting the host
RT ubiquitin system.";
RL Nat. Immunol. 16:237-245(2015).
RN [18]
RP METHYLATION (MICROBIAL INFECTION).
RX PubMed=27445336; DOI=10.1074/jbc.m116.734079;
RA Zhang Y., Muehlen S., Oates C.V., Pearson J.S., Hartland E.L.;
RT "Identification of a distinct substrate-binding domain in the bacterial
RT cysteine methyltransferase effectors NleE and OspZ.";
RL J. Biol. Chem. 291:20149-20162(2016).
CC -!- FUNCTION: Adapter required to activate the JNK and NF-kappa-B signaling
CC pathways through the specific recognition of 'Lys-63'-linked
CC polyubiquitin chains by its RanBP2-type zinc finger (NZF)
CC (PubMed:14633987, PubMed:14766965, PubMed:15327770, PubMed:22158122).
CC Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked
CC polyubiquitin chains (PubMed:14633987, PubMed:14766965,
CC PubMed:15327770, PubMed:22158122). The RanBP2-type zinc finger (NZF)
CC specifically recognizes Lys-63'-linked polyubiquitin chains unanchored
CC or anchored to the substrate proteins such as RIPK1/RIP1: this acts as
CC a scaffold to organize a large signaling complex to promote
CC autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-
CC kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (PubMed:15327770,
CC PubMed:22158122). {ECO:0000269|PubMed:14633987,
CC ECO:0000269|PubMed:14766965, ECO:0000269|PubMed:15327770,
CC ECO:0000269|PubMed:22158122}.
CC -!- FUNCTION: [Isoform 2]: May be an oncogenic factor.
CC {ECO:0000269|PubMed:14766965}.
CC -!- SUBUNIT: Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6
CC (PubMed:14633987, PubMed:14670075, PubMed:14766965). The minimal TAB3-
CC containing complex (TAB1-MAP3K7-TAB3) appears not to contain TAB2
CC (PubMed:14670075). However, it seems sensible to consider that TAB2 may
CC also join this complex and may act in a cooperative manner with TAB3
CC (PubMed:14670075). Interacts with DYNC2I2 (via the WD domains)
CC (PubMed:19521662). Interacts with RBCK1 (PubMed:17449468). Binds 'Lys-
CC 63'-linked polyubiquitin chains (PubMed:22158122). Interacts with TRIM5
CC (PubMed:21512573). Interacts with TRIM38 (via B30.2/SPRY domain),
CC leading to its translocation to lysosomes and degradation
CC (PubMed:24434549). {ECO:0000269|PubMed:14633987,
CC ECO:0000269|PubMed:14670075, ECO:0000269|PubMed:14766965,
CC ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:19521662,
CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:22158122,
CC ECO:0000269|PubMed:24434549}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis PtpA,
CC which blocks the NF-kappa-B signaling pathway.
CC {ECO:0000269|PubMed:25642820}.
CC -!- INTERACTION:
CC Q8N5C8; Q14457: BECN1; NbExp=9; IntAct=EBI-359964, EBI-949378;
CC Q8N5C8; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-359964, EBI-10181988;
CC Q8N5C8; O43318: MAP3K7; NbExp=4; IntAct=EBI-359964, EBI-358684;
CC Q8N5C8; P57077-4: MAP3K7CL; NbExp=6; IntAct=EBI-359964, EBI-10215880;
CC Q8N5C8; Q13526: PIN1; NbExp=3; IntAct=EBI-359964, EBI-714158;
CC Q8N5C8; Q62073: Map3k7; Xeno; NbExp=2; IntAct=EBI-359964, EBI-1775345;
CC Q8N5C8-1; B7UI22: nleE; Xeno; NbExp=7; IntAct=EBI-15957777, EBI-15957770;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Tab3a;
CC IsoId=Q8N5C8-1; Sequence=Displayed;
CC Name=2; Synonyms=Tab3b;
CC IsoId=Q8N5C8-2; Sequence=VSP_017516;
CC -!- TISSUE SPECIFICITY: Widely expressed. Constitutively overexpressed in
CC certain tumor tissues. {ECO:0000269|PubMed:14670075}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Major transcript.
CC {ECO:0000269|PubMed:14766965}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Minor transcript.
CC {ECO:0000269|PubMed:14766965}.
CC -!- DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two
CC consecutive 'Lys-63'-linked ubiquitins. {ECO:0000269|PubMed:22158122}.
CC -!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression.
CC {ECO:0000269|PubMed:14633987}.
CC -!- PTM: Degraded in a lysosome-dependent manner following interactiuon
CC with TRIM38. {ECO:0000269|PubMed:24434549}.
CC -!- PTM: Phosphorylated at Ser-506 by MAPKAPK2 and MAPKAPK3 following IL1
CC treatment. {ECO:0000269|PubMed:14633987, ECO:0000269|PubMed:14670075,
CC ECO:0000269|PubMed:18021073}.
CC -!- PTM: (Microbial infection) Methylated at Cys-692 by enteropathogenic
CC E.coli protein NleE or S.flexneri protein OspZ: methylation disrupts
CC zinc-binding and ability to bind 'Lys-63'-linked ubiquitin, leading to
CC NF-kappa-B inactivation. {ECO:0000269|PubMed:22158122,
CC ECO:0000269|PubMed:27445336}.
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DR EMBL; AY437560; AAR06179.1; -; mRNA.
DR EMBL; AY371491; AAQ88279.1; -; mRNA.
DR EMBL; AY331591; AAQ92938.1; -; mRNA.
DR EMBL; AY331592; AAQ92939.1; -; mRNA.
DR EMBL; AC108359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032526; AAH32526.1; -; mRNA.
DR CCDS; CCDS14226.1; -. [Q8N5C8-1]
DR RefSeq; NP_690000.3; NM_152787.4. [Q8N5C8-1]
DR RefSeq; XP_005274540.2; XM_005274483.3. [Q8N5C8-2]
DR AlphaFoldDB; Q8N5C8; -.
DR SMR; Q8N5C8; -.
DR BioGRID; 129216; 50.
DR CORUM; Q8N5C8; -.
DR DIP; DIP-32489N; -.
DR IntAct; Q8N5C8; 17.
DR MINT; Q8N5C8; -.
DR STRING; 9606.ENSP00000368215; -.
DR ChEMBL; CHEMBL4295902; -.
DR GlyGen; Q8N5C8; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q8N5C8; -.
DR PhosphoSitePlus; Q8N5C8; -.
DR BioMuta; TAB3; -.
DR DMDM; 229462756; -.
DR EPD; Q8N5C8; -.
DR jPOST; Q8N5C8; -.
DR MassIVE; Q8N5C8; -.
DR PaxDb; Q8N5C8; -.
DR PeptideAtlas; Q8N5C8; -.
DR PRIDE; Q8N5C8; -.
DR ProteomicsDB; 72035; -. [Q8N5C8-1]
DR ProteomicsDB; 72036; -. [Q8N5C8-2]
DR Antibodypedia; 24709; 297 antibodies from 39 providers.
DR DNASU; 257397; -.
DR Ensembl; ENST00000288422.4; ENSP00000288422.4; ENSG00000157625.16. [Q8N5C8-1]
DR Ensembl; ENST00000378930.7; ENSP00000368212.3; ENSG00000157625.16. [Q8N5C8-1]
DR Ensembl; ENST00000378932.6; ENSP00000368214.2; ENSG00000157625.16. [Q8N5C8-2]
DR Ensembl; ENST00000378933.5; ENSP00000368215.1; ENSG00000157625.16. [Q8N5C8-1]
DR GeneID; 257397; -.
DR KEGG; hsa:257397; -.
DR MANE-Select; ENST00000288422.4; ENSP00000288422.4; NM_152787.5; NP_690000.3.
DR UCSC; uc004dck.3; human. [Q8N5C8-1]
DR CTD; 257397; -.
DR DisGeNET; 257397; -.
DR GeneCards; TAB3; -.
DR HGNC; HGNC:30681; TAB3.
DR HPA; ENSG00000157625; Low tissue specificity.
DR MIM; 300480; gene.
DR neXtProt; NX_Q8N5C8; -.
DR OpenTargets; ENSG00000157625; -.
DR PharmGKB; PA165757406; -.
DR VEuPathDB; HostDB:ENSG00000157625; -.
DR eggNOG; ENOG502QVTR; Eukaryota.
DR GeneTree; ENSGT00940000159499; -.
DR HOGENOM; CLU_025065_1_0_1; -.
DR InParanoid; Q8N5C8; -.
DR OMA; WACNLCT; -.
DR OrthoDB; 324984at2759; -.
DR PhylomeDB; Q8N5C8; -.
DR TreeFam; TF332021; -.
DR PathwayCommons; Q8N5C8; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR SignaLink; Q8N5C8; -.
DR SIGNOR; Q8N5C8; -.
DR BioGRID-ORCS; 257397; 5 hits in 702 CRISPR screens.
DR ChiTaRS; TAB3; human.
DR GeneWiki; MAP3K7IP3; -.
DR GenomeRNAi; 257397; -.
DR Pharos; Q8N5C8; Tbio.
DR PRO; PR:Q8N5C8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N5C8; protein.
DR Bgee; ENSG00000157625; Expressed in epithelial cell of pancreas and 192 other tissues.
DR ExpressionAtlas; Q8N5C8; baseline and differential.
DR Genevisible; Q8N5C8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR CDD; cd14362; CUE_TAB2_TAB3; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041911; TAB2/3_CUE.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..712
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 3"
FT /id="PRO_0000226972"
FT DOMAIN 8..51
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 682..712
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 141..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 517..559
FT /evidence="ECO:0000255"
FT COMPBIAS 172..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 506
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000269|PubMed:18021073"
FT MOD_RES 692
FT /note="(Microbial infection) S-methylcysteine"
FT /evidence="ECO:0000269|PubMed:22158122"
FT VAR_SEQ 602..629
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14766965"
FT /id="VSP_017516"
FT VARIANT 394
FT /note="R -> W (in dbSNP:rs5927629)"
FT /id="VAR_055294"
FT MUTAGEN 689
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-692."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 692
FT /note="C->L,M: Abolished Cys methylation and ability to
FT bind 'Lys-63'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 703
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-692."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 706
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-692."
FT /evidence="ECO:0000269|PubMed:22158122"
SQ SEQUENCE 712 AA; 78653 MW; 2FAC686AE5CDB1E5 CRC64;
MAQSSPQLDI QVLHDLRQRF PEIPEGVVSQ CMLQNNNNLE ACCRALSQES SKYLYMEYHS
PDDNRMNRNR LLHINLGIHS PSSYHPGDGA QLNGGRTLVH SSSDGHIDPQ HAAGKQLICL
VQEPHSAPAV VAATPNYNPF FMNEQNRSAA TPPSQPPQQP SSMQTGMNPS AMQGPSPPPP
PPSYMHIPRY STNPITVTVS QNLPSGQTVP RALQILPQIP SNLYGSPGSI YIRQTSQSSS
GRQTPQSTPW QSSPQGPVPH YSQRPLPVYP HQQNYQPSQY SPKQQQIPQS AYHSPPPSQC
PSPFSSPQHQ VQPSQLGHIF MPPSPSTTPP HPYQQGPPSY QKQGSHSVAY LPYTASSLSK
GSMKKIEITV EPSQRPGTAI NRSPSPISNQ PSPRNQHSLY TATTPPSSSP SRGISSQPKP
PFSVNPVYIT YTQPTGPSCT PSPSPRVIPN PTTVFKITVG RATTENLLNL VDQEERSAAP
EPIQPISVIP GSGGEKGSHK YQRSSSSGSD DYAYTQALLL HQRARMERLA KQLKLEKEEL
ERLKSEVNGM EHDLMQRRLR RVSCTTAIPT PEEMTRLRSM NRQLQINVDC TLKEVDLLQS
RGNFDPKAMN NFYDNIEPGP VVPPKPSKKD SSDPCTIERK ARRISVTSKV QADIHDTQAA
AADEHRTGST QSPRTQPRDE DYEGAPWNCD SCTFLNHPAL NRCEQCEMPR YT
