TRAF1_HUMAN
ID TRAF1_HUMAN Reviewed; 416 AA.
AC Q13077; B4DJ77; Q658U1; Q8NF13;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=TNF receptor-associated factor 1;
DE AltName: Full=Epstein-Barr virus-induced protein 6;
GN Name=TRAF1; Synonyms=EBI6;
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).
RC TISSUE=Lymphoma;
RX PubMed=7859281; DOI=10.1016/0092-8674(95)90489-1;
RA Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C.,
RA Kieff E.;
RT "The Epstein-Barr virus transforming protein LMP1 engages signaling
RT proteins for the tumor necrosis factor receptor family.";
RL Cell 80:389-399(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen, and Substantia nigra;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP INTERACTION WITH TRAF2 AND TNFRSF1B.
RX PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
RA Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
RT "A novel family of putative signal transducers associated with the
RT cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
RL Cell 78:681-692(1994).
RN [9]
RP INTERACTION WITH TANK.
RX PubMed=8710854; DOI=10.1073/pnas.93.16.8241;
RA Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.;
RT "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated
RT signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996).
RN [10]
RP INTERACTION WITH TNFRSF8.
RX PubMed=8627180; DOI=10.1084/jem.183.2.669;
RA Lee S.Y., Park C.G., Choi Y.;
RT "T cell receptor-dependent cell death of T cell hybridomas mediated by the
RT CD30 cytoplasmic domain in association with tumor necrosis factor receptor-
RT associated factors.";
RL J. Exp. Med. 183:669-674(1996).
RN [11]
RP INTERACTION WITH TNFRSF5.
RX PubMed=9718306; DOI=10.1021/bi981067q;
RA Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.;
RT "CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions:
RT regulation of CD40 signaling through multiple TRAF binding sites and TRAF
RT hetero-oligomerization.";
RL Biochemistry 37:11836-11845(1998).
RN [12]
RP INTERACTION WITH RIPK2.
RX PubMed=9705938; DOI=10.1016/s0960-9822(07)00352-1;
RA Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L., Mattmann C.,
RA Tschopp J.;
RT "Identification of CARDIAK, a RIP-like kinase that associates with caspase-
RT 1.";
RL Curr. Biol. 8:885-888(1998).
RN [13]
RP INTERACTION WITH RIPK2.
RX PubMed=9642260; DOI=10.1074/jbc.273.27.16968;
RA McCarthy J.V., Ni J., Dixit V.M.;
RT "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.";
RL J. Biol. Chem. 273:16968-16975(1998).
RN [14]
RP INTERACTION WITH TNFRSF11A.
RX PubMed=9774460; DOI=10.1074/jbc.273.43.28355;
RA Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.;
RT "The TRAF family of signal transducers mediates NF-kappaB activation by the
RT TRANCE receptor.";
RL J. Biol. Chem. 273:28355-28359(1998).
RN [15]
RP INTERACTION WITH TNFRSF9.
RX PubMed=9607925; DOI=10.1084/jem.187.11.1849;
RA Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D.,
RA Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H.;
RT "CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-
RT 1BB ligand.";
RL J. Exp. Med. 187:1849-1862(1998).
RN [16]
RP INTERACTION WITH TNFRSF4 AND TNFRSF9.
RX PubMed=9418902; DOI=10.1128/mcb.18.1.558;
RA Arch R.H., Thompson C.B.;
RT "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth
RT factor receptor subfamily that bind TNF receptor-associated factors and
RT activate nuclear factor kappaB.";
RL Mol. Cell. Biol. 18:558-565(1998).
RN [17]
RP INTERACTION WITH TNFRSF18.
RX PubMed=10037686; DOI=10.1074/jbc.274.10.6056;
RA Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D.,
RA Wang S.-X., Kwon B.S.;
RT "Identification of a novel activation-inducible protein of the tumor
RT necrosis factor receptor superfamily and its ligand.";
RL J. Biol. Chem. 274:6056-6061(1999).
RN [18]
RP FUNCTION, CLEAVAGE BY CASP8, MUTAGENESIS OF ASP-163, AND DOMAIN.
RX PubMed=10692572; DOI=10.1016/s0014-5793(00)01206-0;
RA Irmler M., Steiner V., Ruegg C., Wajant H., Tschopp J.;
RT "Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas
RT ligand-mediated apoptosis.";
RL FEBS Lett. 468:129-133(2000).
RN [19]
RP INTERACTION WITH TNFRSF19.
RX PubMed=10809768; DOI=10.1074/jbc.275.20.15336;
RA Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.;
RT "TAJ, a novel member of the tumor necrosis factor receptor family,
RT activates the c-Jun N-terminal kinase pathway and mediates caspase-
RT independent cell death.";
RL J. Biol. Chem. 275:15336-15342(2000).
RN [20]
RP INTERACTION WITH TNFRSF17.
RX PubMed=10903733; DOI=10.4049/jimmunol.165.3.1322;
RA Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J.,
RA Devergne O., Tsapis A.;
RT "TNF receptor family member BCMA (B cell maturation) associates with TNF
RT receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-
RT kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein
RT kinase.";
RL J. Immunol. 165:1322-1330(2000).
RN [21]
RP INTERACTION WITH TNFRSF19L.
RX PubMed=11313261; DOI=10.1182/blood.v97.9.2702;
RA Sica G.L., Zhu G., Tamada K., Liu D., Ni J., Chen L.;
RT "RELT, a new member of the tumor necrosis factor receptor superfamily, is
RT selectively expressed in hematopoietic tissues and activates transcription
RT factor NF-kappaB.";
RL Blood 97:2702-2707(2001).
RN [22]
RP INTERACTION WITH EDAR.
RX PubMed=11035039; DOI=10.1074/jbc.m008356200;
RA Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.;
RT "The ectodermal dysplasia receptor activates the nuclear factor-kappaB,
RT JNK, and cell death pathways and binds to ectodysplasin A.";
RL J. Biol. Chem. 276:2668-2677(2001).
RN [23]
RP INTERACTION WITH BIRC2.
RX PubMed=11907583; DOI=10.1038/416345a;
RA Li X., Yang Y., Ashwell J.D.;
RT "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2.";
RL Nature 416:345-347(2002).
RN [24]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15383523; DOI=10.1074/jbc.m407284200;
RA He L., Grammer A.C., Wu X., Lipsky P.E.;
RT "TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate
RT NF-{kappa}B activation.";
RL J. Biol. Chem. 279:55855-55865(2004).
RN [25]
RP UBIQUITINATION AT LYS-185 AND LYS-193, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND MUTAGENESIS OF LYS-185 AND LYS-193.
RX PubMed=15468071; DOI=10.1002/pmic.200401000;
RA Lee J.S., Hong U.S., Lee T.H., Yoon S.K., Yoon J.B.;
RT "Mass spectrometric analysis of tumor necrosis factor receptor-associated
RT factor 1 ubiquitination mediated by cellular inhibitor of apoptosis 2.";
RL Proteomics 4:3376-3382(2004).
RN [26]
RP FUNCTION, INTERACTION WITH TICAM1, CLEAVAGE BY CASP8, AND MUTAGENESIS OF
RP ASP-163.
RX PubMed=16323247; DOI=10.1002/eji.200535415;
RA Su X., Li S., Meng M., Qian W., Xie W., Chen D., Zhai Z., Shu H.B.;
RT "TNF receptor-associated factor-1 (TRAF1) negatively regulates Toll/IL-1
RT receptor domain-containing adaptor inducing IFN-beta (TRIF)-mediated
RT signaling.";
RL Eur. J. Immunol. 36:199-206(2006).
RN [27]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=18429822; DOI=10.1111/j.1365-2443.2008.01182.x;
RA Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y.;
RT "Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-
RT mediated phosphorylation of TRAF1.";
RL Genes Cells 13:509-520(2008).
RN [28]
RP FUNCTION, AND INTERACTION WITH TNFRSF13C.
RX PubMed=19698991; DOI=10.1016/j.molimm.2009.07.029;
RA Lavorgna A., De Filippi R., Formisano S., Leonardi A.;
RT "TNF receptor-associated factor 1 is a positive regulator of the NF-kappaB
RT alternative pathway.";
RL Mol. Immunol. 46:3278-3282(2009).
RN [29]
RP FUNCTION, AND INTERACTION WITH TNFRSF1A; TNFRSF1B AND TRAF2.
RX PubMed=19287455; DOI=10.1038/onc.2009.29;
RA Wicovsky A., Henkler F., Salzmann S., Scheurich P., Kneitz C., Wajant H.;
RT "Tumor necrosis factor receptor-associated factor-1 enhances
RT proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2
RT cooperation.";
RL Oncogene 28:1769-1781(2009).
RN [30]
RP INTERACTION WITH BIRC2.
RX PubMed=20447407; DOI=10.1016/j.jmb.2010.04.055;
RA Mace P.D., Smits C., Vaux D.L., Silke J., Day C.L.;
RT "Asymmetric recruitment of cIAPs by TRAF2.";
RL J. Mol. Biol. 400:8-15(2010).
RN [31]
RP UBIQUITINATION.
RX PubMed=19937093; DOI=10.1007/s11010-009-0315-y;
RA Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P.,
RA Xing G., He F., Zhang L.;
RT "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination
RT and degradation.";
RL Mol. Cell. Biochem. 338:11-17(2010).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 181-244 IN COMPLEX WITH TRAF2 AND
RP BIRC3, SUBUNIT, AND FUNCTION.
RX PubMed=20385093; DOI=10.1016/j.molcel.2010.03.009;
RA Zheng C., Kabaleeswaran V., Wang Y., Cheng G., Wu H.;
RT "Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2
RT complexes: affinity, specificity, and regulation.";
RL Mol. Cell 38:101-113(2010).
RN [33]
RP VARIANT [LARGE SCALE ANALYSIS] THR-139.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
CC -!- FUNCTION: Adapter molecule that regulates the activation of NF-kappa-B
CC and JNK. Plays a role in the regulation of cell survival and apoptosis.
CC The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-
CC protein ligase complex that promotes ubiquitination of target proteins,
CC such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3
CC protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
CC {ECO:0000269|PubMed:10692572, ECO:0000269|PubMed:16323247,
CC ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:19287455,
CC ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093}.
CC -!- SUBUNIT: Homotrimer (PubMed:15383523, PubMed:20385093). Heterotrimer
CC with TRAF2 (PubMed:8069916, PubMed:19287455, PubMed:20385093).
CC Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40,
CC TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C, TNFRSF18/AITR,
CC TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr
CC virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and RIPK2 (PubMed:10037686,
CC PubMed:10809768, PubMed:10903733, PubMed:11035039, PubMed:11313261,
CC PubMed:16323247, PubMed:19287455, PubMed:19698991, PubMed:8069916,
CC PubMed:8627180, PubMed:8710854, PubMed:9418902, PubMed:9607925,
CC PubMed:9642260, PubMed:9705938, PubMed:9718306, PubMed:9774460).
CC Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3
CC molecule interacts with a heterotrimer formed by TRAF1 and TRAF2
CC (PubMed:11907583, PubMed:20447407, PubMed:20385093). Interacts with
CC NFATC2IP, TRAFD1 and with HIVEP3 (By similarity). Interacts with
CC MAP3K14. Interacts with GPS2 (By similarity).
CC {ECO:0000250|UniProtKB:P39428, ECO:0000269|PubMed:10037686,
CC ECO:0000269|PubMed:10809768, ECO:0000269|PubMed:10903733,
CC ECO:0000269|PubMed:11035039, ECO:0000269|PubMed:11313261,
CC ECO:0000269|PubMed:11907583, ECO:0000269|PubMed:15383523,
CC ECO:0000269|PubMed:16323247, ECO:0000269|PubMed:19287455,
CC ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093,
CC ECO:0000269|PubMed:20447407, ECO:0000269|PubMed:8069916,
CC ECO:0000269|PubMed:8627180, ECO:0000269|PubMed:8710854,
CC ECO:0000269|PubMed:9418902, ECO:0000269|PubMed:9607925,
CC ECO:0000269|PubMed:9642260, ECO:0000269|PubMed:9705938,
CC ECO:0000269|PubMed:9718306, ECO:0000269|PubMed:9774460}.
CC -!- INTERACTION:
CC Q13077; Q9NQ94: A1CF; NbExp=6; IntAct=EBI-359224, EBI-2809489;
CC Q13077; Q08043: ACTN3; NbExp=3; IntAct=EBI-359224, EBI-2880652;
CC Q13077; Q02040-3: AKAP17A; NbExp=3; IntAct=EBI-359224, EBI-10222656;
CC Q13077; P29972: AQP1; NbExp=3; IntAct=EBI-359224, EBI-745213;
CC Q13077; Q03989: ARID5A; NbExp=3; IntAct=EBI-359224, EBI-948603;
CC Q13077; Q8N5N6: ARSJ; NbExp=3; IntAct=EBI-359224, EBI-10266832;
CC Q13077; A0AVN2: BARD1; NbExp=3; IntAct=EBI-359224, EBI-9977322;
CC Q13077; Q99728: BARD1; NbExp=3; IntAct=EBI-359224, EBI-473181;
CC Q13077; P41182: BCL6; NbExp=5; IntAct=EBI-359224, EBI-765407;
CC Q13077; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-359224, EBI-745073;
CC Q13077; Q13490: BIRC2; NbExp=5; IntAct=EBI-359224, EBI-514538;
CC Q13077; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-359224, EBI-8643161;
CC Q13077; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-359224, EBI-747505;
CC Q13077; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-359224, EBI-739879;
CC Q13077; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-359224, EBI-12020542;
CC Q13077; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-359224, EBI-718719;
CC Q13077; Q8IYX3: CCDC116; NbExp=6; IntAct=EBI-359224, EBI-744311;
CC Q13077; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-359224, EBI-744556;
CC Q13077; Q96HB5-4: CCDC120; NbExp=4; IntAct=EBI-359224, EBI-10185348;
CC Q13077; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-359224, EBI-10247802;
CC Q13077; Q8N715: CCDC185; NbExp=3; IntAct=EBI-359224, EBI-740814;
CC Q13077; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-359224, EBI-10238351;
CC Q13077; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-359224, EBI-10175300;
CC Q13077; Q99618: CDCA3; NbExp=6; IntAct=EBI-359224, EBI-739534;
CC Q13077; Q07002: CDK18; NbExp=3; IntAct=EBI-359224, EBI-746238;
CC Q13077; P38936: CDKN1A; NbExp=3; IntAct=EBI-359224, EBI-375077;
CC Q13077; P42772: CDKN2B; NbExp=7; IntAct=EBI-359224, EBI-711280;
CC Q13077; O15519: CFLAR; NbExp=6; IntAct=EBI-359224, EBI-514941;
CC Q13077; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-359224, EBI-743375;
CC Q13077; P10606: COX5B; NbExp=3; IntAct=EBI-359224, EBI-1053725;
CC Q13077; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-359224, EBI-739773;
CC Q13077; Q49AN0: CRY2; NbExp=3; IntAct=EBI-359224, EBI-2212355;
CC Q13077; Q24JT5: CRYGA; NbExp=3; IntAct=EBI-359224, EBI-10239205;
CC Q13077; Q6BCY4: CYB5R2; NbExp=3; IntAct=EBI-359224, EBI-744761;
CC Q13077; Q8TB45: DEPTOR; NbExp=3; IntAct=EBI-359224, EBI-2359040;
CC Q13077; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-359224, EBI-9679045;
CC Q13077; Q7L591: DOK3; NbExp=4; IntAct=EBI-359224, EBI-2834978;
CC Q13077; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-359224, EBI-10694655;
CC Q13077; Q9UII6: DUSP13; NbExp=3; IntAct=EBI-359224, EBI-749800;
CC Q13077; Q9H596: DUSP21; NbExp=3; IntAct=EBI-359224, EBI-7357329;
CC Q13077; Q13115: DUSP4; NbExp=3; IntAct=EBI-359224, EBI-6591081;
CC Q13077; Q9HAK2: EBF2; NbExp=3; IntAct=EBI-359224, EBI-12267154;
CC Q13077; Q13011: ECH1; NbExp=4; IntAct=EBI-359224, EBI-711968;
CC Q13077; Q08426: EHHADH; NbExp=3; IntAct=EBI-359224, EBI-2339219;
CC Q13077; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-359224, EBI-744099;
CC Q13077; Q01844: EWSR1; NbExp=3; IntAct=EBI-359224, EBI-739737;
CC Q13077; Q3B820: FAM161A; NbExp=5; IntAct=EBI-359224, EBI-719941;
CC Q13077; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-359224, EBI-7225287;
CC Q13077; Q9NVL1: FAM86C1P; NbExp=3; IntAct=EBI-359224, EBI-751617;
CC Q13077; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-359224, EBI-10244131;
CC Q13077; Q96D16: FBXL18; NbExp=3; IntAct=EBI-359224, EBI-744419;
CC Q13077; P15408: FOSL2; NbExp=5; IntAct=EBI-359224, EBI-3893419;
CC Q13077; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-359224, EBI-372506;
CC Q13077; P15976-2: GATA1; NbExp=3; IntAct=EBI-359224, EBI-9090198;
CC Q13077; P23769: GATA2; NbExp=3; IntAct=EBI-359224, EBI-2806671;
CC Q13077; Q8WXI9: GATAD2B; NbExp=4; IntAct=EBI-359224, EBI-923440;
CC Q13077; P28676: GCA; NbExp=3; IntAct=EBI-359224, EBI-947242;
CC Q13077; O75603: GCM2; NbExp=3; IntAct=EBI-359224, EBI-10188645;
CC Q13077; P55040: GEM; NbExp=6; IntAct=EBI-359224, EBI-744104;
CC Q13077; Q14161: GIT2; NbExp=2; IntAct=EBI-359224, EBI-1046878;
CC Q13077; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-359224, EBI-12232117;
CC Q13077; O76003: GLRX3; NbExp=5; IntAct=EBI-359224, EBI-374781;
CC Q13077; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-359224, EBI-745707;
CC Q13077; P63218: GNG5; NbExp=3; IntAct=EBI-359224, EBI-10220734;
CC Q13077; Q9H8Y8: GORASP2; NbExp=7; IntAct=EBI-359224, EBI-739467;
CC Q13077; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-359224, EBI-2514791;
CC Q13077; A0A087WSW0: HELT; NbExp=3; IntAct=EBI-359224, EBI-12057631;
CC Q13077; Q9UBP5: HEY2; NbExp=6; IntAct=EBI-359224, EBI-750630;
CC Q13077; O14964: HGS; NbExp=3; IntAct=EBI-359224, EBI-740220;
CC Q13077; P52272: HNRNPM; NbExp=3; IntAct=EBI-359224, EBI-486809;
CC Q13077; P49639: HOXA1; NbExp=3; IntAct=EBI-359224, EBI-740785;
CC Q13077; P09067: HOXB5; NbExp=3; IntAct=EBI-359224, EBI-3893317;
CC Q13077; P31273: HOXC8; NbExp=3; IntAct=EBI-359224, EBI-1752118;
CC Q13077; P35452: HOXD12; NbExp=3; IntAct=EBI-359224, EBI-10206752;
CC Q13077; Q15040: JOSD1; NbExp=3; IntAct=EBI-359224, EBI-2510602;
CC Q13077; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-359224, EBI-2556193;
CC Q13077; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-359224, EBI-10188326;
CC Q13077; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-359224, EBI-6426443;
CC Q13077; P12035: KRT3; NbExp=3; IntAct=EBI-359224, EBI-2430095;
CC Q13077; O95678: KRT75; NbExp=3; IntAct=EBI-359224, EBI-2949715;
CC Q13077; Q6PJG3: LATS1; NbExp=3; IntAct=EBI-359224, EBI-10253976;
CC Q13077; Q96JN0: LCOR; NbExp=3; IntAct=EBI-359224, EBI-746045;
CC Q13077; Q96JN0-2: LCOR; NbExp=3; IntAct=EBI-359224, EBI-10961483;
CC Q13077; Q96GY3: LIN37; NbExp=3; IntAct=EBI-359224, EBI-748884;
CC Q13077; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-359224, EBI-12028858;
CC Q13077; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-359224, EBI-739832;
CC Q13077; Q6UXK5: LRRN1; NbExp=3; IntAct=EBI-359224, EBI-12136157;
CC Q13077; Q96GV9: MACIR; NbExp=3; IntAct=EBI-359224, EBI-2350695;
CC Q13077; Q15555: MAPRE2; NbExp=9; IntAct=EBI-359224, EBI-739717;
CC Q13077; P43243: MATR3; NbExp=3; IntAct=EBI-359224, EBI-352602;
CC Q13077; Q9H7H0: METTL17; NbExp=7; IntAct=EBI-359224, EBI-749353;
CC Q13077; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-359224, EBI-14086479;
CC Q13077; Q6PF18: MORN3; NbExp=8; IntAct=EBI-359224, EBI-9675802;
CC Q13077; P00540: MOS; NbExp=6; IntAct=EBI-359224, EBI-1757866;
CC Q13077; A6NI15: MSGN1; NbExp=3; IntAct=EBI-359224, EBI-11991020;
CC Q13077; Q9P2K5-2: MYEF2; NbExp=3; IntAct=EBI-359224, EBI-10318831;
CC Q13077; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-359224, EBI-744402;
CC Q13077; O76041: NEBL; NbExp=4; IntAct=EBI-359224, EBI-2880203;
CC Q13077; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-359224, EBI-1210753;
CC Q13077; Q9BVL2: NUP58; NbExp=9; IntAct=EBI-359224, EBI-2811583;
CC Q13077; Q7RTU3: OLIG3; NbExp=6; IntAct=EBI-359224, EBI-10225049;
CC Q13077; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-359224, EBI-11022007;
CC Q13077; Q5JS98: PBX3; NbExp=3; IntAct=EBI-359224, EBI-10244393;
CC Q13077; Q96AL5: PBX3; NbExp=3; IntAct=EBI-359224, EBI-741171;
CC Q13077; Q08499: PDE4D; NbExp=3; IntAct=EBI-359224, EBI-1642831;
CC Q13077; Q96BD5: PHF21A; NbExp=4; IntAct=EBI-359224, EBI-745085;
CC Q13077; Q13526: PIN1; NbExp=3; IntAct=EBI-359224, EBI-714158;
CC Q13077; P78337: PITX1; NbExp=3; IntAct=EBI-359224, EBI-748265;
CC Q13077; Q99697-2: PITX2; NbExp=3; IntAct=EBI-359224, EBI-12138495;
CC Q13077; Q16512: PKN1; NbExp=3; IntAct=EBI-359224, EBI-602382;
CC Q13077; Q494U1: PLEKHN1; NbExp=4; IntAct=EBI-359224, EBI-10241513;
CC Q13077; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-359224, EBI-12014286;
CC Q13077; Q3SYA9: POM121L1P; NbExp=3; IntAct=EBI-359224, EBI-10241319;
CC Q13077; Q969H6: POP5; NbExp=6; IntAct=EBI-359224, EBI-366525;
CC Q13077; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-359224, EBI-1105153;
CC Q13077; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-359224, EBI-12000762;
CC Q13077; Q9NQW5: PRDM7; NbExp=3; IntAct=EBI-359224, EBI-10312471;
CC Q13077; P25786: PSMA1; NbExp=3; IntAct=EBI-359224, EBI-359352;
CC Q13077; P20618: PSMB1; NbExp=7; IntAct=EBI-359224, EBI-372273;
CC Q13077; Q2TAL8: QRICH1; NbExp=6; IntAct=EBI-359224, EBI-2798044;
CC Q13077; Q9UJF2: RASAL2; NbExp=3; IntAct=EBI-359224, EBI-359444;
CC Q13077; Q8WWW0: RASSF5; NbExp=3; IntAct=EBI-359224, EBI-367390;
CC Q13077; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-359224, EBI-740773;
CC Q13077; Q8IUH3: RBM45; NbExp=3; IntAct=EBI-359224, EBI-2512147;
CC Q13077; Q8IUH3-3: RBM45; NbExp=3; IntAct=EBI-359224, EBI-10964453;
CC Q13077; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-359224, EBI-1504830;
CC Q13077; Q13546: RIPK1; NbExp=6; IntAct=EBI-359224, EBI-358507;
CC Q13077; Q96MK2: RIPOR3; NbExp=3; IntAct=EBI-359224, EBI-12010512;
CC Q13077; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-359224, EBI-10226430;
CC Q13077; Q14D33: RTP5; NbExp=3; IntAct=EBI-359224, EBI-10217913;
CC Q13077; Q96NU1: SAMD11; NbExp=3; IntAct=EBI-359224, EBI-14067109;
CC Q13077; Q9BWG6: SCNM1; NbExp=8; IntAct=EBI-359224, EBI-748391;
CC Q13077; Q92529: SHC3; NbExp=3; IntAct=EBI-359224, EBI-79084;
CC Q13077; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-359224, EBI-10313866;
CC Q13077; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-359224, EBI-11955083;
CC Q13077; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-359224, EBI-17172855;
CC Q13077; Q6ZT89: SLC25A48; NbExp=3; IntAct=EBI-359224, EBI-10255185;
CC Q13077; P12236: SLC25A6; NbExp=3; IntAct=EBI-359224, EBI-356254;
CC Q13077; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-359224, EBI-9675976;
CC Q13077; Q13573: SNW1; NbExp=3; IntAct=EBI-359224, EBI-632715;
CC Q13077; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-359224, EBI-12288855;
CC Q13077; Q5T0L3: SPATA46; NbExp=3; IntAct=EBI-359224, EBI-750105;
CC Q13077; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-359224, EBI-742688;
CC Q13077; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-359224, EBI-10172867;
CC Q13077; Q13188: STK3; NbExp=6; IntAct=EBI-359224, EBI-992580;
CC Q13077; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-359224, EBI-6872807;
CC Q13077; O95759: TBC1D8; NbExp=3; IntAct=EBI-359224, EBI-10979580;
CC Q13077; O95935: TBX18; NbExp=3; IntAct=EBI-359224, EBI-12085364;
CC Q13077; Q15560: TCEA2; NbExp=3; IntAct=EBI-359224, EBI-710310;
CC Q13077; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-359224, EBI-11746252;
CC Q13077; P56279: TCL1A; NbExp=8; IntAct=EBI-359224, EBI-749995;
CC Q13077; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-359224, EBI-10176734;
CC Q13077; Q15561: TEAD4; NbExp=6; IntAct=EBI-359224, EBI-747736;
CC Q13077; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-359224, EBI-11952651;
CC Q13077; Q01664: TFAP4; NbExp=6; IntAct=EBI-359224, EBI-2514218;
CC Q13077; A0A024R4Q5: TFPT; NbExp=4; IntAct=EBI-359224, EBI-11527449;
CC Q13077; Q9BT49: THAP7; NbExp=6; IntAct=EBI-359224, EBI-741350;
CC Q13077; Q08117: TLE5; NbExp=3; IntAct=EBI-359224, EBI-717810;
CC Q13077; Q08117-2: TLE5; NbExp=6; IntAct=EBI-359224, EBI-11741437;
CC Q13077; Q13077: TRAF1; NbExp=4; IntAct=EBI-359224, EBI-359224;
CC Q13077; Q12933: TRAF2; NbExp=11; IntAct=EBI-359224, EBI-355744;
CC Q13077; Q9Y4K3: TRAF6; NbExp=17; IntAct=EBI-359224, EBI-359276;
CC Q13077; P36406: TRIM23; NbExp=3; IntAct=EBI-359224, EBI-740098;
CC Q13077; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-359224, EBI-5235829;
CC Q13077; Q9Y260: TRPV6; NbExp=3; IntAct=EBI-359224, EBI-750052;
CC Q13077; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-359224, EBI-10687282;
CC Q13077; Q9Y5U2: TSSC4; NbExp=3; IntAct=EBI-359224, EBI-717229;
CC Q13077; O75604: USP2; NbExp=3; IntAct=EBI-359224, EBI-743272;
CC Q13077; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-359224, EBI-11737646;
CC Q13077; Q14119: VEZF1; NbExp=3; IntAct=EBI-359224, EBI-11980193;
CC Q13077; Q9BTA9: WAC; NbExp=3; IntAct=EBI-359224, EBI-749118;
CC Q13077; Q05516: ZBTB16; NbExp=5; IntAct=EBI-359224, EBI-711925;
CC Q13077; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-359224, EBI-740767;
CC Q13077; Q9BQ24: ZFYVE21; NbExp=3; IntAct=EBI-359224, EBI-2849569;
CC Q13077; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-359224, EBI-8656416;
CC Q13077; Q15915: ZIC1; NbExp=3; IntAct=EBI-359224, EBI-11963196;
CC Q13077; Q15973: ZNF124; NbExp=6; IntAct=EBI-359224, EBI-2555767;
CC Q13077; P17024: ZNF20; NbExp=6; IntAct=EBI-359224, EBI-717634;
CC Q13077; P17027: ZNF23; NbExp=3; IntAct=EBI-359224, EBI-5657766;
CC Q13077; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-359224, EBI-740727;
CC Q13077; Q8IYI8: ZNF440; NbExp=7; IntAct=EBI-359224, EBI-726439;
CC Q13077; Q9ULM2: ZNF490; NbExp=3; IntAct=EBI-359224, EBI-1105370;
CC Q13077; Q8TBZ5: ZNF502; NbExp=7; IntAct=EBI-359224, EBI-10273699;
CC Q13077; Q96KM6: ZNF512B; NbExp=7; IntAct=EBI-359224, EBI-1049952;
CC Q13077; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-359224, EBI-10273713;
CC Q13077; Q7Z3I7: ZNF572; NbExp=6; IntAct=EBI-359224, EBI-10172590;
CC Q13077; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-359224, EBI-745520;
CC Q13077; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-359224, EBI-6427977;
CC Q13077; Q7L945: ZNF627; NbExp=3; IntAct=EBI-359224, EBI-2797561;
CC Q13077; Q5T619: ZNF648; NbExp=3; IntAct=EBI-359224, EBI-11985915;
CC Q13077; Q6ZS27-3: ZNF662; NbExp=3; IntAct=EBI-359224, EBI-10255155;
CC Q13077; Q96BR6: ZNF669; NbExp=3; IntAct=EBI-359224, EBI-12006574;
CC Q13077; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-359224, EBI-16429014;
CC Q13077; Q08AG5: ZNF844; NbExp=3; IntAct=EBI-359224, EBI-10225757;
CC Q13077; B2R8Y4; NbExp=3; IntAct=EBI-359224, EBI-10175581;
CC Q13077; Q5W150; NbExp=3; IntAct=EBI-359224, EBI-10248148;
CC Q13077; Q96EJ4; NbExp=5; IntAct=EBI-359224, EBI-750454;
CC Q13077; Q9NWL9; NbExp=3; IntAct=EBI-359224, EBI-10315054;
CC Q13077; P09022: Hoxa1; Xeno; NbExp=4; IntAct=EBI-359224, EBI-3957603;
CC Q13077; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-359224, EBI-25475920;
CC Q13077; P69974: yscK; Xeno; NbExp=2; IntAct=EBI-359224, EBI-2842860;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13077-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13077-2; Sequence=VSP_043092;
CC -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC oligomerization. {ECO:0000269|PubMed:10692572}.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC {ECO:0000269|PubMed:10692572}.
CC -!- DOMAIN: Cleavage by CASP8 liberates a C-terminal fragment that promotes
CC apoptosis and inhibits the activation of NF-kappa-B in response to TNF
CC signaling. {ECO:0000269|PubMed:10692572}.
CC -!- PTM: Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:15468071,
CC ECO:0000269|PubMed:19937093}.
CC -!- CAUTION: Lacks a RING domain and has therefore no E3 ubiquitin-protein
CC ligase activity by itself. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03449.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U19261; AAA62309.1; -; mRNA.
DR EMBL; AK090468; BAC03449.1; ALT_FRAME; mRNA.
DR EMBL; AK295959; BAG58739.1; -; mRNA.
DR EMBL; AK315476; BAG37860.1; -; mRNA.
DR EMBL; AL832989; CAH56343.1; -; mRNA.
DR EMBL; BT019408; AAV38215.1; -; mRNA.
DR EMBL; AC006430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87479.1; -; Genomic_DNA.
DR EMBL; BC024145; AAH24145.1; -; mRNA.
DR CCDS; CCDS55335.1; -. [Q13077-2]
DR CCDS; CCDS6825.1; -. [Q13077-1]
DR PIR; B55649; B55649.
DR RefSeq; NP_001177874.1; NM_001190945.1. [Q13077-1]
DR RefSeq; NP_001177876.1; NM_001190947.1. [Q13077-2]
DR RefSeq; NP_005649.1; NM_005658.4. [Q13077-1]
DR PDB; 3M0D; X-ray; 2.80 A; C=181-244.
DR PDB; 5E1T; X-ray; 2.80 A; A/B/C=220-416.
DR PDB; 5H10; X-ray; 3.21 A; A/B/C=220-416.
DR PDBsum; 3M0D; -.
DR PDBsum; 5E1T; -.
DR PDBsum; 5H10; -.
DR AlphaFoldDB; Q13077; -.
DR SMR; Q13077; -.
DR BioGRID; 113037; 302.
DR DIP; DIP-27514N; -.
DR IntAct; Q13077; 255.
DR MINT; Q13077; -.
DR STRING; 9606.ENSP00000362994; -.
DR iPTMnet; Q13077; -.
DR PhosphoSitePlus; Q13077; -.
DR BioMuta; TRAF1; -.
DR DMDM; 6707734; -.
DR EPD; Q13077; -.
DR jPOST; Q13077; -.
DR MassIVE; Q13077; -.
DR MaxQB; Q13077; -.
DR PaxDb; Q13077; -.
DR PeptideAtlas; Q13077; -.
DR PRIDE; Q13077; -.
DR ProteomicsDB; 59136; -. [Q13077-1]
DR ProteomicsDB; 59137; -. [Q13077-2]
DR Antibodypedia; 807; 384 antibodies from 41 providers.
DR DNASU; 7185; -.
DR Ensembl; ENST00000373887.8; ENSP00000362994.3; ENSG00000056558.11. [Q13077-1]
DR Ensembl; ENST00000540010.1; ENSP00000443183.1; ENSG00000056558.11. [Q13077-1]
DR Ensembl; ENST00000546084.5; ENSP00000438583.1; ENSG00000056558.11. [Q13077-2]
DR GeneID; 7185; -.
DR KEGG; hsa:7185; -.
DR MANE-Select; ENST00000373887.8; ENSP00000362994.3; NM_005658.5; NP_005649.1.
DR UCSC; uc004bku.3; human. [Q13077-1]
DR CTD; 7185; -.
DR DisGeNET; 7185; -.
DR GeneCards; TRAF1; -.
DR HGNC; HGNC:12031; TRAF1.
DR HPA; ENSG00000056558; Tissue enhanced (lymphoid).
DR MIM; 601711; gene.
DR neXtProt; NX_Q13077; -.
DR OpenTargets; ENSG00000056558; -.
DR PharmGKB; PA36708; -.
DR VEuPathDB; HostDB:ENSG00000056558; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000161076; -.
DR HOGENOM; CLU_021061_0_0_1; -.
DR InParanoid; Q13077; -.
DR OMA; CSWSGIM; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; Q13077; -.
DR TreeFam; TF321154; -.
DR PathwayCommons; Q13077; -.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR SignaLink; Q13077; -.
DR SIGNOR; Q13077; -.
DR BioGRID-ORCS; 7185; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; TRAF1; human.
DR EvolutionaryTrace; Q13077; -.
DR GeneWiki; TRAF1; -.
DR GenomeRNAi; 7185; -.
DR Pharos; Q13077; Tbio.
DR PRO; PR:Q13077; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13077; protein.
DR Bgee; ENSG00000056558; Expressed in granulocyte and 106 other tissues.
DR Genevisible; Q13077; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR CDD; cd03779; MATH_TRAF1; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
DR InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR027136; TRAF1.
DR InterPro; IPR037306; TRAF1_MATH.
DR InterPro; IPR032070; TRAF_BIRC3-bd.
DR PANTHER; PTHR10131; PTHR10131; 1.
DR PANTHER; PTHR10131:SF96; PTHR10131:SF96; 1.
DR Pfam; PF16673; TRAF_BIRC3_bd; 1.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..416
FT /note="TNF receptor-associated factor 1"
FT /id="PRO_0000056397"
FT DOMAIN 266..412
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..264
FT SITE 163..164
FT /note="Cleavage; by CASP8"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39428"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:15468071"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:15468071"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043092"
FT VARIANT 139
FT /note="M -> T (in dbSNP:rs113495277)"
FT /evidence="ECO:0000269|PubMed:18987736"
FT /id="VAR_054161"
FT MUTAGEN 163
FT /note="D->A: Abolishes CASP8-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:10692572,
FT ECO:0000269|PubMed:16323247"
FT MUTAGEN 185
FT /note="K->R: Nearly abolished ubiquitination; when
FT associated with R-193."
FT /evidence="ECO:0000269|PubMed:15468071"
FT MUTAGEN 193
FT /note="K->R: Nearly abolished ubiquitination; when
FT associated with R-185."
FT /evidence="ECO:0000269|PubMed:15468071"
FT HELIX 183..241
FT /evidence="ECO:0007829|PDB:3M0D"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:5E1T"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:5E1T"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5E1T"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5E1T"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:5E1T"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:5E1T"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:5H10"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:5E1T"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:5H10"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5E1T"
FT STRAND 405..412
FT /evidence="ECO:0007829|PDB:5E1T"
SQ SEQUENCE 416 AA; 46164 MW; A956A123A40D284A CRC64;
MASSSGSSPR PAPDENEFPF GCPPTVCQDP KEPRALCCAG CLSENPRNGE DQICPKCRGE
DLQSISPGSR LRTQEKAHPE VAEAGIGCPF AGVGCSFKGS PQSVQEHEVT SQTSHLNLLL
GFMKQWKARL GCGLESGPMA LEQNLSDLQL QAAVEVAGDL EVDCYRAPCS ESQEELALQH
FMKEKLLAEL EGKLRVFENI VAVLNKEVEA SHLALATSIH QSQLDRERIL SLEQRVVELQ
QTLAQKDQAL GKLEQSLRLM EEASFDGTFL WKITNVTRRC HESACGRTVS LFSPAFYTAK
YGYKLCLRLY LNGDGTGKRT HLSLFIVIMR GEYDALLPWP FRNKVTFMLL DQNNREHAID
AFRPDLSSAS FQRPQSETNV ASGCPLFFPL SKLQSPKHAY VKDDTMFLKC IVETST
