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TNF receptor-associated factor 3 (EC 2 3 2 27) (CAP-1) (CD40 receptor-associated factor 1) (CRAF1) (CD40-binding protein) (CD40BP) (LMP1-associated protein 1) (LAP1) (RING-type E3 ubiquitin transferase TRAF3)

 TRAF3_HUMAN             Reviewed;         568 AA.
Q13114; B7Z8C4; Q12990; Q13076; Q13947; Q6AZX1; Q9UNL1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
17-JUN-2020, entry version 225.
RecName: Full=TNF receptor-associated factor 3;
EC=2.3.2.27;
AltName: Full=CAP-1;
AltName: Full=CD40 receptor-associated factor 1;
Short=CRAF1;
AltName: Full=CD40-binding protein;
Short=CD40BP;
AltName: Full=LMP1-associated protein 1;
Short=LAP1;
AltName: Full=RING-type E3 ubiquitin transferase TRAF3 {ECO:0000305};
Name=TRAF3; Synonyms=CAP1, CRAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TNFRSF5.
PubMed=7527023;
Hu H.M., O'Rourke K., Boguski M.S., Dixit V.M.;
"A novel RING finger protein interacts with the cytoplasmic domain of
CD40.";
J. Biol. Chem. 269:30069-30072(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND INTERACTION
WITH EBV LMP-1.
TISSUE=Lymphoma;
PubMed=7859281; DOI=10.1016/0092-8674(95)90489-1;
Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C.,
Kieff E.;
"The Epstein-Barr virus transforming protein LMP1 engages signaling
proteins for the tumor necrosis factor receptor family.";
Cell 80:389-399(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, AND
VARIANT THR-129.
TISSUE=Fetal brain;
PubMed=7530216; DOI=10.1016/0014-5793(94)01406-q;
Sato T., Irie S., Reed J.C.;
"A novel member of the TRAF family of putative signal transducing proteins
binds to the cytosolic domain of CD40.";
FEBS Lett. 358:113-118(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, AND
VARIANT THR-129.
PubMed=7533327; DOI=10.1126/science.7533327;
Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.;
"Involvement of CRAF1, a relative of TRAF, in CD40 signaling.";
Science 267:1494-1498(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 536-568.
PubMed=10199393; DOI=10.1016/s0161-5890(98)00099-6;
van Eyndhoven W.G., Frank D., Kalachikov S., Cleary A.M., Hong D.I.,
Cho E., Nasr S., Perez A.J., Mackus W.J.M., Cayanis E., Wellington S.,
Fischer S.G., Warburton D., Lederman S.;
"A single gene for human TRAF-3 at chromosome 14q32.3 encodes a variety of
mRNA species by alternative polyadenylation, mRNA splicing and
transcription initiation.";
Mol. Immunol. 35:1189-1206(1998).
[10]
INTERACTION WITH LTBR.
PubMed=8663299; DOI=10.1074/jbc.271.25.14661;
Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H.,
Okumura K.;
"TRAF5, an activator of NF-kappaB and putative signal transducer for the
lymphotoxin-beta receptor.";
J. Biol. Chem. 271:14661-14664(1996).
[11]
INTERACTION WITH TANK.
PubMed=8710854; DOI=10.1073/pnas.93.16.8241;
Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.;
"I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated
signal transduction.";
Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996).
[12]
INTERACTION WITH TNFRSF8.
PubMed=9168896; DOI=10.1006/bbrc.1997.6509;
Boucher L.-M., Marengere L.E., Lu Y., Thukral S., Mak T.W.;
"Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other
members of the TNF receptor superfamily.";
Biochem. Biophys. Res. Commun. 233:592-600(1997).
[13]
INTERACTION WITH TNFRSF14.
PubMed=9162022; DOI=10.1074/jbc.272.22.14029;
Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.;
"Herpesvirus entry mediator, a member of the tumor necrosis factor receptor
(TNFR) family, interacts with members of the TNFR-associated factor family
and activates the transcription factors NF-kappaB and AP-1.";
J. Biol. Chem. 272:14029-14032(1997).
[14]
INTERACTION WITH MAP3K14.
PubMed=9275204; DOI=10.1073/pnas.94.18.9792;
Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M.;
"Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of
nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at
TNF receptor-associated factor 2.";
Proc. Natl. Acad. Sci. U.S.A. 94:9792-9796(1997).
[15]
INTERACTION WITH TNFRSF5 AND TRAF5.
PubMed=9718306; DOI=10.1021/bi981067q;
Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.;
"CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions:
regulation of CD40 signaling through multiple TRAF binding sites and TRAF
hetero-oligomerization.";
Biochemistry 37:11836-11845(1998).
[16]
INTERACTION WITH TNFRSF4.
PubMed=9488716; DOI=10.1074/jbc.273.10.5808;
Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.;
"Activation of OX40 signal transduction pathways leads to tumor necrosis
factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB
activation.";
J. Biol. Chem. 273:5808-5814(1998).
[17]
INTERACTION WITH TNFRSF11A.
PubMed=9774460; DOI=10.1074/jbc.273.43.28355;
Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.;
"The TRAF family of signal transducers mediates NF-kappaB activation by the
TRANCE receptor.";
J. Biol. Chem. 273:28355-28359(1998).
[18]
INTERACTION WITH MAP3K5.
PubMed=9774977; DOI=10.1016/s1097-2765(00)80283-x;
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M.,
Miyazono K., Ichijo H.;
"ASK1 is essential for JNK/SAPK activation by TRAF2.";
Mol. Cell 2:389-395(1998).
[19]
INTERACTION WITH TNFRSF4 AND TNFRSF9.
PubMed=9418902; DOI=10.1128/mcb.18.1.558;
Arch R.H., Thompson C.B.;
"4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth
factor receptor subfamily that bind TNF receptor-associated factors and
activate nuclear factor kappaB.";
Mol. Cell. Biol. 18:558-565(1998).
[20]
INTERACTION WITH TNFRSF18.
TISSUE=T-cell;
PubMed=10037686; DOI=10.1074/jbc.274.10.6056;
Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D.,
Wang S.-X., Kwon B.S.;
"Identification of a novel activation-inducible protein of the tumor
necrosis factor receptor superfamily and its ligand.";
J. Biol. Chem. 274:6056-6061(1999).
[21]
INTERACTION WITH MAP3K5.
PubMed=10523862; DOI=10.1038/sj.onc.1202975;
Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.;
"Mediation of TNF receptor-associated factor effector functions by
apoptosis signal-regulating kinase-1 (ASK1).";
Oncogene 18:5814-5820(1999).
[22]
INTERACTION WITH TNFRSF19.
PubMed=10809768; DOI=10.1074/jbc.275.20.15336;
Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.;
"TAJ, a novel member of the tumor necrosis factor receptor family,
activates the c-Jun N-terminal kinase pathway and mediates caspase-
independent cell death.";
J. Biol. Chem. 275:15336-15342(2000).
[23]
INTERACTION WITH TTRAP.
PubMed=10764746; DOI=10.1074/jbc.m000531200;
Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I.,
Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.;
"TTRAP, a novel protein that associates with CD40, tumor necrosis factor
(TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that
inhibits nuclear factor-kappa B activation.";
J. Biol. Chem. 275:18586-18593(2000).
[24]
INTERACTION WITH TRAF3IP1.
PubMed=10791955; DOI=10.1074/jbc.m001095200;
Ling L., Goeddel D.V.;
"MIP-T3, a novel protein linking tumor necrosis factor receptor-associated
factor 3 to the microtubule network.";
J. Biol. Chem. 275:23852-23860(2000).
[25]
INTERACTION WITH TNFRSF17.
PubMed=10903733; DOI=10.4049/jimmunol.165.3.1322;
Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J.,
Devergne O., Tsapis A.;
"TNF receptor family member BCMA (B cell maturation) associates with TNF
receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-
kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein
kinase.";
J. Immunol. 165:1322-1330(2000).
[26]
INTERACTION WITH EDAR.
PubMed=11035039; DOI=10.1074/jbc.m008356200;
Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.;
"The ectodermal dysplasia receptor activates the nuclear factor-kappaB,
JNK, and cell death pathways and binds to ectodysplasin A.";
J. Biol. Chem. 276:2668-2677(2001).
[27]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=15383523; DOI=10.1074/jbc.m407284200;
He L., Grammer A.C., Wu X., Lipsky P.E.;
"TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate
NF-{kappa}B activation.";
J. Biol. Chem. 279:55855-55865(2004).
[28]
FUNCTION, PROTEASOMAL DEGRADATION, AND INTERACTION WITH MAP3K14.
PubMed=15084608; DOI=10.1074/jbc.m403286200;
Liao G., Zhang M., Harhaj E.W., Sun S.C.;
"Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor
receptor-associated factor 3-induced degradation.";
J. Biol. Chem. 279:26243-26250(2004).
[29]
INTERACTION WITH OTUD5 AND TBK1, FUNCTION AS E3 PROTEIN-UBIQUITIN LIGASE,
AND UBIQUITINATION.
PubMed=17991829; DOI=10.1126/science.1145918;
Kayagaki N., Phung Q., Chan S., Chaudhari R., Quan C., O'Rourke K.M.,
Eby M., Pietras E., Cheng G., Bazan J.F., Zhang Z., Arnott D., Dixit V.M.;
"DUBA: a deubiquitinase that regulates type I interferon production.";
Science 318:1628-1632(2007).
[30]
INTERACTION WITH SRC.
PubMed=19419966; DOI=10.1074/jbc.m808233200;
Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.;
"The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-
elicited antiviral signaling.";
J. Biol. Chem. 284:19122-19131(2009).
[31]
UBIQUITINATION, MUTAGENESIS OF TYR-441 AND GLN-443, AND INTERACTION WITH
RNF216 AND MAVS.
PubMed=19893624; DOI=10.1371/journal.ppat.1000650;
Nakhaei P., Mesplede T., Solis M., Sun Q., Zhao T., Yang L., Chuang T.H.,
Ware C.F., Lin R., Hiscott J.;
"The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
signaling pathway by targeting TRAF3 for degradation.";
PLoS Pathog. 5:E1000650-E1000650(2009).
[32]
UBIQUITINATION, AND INTERACTION WITH OTUB1 AND OTUB2.
PubMed=19996094; DOI=10.1074/jbc.m109.074971;
Li S., Zheng H., Mao A.P., Zhong B., Li Y., Liu Y., Gao Y., Ran Y.,
Tien P., Shu H.B.;
"Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated
deubiquitination of TRAF3 and TRAF6.";
J. Biol. Chem. 285:4291-4297(2010).
[33]
FUNCTION, INTERACTION WITH BIRC2 AND BIRC3, SUBCELLULAR LOCATION, AND
UBIQUITINATION.
PubMed=20097753; DOI=10.1074/jbc.m109.071043;
Mao A.P., Li S., Zhong B., Li Y., Yan J., Li Q., Teng C., Shu H.B.;
"Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for
induction of interferon-beta (IFN-beta) and cellular antiviral response.";
J. Biol. Chem. 285:9470-9476(2010).
[34]
FUNCTION.
PubMed=20185819; DOI=10.1074/jbc.m109.076091;
Bista P., Zeng W., Ryan S., Bailly V., Browning J.L., Lukashev M.E.;
"TRAF3 controls activation of the canonical and alternative NFkappaB by the
lymphotoxin beta receptor.";
J. Biol. Chem. 285:12971-12978(2010).
[35]
UBIQUITINATION, AND FUNCTION.
PubMed=19937093; DOI=10.1007/s11010-009-0315-y;
Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P.,
Xing G., He F., Zhang L.;
"Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination
and degradation.";
Mol. Cell. Biochem. 338:11-17(2010).
[36]
INTERACTION WITH OPTN AND TBK1.
PubMed=20174559; DOI=10.1371/journal.ppat.1000778;
Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M.,
Kohl A., Elliott R.M., Macdonald A.;
"Optineurin negatively regulates the induction of IFNbeta in response to
RNA virus infection.";
PLoS Pathog. 6:E1000778-E1000778(2010).
[37]
INTERACTION WITH CARD14.
PubMed=21302310; DOI=10.1002/jcp.22667;
Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.;
"Alternative splicing of CARMA2/CARD14 transcripts generates protein
variants with differential effect on NF-kappaB activation and endoplasmic
reticulum stress-induced cell death.";
J. Cell. Physiol. 226:3121-3131(2011).
[38]
INTERACTION WITH PTPN22.
PubMed=23871208; DOI=10.1016/j.immuni.2013.06.013;
Wang Y., Shaked I., Stanford S.M., Zhou W., Curtsinger J.M., Mikulski Z.,
Shaheen Z.R., Cheng G., Sawatzke K., Campbell A.M., Auger J.L., Bilgic H.,
Shoyama F.M., Schmeling D.O., Balfour H.H. Jr., Hasegawa K., Chan A.C.,
Corbett J.A., Binstadt B.A., Mescher M.F., Ley K., Bottini N.,
Peterson E.J.;
"The autoimmunity-associated gene PTPN22 potentiates toll-like receptor-
driven, type 1 interferon-dependent immunity.";
Immunity 39:111-122(2013).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[40]
INTERACTION WITH DDX3X; IKBKE; IRF3 AND MAVS, UBIQUITINATION, AND
MUTAGENESIS OF 68-CYS--HIS-70.
PubMed=27980081; DOI=10.1042/bcj20160956;
Gu L., Fullam A., McCormack N., Hoehn Y., Schroeder M.;
"DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-
ordinate assembly of signalling complexes downstream from MAVS.";
Biochem. J. 474:571-587(2017).
[41]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 341-568, AND X-RAY CRYSTALLOGRAPHY
(3.5 ANGSTROMS) OF 341-568 IN COMPLEX WITH TNFRSF5.
PubMed=10984535; DOI=10.1073/pnas.97.19.10395;
Ni C.Z., Welsh K., Leo E., Chiou C.K., Wu H., Reed J.C., Ely K.R.;
"Molecular basis for CD40 signaling mediated by TRAF3.";
Proc. Natl. Acad. Sci. U.S.A. 97:10395-10399(2000).
[42]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH TANK, AND
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF5.
PubMed=12005438; DOI=10.1016/s0969-2126(02)00733-5;
Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C.,
Satterthwait A.C., Cheng G., Ely K.R.;
"Downstream regulator TANK binds to the CD40 recognition site on TRAF3.";
Structure 10:403-411(2002).
[43]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH LTBR,
MUTAGENESIS OF TYR-459; PHE-512 AND PHE-521, INTERACTION WITH TANK AND
CD40, AND SUBUNIT.
PubMed=14517219; DOI=10.1074/jbc.m309381200;
Li C., Norris P.S., Ni C.Z., Havert M.L., Chiong E.M., Tran B.R.,
Cabezas E., Reed J.C., Satterthwait A.C., Ware C.F., Ely K.R.;
"Structurally distinct recognition motifs in lymphotoxin-beta receptor and
CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated
signaling.";
J. Biol. Chem. 278:50523-50529(2003).
[44]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF13C
PEPTIDE, SUBUNIT, AND INTERACTION WITH TNFRSF13C.
PubMed=15585864; DOI=10.4049/jimmunol.173.12.7394;
Ni C.Z., Oganesyan G., Welsh K., Zhu X., Reed J.C., Satterthwait A.C.,
Cheng G., Ely K.R.;
"Key molecular contacts promote recognition of the BAFF receptor by TNF
receptor-associated factor 3: implications for intracellular signaling
regulation.";
J. Immunol. 173:7394-7400(2004).
[45]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 377-568 IN COMPLEX WITH
EPSTEIN-BARR VIRUS PROTEIN LMP1, AND SUBUNIT.
PubMed=16009714; DOI=10.1074/jbc.m502511200;
Wu S., Xie P., Welsh K., Li C., Ni C.Z., Zhu X., Reed J.C.,
Satterthwait A.C., Bishop G.A., Ely K.R.;
"LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B
lymphocytes for binding to TRAF3.";
J. Biol. Chem. 280:33620-33626(2005).
[46]
STRUCTURE BY NMR OF 43-101.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the zinc finger, C3HC4 type (RING finger) domain of
TNF receptor-associated factor 3.";
Submitted (FEB-2008) to the PDB data bank.
[47]
VARIANT IIAE5 TRP-118.
PubMed=20832341; DOI=10.1016/j.immuni.2010.08.014;
Perez de Diego R., Sancho-Shimizu V., Lorenzo L., Puel A., Plancoulaine S.,
Picard C., Herman M., Cardon A., Durandy A., Bustamante J.,
Vallabhapurapu S., Bravo J., Warnatz K., Chaix Y., Cascarrigny F.,
Lebon P., Rozenberg F., Karin M., Tardieu M., Al-Muhsen S., Jouanguy E.,
Zhang S.Y., Abel L., Casanova J.L.;
"Human TRAF3 adaptor molecule deficiency leads to impaired Toll-like
receptor 3 response and susceptibility to herpes simplex encephalitis.";
Immunity 33:400-411(2010).
-!- FUNCTION: Regulates pathways leading to the activation of NF-kappa-B
and MAP kinases, and plays a central role in the regulation of B-cell
survival. Part of signaling pathways leading to the production of
cytokines and interferon. Required for normal antibody isotype
switching from IgM to IgG. Plays a role T-cell dependent immune
responses. Plays a role in the regulation of antiviral responses. Is an
essential constituent of several E3 ubiquitin-protein ligase complexes.
May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-
linked ubiquitination of target proteins. Inhibits activation of NF-
kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated
activation of NF-kappa-B. Down-regulates proteolytic processing of
NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B.
Promotes ubiquitination and proteasomal degradation of MAP3K14.
{ECO:0000269|PubMed:15084608, ECO:0000269|PubMed:15383523,
ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:19937093,
ECO:0000269|PubMed:20097753, ECO:0000269|PubMed:20185819}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
[acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
EC=2.3.2.27;
-!- SUBUNIT: Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with
LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C
TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14,
TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with
TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same
binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts
with OTUB1, OTUB2 and OTUD5. Interacts with RNF216, OPTN and TBK1.
Identified in a complex with TRAF2, MAP3K14 and BIRC3. Interacts with
BIRC2 and BIRC3. Upon exposure to bacterial lipopolysaccharide (LPS),
recruited to a transient complex containing TLR4, TRAF3, TRAF6, IKBKG,
MAP3K7, MYD88, TICAM1, BIRC2, BIRC3 and UBE2N (By similarity).
Interacts with Epstein-Barr virus protein LMP1. Interacts (via RING-
type zinc finger domain) with SRC. Interacts with CARD14. Interacts
(via MATH domain) with PTPN22; the interaction promotes TRAF3
polyubiquitination (PubMed:23871208). Interacts with MAVS
(PubMed:19893624, PubMed:27980081). Directly interacts with DDX3X; this
interaction stimulates TRAF3 'Lys-63' ubiquitination (PubMed:27980081).
Interacts with IRF3 (PubMed:27980081). Interacts with IKBKE in the
course of Sendai virus infection (PubMed:27980081). {ECO:0000250,
ECO:0000269|PubMed:10037686, ECO:0000269|PubMed:10523862,
ECO:0000269|PubMed:10764746, ECO:0000269|PubMed:10791955,
ECO:0000269|PubMed:10809768, ECO:0000269|PubMed:10903733,
ECO:0000269|PubMed:10984535, ECO:0000269|PubMed:11035039,
ECO:0000269|PubMed:12005438, ECO:0000269|PubMed:14517219,
ECO:0000269|PubMed:15084608, ECO:0000269|PubMed:15383523,
ECO:0000269|PubMed:15585864, ECO:0000269|PubMed:16009714,
ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:19419966,
ECO:0000269|PubMed:19893624, ECO:0000269|PubMed:19996094,
ECO:0000269|PubMed:20097753, ECO:0000269|PubMed:20174559,
ECO:0000269|PubMed:21302310, ECO:0000269|PubMed:23871208,
ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:7527023,
ECO:0000269|PubMed:7530216, ECO:0000269|PubMed:7533327,
ECO:0000269|PubMed:7859281, ECO:0000269|PubMed:8663299,
ECO:0000269|PubMed:8710854, ECO:0000269|PubMed:9162022,
ECO:0000269|PubMed:9168896, ECO:0000269|PubMed:9275204,
ECO:0000269|PubMed:9418902, ECO:0000269|PubMed:9488716,
ECO:0000269|PubMed:9718306, ECO:0000269|PubMed:9774460,
ECO:0000269|PubMed:9774977}.
-!- INTERACTION:
Q13114; Q8N9N2-2: ASCC1; NbExp=3; IntAct=EBI-357631, EBI-10962548;
Q13114; Q86UB2: BIVM; NbExp=6; IntAct=EBI-357631, EBI-12191873;
Q13114; P15056: BRAF; NbExp=2; IntAct=EBI-357631, EBI-365980;
Q13114; Q5T681: C10orf62; NbExp=3; IntAct=EBI-357631, EBI-744052;
Q13114; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-357631, EBI-10961312;
Q13114; Q52MB2: CCDC184; NbExp=3; IntAct=EBI-357631, EBI-10179526;
Q13114; P25942: CD40; NbExp=3; IntAct=EBI-357631, EBI-525714;
Q13114; Q16543: CDC37; NbExp=3; IntAct=EBI-357631, EBI-295634;
Q13114; Q9HAV5: EDA2R; NbExp=2; IntAct=EBI-357631, EBI-526033;
Q13114; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-357631, EBI-948296;
Q13114; Q9Y547: HSPB11; NbExp=3; IntAct=EBI-357631, EBI-747101;
Q13114; Q96PC2: IP6K3; NbExp=5; IntAct=EBI-357631, EBI-10990676;
Q13114; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-357631, EBI-739832;
Q13114; P36941: LTBR; NbExp=2; IntAct=EBI-357631, EBI-3509981;
Q13114; Q99558: MAP3K14; NbExp=7; IntAct=EBI-357631, EBI-358011;
Q13114; Q17RL8: PDZD4; NbExp=3; IntAct=EBI-357631, EBI-10239064;
Q13114; O75928-2: PIAS2; NbExp=3; IntAct=EBI-357631, EBI-348567;
Q13114; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-357631, EBI-11956563;
Q13114; P28062-2: PSMB8; NbExp=3; IntAct=EBI-357631, EBI-372312;
Q13114; Q9Y2R2: PTPN22; NbExp=2; IntAct=EBI-357631, EBI-1211241;
Q13114; P54725: RAD23A; NbExp=3; IntAct=EBI-357631, EBI-746453;
Q13114; Q13546: RIPK1; NbExp=3; IntAct=EBI-357631, EBI-358507;
Q13114; O43353: RIPK2; NbExp=5; IntAct=EBI-357631, EBI-358522;
Q13114; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-357631, EBI-10226430;
Q13114; P78317: RNF4; NbExp=3; IntAct=EBI-357631, EBI-2340927;
Q13114; O95721: SNAP29; NbExp=4; IntAct=EBI-357631, EBI-490676;
Q13114; Q92844: TANK; NbExp=6; IntAct=EBI-357631, EBI-356349;
Q13114; Q13114: TRAF3; NbExp=5; IntAct=EBI-357631, EBI-357631;
Q13114; Q8TDR0: TRAF3IP1; NbExp=8; IntAct=EBI-357631, EBI-928811;
Q13114; O00463: TRAF5; NbExp=4; IntAct=EBI-357631, EBI-523498;
Q13114; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357631, EBI-10180829;
Q13114; P61964: WDR5; NbExp=2; IntAct=EBI-357631, EBI-540834;
Q13114; Q96HA8: WDYHV1; NbExp=3; IntAct=EBI-357631, EBI-741158;
Q13114; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-357631, EBI-2859943;
Q13114; Q15326: ZMYND11; NbExp=2; IntAct=EBI-357631, EBI-2623509;
Q13114; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-357631, EBI-7252920;
Q13114; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-357631, EBI-6115874;
Q13114; P15314: Irf1; Xeno; NbExp=2; IntAct=EBI-357631, EBI-6115486;
Q13114; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-357631, EBI-6115394;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Endosome
{ECO:0000250|UniProtKB:Q60803}. Mitochondrion. Note=Undergoes
endocytosis together with TLR4 upon LPS signaling (By similarity).
Associated with mitochondria in response to virus.
{ECO:0000250|UniProtKB:Q60803}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13114-1; Sequence=Displayed;
Name=2;
IsoId=Q13114-2; Sequence=VSP_040040;
-!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
-!- DOMAIN: The Ring-type zinc finger domain is required for its function
in down-regulation of NFKB2 proteolytic processing.
{ECO:0000250|UniProtKB:Q60803}.
-!- PTM: Undergoes 'Lys-48'-linked polyubiquitination, leading to its
proteasomal degradation in response to signaling by TNFSF13B, TLR4 or
through CD40. 'Lys-48'-linked polyubiquitinated form is deubiquitinated
by OTUD7B, preventing TRAF3 proteolysis and over-activation of non-
canonical NF-kappa-B. Undergoes 'Lys-63'-linked ubiquitination during
early stages of virus infection, and 'Lys-48'-linked ubiquitination
during later stages. Undergoes both 'Lys-48'-linked and 'Lys-63'-linked
ubiquitination in response to TLR3 and TLR4 signaling. Deubiquitinated
by OTUB1, OTUB2 and OTUD5. {ECO:0000269|PubMed:17991829,
ECO:0000269|PubMed:19893624, ECO:0000269|PubMed:19937093,
ECO:0000269|PubMed:19996094, ECO:0000269|PubMed:20097753,
ECO:0000269|PubMed:27980081}.
-!- DISEASE: Encephalopathy, acute, infection-induced, Herpes-specific, 5
(IIAE5) [MIM:614849]: A rare complication of human herpesvirus 1 (HHV-
1) infection, occurring in only a small minority of HHV-1 infected
individuals. It is characterized by hemorrhagic necrosis of parts of
the temporal and frontal lobes. Onset is over several days and involves
fever, headache, seizures, stupor, and often coma, frequently with a
fatal outcome. {ECO:0000269|PubMed:20832341}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TRAF3ID271.html";
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EMBL; U15637; AAA56753.1; -; mRNA.
EMBL; U19260; AAA65732.1; -; mRNA.
EMBL; L38509; AAA68195.1; -; mRNA.
EMBL; U21092; AAC50112.1; -; mRNA.
EMBL; BX247977; CAD62311.1; -; mRNA.
EMBL; AK303172; BAH13910.1; -; mRNA.
EMBL; AL117209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC075087; AAH75087.1; -; mRNA.
EMBL; BC075086; AAH75086.1; -; mRNA.
EMBL; AF110908; AAD29276.1; -; mRNA.
CCDS; CCDS55946.1; -. [Q13114-2]
CCDS; CCDS9975.1; -. [Q13114-1]
PIR; A55960; A55960.
PIR; S68467; S68467.
RefSeq; NP_001186356.1; NM_001199427.1. [Q13114-2]
RefSeq; NP_003291.2; NM_003300.3. [Q13114-1]
RefSeq; NP_663777.1; NM_145725.2. [Q13114-1]
RefSeq; NP_663778.1; NM_145726.2.
RefSeq; XP_011535420.1; XM_011537118.2. [Q13114-2]
RefSeq; XP_016877106.1; XM_017021617.1. [Q13114-1]
RefSeq; XP_016877107.1; XM_017021618.1. [Q13114-1]
PDB; 1FLK; X-ray; 2.80 A; A/B=341-568.
PDB; 1FLL; X-ray; 3.50 A; A/B=341-568.
PDB; 1KZZ; X-ray; 3.50 A; A=377-568.
PDB; 1L0A; X-ray; 2.90 A; A=377-568.
PDB; 1RF3; X-ray; 3.50 A; A=377-568.
PDB; 1ZMS; X-ray; 2.80 A; A=377-568.
PDB; 2ECY; NMR; -; A=43-101.
PDB; 2GKW; X-ray; 2.70 A; A=377-568.
PDBsum; 1FLK; -.
PDBsum; 1FLL; -.
PDBsum; 1KZZ; -.
PDBsum; 1L0A; -.
PDBsum; 1RF3; -.
PDBsum; 1ZMS; -.
PDBsum; 2ECY; -.
PDBsum; 2GKW; -.
SMR; Q13114; -.
BioGRID; 113039; 134.
CORUM; Q13114; -.
DIP; DIP-6222N; -.
IntAct; Q13114; 71.
MINT; Q13114; -.
STRING; 9606.ENSP00000454207; -.
MoonDB; Q13114; Predicted.
iPTMnet; Q13114; -.
PhosphoSitePlus; Q13114; -.
BioMuta; TRAF3; -.
DMDM; 116242824; -.
EPD; Q13114; -.
jPOST; Q13114; -.
MassIVE; Q13114; -.
MaxQB; Q13114; -.
PaxDb; Q13114; -.
PeptideAtlas; Q13114; -.
PRIDE; Q13114; -.
ProteomicsDB; 59165; -. [Q13114-1]
ProteomicsDB; 59166; -. [Q13114-2]
Antibodypedia; 129; 510 antibodies.
Ensembl; ENST00000392745; ENSP00000376500; ENSG00000131323. [Q13114-1]
Ensembl; ENST00000539721; ENSP00000445998; ENSG00000131323. [Q13114-2]
Ensembl; ENST00000560371; ENSP00000454207; ENSG00000131323. [Q13114-1]
GeneID; 7187; -.
KEGG; hsa:7187; -.
UCSC; uc001ymc.3; human. [Q13114-1]
CTD; 7187; -.
DisGeNET; 7187; -.
EuPathDB; HostDB:ENSG00000131323.14; -.
GeneCards; TRAF3; -.
HGNC; HGNC:12033; TRAF3.
HPA; ENSG00000131323; Low tissue specificity.
MalaCards; TRAF3; -.
MIM; 601896; gene.
MIM; 614849; phenotype.
neXtProt; NX_Q13114; -.
OpenTargets; ENSG00000131323; -.
Orphanet; 1930; Herpes simplex virus encephalitis.
PharmGKB; PA36710; -.
eggNOG; ENOG410ISDV; Eukaryota.
eggNOG; ENOG410YQ97; LUCA.
GeneTree; ENSGT00940000160538; -.
HOGENOM; CLU_021061_4_1_1; -.
InParanoid; Q13114; -.
KO; K03174; -.
OMA; MVTLQKH; -.
OrthoDB; 918518at2759; -.
PhylomeDB; Q13114; -.
TreeFam; TF321154; -.
Reactome; R-HSA-5602571; TRAF3 deficiency - HSE.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
SignaLink; Q13114; -.
SIGNOR; Q13114; -.
BioGRID-ORCS; 7187; 9 hits in 795 CRISPR screens.
ChiTaRS; TRAF3; human.
EvolutionaryTrace; Q13114; -.
GeneWiki; TRAF3; -.
GenomeRNAi; 7187; -.
Pharos; Q13114; Tbio.
PRO; PR:Q13114; -.
Proteomes; UP000005640; Chromosome 14.
RNAct; Q13114; protein.
Bgee; ENSG00000131323; Expressed in frontal cortex and 199 other tissues.
ExpressionAtlas; Q13114; baseline and differential.
Genevisible; Q13114; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:InterPro.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0050688; P:regulation of defense response to virus; ISS:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0032648; P:regulation of interferon-beta production; ISS:UniProtKB.
GO; GO:0030162; P:regulation of proteolysis; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0008063; P:Toll signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
CDD; cd03777; MATH_TRAF3; 1.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027128; TRAF3.
InterPro; IPR037304; TRAF3_MATH.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
InterPro; IPR001293; Znf_TRAF.
PANTHER; PTHR10131; PTHR10131; 1.
PANTHER; PTHR10131:SF76; PTHR10131:SF76; 1.
Pfam; PF02176; zf-TRAF; 1.
PIRSF; PIRSF015614; TRAF; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 3.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
PROSITE; PS50145; ZF_TRAF; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
Disease mutation; Endosome; Immunity; Metal-binding; Mitochondrion;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1..568
/note="TNF receptor-associated factor 3"
/id="PRO_0000056401"
DOMAIN 415..560
/note="MATH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
ZN_FING 68..77
/note="RING-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 135..190
/note="TRAF-type 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
ZN_FING 191..249
/note="TRAF-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
COILED 267..338
/evidence="ECO:0000255"
MOD_RES 9
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
VAR_SEQ 191..273
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_040040"
VARIANT 118
/note="R -> W (in IIAE5; dbSNP:rs143813189)"
/evidence="ECO:0000269|PubMed:20832341"
/id="VAR_069081"
VARIANT 129
/note="M -> T (in dbSNP:rs1131877)"
/evidence="ECO:0000269|PubMed:7530216,
ECO:0000269|PubMed:7533327"
/id="VAR_052149"
MUTAGEN 68..70
/note="CGH->AGA: Loss of ubiquitination activity, impaired
interaction with MAVS and IRF3. No effect on interaction
with IKBKE, nor with DDX3X."
/evidence="ECO:0000269|PubMed:27980081"
MUTAGEN 441
/note="Y->A: Abolishes interaction with RNF216; when
associated with A-443."
/evidence="ECO:0000269|PubMed:19893624"
MUTAGEN 443
/note="Q->A: Abolishes interaction with RNF216; when
associated with A-441."
/evidence="ECO:0000269|PubMed:19893624"
MUTAGEN 459
/note="Y->A: Abolishes interaction with LTBR, CD40 and
TANK."
/evidence="ECO:0000269|PubMed:14517219"
MUTAGEN 512
/note="F->E: Abolishes interaction with LTBR, CD40 and
TANK."
/evidence="ECO:0000269|PubMed:14517219"
MUTAGEN 521
/note="F->A: Abolishes interaction with LTBR, CD40 and
TANK."
/evidence="ECO:0000269|PubMed:14517219"
CONFLICT 134
/note="Missing (in Ref. 4; AAA56753)"
/evidence="ECO:0000305"
CONFLICT 158
/note="L -> F (in Ref. 6; BAH13910)"
/evidence="ECO:0000305"
CONFLICT 218..242
/note="Missing (in Ref. 3; AAA68195)"
/evidence="ECO:0000305"
CONFLICT 339
/note="P -> S (in Ref. 3; AAA68195)"
/evidence="ECO:0000305"
CONFLICT 405
/note="R -> G (in Ref. 4; AAA56753)"
/evidence="ECO:0000305"
TURN 54..56
/evidence="ECO:0000244|PDB:2ECY"
STRAND 59..62
/evidence="ECO:0000244|PDB:2ECY"
STRAND 67..69
/evidence="ECO:0000244|PDB:2ECY"
HELIX 74..81
/evidence="ECO:0000244|PDB:2ECY"
TURN 89..91
/evidence="ECO:0000244|PDB:2ECY"
TURN 97..99
/evidence="ECO:0000244|PDB:2ECY"
TURN 365..373
/evidence="ECO:0000244|PDB:1FLK"
TURN 375..377
/evidence="ECO:0000244|PDB:1FLL"
HELIX 378..410
/evidence="ECO:0000244|PDB:2GKW"
STRAND 415..423
/evidence="ECO:0000244|PDB:2GKW"
HELIX 425..433
/evidence="ECO:0000244|PDB:2GKW"
STRAND 438..441
/evidence="ECO:0000244|PDB:1L0A"
STRAND 445..448
/evidence="ECO:0000244|PDB:2GKW"
STRAND 453..459
/evidence="ECO:0000244|PDB:2GKW"
HELIX 464..466
/evidence="ECO:0000244|PDB:2GKW"
TURN 467..469
/evidence="ECO:0000244|PDB:2GKW"
STRAND 470..478
/evidence="ECO:0000244|PDB:2GKW"
HELIX 483..485
/evidence="ECO:0000244|PDB:2GKW"
STRAND 494..498
/evidence="ECO:0000244|PDB:2GKW"
STRAND 502..504
/evidence="ECO:0000244|PDB:1FLK"
STRAND 508..512
/evidence="ECO:0000244|PDB:2GKW"
STRAND 521..523
/evidence="ECO:0000244|PDB:1FLK"
STRAND 525..528
/evidence="ECO:0000244|PDB:2GKW"
STRAND 532..539
/evidence="ECO:0000244|PDB:2GKW"
HELIX 540..545
/evidence="ECO:0000244|PDB:2GKW"
STRAND 553..560
/evidence="ECO:0000244|PDB:2GKW"
STRAND 563..565
/evidence="ECO:0000244|PDB:1ZMS"
SEQUENCE 568 AA; 64490 MW; 9456E440C0A90FBF CRC64;
MESSKKMDSP GALQTNPPLK LHTDRSAGTP VFVPEQGGYK EKFVKTVEDK YKCEKCHLVL
CSPKQTECGH RFCESCMAAL LSSSSPKCTA CQESIVKDKV FKDNCCKREI LALQIYCRNE
SRGCAEQLML GHLLVHLKND CHFEELPCVR PDCKEKVLRK DLRDHVEKAC KYREATCSHC
KSQVPMIALQ KHEDTDCPCV VVSCPHKCSV QTLLRSELSA HLSECVNAPS TCSFKRYGCV
FQGTNQQIKA HEASSAVQHV NLLKEWSNSL EKKVSLLQNE SVEKNKSIQS LHNQICSFEI
EIERQKEMLR NNESKILHLQ RVIDSQAEKL KELDKEIRPF RQNWEEADSM KSSVESLQNR
VTELESVDKS AGQVARNTGL LESQLSRHDQ MLSVHDIRLA DMDLRFQVLE TASYNGVLIW
KIRDYKRRKQ EAVMGKTLSL YSQPFYTGYF GYKMCARVYL NGDGMGKGTH LSLFFVIMRG
EYDALLPWPF KQKVTLMLMD QGSSRRHLGD AFKPDPNSSS FKKPTGEMNI ASGCPVFVAQ
TVLENGTYIK DDTIFIKVIV DTSDLPDP


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Pathways :
WP2292: Chemokine signaling pathway
WP1309: Toll-like receptor signaling pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP949: Toll-like receptor signaling pathway
WP1271: Toll-like receptor signaling pathway
WP75: Toll-like receptor signaling pathway
WP1384: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1067: Toll-like receptor signaling pathway
WP1183: Toll-like receptor signaling pathway
WP2199: Seed Development
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP2328: Allograft rejection
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP211: BMP signaling pathway

Related Genes :
[TRAF3 CAP1 CRAF1] TNF receptor-associated factor 3 (EC 2.3.2.27) (CAP-1) (CD40 receptor-associated factor 1) (CRAF1) (CD40-binding protein) (CD40BP) (LMP1-associated protein 1) (LAP1) (RING-type E3 ubiquitin transferase TRAF3)
[Traf3 Craf1 Trafamn] TNF receptor-associated factor 3 (EC 2.3.2.27) (CD40 receptor-associated factor 1) (CRAF1) (RING-type E3 ubiquitin transferase TRAF3) (TRAFAMN)
[CD40 TNFRSF5] Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (Bp50) (CD40L receptor) (CDw40) (CD antigen CD40)
[TRAF2 TRAP3] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[CD40LG CD40L TNFSF5 TRAP] CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[Cd40lg Cd40l Tnfsf5] CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[TRAF1 EBI6] TNF receptor-associated factor 1 (Epstein-Barr virus-induced protein 6)
[TRAF7 RFWD1 RNF119] E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.27) (RING finger and WD repeat-containing protein 1) (RING finger protein 119) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7)
[traf6 si:dkey-56p7.3 zgc:63704] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[BIRC2 API1 MIHB RNF48] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)
[Cd40lg Cd40l Tnfsf5] CD40 ligand (CD40-L) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[CD40LG CD40L TNFSF5] CD40 ligand (CD40-L) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[CD40LG CD40L TNFSF5] CD40 ligand (CD40-L) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[CD40LG CD40L TNFSF5] CD40 ligand (CD40-L) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[RNF31 ZIBRA] E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31) (Zinc in-between-RING-finger ubiquitin-associated domain protein)
[CD40LG CD40L TNFSF5] CD40 ligand (CD40-L) (Tumor necrosis factor ligand superfamily member 5) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[Birc2] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (Inhibitor of apoptosis protein 2) (mIAP2) (RING-type E3 ubiquitin transferase BIRC2)
[Rnf31 Paul] E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (Putative Ariadne-like ubiquitin ligase) (PAUL) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31)
[LMP1 BNLF1] Latent membrane protein 1 (LMP-1) (Protein p63) [Cleaved into: Protein p25]
[AMFR RNF45] E3 ubiquitin-protein ligase AMFR (EC 2.3.2.27) (Autocrine motility factor receptor) (AMF receptor) (RING finger protein 45) (RING-type E3 ubiquitin transferase AMFR) (gp78)
[LNX1 LNX PDZRN2 UNQ574/PRO1136] E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb-protein X 1) (Numb-binding protein 1) (PDZ domain-containing RING finger protein 2) (RING-type E3 ubiquitin transferase LNX)
[Amfr] E3 ubiquitin-protein ligase AMFR (EC 2.3.2.27) (Autocrine motility factor receptor) (AMF receptor) (RING-type E3 ubiquitin transferase AMFR)

Bibliography :