TRAF5_HUMAN
ID TRAF5_HUMAN Reviewed; 557 AA.
AC O00463; B4DIS9; B4E0A2; Q6FHY1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=TNF receptor-associated factor 5;
DE AltName: Full=RING finger protein 84;
GN Name=TRAF5; Synonyms=RNF84;
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), AND INTERACTION WITH TNFRSF5;
RP TNFRSF8 AND LTBR.
RX PubMed=9511754; DOI=10.1016/s0378-1119(97)00616-1;
RA Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M.,
RA Yamamoto T., Inoue J.;
RT "Cloning and characterization of a cDNA encoding the human homolog of tumor
RT necrosis factor receptor-associated factor 5 (TRAF5).";
RL Gene 207:135-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP TYR-268.
RC TISSUE=Hippocampus, and Thymus;
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).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-557 (ISOFORM 1).
RX PubMed=9177772; DOI=10.1006/geno.1997.4697;
RA Nakano H., Shindo M., Yamada K., Yoshida M.C., Santee S.M., Ware C.F.,
RA Jenkins N.A., Gilbert D.J., Yagita H., Copeland N.G., Okumura K.;
RT "Human TNF receptor-associated factor 5 (TRAF5): cDNA cloning, expression
RT and assignment of the TRAF5 gene to chromosome 1q32.";
RL Genomics 42:26-32(1997).
RN [8]
RP REVIEW.
RX PubMed=11384837; DOI=10.1016/s0898-6568(01)00160-7;
RA Wajant H., Henkler F., Scheurich P.;
RT "The TNF-receptor-associated factor family: scaffold molecules for cytokine
RT receptors, kinases and their regulators.";
RL Cell. Signal. 13:389-400(2001).
RN [9]
RP REVIEW.
RX PubMed=11607847; DOI=10.1038/sj.onc.1204788;
RA Bradley J.R., Pober J.S.;
RT "Tumor necrosis factor receptor-associated factors (TRAFs).";
RL Oncogene 20:6482-6491(2001).
RN [10]
RP INTERACTION WITH TNFRSF14.
RX PubMed=9162022; DOI=10.1074/jbc.272.22.14029;
RA Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.;
RT "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor
RT (TNFR) family, interacts with members of the TNFR-associated factor family
RT and activates the transcription factors NF-kappaB and AP-1.";
RL J. Biol. Chem. 272:14029-14032(1997).
RN [11]
RP INTERACTION WITH TNFRSF14.
RX PubMed=9153189; DOI=10.1074/jbc.272.21.13471;
RA Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.;
RT "ATAR, a novel tumor necrosis factor receptor family member, signals
RT through TRAF2 and TRAF5.";
RL J. Biol. Chem. 272:13471-13474(1997).
RN [12]
RP INTERACTION WITH MAP3K14.
RX PubMed=9275204; DOI=10.1073/pnas.94.18.9792;
RA Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M.;
RT "Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of
RT nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at
RT TNF receptor-associated factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9792-9796(1997).
RN [13]
RP INTERACTION WITH TNFRSF8.
RX PubMed=8999898; DOI=10.1074/jbc.272.4.2042;
RA Aizawa S., Nakano H., Ishida T., Horie R., Nagai M., Ito K., Yagita H.,
RA Okumura K., Inoue J., Watanabe T.;
RT "Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2 are
RT involved in CD30-mediated NFkappaB activation.";
RL J. Biol. Chem. 272:2042-2045(1997).
RN [14]
RP INTERACTION WITH MAP3K5.
RX PubMed=9774977; DOI=10.1016/s1097-2765(00)80283-x;
RA Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M.,
RA Miyazono K., Ichijo H.;
RT "ASK1 is essential for JNK/SAPK activation by TRAF2.";
RL Mol. Cell 2:389-395(1998).
RN [15]
RP INTERACTION WITH TNFRSF5 AND TRAF3.
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 [16]
RP INTERACTION WITH TNFRSF4.
RX PubMed=9488716; DOI=10.1074/jbc.273.10.5808;
RA Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.;
RT "Activation of OX40 signal transduction pathways leads to tumor necrosis
RT factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB
RT activation.";
RL J. Biol. Chem. 273:5808-5814(1998).
RN [17]
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 [18]
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 [19]
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 [20]
RP INTERACTION WITH TDP2.
RX PubMed=10764746; DOI=10.1074/jbc.m000531200;
RA Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I.,
RA Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.;
RT "TTRAP, a novel protein that associates with CD40, tumor necrosis factor
RT (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that
RT inhibits nuclear factor-kappa B activation.";
RL J. Biol. Chem. 275:18586-18593(2000).
RN [21]
RP INTERACTION WITH TNFRSF13B.
RX PubMed=10880535; DOI=10.1084/jem.192.1.137;
RA Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M.,
RA Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R.,
RA Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J., Delaney J.,
RA Meng S.-Y., Boyle W.J., Hsu H.;
RT "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor
RT family member involved in B cell regulation.";
RL J. Exp. Med. 192:137-143(2000).
RN [22]
RP INTERACTION WITH TNFRSF17.
RX PubMed=10908663; DOI=10.1073/pnas.160213497;
RA Shu H.-B., Johnson H.;
RT "B cell maturation protein is a receptor for the tumor necrosis factor
RT family member TALL-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000).
RN [23]
RP FUNCTION, INTERACTION WITH EIF2AK2, AND SUBCELLULAR LOCATION.
RX PubMed=15121867; DOI=10.1128/mcb.24.10.4502-4512.2004;
RA Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H.,
RA Alcami J., Esteban M.;
RT "TRAF family proteins link PKR with NF-kappa B activation.";
RL Mol. Cell. Biol. 24:4502-4512(2004).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Adapter protein and signal transducer that links members of
CC the tumor necrosis factor receptor family to different signaling
CC pathways by association with the receptor cytoplasmic domain and
CC kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to
CC be involved in apoptosis. Plays a role in mediating activation of NF-
CC kappa-B by EIF2AK2/PKR. {ECO:0000269|PubMed:15121867}.
CC -!- SUBUNIT: Homotrimer (Probable). Heteromer with TRAF3. Associates with
CC TNFRSF5/CD40 through interaction with TRAF3. Associates with
CC LTBR/TNFRSF3, TNFRSF4, TNFRSF8/CD30, TNFRSF11A/RANK, TNFRSF13B/TACI,
CC TNFRSF14, TNFRSF17, TNFRSF19/TROY, RIPK2, MAP3K14, MAP3K5, and TRAF and
CC TNF receptor associated protein TDP2. Interacts (via C-terminus) with
CC EIF2AK2/PKR (via the kinase catalytic domain).
CC {ECO:0000269|PubMed:10764746, ECO:0000269|PubMed:10809768,
CC ECO:0000269|PubMed:10880535, ECO:0000269|PubMed:10908663,
CC ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:8999898,
CC ECO:0000269|PubMed:9153189, ECO:0000269|PubMed:9162022,
CC ECO:0000269|PubMed:9275204, ECO:0000269|PubMed:9488716,
CC ECO:0000269|PubMed:9511754, ECO:0000269|PubMed:9642260,
CC ECO:0000269|PubMed:9718306, ECO:0000269|PubMed:9774460,
CC ECO:0000269|PubMed:9774977, ECO:0000305}.
CC -!- INTERACTION:
CC O00463; Q52MB2: CCDC184; NbExp=6; IntAct=EBI-523498, EBI-10179526;
CC O00463; Q16543: CDC37; NbExp=3; IntAct=EBI-523498, EBI-295634;
CC O00463; Q96Q77: CIB3; NbExp=3; IntAct=EBI-523498, EBI-10292696;
CC O00463; Q16206-2: ENOX2; NbExp=3; IntAct=EBI-523498, EBI-10179508;
CC O00463; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-523498, EBI-8468186;
CC O00463; Q9NVF7: FBXO28; NbExp=4; IntAct=EBI-523498, EBI-740282;
CC O00463; O95995: GAS8; NbExp=3; IntAct=EBI-523498, EBI-1052570;
CC O00463; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-523498, EBI-739467;
CC O00463; Q86YM7: HOMER1; NbExp=4; IntAct=EBI-523498, EBI-746815;
CC O00463; O75031: HSF2BP; NbExp=3; IntAct=EBI-523498, EBI-7116203;
CC O00463; P13473-2: LAMP2; NbExp=3; IntAct=EBI-523498, EBI-21591415;
CC O00463; P61968: LMO4; NbExp=3; IntAct=EBI-523498, EBI-2798728;
CC O00463; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-523498, EBI-739832;
CC O00463; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-523498, EBI-16439278;
CC O00463; Q13287: NMI; NbExp=12; IntAct=EBI-523498, EBI-372942;
CC O00463; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-523498, EBI-741158;
CC O00463; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-523498, EBI-9090919;
CC O00463; O14832: PHYH; NbExp=3; IntAct=EBI-523498, EBI-721853;
CC O00463; O75928-2: PIAS2; NbExp=3; IntAct=EBI-523498, EBI-348567;
CC O00463; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-523498, EBI-14066006;
CC O00463; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-523498, EBI-79165;
CC O00463; P25786: PSMA1; NbExp=3; IntAct=EBI-523498, EBI-359352;
CC O00463; P54725: RAD23A; NbExp=3; IntAct=EBI-523498, EBI-746453;
CC O00463; P78317: RNF4; NbExp=5; IntAct=EBI-523498, EBI-2340927;
CC O00463; O00560: SDCBP; NbExp=8; IntAct=EBI-523498, EBI-727004;
CC O00463; P55735: SEC13; NbExp=3; IntAct=EBI-523498, EBI-1046596;
CC O00463; P55735-3: SEC13; NbExp=3; IntAct=EBI-523498, EBI-12235008;
CC O00463; P50453: SERPINB9; NbExp=6; IntAct=EBI-523498, EBI-711626;
CC O00463; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-523498, EBI-5235340;
CC O00463; Q07955: SRSF1; NbExp=2; IntAct=EBI-523498, EBI-398920;
CC O00463; P31948: STIP1; NbExp=3; IntAct=EBI-523498, EBI-1054052;
CC O00463; P63165: SUMO1; NbExp=3; IntAct=EBI-523498, EBI-80140;
CC O00463; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-523498, EBI-741515;
CC O00463; Q9BT49: THAP7; NbExp=3; IntAct=EBI-523498, EBI-741350;
CC O00463; Q92956: TNFRSF14; NbExp=5; IntAct=EBI-523498, EBI-1056653;
CC O00463; Q12933: TRAF2; NbExp=5; IntAct=EBI-523498, EBI-355744;
CC O00463; Q13114: TRAF3; NbExp=4; IntAct=EBI-523498, EBI-357631;
CC O00463; O00463: TRAF5; NbExp=5; IntAct=EBI-523498, EBI-523498;
CC O00463; Q9Y4K3: TRAF6; NbExp=15; IntAct=EBI-523498, EBI-359276;
CC O00463; P62699: YPEL5; NbExp=3; IntAct=EBI-523498, EBI-11721624;
CC O00463; Q6FIF0: ZFAND6; NbExp=3; IntAct=EBI-523498, EBI-724630;
CC O00463; Q8N720: ZNF655; NbExp=3; IntAct=EBI-523498, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15121867}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:15121867}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00463-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00463-2; Sequence=VSP_055449;
CC Name=3;
CC IsoId=O00463-3; Sequence=VSP_055450;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis,
CC ovary, small intestine, colon, and peripheral blood.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB000509; BAA25262.1; -; mRNA.
DR EMBL; AK295766; BAG58591.1; -; mRNA.
DR EMBL; AK303286; BAG64364.1; -; mRNA.
DR EMBL; CR536557; CAG38794.1; -; mRNA.
DR EMBL; AL590101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93420.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93422.1; -; Genomic_DNA.
DR EMBL; BC029600; AAH29600.1; -; mRNA.
DR EMBL; U69108; AAC51329.1; -; mRNA.
DR CCDS; CCDS1497.1; -. [O00463-1]
DR PIR; JC6539; JC6539.
DR RefSeq; NP_001029082.1; NM_001033910.2. [O00463-1]
DR RefSeq; NP_001306136.1; NM_001319207.1. [O00463-2]
DR RefSeq; NP_004610.1; NM_004619.3. [O00463-1]
DR RefSeq; NP_665702.1; NM_145759.2. [O00463-1]
DR RefSeq; XP_011508261.1; XM_011509959.2. [O00463-2]
DR RefSeq; XP_011508262.1; XM_011509960.2. [O00463-2]
DR RefSeq; XP_016857710.1; XM_017002221.1. [O00463-1]
DR PDB; 7L3L; X-ray; 2.80 A; A/C=23-164.
DR PDBsum; 7L3L; -.
DR AlphaFoldDB; O00463; -.
DR SMR; O00463; -.
DR BioGRID; 113040; 98.
DR IntAct; O00463; 62.
DR MINT; O00463; -.
DR STRING; 9606.ENSP00000261464; -.
DR iPTMnet; O00463; -.
DR PhosphoSitePlus; O00463; -.
DR BioMuta; TRAF5; -.
DR EPD; O00463; -.
DR jPOST; O00463; -.
DR MassIVE; O00463; -.
DR MaxQB; O00463; -.
DR PaxDb; O00463; -.
DR PeptideAtlas; O00463; -.
DR PRIDE; O00463; -.
DR ProteomicsDB; 47913; -. [O00463-1]
DR Antibodypedia; 1975; 312 antibodies from 39 providers.
DR DNASU; 7188; -.
DR Ensembl; ENST00000261464.10; ENSP00000261464.5; ENSG00000082512.15. [O00463-1]
DR Ensembl; ENST00000336184.6; ENSP00000336825.2; ENSG00000082512.15. [O00463-1]
DR Ensembl; ENST00000367004.3; ENSP00000355971.3; ENSG00000082512.15. [O00463-1]
DR GeneID; 7188; -.
DR KEGG; hsa:7188; -.
DR MANE-Select; ENST00000261464.10; ENSP00000261464.5; NM_001033910.3; NP_001029082.1.
DR UCSC; uc001hih.4; human. [O00463-1]
DR CTD; 7188; -.
DR DisGeNET; 7188; -.
DR GeneCards; TRAF5; -.
DR HGNC; HGNC:12035; TRAF5.
DR HPA; ENSG00000082512; Low tissue specificity.
DR MIM; 602356; gene.
DR neXtProt; NX_O00463; -.
DR OpenTargets; ENSG00000082512; -.
DR PharmGKB; PA36712; -.
DR VEuPathDB; HostDB:ENSG00000082512; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000160954; -.
DR HOGENOM; CLU_021061_4_1_1; -.
DR InParanoid; O00463; -.
DR OMA; HEKNDCP; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; O00463; -.
DR TreeFam; TF321154; -.
DR PathwayCommons; O00463; -.
DR SignaLink; O00463; -.
DR SIGNOR; O00463; -.
DR BioGRID-ORCS; 7188; 10 hits in 1118 CRISPR screens.
DR ChiTaRS; TRAF5; human.
DR GeneWiki; TRAF5; -.
DR GenomeRNAi; 7188; -.
DR Pharos; O00463; Tbio.
DR PRO; PR:O00463; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00463; protein.
DR Bgee; ENSG00000082512; Expressed in saphenous vein and 173 other tissues.
DR Genevisible; O00463; HS.
DR GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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; IBA:GO_Central.
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:0097400; P:interleukin-17-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
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; IPR027130; TRAF5.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR10131; PTHR10131; 1.
DR PANTHER; PTHR10131:SF83; PTHR10131:SF83; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF02176; zf-TRAF; 1.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..557
FT /note="TNF receptor-associated factor 5"
FT /id="PRO_0000056405"
FT DOMAIN 403..549
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT ZN_FING 45..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 127..181
FT /note="TRAF-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 182..239
FT /note="TRAF-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 345..557
FT /note="Interaction with EIF2AK2/PKR"
FT /evidence="ECO:0000269|PubMed:15121867"
FT COILED 237..342
FT /evidence="ECO:0000255"
FT VAR_SEQ 126
FT /note="Q -> QQVPLACCYLLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055449"
FT VAR_SEQ 127..232
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055450"
FT VARIANT 120
FT /note="V -> G (in dbSNP:rs3946808)"
FT /id="VAR_052151"
FT VARIANT 186
FT /note="N -> H (in dbSNP:rs2271458)"
FT /id="VAR_020117"
FT VARIANT 268
FT /note="H -> Y (in dbSNP:rs200398415)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_071060"
FT VARIANT 358
FT /note="L -> V (in dbSNP:rs2230780)"
FT /id="VAR_052152"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:7L3L"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:7L3L"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:7L3L"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:7L3L"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7L3L"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7L3L"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:7L3L"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7L3L"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:7L3L"
SQ SEQUENCE 557 AA; 64406 MW; 86EB3724CE111176 CRC64;
MAYSEEHKGM PCGFIRQNSG NSISLDFEPS IEYQFVERLE ERYKCAFCHS VLHNPHQTGC
GHRFCQHCIL SLRELNTVPI CPVDKEVIKS QEVFKDNCCK REVLNLYVYC SNAPGCNAKV
ILGRYQDHLQ QCLFQPVQCS NEKCREPVLR KDLKEHLSAS CQFRKEKCLY CKKDVVVINL
QNHEENLCPE YPVFCPNNCA KIILKTEVDE HLAVCPEAEQ DCPFKHYGCA VTDKRRNLQQ
HEHSALREHM RLVLEKNVQL EEQISDLHKS LEQKESKIQQ LAETIKKLEK EFKQFAQLFG
KNGSFLPNIQ VFASHIDKSA WLEAQVHQLL QMVNQQQNKF DLRPLMEAVD TVKQKITLLE
NNDQRLAVLE EETNKHDTHI NIHKAQLSKN EERFKLLEGT CYNGKLIWKV TDYKMKKREA
VDGHTVSIFS QSFYTSRCGY RLCARAYLNG DGSGRGSHLS LYFVVMRGEF DSLLQWPFRQ
RVTLMLLDQS GKKNIMETFK PDPNSSSFKR PDGEMNIASG CPRFVAHSVL ENAKNAYIKD
DTLFLKVAVD LTDLEDL
