TRAF1_MOUSE
ID TRAF1_MOUSE Reviewed; 409 AA.
AC P39428; Q8CE28;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=TNF receptor-associated factor 1;
GN Name=Traf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-135 AND 390-402, AND
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH TRAIP.
RX PubMed=9104814; DOI=10.1084/jem.185.7.1275;
RA Lee S.Y., Lee S.Y., Choi Y.;
RT "TRAF-interacting protein (TRIP): a novel component of the tumor necrosis
RT factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits
RT TRAF2-mediated NF-kappaB activation.";
RL J. Exp. Med. 185:1275-1285(1997).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11672546; DOI=10.1016/s1074-7613(01)00207-2;
RA Tsitsikov E.N., Laouini D., Dunn I.F., Sannikova T.Y., Davidson L.,
RA Alt F.W., Geha R.S.;
RT "TRAF1 is a negative regulator of TNF signaling. enhanced TNF signaling in
RT TRAF1-deficient mice.";
RL Immunity 15:647-657(2001).
RN [7]
RP INTERACTION WITH HIVEP3.
RX PubMed=11804591; DOI=10.1016/s1097-2765(01)00434-8;
RA Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
RT "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-
RT driven responses and interacts with TRAF2.";
RL Mol. Cell 9:121-131(2002).
RN [8]
RP INTERACTION WITH NFATC2IP.
RX PubMed=16352630; DOI=10.1093/intimm/dxh354;
RA Bryce P.J., Oyoshi M.K., Kawamoto S., Oettgen H.C., Tsitsikov E.N.;
RT "TRAF1 regulates Th2 differentiation, allergic inflammation and nuclear
RT localization of the Th2 transcription factor, NIP45.";
RL Int. Immunol. 18:101-111(2006).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT SER-139, INTERACTION WITH TNFRSF1B, AND
RP MUTAGENESIS OF SER-139.
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 [10]
RP INTERACTION WITH TRAFD1.
RX PubMed=18849341; DOI=10.1074/jbc.m806923200;
RA Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.;
RT "FLN29 deficiency reveals its negative regulatory role in the Toll-like
RT receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase
RT signaling pathway.";
RL J. Biol. Chem. 283:33858-33864(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP INTERACTION WITH GPS2.
RX PubMed=22424771; DOI=10.1016/j.molcel.2012.01.025;
RA Cardamone M.D., Krones A., Tanasa B., Taylor H., Ricci L., Ohgi K.A.,
RA Glass C.K., Rosenfeld M.G., Perissi V.;
RT "A protective strategy against hyperinflammatory responses requiring the
RT nontranscriptional actions of GPS2.";
RL Mol. Cell 46:91-104(2012).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11672546,
CC ECO:0000269|PubMed:18429822}.
CC -!- SUBUNIT: Homotrimer (By similarity). Heterotrimer with TRAF2
CC (PubMed:8069916). Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2,
CC TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK,
CC TNFRSF13C, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT,
CC XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and
CC RIPK2 (PubMed:8069916, PubMed:9104814, PubMed:18429822). Interacts with
CC BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts
CC with a heterotrimer formed by TRAF1 and TRAF2. Interacts with MAP3K14
CC (By similarity). Interacts with NFATC2IP, TRAFD1 and with HIVEP3
CC (PubMed:11804591, PubMed:16352630, PubMed:18849341). Interacts with
CC GPS2 (PubMed:22424771). {ECO:0000250|UniProtKB:Q13077,
CC ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:16352630,
CC ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:18849341,
CC ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:8069916,
CC ECO:0000269|PubMed:9104814}.
CC -!- INTERACTION:
CC P39428; P50247: Ahcy; NbExp=3; IntAct=EBI-520123, EBI-646982;
CC P39428; Q9Z104: Hmg20b; NbExp=3; IntAct=EBI-520123, EBI-646920;
CC P39428; Q8C886: Plekhn1; NbExp=6; IntAct=EBI-520123, EBI-646708;
CC P39428; P70347-1: Tank; NbExp=12; IntAct=EBI-520123, EBI-646125;
CC P39428; Q924A0: Tcf7l2; NbExp=6; IntAct=EBI-520123, EBI-646713;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC oligomerization. {ECO:0000250}.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
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:0000250}.
CC -!- PTM: Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent
CC proteasomal degradation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice have normal B-cell
CC proliferation and antibody response, but increased T-cell proliferation
CC in response to CD3 signaling. Their T-cells show enhanced activation of
CC JNK and NF-kappa-B. Mice are highly susceptible to TNF-induced skin
CC necrosis. {ECO:0000269|PubMed:11672546}.
CC -!- CAUTION: Lacks a RING domain and has therefore no E3 ubiquitin-protein
CC ligase activity by itself. {ECO:0000305}.
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DR EMBL; L35302; AAC37663.1; -; mRNA.
DR EMBL; AK029135; BAC26315.1; -; mRNA.
DR EMBL; AK169515; BAE41205.1; -; mRNA.
DR EMBL; AK172598; BAE43086.1; -; mRNA.
DR EMBL; AL929068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08637.1; -; Genomic_DNA.
DR CCDS; CCDS15956.1; -.
DR PIR; A54750; A54750.
DR RefSeq; NP_001313530.1; NM_001326601.1.
DR RefSeq; NP_033447.2; NM_009421.4.
DR RefSeq; XP_011237352.1; XM_011239050.2.
DR RefSeq; XP_011237353.1; XM_011239051.2.
DR RefSeq; XP_011237354.1; XM_011239052.2.
DR RefSeq; XP_011237355.1; XM_011239053.2.
DR RefSeq; XP_011237356.1; XM_011239054.2.
DR RefSeq; XP_017172618.1; XM_017317129.1.
DR AlphaFoldDB; P39428; -.
DR SMR; P39428; -.
DR BioGRID; 204302; 6.
DR DIP; DIP-260N; -.
DR IntAct; P39428; 35.
DR STRING; 10090.ENSMUSP00000130759; -.
DR MoonDB; P39428; Predicted.
DR iPTMnet; P39428; -.
DR PhosphoSitePlus; P39428; -.
DR EPD; P39428; -.
DR jPOST; P39428; -.
DR MaxQB; P39428; -.
DR PaxDb; P39428; -.
DR PeptideAtlas; P39428; -.
DR PRIDE; P39428; -.
DR ProteomicsDB; 260735; -.
DR Antibodypedia; 807; 384 antibodies from 41 providers.
DR DNASU; 22029; -.
DR Ensembl; ENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
DR Ensembl; ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
DR Ensembl; ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
DR GeneID; 22029; -.
DR KEGG; mmu:22029; -.
DR UCSC; uc008jjj.1; mouse.
DR CTD; 7185; -.
DR MGI; MGI:101836; Traf1.
DR VEuPathDB; HostDB:ENSMUSG00000026875; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000161076; -.
DR HOGENOM; CLU_021061_0_0_1; -.
DR InParanoid; P39428; -.
DR OMA; CSWSGIM; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; P39428; -.
DR TreeFam; TF321154; -.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR BioGRID-ORCS; 22029; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Traf1; mouse.
DR PRO; PR:P39428; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P39428; protein.
DR Bgee; ENSMUSG00000026875; Expressed in peripheral lymph node and 107 other tissues.
DR ExpressionAtlas; P39428; baseline and differential.
DR Genevisible; P39428; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
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 Apoptosis; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..409
FT /note="TNF receptor-associated factor 1"
FT /id="PRO_0000056398"
FT DOMAIN 259..405
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT COILED 167..256
FT /evidence="ECO:0000250"
FT SITE 156..157
FT /note="Cleavage; by CASP8"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18429822"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13077"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13077"
FT MUTAGEN 139
FT /note="S->A: Loss of phosphorylation site. Reduces global
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:18429822"
FT CONFLICT 222
FT /note="I -> L (in Ref. 1; AAC37663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 45465 MW; ADD7F997169D9AAD CRC64;
MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK CRADNLHPVS
PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH EATSQSSHLY LLLAVLKEWK
SSPGSNLGSA PMALERNLSE LQLQAAVEAT GDLEVDCYRA PCCESQEELA LQHLVKEKLL
AQLEEKLRVF ANIVAVLNKE VEASHLALAA SIHQSQLDRE HILSLEQRVV ELQQTLAQKD
QVLGKLEHSL RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL
RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH AIDAFRPDLS
SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF LKCIVDTSA
