Q13077 (TRAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TNF receptor-associated factor 1

Alternative name(s):
Epstein-Barr virus-induced protein 6

Gene names

Name:	TRAF1
Synonyms:	EBI6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2. Ref.18 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32
Subunit structure	Homotrimer. Heterotrimer with TRAF2. Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and RIPK2. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2. Interacts with NFATC2IP, TRAFD1 and with HIVEP3 By similarity. Interacts with MAP3K14. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.32
Domain	The coiled coil domain mediates homo- and hetero-oligomerization. Ref.18 The MATH/TRAF domain binds to receptor cytoplasmic domains. Ref.18 Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling. Ref.18
Post-translational modification	Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation.
Sequence similarities	Contains 1 MATH domain.
Caution	Lacks a RING domain and has therefore no E3 ubiquitin-protein ligase activity by itself.
Sequence caution	The sequence BAC03449.1 differs from that shown. Reason: Frameshift at position 111.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.18. Source: UniProtKB protein complex assembly Traceable author statement Ref.8. Source: ProtInc regulation of apoptotic process Inferred from direct assay Ref.18. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Traceable author statement Ref.8. Source: ProtInc
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GIT2	Q14161	2	EBI-359224,EBI-1046878
Hoxa1	P09022	4	EBI-359224,EBI-3957603	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13077-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13077-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 416

416

TNF receptor-associated factor 1

PRO_0000056397

Regions

Domain

266 – 412

147

MATH

Coiled coil

182 – 264

83

Sites

Site

163 – 164

2

Cleavage; by CASP8

Amino acid modifications

Modified residue

69

1

Phosphoserine By similarity

Modified residue

146

1

Phosphoserine By similarity

Cross-link

185

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25

Cross-link

193

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25

Natural variations

Alternative sequence

1 – 122

122

Missing in isoform 2.

VSP_043092

Natural variant

139

1

M → T. Ref.33

VAR_054161

Experimental info

Mutagenesis

163

1

D → A: Abolishes CASP8-mediated cleavage. Ref.18 Ref.26

Mutagenesis

185

1

K → R: Nearly abolished ubiquitination; when associated with R-193. Ref.25

Mutagenesis

193

1

K → R: Nearly abolished ubiquitination; when associated with R-185. Ref.25

Secondary structure

1

.

.

.

416

Helix Strand Turn

Details...

Helix

183 – 241

59

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A956A123A40D284A	FASTA	416	46,164
	10 20 30 40 50 60 MASSSGSSPR PAPDENEFPF GCPPTVCQDP KEPRALCCAG CLSENPRNGE DQICPKCRGE 70 80 90 100 110 120 DLQSISPGSR LRTQEKAHPE VAEAGIGCPF AGVGCSFKGS PQSVQEHEVT SQTSHLNLLL 130 140 150 160 170 180 GFMKQWKARL GCGLESGPMA LEQNLSDLQL QAAVEVAGDL EVDCYRAPCS ESQEELALQH 190 200 210 220 230 240 FMKEKLLAEL EGKLRVFENI VAVLNKEVEA SHLALATSIH QSQLDRERIL SLEQRVVELQ 250 260 270 280 290 300 QTLAQKDQAL GKLEQSLRLM EEASFDGTFL WKITNVTRRC HESACGRTVS LFSPAFYTAK 310 320 330 340 350 360 YGYKLCLRLY LNGDGTGKRT HLSLFIVIMR GEYDALLPWP FRNKVTFMLL DQNNREHAID 370 380 390 400 410 AFRPDLSSAS FQRPQSETNV ASGCPLFFPL SKLQSPKHAY VKDDTMFLKC IVETST
	Isoform 2 [UniParc]. Checksum: 99A72217E03E143C	FASTA	294	33,296
	10 20 30 40 50 60 MKQWKARLGC GLESGPMALE QNLSDLQLQA AVEVAGDLEV DCYRAPCSES QEELALQHFM 70 80 90 100 110 120 KEKLLAELEG KLRVFENIVA VLNKEVEASH LALATSIHQS QLDRERILSL EQRVVELQQT 130 140 150 160 170 180 LAQKDQALGK LEQSLRLMEE ASFDGTFLWK ITNVTRRCHE SACGRTVSLF SPAFYTAKYG 190 200 210 220 230 240 YKLCLRLYLN GDGTGKRTHL SLFIVIMRGE YDALLPWPFR NKVTFMLLDQ NNREHAIDAF 250 260 270 280 290 RPDLSSASFQ RPQSETNVAS GCPLFFPLSK LQSPKHAYVK DDTMFLKCIV ETST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family." Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C., Kieff E. Cell 80:389-399(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lymphoma.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Spleen and Substantia nigra.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Stomach.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[8]	"A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor." Rothe M., Wong S.C., Henzel W.J., Goeddel D.V. Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF2 AND TNFRSF1B.
[9]	"I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction." Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V. Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TANK.
[10]	"T cell receptor-dependent cell death of T cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors." Lee S.Y., Park C.G., Choi Y. J. Exp. Med. 183:669-674(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF8.
[11]	"CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization." Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R. Biochemistry 37:11836-11845(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF5.
[12]	"Identification of CARDIAK, a RIP-like kinase that associates with caspase-1." Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L., Mattmann C., Tschopp J. Curr. Biol. 8:885-888(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIPK2.
[13]	"RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase." McCarthy J.V., Ni J., Dixit V.M. J. Biol. Chem. 273:16968-16975(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIPK2.
[14]	"The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor." Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y. J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF11A.
[15]	"CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand." Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D., Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H. J. Exp. Med. 187:1849-1862(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF9.
[16]	"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." Arch R.H., Thompson C.B. Mol. Cell. Biol. 18:558-565(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF4 AND TNFRSF9.
[17]	"Identification of a novel activation-inducible protein of the tumor necrosis factor receptor superfamily and its ligand." 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. J. Biol. Chem. 274:6056-6061(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF18.
[18]	"Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas ligand-mediated apoptosis." Irmler M., Steiner V., Ruegg C., Wajant H., Tschopp J. FEBS Lett. 468:129-133(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE BY CASP8, MUTAGENESIS OF ASP-163, DOMAIN.
[19]	"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." Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M. J. Biol. Chem. 275:15336-15342(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF19.
[20]	"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." Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J., Devergne O., Tsapis A. J. Immunol. 165:1322-1330(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF17.
[21]	"RELT, a new member of the tumor necrosis factor receptor superfamily, is selectively expressed in hematopoietic tissues and activates transcription factor NF-kappaB." Sica G.L., Zhu G., Tamada K., Liu D., Ni J., Chen L. Blood 97:2702-2707(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNFRSF19L.
[22]	"The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A." Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M. J. Biol. Chem. 276:2668-2677(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EDAR.
[23]	"TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2." Li X., Yang Y., Ashwell J.D. Nature 416:345-347(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIRC2.
[24]	"TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation." He L., Grammer A.C., Wu X., Lipsky P.E. J. Biol. Chem. 279:55855-55865(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[25]	"Mass spectrometric analysis of tumor necrosis factor receptor-associated factor 1 ubiquitination mediated by cellular inhibitor of apoptosis 2." Lee J.S., Hong U.S., Lee T.H., Yoon S.K., Yoon J.B. Proteomics 4:3376-3382(2004) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-185 AND LYS-193, MASS SPECTROMETRY, MUTAGENESIS OF LYS-185 AND LYS-193.
[26]	"TNF receptor-associated factor-1 (TRAF1) negatively regulates Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF)-mediated signaling." Su X., Li S., Meng M., Qian W., Xie W., Chen D., Zhai Z., Shu H.B. Eur. J. Immunol. 36:199-206(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TICAM1, CLEAVAGE BY CASP8, MUTAGENESIS OF ASP-163.
[27]	"Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-mediated phosphorylation of TRAF1." Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y. Genes Cells 13:509-520(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[28]	"TNF receptor-associated factor 1 is a positive regulator of the NF-kappaB alternative pathway." Lavorgna A., De Filippi R., Formisano S., Leonardi A. Mol. Immunol. 46:3278-3282(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TNFRSF13C.
[29]	"Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation." Wicovsky A., Henkler F., Salzmann S., Scheurich P., Kneitz C., Wajant H. Oncogene 28:1769-1781(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TNFRSF1A; TNFRSF1B AND TRAF2.
[30]	"Asymmetric recruitment of cIAPs by TRAF2." Mace P.D., Smits C., Vaux D.L., Silke J., Day C.L. J. Mol. Biol. 400:8-15(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIRC2.
[31]	"Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation." Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L. Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[32]	"Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation." Zheng C., Kabaleeswaran V., Wang Y., Cheng G., Wu H. Mol. Cell 38:101-113(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 181-244 IN COMPLEX WITH TRAF2 AND BIRC3, SUBUNIT, FUNCTION.
[33]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-139.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U19261 mRNA. Translation: AAA62309.1.
AK090468 mRNA. Translation: BAC03449.1. Frameshift.
AK295959 mRNA. Translation: BAG58739.1.
AK315476 mRNA. Translation: BAG37860.1.
AL832989 mRNA. Translation: CAH56343.1.
BT019408 mRNA. Translation: AAV38215.1.
AC006430 Genomic DNA. No translation available.
CH471090 Genomic DNA. Translation: EAW87479.1.
BC024145 mRNA. Translation: AAH24145.1.

IPI

IPI00011549.
IPI00984225.

PIR

B55649.

RefSeq

NP_001177874.1. NM_001190945.1.
NP_001177876.1. NM_001190947.1.
NP_005649.1. NM_005658.4.

UniGene

Hs.531251.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M0D	X-ray	2.80	C	181-244	[»]

ProteinModelPortal

Q13077.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27514N.

IntAct

Q13077. 19 interactions.

MINT

MINT-1131534.

STRING

9606.ENSP00000362994.

PTM databases

PhosphoSite

Q13077.

Polymorphism databases

DMDM

6707734.

Proteomic databases

PaxDb

Q13077.

PRIDE

Q13077.

Protocols and materials databases

DNASU

7185.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373887; ENSP00000362994; ENSG00000056558.
ENST00000540010; ENSP00000443183; ENSG00000056558.
ENST00000546084; ENSP00000438583; ENSG00000056558.

GeneID

7185.

KEGG

hsa:7185.

UCSC

uc004bku.2. human.

Organism-specific databases

CTD

7185.

GeneCards

GC09M123664.

HGNC

HGNC:12031. TRAF1.

HPA

CAB009593.
HPA001852.

MIM

601711. gene.

neXtProt

NX_Q13077.

PharmGKB

PA36708.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264247.

HOGENOM

HOG000231558.

HOVERGEN

HBG058222.

InParanoid

Q13077.

KO

K03172.

OMA

RRCHESA.

OrthoDB

EOG42Z4Q6.

PhylomeDB

Q13077.

Enzyme and pathway databases

Pathway_Interaction_DB

hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
tnfpathway. TNF receptor signaling pathway.

Gene expression databases

Bgee

Q13077.

CleanEx

HS_TRAF1.

Genevestigator

Q13077.

GermOnline

ENSG00000056558. Homo sapiens.

Family and domain databases

InterPro

IPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view]

PANTHER

PTHR10131:SF29. PTHR10131:SF29. 1 hit.

Pfam

PF00917. MATH. 1 hit.
[Graphical view]

PIRSF

PIRSF015614. TRAF. 1 hit.

SMART

SM00061. MATH. 1 hit.
[Graphical view]

SUPFAM

SSF49599. Traf_like. 1 hit.

PROSITE

PS50144. MATH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q13077.

GenomeRNAi

7185.

NextBio

28168.

PMAP-CutDB

Q13077.

SOURCE

Search...

Entry information

Entry name

TRAF1_HUMAN

Accession

Primary (citable) accession number: Q13077
Secondary accession number(s): B4DJ77, Q658U1, Q8NF13

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.