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Q13077 (TRAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNF receptor-associated factor 1
Alternative name(s):
Epstein-Barr virus-induced protein 6
Gene names
Name:TRAF1
Synonyms:EBI6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GIT2Q141612EBI-359224,EBI-1046878
Hoxa1P090224EBI-359224,EBI-3957603From a different organism.
TRAF2Q129333EBI-359224,EBI-355744
TRAF6Q9Y4K33EBI-359224,EBI-359276

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416TNF receptor-associated factor 1
PRO_0000056397

Regions

Domain266 – 412147MATH
Coiled coil182 – 26483

Sites

Site163 – 1642Cleavage; by CASP8

Amino acid modifications

Modified residue1461Phosphoserine By similarity
Cross-link185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25
Cross-link193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25

Natural variations

Alternative sequence1 – 122122Missing in isoform 2.
VSP_043092
Natural variant1391M → T. Ref.33
Corresponds to variant rs113495277 [ dbSNP | Ensembl ].
VAR_054161

Experimental info

Mutagenesis1631D → A: Abolishes CASP8-mediated cleavage. Ref.18 Ref.26
Mutagenesis1851K → R: Nearly abolished ubiquitination; when associated with R-193. Ref.25
Mutagenesis1931K → R: Nearly abolished ubiquitination; when associated with R-185. Ref.25

Secondary structure

... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A956A123A40D284A

FASTA41646,164
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 99A72217E03E143C
Show »

FASTA29433,296

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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. expand/collapse author list , 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.
PIRB55649.
RefSeqNP_001177874.1. NM_001190945.1.
NP_001177876.1. NM_001190947.1.
NP_005649.1. NM_005658.4.
UniGeneHs.531251.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M0DX-ray2.80C181-244[»]
ProteinModelPortalQ13077.
SMRQ13077. Positions 15-112, 181-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113037. 63 interactions.
DIPDIP-27514N.
IntActQ13077. 26 interactions.
MINTMINT-1131534.
STRING9606.ENSP00000362994.

PTM databases

PhosphoSiteQ13077.

Polymorphism databases

DMDM6707734.

Proteomic databases

PaxDbQ13077.
PRIDEQ13077.

Protocols and materials databases

DNASU7185.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373887; ENSP00000362994; ENSG00000056558. [Q13077-1]
ENST00000540010; ENSP00000443183; ENSG00000056558. [Q13077-1]
ENST00000546084; ENSP00000438583; ENSG00000056558. [Q13077-2]
GeneID7185.
KEGGhsa:7185.
UCSCuc004bku.2. human. [Q13077-1]

Organism-specific databases

CTD7185.
GeneCardsGC09M123664.
HGNCHGNC:12031. TRAF1.
HPACAB009593.
HPA001852.
MIM601711. gene.
neXtProtNX_Q13077.
PharmGKBPA36708.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264247.
HOGENOMHOG000231558.
HOVERGENHBG058222.
InParanoidQ13077.
KOK03172.
OMAHFMKEKL.
OrthoDBEOG7966G5.
PhylomeDBQ13077.
TreeFamTF321154.

Enzyme and pathway databases

SignaLinkQ13077.

Gene expression databases

BgeeQ13077.
CleanExHS_TRAF1.
GenevestigatorQ13077.

Family and domain databases

InterProIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view]
PANTHERPTHR10131:SF29. PTHR10131:SF29. 1 hit.
PfamPF00917. MATH. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 1 hit.
PROSITEPS50144. MATH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13077.
GeneWikiTRAF1.
GenomeRNAi7185.
NextBio28168.
PMAP-CutDBQ13077.
PROQ13077.
SOURCESearch...

Entry information

Entry nameTRAF1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM