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Q13077

- TRAF1_HUMAN

UniProt

Q13077 - TRAF1_HUMAN

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Protein
TNF receptor-associated factor 1
Gene
TRAF1, EBI6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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/TNFR2.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei163 – 1642Cleavage; by CASP8

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. thioesterase binding Source: UniProtKB
  3. tumor necrosis factor receptor binding Source: UniProt
  4. ubiquitin protein ligase binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  3. protein complex assembly Source: ProtInc
  4. regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  5. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

SignaLinkiQ13077.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 1
Alternative name(s):
Epstein-Barr virus-induced protein 6
Gene namesi
Name:TRAF1
Synonyms:EBI6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12031. TRAF1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631D → A: Abolishes CASP8-mediated cleavage. 2 Publications
Mutagenesisi185 – 1851K → R: Nearly abolished ubiquitination; when associated with R-193. 1 Publication
Mutagenesisi193 – 1931K → R: Nearly abolished ubiquitination; when associated with R-185. 1 Publication

Organism-specific databases

PharmGKBiPA36708.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416TNF receptor-associated factor 1
PRO_0000056397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461Phosphoserine By similarity
Cross-linki185 – 185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki193 – 193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13077.
PaxDbiQ13077.
PRIDEiQ13077.

PTM databases

PhosphoSiteiQ13077.

Miscellaneous databases

PMAP-CutDBQ13077.

Expressioni

Gene expression databases

BgeeiQ13077.
CleanExiHS_TRAF1.
GenevestigatoriQ13077.

Organism-specific databases

HPAiCAB009593.
HPA001852.

Interactioni

Subunit structurei

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 MAP3K14.21 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113037. 63 interactions.
DIPiDIP-27514N.
IntActiQ13077. 26 interactions.
MINTiMINT-1131534.
STRINGi9606.ENSP00000362994.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi183 – 24159

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M0DX-ray2.80C181-244[»]
ProteinModelPortaliQ13077.
SMRiQ13077. Positions 181-415.

Miscellaneous databases

EvolutionaryTraceiQ13077.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 412147MATH
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili182 – 26483
Add
BLAST

Domaini

The coiled coil domain mediates homo- and hetero-oligomerization.1 Publication
The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling.1 Publication

Sequence similaritiesi

Contains 1 MATH domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264247.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ13077.
KOiK03172.
OMAiHFMKEKL.
OrthoDBiEOG7966G5.
PhylomeDBiQ13077.
TreeFamiTF321154.

Family and domain databases

InterProiIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view]
PANTHERiPTHR10131:SF29. PTHR10131:SF29. 1 hit.
PfamiPF00917. MATH. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13077-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MASSSGSSPR PAPDENEFPF GCPPTVCQDP KEPRALCCAG CLSENPRNGE    50
DQICPKCRGE DLQSISPGSR LRTQEKAHPE VAEAGIGCPF AGVGCSFKGS 100
PQSVQEHEVT SQTSHLNLLL GFMKQWKARL GCGLESGPMA LEQNLSDLQL 150
QAAVEVAGDL EVDCYRAPCS ESQEELALQH FMKEKLLAEL EGKLRVFENI 200
VAVLNKEVEA SHLALATSIH QSQLDRERIL SLEQRVVELQ QTLAQKDQAL 250
GKLEQSLRLM EEASFDGTFL WKITNVTRRC HESACGRTVS LFSPAFYTAK 300
YGYKLCLRLY LNGDGTGKRT HLSLFIVIMR GEYDALLPWP FRNKVTFMLL 350
DQNNREHAID AFRPDLSSAS FQRPQSETNV ASGCPLFFPL SKLQSPKHAY 400
VKDDTMFLKC IVETST 416
Length:416
Mass (Da):46,164
Last modified:November 1, 1996 - v1
Checksum:iA956A123A40D284A
GO
Isoform 2 (identifier: Q13077-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:294
Mass (Da):33,296
Checksum:i99A72217E03E143C
GO

Sequence cautioni

The sequence BAC03449.1 differs from that shown. Reason: Frameshift at position 111.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391M → T.1 Publication
Corresponds to variant rs113495277 [ dbSNP | Ensembl ].
VAR_054161

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 122122Missing in isoform 2.
VSP_043092Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS55335.1. [Q13077-2]
CCDS6825.1. [Q13077-1]
PIRiB55649.
RefSeqiNP_001177874.1. NM_001190945.1. [Q13077-1]
NP_001177876.1. NM_001190947.1. [Q13077-2]
NP_005649.1. NM_005658.4. [Q13077-1]
UniGeneiHs.531251.

Genome annotation databases

EnsembliENST00000373887; ENSP00000362994; ENSG00000056558. [Q13077-1]
ENST00000540010; ENSP00000443183; ENSG00000056558. [Q13077-1]
ENST00000546084; ENSP00000438583; ENSG00000056558. [Q13077-2]
GeneIDi7185.
KEGGihsa:7185.
UCSCiuc004bku.2. human. [Q13077-1]

Polymorphism databases

DMDMi6707734.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS55335.1. [Q13077-2 ]
CCDS6825.1. [Q13077-1 ]
PIRi B55649.
RefSeqi NP_001177874.1. NM_001190945.1. [Q13077-1 ]
NP_001177876.1. NM_001190947.1. [Q13077-2 ]
NP_005649.1. NM_005658.4. [Q13077-1 ]
UniGenei Hs.531251.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3M0D X-ray 2.80 C 181-244 [» ]
ProteinModelPortali Q13077.
SMRi Q13077. Positions 181-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113037. 63 interactions.
DIPi DIP-27514N.
IntActi Q13077. 26 interactions.
MINTi MINT-1131534.
STRINGi 9606.ENSP00000362994.

PTM databases

PhosphoSitei Q13077.

Polymorphism databases

DMDMi 6707734.

Proteomic databases

MaxQBi Q13077.
PaxDbi Q13077.
PRIDEi Q13077.

Protocols and materials databases

DNASUi 7185.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373887 ; ENSP00000362994 ; ENSG00000056558 . [Q13077-1 ]
ENST00000540010 ; ENSP00000443183 ; ENSG00000056558 . [Q13077-1 ]
ENST00000546084 ; ENSP00000438583 ; ENSG00000056558 . [Q13077-2 ]
GeneIDi 7185.
KEGGi hsa:7185.
UCSCi uc004bku.2. human. [Q13077-1 ]

Organism-specific databases

CTDi 7185.
GeneCardsi GC09M123664.
HGNCi HGNC:12031. TRAF1.
HPAi CAB009593.
HPA001852.
MIMi 601711. gene.
neXtProti NX_Q13077.
PharmGKBi PA36708.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264247.
HOGENOMi HOG000231558.
HOVERGENi HBG058222.
InParanoidi Q13077.
KOi K03172.
OMAi HFMKEKL.
OrthoDBi EOG7966G5.
PhylomeDBi Q13077.
TreeFami TF321154.

Enzyme and pathway databases

SignaLinki Q13077.

Miscellaneous databases

EvolutionaryTracei Q13077.
GeneWikii TRAF1.
GenomeRNAii 7185.
NextBioi 28168.
PMAP-CutDB Q13077.
PROi Q13077.
SOURCEi Search...

Gene expression databases

Bgeei Q13077.
CleanExi HS_TRAF1.
Genevestigatori Q13077.

Family and domain databases

InterProi IPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view ]
PANTHERi PTHR10131:SF29. PTHR10131:SF29. 1 hit.
Pfami PF00917. MATH. 1 hit.
[Graphical view ]
PIRSFi PIRSF015614. TRAF. 1 hit.
SMARTi SM00061. MATH. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-139.

Entry informationi

Entry nameiTRAF1_HUMAN
AccessioniPrimary (citable) accession number: Q13077
Secondary accession number(s): B4DJ77, Q658U1, Q8NF13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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