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Protein

TNF receptor-associated factor 1

Gene

TRAF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • thioesterase binding Source: UniProtKB
  • tumor necrosis factor receptor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein complex assembly Source: ProtInc
  • regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • 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 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12031. TRAF1.

Subcellular locationi

GO - Cellular componenti

  • 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.

Polymorphism and mutation databases

BioMutaiTRAF1.
DMDMi6707734.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461PhosphoserineBy 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.2 Publications

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.
GenevisibleiQ13077. HS.

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.By similarity21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B2R8Y43EBI-359224,EBI-10175581
Q5W1503EBI-359224,EBI-10248148
Q9NWL93EBI-359224,EBI-10315054
A1CFQ9NQ943EBI-359224,EBI-2809489
AESQ081173EBI-359224,EBI-717810
AKAP17AQ02040-33EBI-359224,EBI-10222656
ALS2CR11Q53TS83EBI-359224,EBI-739879
AQP1P299723EBI-359224,EBI-745213
ARSJQ8N5N63EBI-359224,EBI-10266832
BARD1A0AVN23EBI-359224,EBI-9977322
BCL6P411823EBI-359224,EBI-765407
BEX2Q9BXY83EBI-359224,EBI-745073
BIRC3Q134892EBI-359224,EBI-517709
C14orf105Q17R993EBI-359224,EBI-10238351
C19orf66Q9NUL53EBI-359224,EBI-10313866
C1orf109Q9NX043EBI-359224,EBI-8643161
C1orf216Q8TAB53EBI-359224,EBI-747505
C5orf30Q96GV93EBI-359224,EBI-2350695
CARHSP1Q9Y2V23EBI-359224,EBI-718719
CCDC116Q8IYX33EBI-359224,EBI-744311
CCDC120Q96HB5-43EBI-359224,EBI-10185348
CCDC146Q8IYE0-23EBI-359224,EBI-10247802
CCHCR1Q8TD31-33EBI-359224,EBI-10175300
CDCA3Q996183EBI-359224,EBI-739534
CDKN1AP389363EBI-359224,EBI-375077
CDKN2BP427723EBI-359224,EBI-711280
CFLARO155193EBI-359224,EBI-514941
CHCHD3Q9NX633EBI-359224,EBI-743375
COX5BP106063EBI-359224,EBI-1053725
CRYGAQ24JT53EBI-359224,EBI-10239205
CYB5R2Q6BCY43EBI-359224,EBI-744761
DEPTORQ8TB453EBI-359224,EBI-2359040
DMRT3Q9NQL93EBI-359224,EBI-9679045
DOK3Q7L5913EBI-359224,EBI-2834978
ECH1Q130113EBI-359224,EBI-711968
EHHADHQ084263EBI-359224,EBI-2339219
EWSR1Q018443EBI-359224,EBI-739737
FAM161AQ3B8203EBI-359224,EBI-719941
FAM86C1Q9NVL13EBI-359224,EBI-751617
FBF1Q8TES7-63EBI-359224,EBI-10244131
FBXL18Q96D163EBI-359224,EBI-744419
FOSL2P154083EBI-359224,EBI-3893419
GATA2P237693EBI-359224,EBI-2806671
GATAD2BQ8WXI93EBI-359224,EBI-923440
GEMP550403EBI-359224,EBI-744104
GIT2Q141612EBI-359224,EBI-1046878
GLRX3O760033EBI-359224,EBI-374781
GMCL1P1Q8NEA93EBI-359224,EBI-745707
GNG5P632183EBI-359224,EBI-10220734
GORASP2Q9H8Y83EBI-359224,EBI-739467
HAUS1Q96CS23EBI-359224,EBI-2514791
HEY2Q9UBP53EBI-359224,EBI-750630
HOXA1P496393EBI-359224,EBI-740785
Hoxa1P090224EBI-359224,EBI-3957603From a different organism.
HOXD12P354523EBI-359224,EBI-10206752
JOSD1Q150403EBI-359224,EBI-2510602
KIAA1217Q5T5P2-63EBI-359224,EBI-10188326
KLHL38Q2WGJ63EBI-359224,EBI-6426443
LATS1Q6PJG33EBI-359224,EBI-10253976
LCORQ96JN03EBI-359224,EBI-8833163
MAPRE2Q155553EBI-359224,EBI-739717
METTL17Q9H7H03EBI-359224,EBI-749353
MORN3Q6PF183EBI-359224,EBI-9675802
MOSP005403EBI-359224,EBI-1757866
MYEF2Q9P2K5-23EBI-359224,EBI-10318831
NEBLO760413EBI-359224,EBI-2880203
NUFIP2A1L3A73EBI-359224,EBI-10172018
NUPL1Q9BVL23EBI-359224,EBI-2811583
OLIG3Q7RTU33EBI-359224,EBI-10225049
PBX3Q5JS983EBI-359224,EBI-10244393
PDE4DQ084993EBI-359224,EBI-1642831
PHF21AQ96BD53EBI-359224,EBI-745085
PIN1Q135263EBI-359224,EBI-714158
PLEKHN1Q494U13EBI-359224,EBI-10241513
POM121L1PQ3SYA93EBI-359224,EBI-10241319
POP5Q969H63EBI-359224,EBI-366525
PPP1R13BQ96KQ43EBI-359224,EBI-1105153
PRDM7Q9NQW53EBI-359224,EBI-10312471
PSMA1P257863EBI-359224,EBI-359352
PSMB1P206183EBI-359224,EBI-372273
QRICH1Q2TAL83EBI-359224,EBI-2798044
RASAL2Q9UJF23EBI-359224,EBI-359444
RASSF5Q8WWW03EBI-359224,EBI-367390
RBM41Q96IZ53EBI-359224,EBI-740773
RBM45Q8IUH33EBI-359224,EBI-2512147
RIPK1Q135463EBI-359224,EBI-358507
RTP5Q14D333EBI-359224,EBI-10217913
SCNM1Q9BWG63EBI-359224,EBI-748391
SIK3Q9Y2K2-33EBI-359224,EBI-10326390
SLC25A48Q6ZT893EBI-359224,EBI-10255185
SLC25A6P122363EBI-359224,EBI-356254
SNW1Q135733EBI-359224,EBI-632715
SPG21Q9NZD83EBI-359224,EBI-742688
SSC5DA1L4H13EBI-359224,EBI-10172867
STK3Q131883EBI-359224,EBI-992580
SYCE1Q8N0S23EBI-359224,EBI-6872807
TCL1AP562793EBI-359224,EBI-749995
TEAD4D3DUQ63EBI-359224,EBI-10176734
TFAP4Q016643EBI-359224,EBI-2514218
THAP7Q9BT493EBI-359224,EBI-741350
TRAF2Q129334EBI-359224,EBI-355744
TRAF6Q9Y4K38EBI-359224,EBI-359276
TRIM23P364063EBI-359224,EBI-740098
TRIM42A1L4B63EBI-359224,EBI-10172216
TRPV6Q9Y2603EBI-359224,EBI-750052
TSSC4Q9Y5U23EBI-359224,EBI-717229
WACQ9BTA93EBI-359224,EBI-749118
ZC2HC1CQ53FD03EBI-359224,EBI-740767
ZFYVE21Q9BQ243EBI-359224,EBI-2849569
ZFYVE26Q96H433EBI-359224,EBI-10286915
ZNF124Q159733EBI-359224,EBI-2555767
ZNF20P170243EBI-359224,EBI-717634
ZNF417Q8TAU33EBI-359224,EBI-740727
ZNF440Q8IYI84EBI-359224,EBI-726439
ZNF502Q8TBZ53EBI-359224,EBI-10273699
ZNF512BQ96KM63EBI-359224,EBI-1049952
ZNF564Q8TBZ83EBI-359224,EBI-10273713
ZNF572A1L4E93EBI-359224,EBI-10172590
ZNF572Q7Z3I73EBI-359224,EBI-10257016
ZNF581Q9P0T43EBI-359224,EBI-745520
ZNF587Q96SQ53EBI-359224,EBI-6427977
ZNF662Q6ZS27-33EBI-359224,EBI-10255155

Protein-protein interaction databases

BioGridi113037. 182 interactions.
DIPiDIP-27514N.
IntActiQ13077. 143 interactions.
MINTiMINT-1131534.
STRINGi9606.ENSP00000362994.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi183 – 24159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M0DX-ray2.80C181-244[»]
ProteinModelPortaliQ13077.
SMRiQ13077. Positions 181-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13077.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 412147MATHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili182 – 26483Add
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.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264247.
GeneTreeiENSGT00550000074359.
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. AlignAdd to basket

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

        10         20         30         40         50
MASSSGSSPR PAPDENEFPF GCPPTVCQDP KEPRALCCAG CLSENPRNGE
60 70 80 90 100
DQICPKCRGE DLQSISPGSR LRTQEKAHPE VAEAGIGCPF AGVGCSFKGS
110 120 130 140 150
PQSVQEHEVT SQTSHLNLLL GFMKQWKARL GCGLESGPMA LEQNLSDLQL
160 170 180 190 200
QAAVEVAGDL EVDCYRAPCS ESQEELALQH FMKEKLLAEL EGKLRVFENI
210 220 230 240 250
VAVLNKEVEA SHLALATSIH QSQLDRERIL SLEQRVVELQ QTLAQKDQAL
260 270 280 290 300
GKLEQSLRLM EEASFDGTFL WKITNVTRRC HESACGRTVS LFSPAFYTAK
310 320 330 340 350
YGYKLCLRLY LNGDGTGKRT HLSLFIVIMR GEYDALLPWP FRNKVTFMLL
360 370 380 390 400
DQNNREHAID AFRPDLSSAS FQRPQSETNV ASGCPLFFPL SKLQSPKHAY
410
VKDDTMFLKC IVETST
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. Curated

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. 1 PublicationVSP_043092Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M0DX-ray2.80C181-244[»]
ProteinModelPortaliQ13077.
SMRiQ13077. Positions 181-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113037. 182 interactions.
DIPiDIP-27514N.
IntActiQ13077. 143 interactions.
MINTiMINT-1131534.
STRINGi9606.ENSP00000362994.

PTM databases

PhosphoSiteiQ13077.

Polymorphism and mutation databases

BioMutaiTRAF1.
DMDMi6707734.

Proteomic databases

MaxQBiQ13077.
PaxDbiQ13077.
PRIDEiQ13077.

Protocols and materials databases

DNASUi7185.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi7185.
GeneCardsiGC09M123664.
HGNCiHGNC:12031. TRAF1.
HPAiCAB009593.
HPA001852.
MIMi601711. gene.
neXtProtiNX_Q13077.
PharmGKBiPA36708.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264247.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ13077.
KOiK03172.
OMAiHFMKEKL.
OrthoDBiEOG7966G5.
PhylomeDBiQ13077.
TreeFamiTF321154.

Enzyme and pathway databases

SignaLinkiQ13077.

Miscellaneous databases

EvolutionaryTraceiQ13077.
GeneWikiiTRAF1.
GenomeRNAii7185.
NextBioi28168.
PMAP-CutDBQ13077.
PROiQ13077.
SOURCEiSearch...

Gene expression databases

BgeeiQ13077.
CleanExiHS_TRAF1.
GenevisibleiQ13077. HS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 147 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

Caution

Lacks a RING domain and has therefore no E3 ubiquitin-protein ligase activity by itself.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.