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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

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
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000056558-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
SignaLinkiQ13077.
SIGNORiQ13077.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12031. TRAF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163D → A: Abolishes CASP8-mediated cleavage. 2 Publications1
Mutagenesisi185K → R: Nearly abolished ubiquitination; when associated with R-193. 1 Publication1
Mutagenesisi193K → R: Nearly abolished ubiquitination; when associated with R-185. 1 Publication1

Organism-specific databases

DisGeNETi7185.
OpenTargetsiENSG00000056558.
PharmGKBiPA36708.

Polymorphism and mutation databases

BioMutaiTRAF1.
DMDMi6707734.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000563971 – 416TNF receptor-associated factor 1Add BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei146PhosphoserineBy similarity1
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki193Glycyl 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei163 – 164Cleavage; by CASP82

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13077.
PaxDbiQ13077.
PeptideAtlasiQ13077.
PRIDEiQ13077.

PTM databases

iPTMnetiQ13077.
PhosphoSitePlusiQ13077.

Miscellaneous databases

PMAP-CutDBQ13077.

Expressioni

Gene expression databases

BgeeiENSG00000056558.
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
itself4EBI-359224,EBI-359224
B2R8Y43EBI-359224,EBI-10175581
Q5W1503EBI-359224,EBI-10248148
Q9NWL93EBI-359224,EBI-10315054
A1CFQ9NQ945EBI-359224,EBI-2809489
AESQ081173EBI-359224,EBI-717810
AESQ08117-25EBI-359224,EBI-11741437
AKAP17AQ02040-33EBI-359224,EBI-10222656
ALS2CR11Q53TS83EBI-359224,EBI-739879
AQP1P299723EBI-359224,EBI-745213
ARSJQ8N5N63EBI-359224,EBI-10266832
BARD1A0AVN23EBI-359224,EBI-9977322
BCL6P411825EBI-359224,EBI-765407
BEX2Q9BXY83EBI-359224,EBI-745073
BIRC3Q134892EBI-359224,EBI-517709
C14orf105Q17R993EBI-359224,EBI-10238351
C1orf109Q9NX045EBI-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
CCHCR1Q8TD31-35EBI-359224,EBI-10175300
CDCA3Q996183EBI-359224,EBI-739534
CDKN1AP389363EBI-359224,EBI-375077
CDKN2BP427725EBI-359224,EBI-711280
CFLARO155195EBI-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
FAM161AQ3B8205EBI-359224,EBI-719941
FAM86C1Q9NVL13EBI-359224,EBI-751617
FBF1Q8TES7-63EBI-359224,EBI-10244131
FBXL18Q96D163EBI-359224,EBI-744419
FOSL2P154085EBI-359224,EBI-3893419
GATA2P237693EBI-359224,EBI-2806671
GATAD2BQ8WXI93EBI-359224,EBI-923440
GEMP550405EBI-359224,EBI-744104
GIT2Q141612EBI-359224,EBI-1046878
GLRX3O760035EBI-359224,EBI-374781
GMCL1P1Q8NEA93EBI-359224,EBI-745707
GNG5P632183EBI-359224,EBI-10220734
GORASP2Q9H8Y85EBI-359224,EBI-739467
HAUS1Q96CS23EBI-359224,EBI-2514791
HEY2Q9UBP55EBI-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
LNX1Q8TBB16EBI-359224,EBI-739832
MAPRE2Q155555EBI-359224,EBI-739717
METTL17Q9H7H03EBI-359224,EBI-749353
MORN3Q6PF187EBI-359224,EBI-9675802
MOSP005405EBI-359224,EBI-1757866
MYEF2Q9P2K5-23EBI-359224,EBI-10318831
NEBLO760413EBI-359224,EBI-2880203
NUFIP2A1L3A73EBI-359224,EBI-10172018
NUP58Q9BVL27EBI-359224,EBI-2811583
OLIG3Q7RTU35EBI-359224,EBI-10225049
PBX3Q5JS985EBI-359224,EBI-10244393
PDE4DQ084993EBI-359224,EBI-1642831
PHF21AQ96BD53EBI-359224,EBI-745085
PIN1Q135263EBI-359224,EBI-714158
PLEKHN1Q494U13EBI-359224,EBI-10241513
POM121L1PQ3SYA95EBI-359224,EBI-10241319
POP5Q969H65EBI-359224,EBI-366525
PPP1R13BQ96KQ43EBI-359224,EBI-1105153
PRDM7Q9NQW53EBI-359224,EBI-10312471
PSMA1P257863EBI-359224,EBI-359352
PSMB1P206185EBI-359224,EBI-372273
QRICH1Q2TAL85EBI-359224,EBI-2798044
RASAL2Q9UJF23EBI-359224,EBI-359444
RASSF5Q8WWW03EBI-359224,EBI-367390
RBM41Q96IZ53EBI-359224,EBI-740773
RBM45Q8IUH33EBI-359224,EBI-2512147
RIPK1Q135465EBI-359224,EBI-358507
RTP5Q14D333EBI-359224,EBI-10217913
RYDENQ9NUL53EBI-359224,EBI-10313866
SCNM1Q9BWG67EBI-359224,EBI-748391
SIK3Q9Y2K2-33EBI-359224,EBI-10326390
SLC25A48Q6ZT893EBI-359224,EBI-10255185
SLC25A6P122363EBI-359224,EBI-356254
SNW1Q135733EBI-359224,EBI-632715
SPG21Q9NZD85EBI-359224,EBI-742688
SSC5DA1L4H13EBI-359224,EBI-10172867
STK3Q131883EBI-359224,EBI-992580
SYCE1Q8N0S23EBI-359224,EBI-6872807
TCL1AP562797EBI-359224,EBI-749995
TEAD4D3DUQ63EBI-359224,EBI-10176734
TFAP4Q016643EBI-359224,EBI-2514218
TFPTA0A024R4Q54EBI-359224,EBI-11527449
THAP7Q9BT495EBI-359224,EBI-741350
TRAF2Q129336EBI-359224,EBI-355744
TRAF6Q9Y4K313EBI-359224,EBI-359276
TRIM23P364063EBI-359224,EBI-740098
TRIM42A1L4B63EBI-359224,EBI-10172216
TRPV6Q9Y2603EBI-359224,EBI-750052
TSSC4Q9Y5U23EBI-359224,EBI-717229
WACQ9BTA93EBI-359224,EBI-749118
ZBTB16Q055164EBI-359224,EBI-711925
ZC2HC1CQ53FD03EBI-359224,EBI-740767
ZFYVE21Q9BQ243EBI-359224,EBI-2849569
ZFYVE26Q96H433EBI-359224,EBI-10286915
ZNF124Q159735EBI-359224,EBI-2555767
ZNF20P170245EBI-359224,EBI-717634
ZNF417Q8TAU33EBI-359224,EBI-740727
ZNF440Q8IYI86EBI-359224,EBI-726439
ZNF502Q8TBZ55EBI-359224,EBI-10273699
ZNF512BQ96KM65EBI-359224,EBI-1049952
ZNF564Q8TBZ85EBI-359224,EBI-10273713
ZNF572A1L4E93EBI-359224,EBI-10172590
ZNF572Q7Z3I73EBI-359224,EBI-10257016
ZNF581Q9P0T43EBI-359224,EBI-745520
ZNF587Q96SQ55EBI-359224,EBI-6427977
ZNF662Q6ZS27-33EBI-359224,EBI-10255155

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi113037. 216 interactors.
DIPiDIP-27514N.
IntActiQ13077. 216 interactors.
MINTiMINT-1131534.
STRINGi9606.ENSP00000362994.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi183 – 241Combined sources59

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ13077.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini266 – 412MATHPROSITE-ProRule annotationAdd BLAST147

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili182 – 264Add BLAST83

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

eggNOGiENOG410ISDN. Eukaryota.
ENOG410YE68. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ13077.
KOiK03172.
OMAiIHQSQLD.
OrthoDBiEOG091G0GHD.
PhylomeDBiQ13077.
TreeFamiTF321154.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
InterProiIPR002083. MATH/TRAF_dom.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
IPR032070. TRAF_BIRC3-bd.
[Graphical view]
PANTHERiPTHR10131:SF29. PTHR10131:SF29. 1 hit.
PfamiPF16673. TRAF_BIRC3_bd. 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 differs from that shown. Reason: Frameshift at position 111.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054161139M → T.1 PublicationCorresponds to variant rs113495277dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0430921 – 122Missing in isoform 2. 1 PublicationAdd BLAST122

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.3. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M0DX-ray2.80C181-244[»]
ProteinModelPortaliQ13077.
SMRiQ13077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113037. 216 interactors.
DIPiDIP-27514N.
IntActiQ13077. 216 interactors.
MINTiMINT-1131534.
STRINGi9606.ENSP00000362994.

PTM databases

iPTMnetiQ13077.
PhosphoSitePlusiQ13077.

Polymorphism and mutation databases

BioMutaiTRAF1.
DMDMi6707734.

Proteomic databases

MaxQBiQ13077.
PaxDbiQ13077.
PeptideAtlasiQ13077.
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.3. human. [Q13077-1]

Organism-specific databases

CTDi7185.
DisGeNETi7185.
GeneCardsiTRAF1.
HGNCiHGNC:12031. TRAF1.
HPAiCAB009593.
HPA001852.
MIMi601711. gene.
neXtProtiNX_Q13077.
OpenTargetsiENSG00000056558.
PharmGKBiPA36708.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ISDN. Eukaryota.
ENOG410YE68. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ13077.
KOiK03172.
OMAiIHQSQLD.
OrthoDBiEOG091G0GHD.
PhylomeDBiQ13077.
TreeFamiTF321154.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000056558-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
SignaLinkiQ13077.
SIGNORiQ13077.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000056558.
CleanExiHS_TRAF1.
GenevisibleiQ13077. HS.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
InterProiIPR002083. MATH/TRAF_dom.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
IPR032070. TRAF_BIRC3-bd.
[Graphical view]
PANTHERiPTHR10131:SF29. PTHR10131:SF29. 1 hit.
PfamiPF16673. TRAF_BIRC3_bd. 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...

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: November 30, 2016
This is version 163 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

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 one 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.