Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

TNF receptor-associated factor 1

Gene

Traf1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 1
Gene namesi
Name:Traf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:101836. Traf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice have normal B-cell proliferation and antibody response, but increased T-cell proliferation in response to CD3 signaling. Their T-cells show enhanced activation of JNK and NF-kappa-B. Mice are highly susceptible to TNF-induced skin necrosis.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi139S → A: Loss of phosphorylation site. Reduces global phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000563981 – 409TNF receptor-associated factor 1Add BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei139Phosphoserine1 Publication1
Cross-linki178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei156 – 157Cleavage; by CASP8By similarity2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP39428.
MaxQBiP39428.
PaxDbiP39428.
PeptideAtlasiP39428.
PRIDEiP39428.

PTM databases

iPTMnetiP39428.
PhosphoSitePlusiP39428.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026875.
CleanExiMM_TRAF1.
ExpressionAtlasiP39428. baseline and differential.
GenevisibleiP39428. MM.

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 MAP3K14 (By similarity). Interacts with NFATC2IP, TRAFD1 and with HIVEP3.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AhcyP502473EBI-520123,EBI-646982
Hmg20bQ9Z1043EBI-520123,EBI-646920
Plekhn1Q8C8866EBI-520123,EBI-646708
TankP70347-112EBI-520123,EBI-646125
Tcf7l2Q924A06EBI-520123,EBI-646713

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204302. 6 interactors.
DIPiDIP-260N.
IntActiP39428. 35 interactors.
MINTiMINT-1518514.
STRINGi10090.ENSMUSP00000028234.

Structurei

3D structure databases

ProteinModelPortaliP39428.
SMRiP39428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 405MATHPROSITE-ProRule annotationAdd BLAST147

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili167 – 256By similarityAdd BLAST90

Domaini

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

Sequence similaritiesi

Contains 1 MATH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410ISDN. Eukaryota.
ENOG410YE68. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiP39428.
KOiK03172.
OMAiIHQSQLD.
OrthoDBiEOG091G0GHD.
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]

Sequencei

Sequence statusi: Complete.

P39428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK
60 70 80 90 100
CRADNLHPVS PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH
110 120 130 140 150
EATSQSSHLY LLLAVLKEWK SSPGSNLGSA PMALERNLSE LQLQAAVEAT
160 170 180 190 200
GDLEVDCYRA PCCESQEELA LQHLVKEKLL AQLEEKLRVF ANIVAVLNKE
210 220 230 240 250
VEASHLALAA SIHQSQLDRE HILSLEQRVV ELQQTLAQKD QVLGKLEHSL
260 270 280 290 300
RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL
310 320 330 340 350
RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH
360 370 380 390 400
AIDAFRPDLS SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF

LKCIVDTSA
Length:409
Mass (Da):45,465
Last modified:July 27, 2011 - v2
Checksum:iADD7F997169D9AAD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222I → L in AAC37663 (PubMed:8069916).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35302 mRNA. Translation: AAC37663.1.
AK029135 mRNA. Translation: BAC26315.1.
AK169515 mRNA. Translation: BAE41205.1.
AK172598 mRNA. Translation: BAE43086.1.
AL929068 Genomic DNA. Translation: CAM27599.1.
CH466542 Genomic DNA. Translation: EDL08637.1.
CCDSiCCDS15956.1.
PIRiA54750.
RefSeqiNP_001313530.1. NM_001326601.1.
NP_033447.2. NM_009421.4.
XP_011237352.1. XM_011239050.2.
XP_011237353.1. XM_011239051.2.
XP_011237354.1. XM_011239052.2.
XP_011237355.1. XM_011239053.2.
XP_011237356.1. XM_011239054.2.
XP_017172618.1. XM_017317129.1.
UniGeneiMm.239514.

Genome annotation databases

EnsembliENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
GeneIDi22029.
KEGGimmu:22029.
UCSCiuc008jjj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35302 mRNA. Translation: AAC37663.1.
AK029135 mRNA. Translation: BAC26315.1.
AK169515 mRNA. Translation: BAE41205.1.
AK172598 mRNA. Translation: BAE43086.1.
AL929068 Genomic DNA. Translation: CAM27599.1.
CH466542 Genomic DNA. Translation: EDL08637.1.
CCDSiCCDS15956.1.
PIRiA54750.
RefSeqiNP_001313530.1. NM_001326601.1.
NP_033447.2. NM_009421.4.
XP_011237352.1. XM_011239050.2.
XP_011237353.1. XM_011239051.2.
XP_011237354.1. XM_011239052.2.
XP_011237355.1. XM_011239053.2.
XP_011237356.1. XM_011239054.2.
XP_017172618.1. XM_017317129.1.
UniGeneiMm.239514.

3D structure databases

ProteinModelPortaliP39428.
SMRiP39428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204302. 6 interactors.
DIPiDIP-260N.
IntActiP39428. 35 interactors.
MINTiMINT-1518514.
STRINGi10090.ENSMUSP00000028234.

PTM databases

iPTMnetiP39428.
PhosphoSitePlusiP39428.

Proteomic databases

EPDiP39428.
MaxQBiP39428.
PaxDbiP39428.
PeptideAtlasiP39428.
PRIDEiP39428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
GeneIDi22029.
KEGGimmu:22029.
UCSCiuc008jjj.1. mouse.

Organism-specific databases

CTDi7185.
MGIiMGI:101836. Traf1.

Phylogenomic databases

eggNOGiENOG410ISDN. Eukaryota.
ENOG410YE68. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiP39428.
KOiK03172.
OMAiIHQSQLD.
OrthoDBiEOG091G0GHD.
TreeFamiTF321154.

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.

Miscellaneous databases

PROiP39428.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026875.
CleanExiMM_TRAF1.
ExpressionAtlasiP39428. baseline and differential.
GenevisibleiP39428. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P39428
Secondary accession number(s): Q8CE28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.