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Reviewed, UniProtKB/Swiss-Prot P39428 (TRAF1_MOUSE)

Last modified October 13, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    TNF receptor-associated factor 1
Gene names
Name: Traf1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and JNK and is involved in apoptosis. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2.

Subunit structure

Homotrimer Probable. Heteromer with TRAF2 and associates with TNFRSF1B/TNFR2 through TRAF2. Associates with TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, TANK/ITRAF and RIPK2 By similarity. Interacts with BIRC2 and BIRC3 N-terminus By similarity. Binds TRAIP. Interacts with NFATC2IP and with HIVEP3.

Subcellular location

Cytoplasm.

Domain

The coiled coil domain mediates homo- and hetero-oligomerization.

The MATH/TRAF domain binds to receptor cytoplasmic domains.

Sequence similarities

Contains 1 MATH domain.

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Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of apoptosis

Inferred from electronic annotation. Source: InterPro

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.1

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

EDARQ9UNE01EBI-520123,EBI-529289From a different organism.
TNFRSF1BP203331EBI-520123,EBI-358983From a different organism.
TNFRSF8P289081EBI-520123,EBI-529023From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409TNF receptor-associated factor 1
PRO_0000056398

Regions

Domain259 – 405147MATH
Coiled coil167 – 25690 Potential

Amino acid modifications

Modified residue631Phosphoserine Ref.5

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Sequences

Sequence LengthMass (Da)Tools
P39428-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EBA7FEE5639FEDDF

FASTA40945,465
        10         20         30         40         50         60 
MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK CRADNLHPVS 

        70         80         90        100        110        120 
PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH EATSQSSHLY LLLAVLKEWK 

       130        140        150        160        170        180 
SSPGSNLGSA PMALERNLSE LQLQAAVEAT GDLEVDCYRA PCCESQEELA LQHLVKEKLL 

       190        200        210        220        230        240 
AQLEEKLRVF ANIVAVLNKE VEASHLALAA SIHQSQLDRE HLLSLEQRVV ELQQTLAQKD 

       250        260        270        280        290        300 
QVLGKLEHSL RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL 

       310        320        330        340        350        360 
RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH AIDAFRPDLS 

       370        380        390        400 
SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF LKCIVDTSA

« Hide

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References

« Hide 'large scale' references
[1]"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: 8069916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-135 AND 390-402, INTERACTION WITH TRAF2 AND TNFRSF1B.
[2]"TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation."
Lee S.Y., Lee S.Y., Choi Y.
J. Exp. Med. 185:1275-1285(1997) [PubMed: 9104814] [Abstract]
Cited for: INTERACTION WITH TRAIP.
[3]"A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-driven responses and interacts with TRAF2."
Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.
Mol. Cell 9:121-131(2002) [PubMed: 11804591] [Abstract]
Cited for: INTERACTION WITH HIVEP3.
[4]"TRAF1 regulates Th2 differentiation, allergic inflammation and nuclear localization of the Th2 transcription factor, NIP45."
Bryce P.J., Oyoshi M.K., Kawamoto S., Oettgen H.C., Tsitsikov E.N.
Int. Immunol. 18:101-111(2006) [PubMed: 16352630] [Abstract]
Cited for: INTERACTION WITH NFATC2IP.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L35302 mRNA. Translation: AAC37663.1.
IPIIPI00135899.
PIRA54750.
UniGeneMm.239514

3D structure databases

HSSPHSSP built from PDB template 1CZY based on UniProtKB Q12933.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:260N.
IntActP39428. 5 interactions.
STRINGP39428.

PTM databases

PhosphoSiteP39428.

Proteomic databases

PRIDEP39428.

Genome annotation databases

EnsemblENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875; Mus musculus. [Genome view]
ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:101836. Traf1.

Phylogenomic databases

HOGENOMP39428.
HOVERGENP39428.

Gene expression databases

ArrayExpressP39428.
BgeeP39428.
CleanExMM_TRAF1.
GenevestigatorP39428.
GermOnlineENSMUSG00000026875. Mus musculus.

Family and domain databases

InterProIPR002083. MATH.
IPR015448. TNF_rcpt-assoc_fac-1.
IPR012227. TNF_recpt_TRAF.
IPR013322. TRAF-type.
[Graphical view]
Gene3DG3DSA:2.60.210.10. TRAF-type. 1 hit.
PANTHERPTHR10131:SF26. TRAF1. 1 hit.
PfamPF00917. MATH. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
[Graphical view]
PROSITEPS50144. MATH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameTRAF1_MOUSE
AccessionPrimary (citable) accession number: P39428
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents