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P39428 (TRAF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNF receptor-associated factor 1
Gene names
Name:Traf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.9

Subunit structure

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. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm.

Domain

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.

Post-translational modification

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

Disruption phenotype

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. Ref.6

Sequence similarities

Contains 1 MATH domain.

Caution

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

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 By similarity

Sites

Site156 – 1572Cleavage; by CASP8 By similarity

Amino acid modifications

Modified residue1391Phosphoserine Ref.9
Cross-link178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis1391S → A: Loss of phosphorylation site. Reduces global phosphorylation. Ref.9
Sequence conflict2221I → L in AAC37663. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39428 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: ADD7F997169D9AAD

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 HILSLEQRVV 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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-135 AND 390-402, INTERACTION WITH TRAF2 AND TNFRSF1B.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Skin, Spleen and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAIP.
[6]"TRAF1 is a negative regulator of TNF signaling. enhanced TNF signaling in TRAF1-deficient mice."
Tsitsikov E.N., Laouini D., Dunn I.F., Sannikova T.Y., Davidson L., Alt F.W., Geha R.S.
Immunity 15:647-657(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIVEP3.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFATC2IP.
[9]"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 AT SER-139, INTERACTION WITH TNFRSF1B, MUTAGENESIS OF SER-139.
[10]"FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase signaling pathway."
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.
J. Biol. Chem. 283:33858-33864(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAFD1.
[11]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15956.1.
PIRA54750.
RefSeqNP_033447.2. NM_009421.3.
XP_006497906.1. XM_006497843.1.
XP_006497907.1. XM_006497844.1.
XP_006497908.1. XM_006497845.1.
UniGeneMm.239514.

3D structure databases

ProteinModelPortalP39428.
SMRP39428. Positions 174-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204302. 6 interactions.
DIPDIP-260N.
IntActP39428. 35 interactions.
MINTMINT-1518514.
STRING10090.ENSMUSP00000108687.

PTM databases

PhosphoSiteP39428.

Proteomic databases

PRIDEP39428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
GeneID22029.
KEGGmmu:22029.
UCSCuc008jjj.1. mouse.

Organism-specific databases

CTD7185.
MGIMGI:101836. Traf1.

Phylogenomic databases

eggNOGNOG264247.
GeneTreeENSGT00550000074359.
HOGENOMHOG000231558.
HOVERGENHBG058222.
InParanoidQ8CE28.
KOK03172.
OMAHFMKEKL.
OrthoDBEOG7966G5.
TreeFamTF321154.

Gene expression databases

BgeeP39428.
CleanExMM_TRAF1.
GenevestigatorP39428.

Family and domain databases

InterProIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view]
PANTHERPTHR10131:SF29. PTHR10131:SF29. 1 hit.
PfamPF00917. MATH. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 1 hit.
PROSITEPS50144. MATH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301776.
PROP39428.
SOURCESearch...

Entry information

Entry nameTRAF1_MOUSE
AccessionPrimary (citable) accession number: P39428
Secondary accession number(s): Q8CE28
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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