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P39428

- TRAF1_MOUSE

UniProt

P39428 - TRAF1_MOUSE

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Protein

TNF receptor-associated factor 1

Gene
Traf1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1572Cleavage; by CASP8 By similarity

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  3. regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  4. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 1
Gene namesi
Name:Traf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:101836. Traf1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi139 – 1391S → A: Loss of phosphorylation site. Reduces global phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409TNF receptor-associated factor 1PRO_0000056398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei139 – 1391Phosphoserine1 Publication
Cross-linki178 – 178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki186 – 186Glycyl 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.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP39428.

PTM databases

PhosphoSiteiP39428.

Expressioni

Gene expression databases

BgeeiP39428.
CleanExiMM_TRAF1.
GenevestigatoriP39428.

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 HIVEP3.6 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

Protein-protein interaction databases

BioGridi204302. 6 interactions.
DIPiDIP-260N.
IntActiP39428. 35 interactions.
MINTiMINT-1518514.
STRINGi10090.ENSMUSP00000108687.

Structurei

3D structure databases

ProteinModelPortaliP39428.
SMRiP39428. Positions 174-409.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 405147MATHAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili167 – 25690 By similarityAdd
BLAST

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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264247.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ8CE28.
KOiK03172.
OMAiHFMKEKL.
OrthoDBiEOG7966G5.
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]

Sequencei

Sequence statusi: Complete.

P39428-1 [UniParc]FASTAAdd to Basket

« Hide

MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK    50
CRADNLHPVS PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH 100
EATSQSSHLY LLLAVLKEWK SSPGSNLGSA PMALERNLSE LQLQAAVEAT 150
GDLEVDCYRA PCCESQEELA LQHLVKEKLL AQLEEKLRVF ANIVAVLNKE 200
VEASHLALAA SIHQSQLDRE HILSLEQRVV ELQQTLAQKD QVLGKLEHSL 250
RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL 300
RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH 350
AIDAFRPDLS SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF 400
LKCIVDTSA 409
Length:409
Mass (Da):45,465
Last modified:July 27, 2011 - v2
Checksum:iADD7F997169D9AAD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221I → L in AAC37663. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_033447.2. NM_009421.3.
XP_006497906.1. XM_006497843.1.
XP_006497907.1. XM_006497844.1.
XP_006497908.1. XM_006497845.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS15956.1.
PIRi A54750.
RefSeqi NP_033447.2. NM_009421.3.
XP_006497906.1. XM_006497843.1.
XP_006497907.1. XM_006497844.1.
XP_006497908.1. XM_006497845.1.
UniGenei Mm.239514.

3D structure databases

ProteinModelPortali P39428.
SMRi P39428. Positions 174-409.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204302. 6 interactions.
DIPi DIP-260N.
IntActi P39428. 35 interactions.
MINTi MINT-1518514.
STRINGi 10090.ENSMUSP00000108687.

PTM databases

PhosphoSitei P39428.

Proteomic databases

PRIDEi P39428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028234 ; ENSMUSP00000028234 ; ENSMUSG00000026875 .
ENSMUST00000113064 ; ENSMUSP00000108687 ; ENSMUSG00000026875 .
ENSMUST00000172159 ; ENSMUSP00000130759 ; ENSMUSG00000026875 .
GeneIDi 22029.
KEGGi mmu:22029.
UCSCi uc008jjj.1. mouse.

Organism-specific databases

CTDi 7185.
MGIi MGI:101836. Traf1.

Phylogenomic databases

eggNOGi NOG264247.
GeneTreei ENSGT00550000074359.
HOGENOMi HOG000231558.
HOVERGENi HBG058222.
InParanoidi Q8CE28.
KOi K03172.
OMAi HFMKEKL.
OrthoDBi EOG7966G5.
TreeFami TF321154.

Miscellaneous databases

NextBioi 301776.
PROi P39428.
SOURCEi Search...

Gene expression databases

Bgeei P39428.
CleanExi MM_TRAF1.
Genevestigatori P39428.

Family and domain databases

InterProi IPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027136. TRAF1.
[Graphical view ]
PANTHERi PTHR10131:SF29. PTHR10131:SF29. 1 hit.
Pfami PF00917. MATH. 1 hit.
[Graphical view ]
PIRSFi PIRSF015614. TRAF. 1 hit.
SMARTi SM00061. MATH. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

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: July 9, 2014
This is version 112 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.

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

External Data

Dasty 3

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