P39428 (TRAF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TNF receptor-associated factor 1

Gene names

Name:

Traf1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Domain	Coiled coil
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ahcy	P50247	3	EBI-520123,EBI-646982
Hmg20b	Q9Z104	3	EBI-520123,EBI-646920
Plekhn1	Q8C886	6	EBI-520123,EBI-646708
Tank	P70347-1	12	EBI-520123,EBI-646125
Tcf7l2	Q924A0	6	EBI-520123,EBI-646713

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	TNF receptor-associated factor 1		PRO_0000056398
Regions
	Domain	259 – 405	147	MATH
	Coiled coil	167 – 256	90	By similarity
Sites
	Site	156 – 157	2	Cleavage; by CASP8 By similarity
Amino acid modifications
	Modified residue	63	1	Phosphoserine Ref.11
	Modified residue	139	1	Phosphoserine Ref.9
	Cross-link	178		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	186		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Mutagenesis	139	1	S → A: Loss of phosphorylation site. Reduces global phosphorylation. Ref.9
	Sequence conflict	222	1	I → L in AAC37663. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39428 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: ADD7F997169D9AAD	FASTA	409	45,465
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00135899.
PIR	A54750.
RefSeq	NP_033447.2. NM_009421.3.
UniGene	Mm.239514.
3D structure databases
HSSP	HSSP built from PDB template 1CZY based on UniProtKB Q12933.
ProteinModelPortal	P39428.
SMR	P39428. Positions 14-54, 174-236, 243-409.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-260N.
IntAct	P39428. 35 interactions.
STRING	10090.ENSMUSP00000108687.
PTM databases
PhosphoSite	P39428.
Proteomic databases
PRIDE	P39428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875. ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875. ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
GeneID	22029.
KEGG	mmu:22029.
Organism-specific databases
CTD	7185.
MGI	MGI:101836. Traf1.
Phylogenomic databases
eggNOG	NOG264247.
GeneTree	ENSGT00550000074359.
HOGENOM	HOG000231558.
HOVERGEN	HBG058222.
InParanoid	Q8CE28.
KO	K03172.
OMA	RRCHESA.
OrthoDB	EOG42Z4Q6.
Gene expression databases
Bgee	P39428.
CleanEx	MM_TRAF1.
Genevestigator	P39428.
GermOnline	ENSMUSG00000026875. Mus musculus.
Family and domain databases
InterPro	IPR002083. MATH. IPR012227. TNF_rcpt--assoc_TRAF. IPR008974. TRAF-like. IPR027136. TRAF1. [Graphical view]
PANTHER	PTHR10131:SF29. PTHR10131:SF29. 1 hit.
Pfam	PF00917. MATH. 1 hit. [Graphical view]
PIRSF	PIRSF015614. TRAF. 1 hit.
SMART	SM00061. MATH. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 1 hit.
PROSITE	PS50144. MATH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301776.
SOURCE	Search...

Entry information

Entry name

TRAF1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program