P70196 (TRAF6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TNF receptor-associated factor 6
EC=6.3.2.-

Alternative name(s):
E3 ubiquitin-protein ligase TRAF6

Gene names

Name:

Traf6

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	530 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation By similarity. Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Ref.5 Ref.6 Ref.11 Ref.12 Ref.16 Ref.17
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homotrimer By similarity. Homooligomer By similarity. N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Binds to TNFRSF5/CD40 and TNFRSF11A/RANK By similarity. Associates with NGFR, TNFRSF17, IRAK2, IRAK3, PELI2, PELI3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor associated protein TDP2. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1 By similarity. Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ. Interacts with IL1RL1. Interacts with AJUBA By similarity. Interacts with TRAFD1. Interacts with TICAM1 and TICAM2. Interacts with ZFAND5. Interacts with ARRB1 and ARRB2 By similarity. Interacts with MAP3K7 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with UBE2N. Interacts with TGFBR1, HDAC1 and RANGAP1. Interacts with AKT1, AKT2 and AKT3. Interacts (via TRAF domains) with NUMBL (via C-terminal) By similarity. Interacts (via TRAF domains) with WDR34 (via WD domains). Interacts with RBCK1 By similarity. Interacts with TRAF3IP2 By similarity. Interacts with LIMD1 (via LIM domains). Interacts with RSAD2/viperin. Interacts with IFIT3 (via N-terminus) By similarity. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) By similarity. Ref.7 Ref.8 Ref.9 Ref.15 Ref.17 Ref.18 Ref.19
Subcellular location	Cytoplasm By similarity. Cytoplasm › cell cortex By similarity. Nucleus By similarity. Lipid droplet. Note: RSAD2/viperin recruits it to the lipid droplet. Ref.19
Tissue specificity	Highly expressed in brain, lung, liver, skeletal muscle, and kidney; lower expression in heart, spleen, and testis.
Domain	The coiled coil domain mediates homo- and hetero-oligomerization. The MATH/TRAF domain binds to receptor cytoplasmic domains.
Post-translational modification	Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1 By similarity. Polyubiquitinated; after cell stimulation with IL-1-beta or TGF-beta. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form By similarity.
Disruption phenotype	Abrogation of IL-1-induced activation of NF-kappa-B, MAPK8/JNK and MAPK14/p38. Animals appears normal at birth but becomes smaller after one week. Show runting, failure of tooth eruption and die after three weeks. Exhibit severe osteopetrosis, thymic atrophy, lymph node deficiency, splenomegaly, and have alopecia and lack sweat glands. Ref.5 Ref.6 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
Sequence similarities	Belongs to the TNF receptor-associated factor family. A subfamily. Contains 1 MATH domain. Contains 1 RING-type zinc finger. Contains 2 TRAF-type zinc fingers.

Ontologies

Keywords
Biological process	Osteogenesis Ubl conjugation pathway
Cellular component	Cytoplasm Lipid droplet Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.16. Source: UniProtKB JNK cascade Inferred from electronic annotation. Source: Compara T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara T-helper 1 type immune response Inferred from mutant phenotype Ref.11. Source: MGI activation of NF-kappaB-inducing kinase activity Inferred from electronic annotation. Source: Compara antigen processing and presentation of exogenous peptide antigen via MHC class II Inferred from mutant phenotype Ref.11. Source: MGI bone resorption Inferred from mutant phenotype Ref.6. Source: UniProtKB cell development Inferred from mutant phenotype Ref.14. Source: MGI interleukin-1-mediated signaling pathway Inferred from mutant phenotype Ref.5. Source: UniProtKB myeloid dendritic cell differentiation Inferred from mutant phenotype Ref.11. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara neural tube closure Inferred from mutant phenotype PubMed 11007897. Source: UniProtKB odontogenesis of dentin-containing tooth Inferred from mutant phenotype PubMed 14699584. Source: MGI ossification Inferred from mutant phenotype Ref.6. Source: MGI osteoclast differentiation Inferred from mutant phenotype Ref.5. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.12. Source: UniProtKB positive regulation of JUN kinase activity Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of T cell cytokine production Inferred from electronic annotation. Source: Compara positive regulation of T cell proliferation Inferred from mutant phenotype Ref.5. Source: UniProtKB positive regulation of interleukin-12 biosynthetic process Inferred from mutant phenotype Ref.11. Source: MGI positive regulation of interleukin-2 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-6 biosynthetic process Inferred from mutant phenotype Ref.11. Source: MGI positive regulation of lipopolysaccharide-mediated signaling pathway Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara protein K63-linked ubiquitination Inferred from direct assay PubMed 16252010. Source: UniProtKB protein autoubiquitination Traceable author statement PubMed 16378096. Source: UniProtKB protein complex assembly Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from electronic annotation. Source: InterPro regulation of immunoglobulin secretion Inferred from direct assay PubMed 12958312. Source: MGI
Cellular_component	CD40 receptor complex Inferred from direct assay PubMed 20614026. Source: BHF-UCL cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 16831874. Source: UniProtKB internal side of plasma membrane Inferred from direct assay PubMed 20614026. Source: BHF-UCL lipid particle Inferred from direct assay Ref.19. Source: UniProtKB nuclear membrane Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	signal transducer activity Traceable author statement Ref.6. Source: MGI ubiquitin-protein ligase activity Inferred from direct assay PubMed 16252010. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cd40	P27512	2	EBI-448028,EBI-525742
Ecsit	Q9QZH6	4	EBI-448028,EBI-527020
Irak1	Q62406-1	4	EBI-448028,EBI-488313
Map3k3	Q61084	4	EBI-448028,EBI-446250
Nr0b2	Q62227	5	EBI-448028,EBI-4310440
Ptpn11	P35235	2	EBI-448028,EBI-397236
Tifa	Q793I8	2	EBI-448028,EBI-524817
Traf3ip2	Q8C0E5	3	EBI-448028,EBI-530713
Trafd1	Q3UDK1	2	EBI-448028,EBI-1396948

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70196-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P70196-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-174: DAGHKCPVDN...CQRPFQKCQV → YLILRKHGAL...TQPPGKLQSP
     175-530: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 530	530	TNF receptor-associated factor 6		PRO_0000056408
Regions
	Domain	358 – 507	150	MATH
	Zinc finger	70 – 109	40	RING-type
	Zinc finger	150 – 202	53	TRAF-type 1
	Zinc finger	203 – 259	57	TRAF-type 2
	Region	1 – 362	362	Interaction with TAX1BP1 By similarity
	Coiled coil	299 – 356	58	Potential
Amino acid modifications
	Cross-link	124		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
	Cross-link	124		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
	Cross-link	142		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	461		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	100 – 174	75	DAGHK…QKCQV → YLILRKHGALQQPNVKSMLE TGHPKNRQTENTGQEHSRMD RNLRQLGSHPSLYYGMNRGL LPCLPTQPPGKLQSP in isoform 2.		VSP_007404
	Alternative sequence	175 – 530	356	Missing in isoform 2.		VSP_007405
Experimental info
	Sequence conflict	251	1	E → Q in BAA12705. Ref.1
	Sequence conflict	251	1	E → Q in BAC30850. Ref.2
	Sequence conflict	367	1	N → K in BAA12705. Ref.1
	Sequence conflict	367	1	N → K in BAC30850. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 9, 2010. Version 2. Checksum: F8389250425E4E2D	FASTA	530	60,070
	10 20 30 40 50 60 MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM EEIQGYDVEF 70 80 90 100 110 120 DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD AGHKCPVDNE ILLENQLFPD 130 140 150 160 170 180 NFAKREILSL TVKCPNKGCL QKMELRHLED HQVHCEFALV NCPQCQRPFQ KCQVNTHIIE 190 200 210 220 230 240 DCPRRQVSCV NCAVSMAYEE KEIHDQSCPL ANIICEYCGT ILIREQMPNH YDLDCPTAPI 250 260 270 280 290 300 PCTFSVFGCH EKMQRNHLAR HLQENTQLHM RLLAQAVHNV NLALRPCDAA SPSRGCRPED 310 320 330 340 350 360 PNYEETIKQL ESRLVRQDHQ IRELTAKMET QSMYVGELKR TIRTLEDKVA EMEAQQCNGI 370 380 390 400 410 420 YIWKIGNFGM HLKSQEEERP VVIHSPGFYT GRPGYKLCMR LHLQLPTAQR CANYISLFVH 430 440 450 460 470 480 TMQGEYDSHL PWPFQGTIRL TILDQSEALI RQNHEEVMDA KPELLAFQRP TIPRNPKGFG 490 500 510 520 530 YVTFMHLEAL RQGTFIKDDT LLVRCEVSTR FDMGGLRKEG FQPRSTDAGV
	Isoform 2 [UniParc]. Checksum: F66189179AA9F9D3	FASTA	174	18,961
	10 20 30 40 50 60 MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM EEIQGYDVEF 70 80 90 100 110 120 DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRY LILRKHGALQ QPNVKSMLET 130 140 150 160 170 GHPKNRQTEN TGQEHSRMDR NLRQLGSHPS LYYGMNRGLL PCLPTQPPGK LQSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region." Ishida T., Mizushima S., Azuma S., Kobayashi N., Tojo T., Suzuki K., Aizawa S., Watanabe T., Mosialos G., Kieff E., Yamamoto T., Inoue J. J. Biol. Chem. 271:28745-28748(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/Kaplan. Tissue: T-cell lymphoma.
[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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Aorta and Vein.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice." Naito A., Azuma S., Tanaka S., Miyazaki T., Takaki S., Takatsu K., Nakao K., Nakamura K., Katsuki M., Yamamoto T., Inoue J. Genes Cells 4:353-362(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]	"TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling." Lomaga M.A., Yeh W.C., Sarosi I., Duncan G.S., Furlonger C., Ho A., Morony S., Capparelli C., Van G., Kaufman S., van der Heiden A., Itie A., Wakeham A., Khoo W., Sasaki T., Cao Z., Penninger J.M., Paige C.J. , Lacey D.L., Dunstan C.R., Boyle W.J., Goeddel D.V., Mak T.W. Genes Dev. 13:1015-1024(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]	"The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway." Sanz L., Diaz-Meco M.T., Nakano H., Moscat J. EMBO J. 19:1576-1586(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SQSTM1 AND PRKCZ.
[8]	"Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin 17 signal transduction." Schwandner R., Yamaguchi K., Cao Z. J. Exp. Med. 191:1233-1240(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IL17R.
[9]	"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor." Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J. J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SQSTM1; PRKCZ AND NGFR.
[10]	"TRAF6-deficient mice display hypohidrotic ectodermal dysplasia." Naito A., Yoshida H., Nishioka E., Satoh M., Azuma S., Yamamoto T., Nishikawa S., Inoue J. Proc. Natl. Acad. Sci. U.S.A. 99:8766-8771(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[11]	"TRAF6 is a critical factor for dendritic cell maturation and development." Kobayashi T., Walsh P.T., Walsh M.C., Speirs K.M., Chiffoleau E., King C.G., Hancock W.W., Caamano J.H., Hunter C.A., Scott P., Turka L.A., Choi Y. Immunity 19:353-363(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[12]	"TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent pathway but not toll/IL-1 receptor domain-containing adaptor-inducing IFN-beta (TRIF)-dependent pathway in TLR signaling." Gohda J., Matsumura T., Inoue J. J. Immunol. 173:2913-2917(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[13]	"The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination." Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T., Moscat J. J. Biol. Chem. 280:35625-35629(2005) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[14]	"Dependence of self-tolerance on TRAF6-directed development of thymic stroma." Akiyama T., Maeda S., Yamane S., Ogino K., Kasai M., Kajiura F., Matsumoto M., Inoue J. Science 308:248-251(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[15]	"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1." Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S., Kim I.H., Kim S.J., Park S.H. Nat. Immunol. 7:1057-1065(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; MYD88 AND PELI1.
[16]	"Characteristics and biological functions of TRAF6." Inoue J., Gohda J., Akiyama T. Adv. Exp. Med. Biol. 597:72-79(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[17]	"The LIM protein, Limd1, regulates AP-1 activation through an interaction with Traf6 to influence osteoclast development." Feng Y., Zhao H., Luderer H.F., Epple H., Faccio R., Ross F.P., Teitelbaum S.L., Longmore G.D. J. Biol. Chem. 282:39-48(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMD1.
[18]	"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.
[19]	"Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells." Saitoh T., Satoh T., Yamamoto N., Uematsu S., Takeuchi O., Kawai T., Akira S. Immunity 34:352-363(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RSAD2, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D84655 mRNA. Translation: BAA12705.1. AK041172 mRNA. Translation: BAC30850.1. AK155434 mRNA. Translation: BAE33263.1. AL929571 Genomic DNA. Translation: CAM20505.1. CH466519 Genomic DNA. Translation: EDL27656.1. CH466519 Genomic DNA. Translation: EDL27657.1. BC060705 mRNA. Translation: AAH60705.1.
IPI	IPI00136488. IPI00222919.
RefSeq	NP_033450.2. NM_009424.2.
UniGene	Mm.292729.
3D structure databases
ProteinModelPortal	P70196.
SMR	P70196. Positions 54-210, 317-516.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29812N.
IntAct	P70196. 28 interactions.
MINT	MINT-252449.
STRING	10090.ENSMUSP00000004949.
PTM databases
PhosphoSite	P70196.
Proteomic databases
PaxDb	P70196.
PRIDE	P70196.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164.
GeneID	22034.
KEGG	mmu:22034.
UCSC	uc008lhl.1. mouse. uc008lhm.1. mouse.
Organism-specific databases
CTD	7189.
MGI	MGI:108072. Traf6.
Phylogenomic databases
eggNOG	NOG289765.
GeneTree	ENSGT00550000074359.
HOGENOM	HOG000006625.
HOVERGEN	HBG060248.
InParanoid	Q6P9M0.
KO	K03175.
OMA	SEAPIRQ.
OrthoDB	EOG4320XV.
Enzyme and pathway databases
Reactome	REACT_107772. Immune System. REACT_115202. Signal Transduction.
UniPathway	UPA00143.
Gene expression databases
Bgee	P70196.
CleanEx	MM_TRAF6.
Genevestigator	P70196.
GermOnline	ENSMUSG00000027164. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR002083. MATH. IPR012227. TNF_rcpt--assoc_TRAF. IPR008974. TRAF-like. IPR027139. TRAF6. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. IPR001293. Znf_TRAF. [Graphical view]
PANTHER	PTHR10131:SF48. PTHR10131:SF48. 1 hit.
Pfam	PF00917. MATH. 1 hit. [Graphical view]
PIRSF	PIRSF015614. TRAF. 1 hit.
SMART	SM00061. MATH. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 3 hits.
PROSITE	PS50144. MATH. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. PS50145. ZF_TRAF. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	301798.
SOURCE	Search...

Entry information

Entry name

TRAF6_MOUSE

Accession

Primary (citable) accession number: P70196
Secondary accession number(s): Q6P9M0, Q8BLV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program