[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH IRAK1. DOI=10.1038/383443a0; PubMed=8837778 [NCBI, ExPASy, EBI, Israel, Japan] Cao Z., Xiong J., Takeuchi M., Kurama T., Goeddel D.V.; "TRAF6 is a signal transducer for interleukin-1."; Nature 383:443-446(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. SeattleSNPs program for genomic applications; Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	REVIEW. DOI=10.1016/S0898-6568(01)00160-7; PubMed=11384837 [NCBI, ExPASy, EBI, Israel, Japan] Wajant H., Henkler F., Scheurich P.; "The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators."; Cell. Signal. 13:389-400(2001).
[5]	REVIEW. DOI=10.1038/sj.onc.1204788; PubMed=11607847 [NCBI, ExPASy, EBI, Israel, Japan] Bradley J.R., Pober J.S.; "Tumor necrosis factor receptor-associated factors (TRAFs)."; Oncogene 20:6482-6491(2001).
[6]	INTERACTION WITH MAP3K14. DOI=10.1038/385540a0; PubMed=9020361 [NCBI, ExPASy, EBI, Israel, Japan] Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.; "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1."; Nature 385:540-544(1997).
[7]	INTERACTION WITH IRAK2. DOI=10.1126/science.278.5343.1612; PubMed=9374458 [NCBI, ExPASy, EBI, Israel, Japan] Muzio M., Ni J., Feng P., Dixit V.M.; "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling."; Science 278:1612-1615(1997).
[8]	INTERACTION WITH RIPK2. DOI=10.1074/jbc.273.27.16968; PubMed=9642260 [NCBI, ExPASy, EBI, Israel, Japan] McCarthy J.V., Ni J., Dixit V.M.; "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."; J. Biol. Chem. 273:16968-16975(1998).
[9]	INTERACTION WITH TNFRSF11A. DOI=10.1074/jbc.273.43.28355; PubMed=9774460 [NCBI, ExPASy, EBI, Israel, Japan] Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.; "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."; J. Biol. Chem. 273:28355-28359(1998).
[10]	INTERACTION WITH TNFRSF5. DOI=10.1084/jem.187.2.237; PubMed=9432981 [NCBI, ExPASy, EBI, Israel, Japan] Kashiwada M., Shirakata Y., Inoue J., Nakano H., Okazaki K., Okumura K., Yamamoto T., Nagaoka H., Takemori T.; "Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway."; J. Exp. Med. 187:237-244(1998).
[11]	INTERACTION WITH MAP3K5. DOI=10.1016/S1097-2765(00)80283-X; PubMed=9774977 [NCBI, ExPASy, EBI, Israel, Japan] Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M., Miyazono K., Ichijo H.; "ASK1 is essential for JNK/SAPK activation by TRAF2."; Mol. Cell 2:389-395(1998).
[12]	INTERACTION WITH MAP3K1. PubMed=10346818 [NCBI, ExPASy, EBI, Israel, Japan] Baud V., Liu Z.-G., Bennett B., Suzuki N., Xia Y., Karin M.; "Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain."; Genes Dev. 13:1297-1308(1999).
[13]	INTERACTION WITH NGFR. DOI=10.1074/jbc.274.5.2597; PubMed=9915784 [NCBI, ExPASy, EBI, Israel, Japan] Khursigara G., Orlinick J.R., Chao M.V.; "Association of the p75 neurotrophin receptor with TRAF6."; J. Biol. Chem. 274:2597-2600(1999).
[14]	INTERACTION WITH IRAK3. DOI=10.1074/jbc.274.27.19403; PubMed=10383454 [NCBI, ExPASy, EBI, Israel, Japan] Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.; "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family."; J. Biol. Chem. 274:19403-19410(1999).
[15]	INTERACTION WITH NGFR. DOI=10.1074/jbc.274.42.30202; PubMed=10514511 [NCBI, ExPASy, EBI, Israel, Japan] Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H., Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.; "TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction."; J. Biol. Chem. 274:30202-30208(1999).
[16]	INTERACTION WITH TNFRSF11A AND CSK. DOI=10.1016/S1097-2765(00)80232-4; PubMed=10635328 [NCBI, ExPASy, EBI, Israel, Japan] Wong B.R., Besser D., Kim N., Arron J.R., Vologodskaia M., Hanafusa H., Choi Y.; "TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src."; Mol. Cell 4:1041-1049(1999).
[17]	INTERACTION WITH MAP3K5. DOI=10.1038/sj.onc.1202975; PubMed=10523862 [NCBI, ExPASy, EBI, Israel, Japan] Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.; "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)."; Oncogene 18:5814-5820(1999).
[18]	INTERACTION WITH UBE2V1, AND FUNCTION AS A E3 UBIQUITIN LIGASE. DOI=10.1016/S0092-8674(00)00126-4; PubMed=11057907 [NCBI, ExPASy, EBI, Israel, Japan] Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J.; "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain."; Cell 103:351-361(2000).
[19]	INTERACTION WITH TTRAP. DOI=10.1074/jbc.M000531200; PubMed=10764746 [NCBI, ExPASy, EBI, Israel, Japan] Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.; "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."; J. Biol. Chem. 275:18586-18593(2000).
[20]	INTERACTION WITH TNFRSF17. DOI=10.1073/pnas.160213497; PubMed=10908663 [NCBI, ExPASy, EBI, Israel, Japan] Shu H.-B., Johnson H.; "B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1."; Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000).
[21]	INTERACTION WITH TAX1BP1. DOI=10.1073/pnas.170279097; PubMed=10920205 [NCBI, ExPASy, EBI, Israel, Japan] Ling L., Goeddel D.V.; "T6BP, a TRAF6-interacting protein involved in IL-1 signaling."; Proc. Natl. Acad. Sci. U.S.A. 97:9567-9572(2000).
[22]	INTERACTION WITH ZNF675. DOI=10.1074/jbc.M110964200; PubMed=11751921 [NCBI, ExPASy, EBI, Israel, Japan] Shin J.N., Kim I., Lee J.S., Koh G.Y., Lee Z.H., Kim H.-H.; "A novel zinc finger protein that inhibits osteoclastogenesis and the function of tumor necrosis factor receptor-associated factor 6."; J. Biol. Chem. 277:8346-8353(2002).
[23]	INTERACTION WITH IRAK4. DOI=10.1073/pnas.082100399; PubMed=11960013 [NCBI, ExPASy, EBI, Israel, Japan] Li S., Strelow A., Fontana E.J., Wesche H.; "IRAK4: a novel member of the IRAK family with the properties of an IRAK-kinase."; Proc. Natl. Acad. Sci. U.S.A. 99:5567-5572(2002).
[24]	INTERACTION WITH PELI1. DOI=10.1074/jbc.M212112200; PubMed=12496252 [NCBI, ExPASy, EBI, Israel, Japan] Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X.; "Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex."; J. Biol. Chem. 278:10952-10956(2003).
[25]	INTERACTION WITH PELI1 AND PELI2. DOI=10.1016/S0014-5793(03)00533-7; PubMed=12804775 [NCBI, ExPASy, EBI, Israel, Japan] Jensen L.E., Whitehead A.S.; "Pellino2 activates the mitogen activated protein kinase pathway."; FEBS Lett. 545:199-202(2003).
[26]	INTERACTION WITH TICAM2. DOI=10.1074/jbc.M303451200; PubMed=12721283 [NCBI, ExPASy, EBI, Israel, Japan] Bin L.-H., Xu L.-G., Shu H.-B.; "TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing adapter protein involved in TIR signaling."; J. Biol. Chem. 278:24526-24532(2003).
[27]	INTERACTION WITH PELI3. PubMed=12874243 [NCBI, ExPASy, EBI, Israel, Japan] Jensen L.E., Whitehead A.S.; "Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein."; J. Immunol. 171:1500-1506(2003).
[28]	INTERACTION WITH TICAM1. PubMed=14530355 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K., Akira S.; "Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling."; J. Immunol. 171:4304-4310(2003).
[29]	INTERACTION WITH TICAM1. DOI=10.1074/jbc.M311629200; PubMed=14739303 [NCBI, ExPASy, EBI, Israel, Japan] Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.; "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."; J. Biol. Chem. 279:15652-15661(2004).
[30]	INTERACTION WITH MAVS. DOI=10.1016/j.cell.2005.08.012; PubMed=16125763 [NCBI, ExPASy, EBI, Israel, Japan] Seth R.B., Sun L., Ea C.-K., Chen Z.J.; "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."; Cell 122:669-682(2005).
[31]	INTERACTION WITH IL1RL1. DOI=10.1016/j.immuni.2005.09.015; PubMed=16286016 [NCBI, ExPASy, EBI, Israel, Japan] Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K., Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F., Kastelein R.A.; "IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST 2 and induces T helper type 2-associated cytokines."; Immunity 23:479-490(2005).
[32]	INTERACTION WITH TRAFD1. DOI=10.1074/jbc.M508221200; PubMed=16221674 [NCBI, ExPASy, EBI, Israel, Japan] Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T., Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.; "FLN29, a novel interferon- and LPS-inducible gene acting as a negative regulator of toll-like receptor signaling."; J. Biol. Chem. 280:41289-41297(2005).
[33]	INTERACTION WITH MAVS. DOI=10.1016/j.molcel.2005.08.014; PubMed=16153868 [NCBI, ExPASy, EBI, Israel, Japan] Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.; "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."; Mol. Cell 19:727-740(2005).
[34]	INTERACTION WITH JUB. DOI=10.1128/MCB.25.10.4010-4022.2005; PubMed=15870274 [NCBI, ExPASy, EBI, Israel, Japan] Feng Y., Longmore G.D.; "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex."; Mol. Cell. Biol. 25:4010-4022(2005).
[35]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 347-506 IN COMPLEX WITH TNFRSF11A, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-506 IN COMPLEX WITH TNFRSF5. DOI=10.1038/nature00888; PubMed=12140561 [NCBI, ExPASy, EBI, Israel, Japan] Ye H., Arron J.R., Lamothe B., Cirilli M., Kobayashi T., Shevde N.K., Segal D., Dzivenu O.K., Vologodskaia M., Yim M., Du K., Singh S., Pike J.W., Darnay B.G., Choi Y., Wu H.; "Distinct molecular mechanism for initiating TRAF6 signalling."; Nature 418:443-447(2002).

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. Also involved in the IL-1 signaling pathway via MYD88 and IRAK kinases. Seems to be involved in IL-17 signaling (By similarity). Mediates activation of NF-kappa-B and JNK. May function as an E3 ubiquitin ligase.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Homotrimer (Probable). Binds to TNFRSF5/CD40 and TNFRSF11A/RANK. Associates with NGFR, TNFRSF17, IRAK1, IRAK2, IRAK3, IRAK4, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, and TRAF-interacting protein TRIP and TRAF and TNF receptor associated protein TTRAP. Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ (By similarity). Interacts with PELI1, PELI2 and PELI3. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1. Interacts with IL1RL1. Interacts with TRAFD1. Interacts with ZNF675. Interacts with JUB. Interacts with TICAM1 and TICAM2.
INTERACTION:
P25942:CD40; NbExp=1; IntAct=EBI-359276, EBI-525714;
P17812:CTPS; NbExp=1; IntAct=EBI-359276, EBI-1042983;
Q9QZH6:Ecsit (xeno); NbExp=1; IntAct=EBI-359276, EBI-527020;
Q9HAV5:EDA2R; NbExp=1; IntAct=EBI-359276, EBI-526033;
O60573:EIF4E2; NbExp=1; IntAct=EBI-359276, EBI-398610;
P58107:EPPK1; NbExp=1; IntAct=EBI-359276, EBI-297954;
Q14697:GANAB; NbExp=1; IntAct=EBI-359276, EBI-348004;
P14778:IL1R1; NbExp=1; IntAct=EBI-359276, EBI-525905;
Q01638:IL1RL1; NbExp=1; IntAct=EBI-359276, EBI-993762;
P51617:IRAK1; NbExp=3; IntAct=EBI-359276, EBI-358664;
O43187:IRAK2; NbExp=1; IntAct=EBI-359276, EBI-447733;
Q9Y616:IRAK3; NbExp=1; IntAct=EBI-359276, EBI-447690;
Q99558:MAP3K14; NbExp=1; IntAct=EBI-359276, EBI-358011;
P33993:MCM7; NbExp=1; IntAct=EBI-359276, EBI-355924;
P11586:MTHFD1; NbExp=1; IntAct=EBI-359276, EBI-709638;
P49321:NASP; NbExp=1; IntAct=EBI-359276, EBI-716205;
Q6GQQ9:OTUD7B; NbExp=1; IntAct=EBI-359276, EBI-527784;
P22234:PAICS; NbExp=1; IntAct=EBI-359276, EBI-712261;
Q8N2H9-1:PELI3; NbExp=1; IntAct=EBI-359276, EBI-448466;
Q8N2H9-2:PELI3; NbExp=1; IntAct=EBI-359276, EBI-448472;
O15067:PFAS; NbExp=1; IntAct=EBI-359276, EBI-1052653;
P26639:TARS; NbExp=1; IntAct=EBI-359276, EBI-1042683;
Q86VP1:TAX1BP1; NbExp=1; IntAct=EBI-359276, EBI-529518;
Q9UDY2:TJP2; NbExp=1; IntAct=EBI-359276, EBI-1042602;
P21580:TNFAIP3; NbExp=1; IntAct=EBI-359276, EBI-527670;
Q9Y6Q6:TNFRSF11A; NbExp=1; IntAct=EBI-359276, EBI-525675;
O14545:TRAFD1; NbExp=1; IntAct=EBI-359276, EBI-1396921;
Q86XR7:TRAM; NbExp=1; IntAct=EBI-359276, EBI-525927;
P26640:VARS; NbExp=1; IntAct=EBI-359276, EBI-355765;
Q5VYM0:VCP; NbExp=1; IntAct=EBI-359276, EBI-1046421;
P21796:VDAC1; NbExp=1; IntAct=EBI-359276, EBI-354158;
Q8TD23:ZNF675; NbExp=3; IntAct=EBI-359276, EBI-528190;
Q9UGI0:ZRANB1; NbExp=1; IntAct=EBI-359276, EBI-527853;
SUBCELLULAR LOCATION: Cytoplasm (Probable).
TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
DOMAIN: The coiled coil domain mediates homo- and hetero-oligomerization.
DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
PTM: Polyubiquitinated (By similarity).
SIMILARITY: Contains 1 MATH domain.
SIMILARITY: Contains 1 RING-type zinc finger.
SIMILARITY: Contains 2 TRAF-type zinc fingers.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/traf6/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U78798; AAB38751.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY228337; AAO38054.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031052; AAH31052.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S71821; S71821.

RefSeq

NP_004611.1; -.
NP_665802.1; -.

UniGene

Hs.591983

3D structure databases

PDB

1LB4; X-ray; 2.40 A; A=348-504.	[ExPASy / RCSB / EBI]
1LB5; X-ray; 2.40 A; A=347-504.	[ExPASy / RCSB / EBI]
1LB6; X-ray; 1.80 A; A=347-504.	[ExPASy / RCSB / EBI]
2ECI; NMR; -; A=43-128.	[ExPASy / RCSB / EBI]
2JMD; NMR; -; A=63-124.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LB4; -.
1LB5; -.
1LB6; -.
2ECI; -.
2JMD; -.

ModBase

Q9Y4K3.

Protein-protein interaction databases

DIP

DIP:27515N; -.

IntAct

Q9Y4K3; -.

PTM databases

PhosphoSite

Q9Y4K3; -.

Enzyme and pathway databases

Reactome

REACT_6900; Signaling in Immune System.

Organism-specific databases

HIX0009567; -.

HGNC:12036; TRAF6.

CAB004605; -.

602355; gene. [NCBI / EBI]

PharmGKB

PA36713; -.

GeneCards

Q9Y4K3.

Gene expression databases

ArrayExpress

Q9Y4K3; -.

CleanEx

HS_TRAF6; -.

GermOnline

ENSG00000175104; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004842;	Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from UniProtKB).
GO:0007250;	Biological process: activation of NF-kappaB-inducing kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0043123;	Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from expression pattern from UniProtKB).
GO:0032743;	Biological process: positive regulation of interleukin-2 production (inferred from mutant phenotype from UniProtKB).
GO:0050870;	Biological process: positive regulation of T cell activation (inferred by curator from UniProtKB).
GO:0002726;	Biological process: positive regulation of T cell cytokine production (inferred from mutant phenotype from UniProtKB).
GO:0000209;	Biological process: protein polyubiquitination (inferred from direct assay from UniProtKB).
GO:0050852;	Biological process: T cell receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002083; MATH.
IPR012227; TNF_recpt_TRAF.
IPR013322; TRAF-type.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR001293; Znf_TRAF.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.210.10; TRAF-type; 1.
G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.

Pfam

PF00917; MATH; 1.
PF00097; zf-C3HC4; 1.
PF02176; zf-TRAF; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF015614; TRAF; 1.

SMART

SM00061; MATH; 1.
SM00184; RING; 1.
SMART graphical view of domain structure.

PROSITE

PS50144; MATH; 1.
PS00518; ZF_RING_1; 1.
PS50089; ZF_RING_2; 1.
PS50145; ZF_TRAF; 2.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q9Y4K3.

Genome annotation databases

Ensembl

ENSG00000175104; Homo sapiens. [Contig view]

GeneID

7189; -.

KEGG

hsa:7189; -.

Phylogenomic databases

HOVERGEN

Q9Y4K3; -.

Other

Q9Y4K3; -.

TRAF6; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Coiled coil; Cytoplasm; Metal-binding; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 522`	`522`	`TNF receptor-associated factor 6.`	`PRO_0000056407`
`DOMAIN`	`350 499`	`150`	`MATH.`
`ZN_FING`	`70 109`	`40`	`RING-type.`
`ZN_FING`	`150 202`	`53`	`TRAF-type 1.`
`ZN_FING`	`203 259`	`57`	`TRAF-type 2.`
`REGION`	`1 354`	`354`	`Interaction with TAX1BP1.`
`COILED`	`288 348`	`61`	`Potential.`
`CONFLICT`	`12 12`		`S -> F (in Ref. 2; AAH31052).`
`STRAND`	`67 70`	`4`
`TURN`	`71 74`	`4`
`TURN`	`91 94`	`4`
`HELIX`	`95 98`	`4`
`TURN`	`99 101`	`3`
`TURN`	`106 108`	`3`
`HELIX`	`114 116`	`3`
`STRAND`	`350 357`	`8`
`HELIX`	`360 368`	`9`
`STRAND`	`373 376`	`4`
`STRAND`	`380 386`	`7`
`STRAND`	`388 395`	`8`
`STRAND`	`401 403`	`3`
`STRAND`	`406 413`	`8`
`HELIX`	`419 421`	`3`
`STRAND`	`428 434`	`7`
`HELIX`	`440 442`	`3`
`STRAND`	`446 451`	`6`
`STRAND`	`471 478`	`8`
`HELIX`	`479 484`	`6`
`STRAND`	`492 501`	`10`

Sequence information

Length: 522 AA [This is the length of the unprocessed precursor]

Molecular weight: 59573 Da [This is the MW of the unprocessed precursor]

CRC64: 5AB9C255CCFEE749 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM EEIQGYDVEF 

        70         80         90        100        110        120 
DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD AGHKCPVDNE ILLENQLFPD 

       130        140        150        160        170        180 
NFAKREILSL MVKCPNEGCL HKMELRHLED HQAHCEFALM DCPQCQRPFQ KFHINIHILK 

       190        200        210        220        230        240 
DCPRRQVSCD NCAASMAFED KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI 

       250        260        270        280        290        300 
PCTFSTFGCH EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH 

       310        320        330        340        350        360 
QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN GIYIWKIGNF 

       370        380        390        400        410        420 
GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA QRCANYISLF VHTMQGEYDS 

       430        440        450        460        470        480 
HLPWPFQGTI RLTILDQSEA PVRQNHEEIM DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE 

       490        500        510        520 
ALRQRTFIKD DTLLVRCEVS TRFDMGSLRR EGFQPRSTDA GV

Q9Y4K3 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools