Reviewed, UniProtKB/Swiss-Prot Q9V3Q6 (M3K7_DROME)

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase kinase kinase 7
    EC=2.7.11.25
Alternative name(s):
    TGF-beta-activated kinase 1
    dTAK1

Gene names

Name:	Tak1
ORF Names:	CG18492

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	678 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Component of a protein kinase signal transduction cascade. Mediator of TGF-beta signal transduction. Responsible for activation of the JNK MAPK pathway (basket, bsk and hemipterous, hep) in response to LPS. Component of the NF-kappa-B pathway; relish-mediated JNK inhibition involves proteasomal degradation of Tak1; certain targets of Relish that are induced during immune responses may facilitate destruction of Tak1 and switch off the JNK cascade. Participates in diverse roles such as control of cell shape and regulation of apoptosis. Ref.1 Ref.5 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Immune response Innate immunity
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	I-kappaB kinase/NF-kappaB cascade Ref.5 Inferred from mutant phenotype. Source: UniProtKB activation of JNKK activity Ref.5 Inferred from mutant phenotype. Source: UniProtKB apoptosis Ref.1 Inferred from genetic interaction. Source: FlyBase dorsal closure Ref.1 Inferred from mutant phenotype. Source: FlyBase innate immune response Inferred from electronic annotation. Source: UniProtKB-KW notum morphogenesis Inferred from mutant phenotype. Source: FlyBase ommatidial rotation Inferred from mutant phenotype. Source: FlyBase positive regulation of antibacterial peptide biosynthetic process Traceable author statement. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase kinase kinase activity Ref.5 Inferred from mutant phenotype. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 678	678	Mitogen-activated protein kinase kinase kinase 7		PRO_0000086254
Regions
	Domain	19 – 271	253	Protein kinase
	Nucleotide binding	25 – 33	9	ATP By similarity
	Compositional bias	621 – 644	24	His-rich
Sites
	Active site	140	1	Proton acceptor By similarity
	Binding site	46	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V3Q6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 87EBA80CDB8CDE45	FASTA	678	75,675
	10 20 30 40 50 60 MATASLDALQ AAYVDFSEIT LREKVGHGSY GVVCKAVWRD KLVAVKEFFA SAEQKDIEKE 70 80 90 100 110 120 VKQLSRVKHP NIIALHGISS YQQATYLIME FAEGGSLHNF LHGKVKPAYS LAHAMSWARQ 130 140 150 160 170 180 CAEGLAYLHA MTPKPLIHRD VKPLNLLLTN KGRNLKICDF GTVADKSTMM TNNRGSAAWM 190 200 210 220 230 240 APEVFEGSKY TEKCDIFSWA IVLWEVLSRK QPFKGIDNAY TIQWKIYKGE RPPLLTTCPK 250 260 270 280 290 300 RIEDLMTACW KTVPEDRPSM QYIVGVMHEI VKDYTGADKA LEYTFVNQQI VTKESDGTVA 310 320 330 340 350 360 AQPDSLSSQE GELSPSSTQL TPTTAANANV NAIAISKTTT SSMTENTSST SSDITPTNSG 370 380 390 400 410 420 QLDNNPLFYM VTNRWDAIPE EESNESRNDS FNLTSSAEAT QRLETIRNGM ILMACKPMEQ 430 440 450 460 470 480 LTLDVEANGF DLSPSESSSS STNAKSDGRE RLTVTDTKPV MMTTDLSNNN GGIHAHSNGL 490 500 510 520 530 540 LSHANGWQAR DEELQEQEHE QEIVNSLDVD VDPDEDENDG TEQSLAEILD PELQPEPPIP 550 560 570 580 590 600 NDAESQLIYR DHRHMAKEYL SVDTNLYYAQ DFKDKLIVQM DRTEREQKQE LLRKMKDKEG 610 620 630 640 650 660 LQSLYNNLQQ QYASRQLAAG HHPQPHPHPH PNQLQHPHSH PPMHFLQDEG CGLLPGSVCG 670 GSESVEEGWV VIPPHHNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TAK1 participates in c-Jun N-terminal kinase signaling during Drosophila development." Takatsu Y., Nakamura M., Stapleton M., Danos M.C., Matsumoto K., O'Connor M.B., Shibuya H., Ueno N. Mol. Cell. Biol. 20:3015-3026(2000) [PubMed: 10757786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Ovary.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Immune activation of NF-kappaB and JNK requires Drosophila TAK1." Silverman N., Zhou R., Erlich R.L., Hunter M., Bernstein E., Schneider D., Maniatis T. J. Biol. Chem. 278:48928-48934(2003) [PubMed: 14519762] [Abstract] Cited for: FUNCTION.
[6]	"Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK-mediated immune response in Drosophila." Park J.M., Brady H., Ruocco M.G., Sun H., Williams D., Lee S.J., Kato T. Jr., Richards N., Chan K., Mercurio F., Karin M., Wasserman S.A. Genes Dev. 18:584-594(2004) [PubMed: 15037551] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF199466 mRNA. Translation: AAF06815.1. AE014298 Genomic DNA. Translation: AAF50895.1. AY051953 mRNA. Translation: AAK93377.1.
RefSeq	NP_524080.1.
UniGene	Dm.6425
3D structure databases
SMR	Q9V3Q6. Positions 13-277.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V3Q6. 1 interaction.
STRING	Q9V3Q6.
Proteomic databases
PRIDE	Q9V3Q6.
Genome annotation databases
Ensembl	FBtr0077319; FBpp0077011; FBgn0026323; Drosophila melanogaster. [Genome view]
GeneID	39659.
KEGG	dme:Dmel_CG18492.
NMPDR	fig|7227.3.peg.18803.
Organism-specific databases
CTD	39659.
FlyBase	FBgn0026323. Tak1.
Phylogenomic databases
eggNOG	inNOG05927.
InParanoid	Q9V3Q6.
OMA	DVEANGF.
OrthoDB	EOG92NJ5Z.
PhylomeDB	Q9V3Q6.
Enzyme and pathway databases
BRENDA	2.7.11.25. 48.
Gene expression databases
Bgee	Q9V3Q6.
GermOnline	CG18492. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR015786. MAPKKK-related. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_prot_kinase_AS. [Graphical view]
PANTHER	PTHR23257:SF92. MAPKKK-related. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	814736.

Entry information

Entry name

M3K7_DROME

Accession

Primary (citable) accession number: Q9V3Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project