Q9V3Q6 (M3K7_DROME) Reviewed, UniProtKB/Swiss-Prot

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)

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	Immunity Innate immunity
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.5. Source: UniProtKB activation of JNKK activity Inferred from mutant phenotype Ref.5. Source: UniProtKB apoptotic process Inferred from genetic interaction Ref.1. Source: FlyBase cellular response to lipopolysaccharide Inferred from mutant phenotype. Source: FlyBase defense response to Gram-negative bacterium Inferred from mutant phenotype. Source: FlyBase defense response to virus Inferred from mutant phenotype. Source: FlyBase dorsal closure Inferred from mutant phenotype Ref.1. 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 JNK cascade 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 Inferred from mutant phenotype Ref.5. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 [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. Strain: Berkeley.
[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. NM_079356.2.
UniGene	Dm.6425.
3D structure databases
ProteinModelPortal	Q9V3Q6.
SMR	Q9V3Q6. Positions 13-280.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1613430.
STRING	Q9V3Q6.
Proteomic databases
PRIDE	Q9V3Q6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077319; FBpp0077011; FBgn0026323.
GeneID	39659.
KEGG	dme:Dmel_CG18492.
NMPDR	fig|7227.3.peg.18803.
Organism-specific databases
CTD	39659.
FlyBase	FBgn0026323. Tak1.
Phylogenomic databases
eggNOG	inNOG05927.
GeneTree	EMGT00050000001111.
InParanoid	Q9V3Q6.
OMA	HMAKEYL.
OrthoDB	EOG4V41PX.
PhylomeDB	Q9V3Q6.
Gene expression databases
Bgee	Q9V3Q6.
GermOnline	CG18492. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
KO	K04427.
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SUPFAM	SSF56112. Kinase_like. 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
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:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project