O43318 (M3K7_HUMAN) 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):
Transforming growth factor-beta-activated kinase 1
Short name=TGF-beta-activated kinase 1

Gene names

Name:	MAP3K7
Synonyms:	TAK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	606 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity. Ref.8 Ref.10 Ref.11 Ref.15 Ref.19 Ref.23 Ref.24 Ref.41
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by proinflammatory cytokines and in response to physical and chemical stresses, including osmotic stress, oxidative stress, arsenic and ultraviolet light irradiation. Activated by 'Lys-63'-linked polyubiquitination and by autophosphorylation. Association with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 promotes activation through autophosphorylation, whereas PPM1B/PP2CB, PP2A and PPP6C dephosphorylation leads to inactivation. Ref.10 Ref.13 Ref.15 Ref.16 Ref.24
Subunit structure	Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3. Identified in the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2. Interacts with PPM1L and PPM1B/PP2CB. Interaction with PP2A and PPP6C leads to its repressed activity. Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B activation. Interacts with WDR34 (via WD domains). Interacts with CYLD and RBCK1. Interacts with TGFBR1; induces MAP3K7/TAK1 activation by TRAF6. Interacts with MAPK8IP1 and SMAD6 By similarity. Interacts with isoform 1 of VRK2. Interacts with DAB2; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation. Interacts with TRIM5. Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30 Ref.31 Ref.33 Ref.35 Ref.41
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. Ref.16
Tissue specificity	Isoform 1A is the most abundant in ovary, skeletal muscle, spleen and blood mononuclear cells. Isoform 1B is highly expressed in brain, kidney and small intestine. Isoform 1C is the major form in prostate. Isoform 1D is the less abundant form. Ref.2
Post-translational modification	Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation. Ubiquitinated, leading to proteasomal degradation By similarity. Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP. Ref.15 Ref.23 Ref.27
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	Apoptosis Stress response Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB phosphorylation Inferred from direct assay Ref.15. Source: UniProtKB JNK cascade Inferred from direct assay Ref.10. Source: UniProtKB MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome T cell receptor signaling pathway Non-traceable author statement PubMed 15125833. Source: UniProtKB TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Inferred from direct assay Ref.10. Source: UniProtKB activation of NF-kappaB-inducing kinase activity Inferred from mutant phenotype Ref.11PubMed 15125833. Source: UniProtKB angiogenesis Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW histone H3 acetylation Inferred from direct assay PubMed 18838386. Source: BHF-UCL innate immune response Traceable author statement. Source: Reactome negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara neural tube formation Inferred from electronic annotation. Source: Compara nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 14982987. Source: UniProtKB positive regulation of JNK cascade Inferred from electronic annotation. Source: Compara positive regulation of JUN kinase activity Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Traceable author statement. Source: Reactome positive regulation of T cell activation Inferred by curator PubMed 15125833. Source: UniProtKB positive regulation of T cell cytokine production Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB positive regulation of interleukin-2 production Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Traceable author statement PubMed 9466656. Source: ProtInc
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 18838386. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Inferred from electronic annotation. Source: Compara MAP kinase kinase kinase activity Inferred from direct assay Ref.15. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAPK8IP1	Q9UQF2	10	EBI-358684,EBI-78404
STAT3	P40763	4	EBI-358684,EBI-518675
TAB2	Q9NYJ8	2	EBI-358684,EBI-358708

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1B (identifier: O43318-1)

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 1A (identifier: O43318-2)

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.

Isoform 1C (identifier: O43318-3)

The sequence of this isoform differs from the canonical sequence as follows:
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Isoform 1D (identifier: O43318-4)

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 606

606

Mitogen-activated protein kinase kinase kinase 7

PRO_0000086252

Regions

Domain

36 – 291

256

Protein kinase

Nucleotide binding

42 – 50

9

ATP By similarity

Region

1 – 300

300

Interaction with MAPK8IP1 By similarity

Compositional bias

8 – 14

7

Poly-Ser

Sites

Active site

156

1

Proton acceptor By similarity

Binding site

63

1

ATP

Amino acid modifications

Modified residue

184

1

Phosphothreonine; by autocatalysis Probable

Modified residue

187

1

Phosphothreonine; by autocatalysis Ref.12 Ref.23 Ref.25 Ref.35 Ref.41

Modified residue

192

1

Phosphoserine; by autocatalysis Ref.12 Ref.13

Modified residue

389

1

Phosphoserine Ref.32 Ref.34 Ref.37 Ref.42

Modified residue

439

1

Phosphoserine Ref.22 Ref.28 Ref.29 Ref.32 Ref.34 Ref.37 Ref.39 Ref.42

Natural variations

Alternative sequence

404 – 430

27

Missing in isoform 1A and isoform 1D.

VSP_004886

Alternative sequence

509 – 518

10

PLAPCPNSKE → ARTSCRTGPG in isoform 1C and isoform 1D.

VSP_004887

Alternative sequence

519 – 606

88

Missing in isoform 1C and isoform 1D.

VSP_004888

Experimental info

Mutagenesis

63

1

K → W: Loss of kinase activity. Ref.19

Secondary structure

1

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606

Helix Strand Turn

Details...

Helix

33 – 35

3

Beta strand

36 – 43

8

Beta strand

46 – 55

10

Beta strand

58 – 64

7

Helix

70 – 83

14

Beta strand

92 – 95

4

Turn

97 – 100

4

Beta strand

101 – 105

5

Helix

112 – 117

6

Beta strand

119 – 123

5

Helix

127 – 145

19

Beta strand

148 – 150

3

Helix

159 – 161

3

Beta strand

162 – 165

4

Turn

166 – 169

4

Beta strand

170 – 173

4

Helix

193 – 195

3

Helix

198 – 201

4

Helix

209 – 224

16

Turn

228 – 232

5

Helix

236 – 244

9

Helix

257 – 266

10

Helix

271 – 273

3

Helix

277 – 287

11

Helix

288 – 290

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1B [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 3D8F8147CD174013	FASTA	606	67,196
	10 20 30 40 50 60 MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV 70 80 90 100 110 120 AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE 130 140 150 160 170 180 PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC 190 200 210 220 230 240 DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM 250 260 270 280 290 300 WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY 310 320 330 340 350 360 PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ 370 380 390 400 410 420 SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTAYSKPKR GHRKTASFGN 430 440 450 460 470 480 ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPTRSHP 490 500 510 520 530 540 WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI 550 560 570 580 590 600 ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ KRQGTS
	Isoform 1A [UniParc]. Checksum: 40EDE237BBB568EE	FASTA	579	64,230
	10 20 30 40 50 60 MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV 70 80 90 100 110 120 AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE 130 140 150 160 170 180 PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC 190 200 210 220 230 240 DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM 250 260 270 280 290 300 WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY 310 320 330 340 350 360 PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ 370 380 390 400 410 420 SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTGNGQPRR RSIQDLTVTG 430 440 450 460 470 480 TEPGQVSSRS SSPSVRMITT SGPTSEKPTR SHPWTPDDST DTNGSDNSIP MAYLTLDHQL 490 500 510 520 530 540 QPLAPCPNSK ESMAVFEQHC KMAQEYMKVQ TEIALLLQRK QELVAELDQD EKDQQNTSRL 550 560 570 VQEHKKLLDE NKSLSTYYQQ CKKQLEVIRS QQQKRQGTS
	Isoform 1C [UniParc]. Checksum: A92C927A8621AF90	FASTA	518	56,706
	10 20 30 40 50 60 MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV 70 80 90 100 110 120 AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE 130 140 150 160 170 180 PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC 190 200 210 220 230 240 DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM 250 260 270 280 290 300 WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY 310 320 330 340 350 360 PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ 370 380 390 400 410 420 SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTAYSKPKR GHRKTASFGN 430 440 450 460 470 480 ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPTRSHP 490 500 510 WTPDDSTDTN GSDNSIPMAY LTLDHQLQAR TSCRTGPG
	Isoform 1D [UniParc]. Checksum: B7D8832E286A99C5	FASTA	491	53,740
	10 20 30 40 50 60 MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV 70 80 90 100 110 120 AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE 130 140 150 160 170 180 PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC 190 200 210 220 230 240 DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM 250 260 270 280 290 300 WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY 310 320 330 340 350 360 PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ 370 380 390 400 410 420 SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTGNGQPRR RSIQDLTVTG 430 440 450 460 470 480 TEPGQVSSRS SSPSVRMITT SGPTSEKPTR SHPWTPDDST DTNGSDNSIP MAYLTLDHQL 490 QARTSCRTGP G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an NF-kappa B-inducing kinase-independent mechanism." Sakurai H., Shigemori N., Hasegawa K., Sugita T. Biochem. Biophys. Res. Commun. 243:545-549(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C). Tissue: Lung.
[2]	"Alternative splicing and gene structure of the transforming growth factor beta-activated kinase 1." Dempsey C.E., Sakurai H., Sugita T., Guesdon F. Biochim. Biophys. Acta 1517:46-52(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1D), TISSUE SPECIFICITY.
[3]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A). Tissue: Trachea.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 1A). Tissue: Uterus.
[8]	"A novel kinase cascade mediated by mitogen-activated protein kinase kinase 6 and MKK3." Moriguchi T., Kuroyanagi N., Yamaguchi K., Gotoh Y., Irie K., Kano T., Shirakabe K., Muro Y., Shibuya H., Matsumoto K., Nishida E., Hagiwara M. J. Biol. Chem. 271:13675-13679(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2K3/MKK3 AND MAP2K6/MKK6.
[9]	"TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction." Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N., Irie K., Nishida E., Matsumoto K. Science 272:1179-1182(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAB1/MAP3K7IP1.
[10]	"TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase." Shirakabe K., Yamaguchi K., Shibuya H., Irie K., Matsuda S., Moriguchi T., Gotoh Y., Matsumoto K., Nishida E. J. Biol. Chem. 272:8141-8144(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, FUNCTION.
[11]	"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway." Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K. Nature 398:252-256(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF6 AND TAB1/MAP3K7IP1, FUNCTION.
[12]	"Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1." Sakurai H., Miyoshi H., Mizukami J., Sugita T. FEBS Lett. 474:141-145(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAB1, PHOSPHORYLATION AT THR-184; THR-187 AND SER-192, ACTIVATION.
[13]	"TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop." Kishimoto K., Matsumoto K., Ninomiya-Tsuji J. J. Biol. Chem. 275:7359-7364(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-192, ENZYME REGULATION.
[14]	"Regulation of the TAK1 signaling pathway by protein phosphatase 2C." Hanada M., Ninomiya-Tsuji J., Komaki K., Ohnishi M., Katsura K., Kanamaru R., Matsumoto K., Tamura S. J. Biol. Chem. 276:5753-5759(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY PPM1B/PP2CB, INTERACTION WITH PPM1B/PP2CB.
[15]	"TAK1 is a ubiquitin-dependent kinase of MKK and IKK." Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J. Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, FUNCTION, ENZYME REGULATION, INTERACTION WITH TAB1/MAP3K7IP2 AND TAB2/MAP3K7IP2, IDENTIFICATION IN THE TRIKA2 COMPLEX.
[16]	"Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol." Jiang Z., Ninomiya-Tsuji J., Qian Y., Matsumoto K., Li X. Mol. Cell. Biol. 22:7158-7167(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IRAK; TAB1/MAP3K7IP1; TAB2/MAP3K7IP2 AND TRAF6, PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
[17]	"Pellino2 activates the mitogen activated protein kinase pathway." Jensen L.E., Whitehead A.S. FEBS Lett. 545:199-202(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PELI1 AND PELI2.
[18]	"Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein." Jensen L.E., Whitehead A.S. J. Immunol. 171:1500-1506(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PELI3.
[19]	"Transforming growth factor-beta1 (TGF-beta)-induced apoptosis of prostate cancer cells involves Smad7-dependent activation of p38 by TGF-beta-activated kinase 1 and mitogen-activated protein kinase kinase 3." Edlund S., Bu S., Schuster N., Aspenstroem P., Heuchel R., Heldin N.E., ten Dijke P., Heldin C.H., Landstrom M. Mol. Biol. Cell 14:529-544(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD7; MAP2K3 AND P38 KINASE, MUTAGENESIS OF LYS-63.
[20]	"TAB3, a new binding partner of the protein kinase TAK1." Cheung P.C., Nebreda A.R., Cohen P. Biochem. J. 378:27-34(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAB3/MAP3K7IP3.
[21]	"Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-stimulated fibronectin synthesis through TGFbeta-activated kinase 1 and activation of the JNK pathway." Hocevar B.A., Prunier C., Howe P.H. J. Biol. Chem. 280:25920-25927(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2.
[22]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway." Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M. EMBO Rep. 7:838-844(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, PHOSPHORYLATION AT THR-187 BY AUTOCATALYSIS, SUBUNIT, FUNCTION.
[24]	"Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-mediated NF-kappaB activation: TAO2 regulates TAK1 pathways." Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J. J. Biol. Chem. 281:28802-28810(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH TAOK1 AND TAOK2.
[25]	"Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway." Kajino T., Ren H., Iemura S., Natsume T., Stefansson B., Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J. J. Biol. Chem. 281:39891-39896(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PP2A AND PPP6C, DEPHOSPHORYLATION AT THR-187 BY PP2A AND PPP6C.
[26]	"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation." Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B. J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBCK1.
[27]	"Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses." Reiley W.W., Jin W., Lee A.J., Wright A., Wu X., Tewalt E.F., Leonard T.O., Norbury C.C., Fitzpatrick L., Zhang M., Sun S.C. J. Exp. Med. 204:1475-1485(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH CYLD, DEUBIQUITINATION BY CYLD.
[28]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY. Tissue: Platelet.
[29]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner." Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M. Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFBR1.
[31]	"Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein." Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A. PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VRK2.
[32]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway." Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y. Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WDR34.
[34]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, MASS SPECTROMETRY.
[35]	"Direct activation of protein kinases by unanchored polyubiquitin chains." Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J. Nature 461:114-119(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAB2, PHOSPHORYLATION AT THR-187.
[36]	"Ubiquitin-mediated activation of TAK1 and IKK." Adhikari A., Xu M., Chen Z.J. Oncogene 26:3214-3226(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ENZYME REGULATION.
[37]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[38]	"The TAK1-TRAF6 signalling pathway." Landstrom M. Int. J. Biochem. Cell Biol. 42:585-589(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
[39]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[40]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]	"TRIM5 is an innate immune sensor for the retrovirus capsid lattice." Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J., Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J. Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRIM5, AUTOPHOSPHORYLATION AT THR-187.
[42]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, MASS SPECTROMETRY.
[43]	"Structural basis for the interaction of TAK1 kinase with its activating protein TAB1." Brown K., Vial S.C., Dedi N., Long J.M., Dunster N.J., Cheetham G.M.T. J. Mol. Biol. 354:1013-1020(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-328 IN COMPLEX WITH TAB1 AND ADENOSINE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB009357 mRNA. Translation: BAA25026.1.
AB009356 mRNA. Translation: BAA25025.1.
AB009358 mRNA. Translation: BAA25027.2.
AF218074 mRNA. Translation: AAF27652.1.
DQ314875 Genomic DNA. Translation: ABC40734.1.
AK315774 mRNA. Translation: BAG38124.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19609.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19610.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19611.1.
AL121964, AL121837 Genomic DNA. Translation: CAI19612.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23530.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23531.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23532.1.
AL121837, AL121964 Genomic DNA. Translation: CAI23533.1.
CH471051 Genomic DNA. Translation: EAW48525.1.
CH471051 Genomic DNA. Translation: EAW48526.1.
CH471051 Genomic DNA. Translation: EAW48527.1.
CH471051 Genomic DNA. Translation: EAW48529.1.
BC017715 mRNA. Translation: AAH17715.1.

IPI

IPI00218566.
IPI00218567.
IPI00295738.

PIR

JC5955.
JC5956.

RefSeq

NP_003179.1. NM_003188.3.
NP_663304.1. NM_145331.2.
NP_663305.1. NM_145332.2.
NP_663306.1. NM_145333.2.

UniGene

Hs.594838.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EVA	X-ray	2.00	A	31-303	[»]
2YIY	X-ray	2.49	A	31-303	[»]
4GS6	X-ray	2.20	A	31-303	[»]

ProteinModelPortal

O43318.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27523N.

IntAct

O43318. 20 interactions.

MINT

MINT-88554.

STRING

9606.ENSP00000358335.

PTM databases

PhosphoSite

O43318.

Proteomic databases

PaxDb

O43318.

PRIDE

O43318.

Protocols and materials databases

DNASU

6885.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369325; ENSP00000358331; ENSG00000135341.
ENST00000369327; ENSP00000358333; ENSG00000135341.
ENST00000369329; ENSP00000358335; ENSG00000135341.
ENST00000369332; ENSP00000358338; ENSG00000135341.

GeneID

6885.

KEGG

hsa:6885.

UCSC

uc003pnz.1. human.
uc003poa.1. human.
uc003pob.1. human.

Organism-specific databases

CTD

6885.

GeneCards

GC06M091282.

HGNC

HGNC:6859. MAP3K7.

HPA

HPA007633.

MIM

602614. gene.

neXtProt

NX_O43318.

PharmGKB

PA30603.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000231735.

HOVERGEN

HBG003485.

InParanoid

O43318.

KO

K04427.

OMA

GSFMDIT.

OrthoDB

EOG4BRWKD.

PhylomeDB

O43318.

Enzyme and pathway databases

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
bmppathway. BMP receptor signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
faspathway. FAS signaling pathway (CD95).
il1pathway. IL1-mediated signaling events.
tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.
tgfbrpathway. TGF-beta receptor signaling.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O43318.

Bgee

O43318.

CleanEx

HS_MAP3K7.

Genevestigator

O43318.

GermOnline

ENSG00000135341. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR017421. MAPKKK7.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF038168. MAPKKK7. 1 hit.

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

BindingDB

O43318.

ChEMBL

CHEMBL5776.

EvolutionaryTrace

O43318.

GenomeRNAi

6885.

NextBio

26899.

SOURCE

Search...

Entry information

Entry name

M3K7_HUMAN

Accession

Primary (citable) accession number: O43318
Secondary accession number(s): B2RE27 , E1P523, O43317, O43319, Q5TDN2, Q5TDN3, Q5TDT7, Q9NTR3, Q9NZ70

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.