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Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)

 M3K7_HUMAN              Reviewed;         606 AA.
O43318; B2RE27; E1P523; O43317; O43319; Q5TDN2; Q5TDN3; Q5TDT7;
Q9NTR3; Q9NZ70;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 196.
RecName: Full=Mitogen-activated protein kinase kinase kinase 7;
EC=2.7.11.25 {ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:12589052};
AltName: Full=Transforming growth factor-beta-activated kinase 1;
Short=TGF-beta-activated kinase 1;
Name=MAP3K7; Synonyms=TAK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C).
TISSUE=Lung;
PubMed=9480845; DOI=10.1006/bbrc.1998.8124;
Sakurai H., Shigemori N., Hasegawa K., Sugita T.;
"TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an
NF-kappa B-inducing kinase-independent mechanism.";
Biochem. Biophys. Res. Commun. 243:545-549(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1D), AND TISSUE SPECIFICITY.
PubMed=11118615; DOI=10.1016/S0167-4781(00)00258-X;
Dempsey C.E., Sakurai H., Sugita T., Guesdon F.;
"Alternative splicing and gene structure of the transforming growth
factor beta-activated kinase 1.";
Biochim. Biophys. Acta 1517:46-52(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
FUNCTION IN PHOSPHORYLATION OF MAP2K3/MKK3 AND MAP2K6/MKK6.
PubMed=8663074; DOI=10.1074/jbc.271.23.13675;
Moriguchi T., Kuroyanagi N., Yamaguchi K., Gotoh Y., Irie K., Kano T.,
Shirakabe K., Muro Y., Shibuya H., Matsumoto K., Nishida E.,
Hagiwara M.;
"A novel kinase cascade mediated by mitogen-activated protein kinase
kinase 6 and MKK3.";
J. Biol. Chem. 271:13675-13679(1996).
[9]
INTERACTION WITH TAB1/MAP3K7IP1.
PubMed=8638164; DOI=10.1126/science.272.5265.1179;
Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y.,
Ueno N., Irie K., Nishida E., Matsumoto K.;
"TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
transduction.";
Science 272:1179-1182(1996).
[10]
ENZYME REGULATION, AND FUNCTION.
PubMed=9079627; DOI=10.1074/jbc.272.13.8141;
Shirakabe K., Yamaguchi K., Shibuya H., Irie K., Matsuda S.,
Moriguchi T., Gotoh Y., Matsumoto K., Nishida E.;
"TAK1 mediates the ceramide signaling to stress-activated protein
kinase/c-Jun N-terminal kinase.";
J. Biol. Chem. 272:8141-8144(1997).
[11]
INTERACTION WITH TRAF6 AND TAB1/MAP3K7IP1, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=10094049; DOI=10.1038/18465;
Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z.,
Matsumoto K.;
"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP
kinase cascade in the IL-1 signalling pathway.";
Nature 398:252-256(1999).
[12]
INTERACTION WITH TAB1, PHOSPHORYLATION AT THR-184; THR-187 AND
SER-192, ACTIVATION, AND CATALYTIC ACTIVITY.
PubMed=10838074; DOI=10.1016/S0014-5793(00)01588-X;
Sakurai H., Miyoshi H., Mizukami J., Sugita T.;
"Phosphorylation-dependent activation of TAK1 mitogen-activated
protein kinase kinase kinase by TAB1.";
FEBS Lett. 474:141-145(2000).
[13]
PHOSPHORYLATION AT SER-192, AND ENZYME REGULATION.
PubMed=10702308; DOI=10.1074/jbc.275.10.7359;
Kishimoto K., Matsumoto K., Ninomiya-Tsuji J.;
"TAK1 mitogen-activated protein kinase kinase kinase is activated by
autophosphorylation within its activation loop.";
J. Biol. Chem. 275:7359-7364(2000).
[14]
DEPHOSPHORYLATION BY PPM1B/PP2CB, AND INTERACTION WITH PPM1B/PP2CB.
PubMed=11104763; DOI=10.1074/jbc.M007773200;
Hanada M., Ninomiya-Tsuji J., Komaki K., Ohnishi M., Katsura K.,
Kanamaru R., Matsumoto K., Tamura S.;
"Regulation of the TAK1 signaling pathway by protein phosphatase 2C.";
J. Biol. Chem. 276:5753-5759(2001).
[15]
UBIQUITINATION, FUNCTION, ENZYME REGULATION, INTERACTION WITH
TAB1/MAP3K7IP2 AND TAB2/MAP3K7IP2, AND IDENTIFICATION IN THE TRIKA2
COMPLEX.
PubMed=11460167; DOI=10.1038/35085597;
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
"TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
Nature 412:346-351(2001).
[16]
INTERACTION WITH IRAK; TAB1/MAP3K7IP1; TAB2/MAP3K7IP2 AND TRAF6,
PHOSPHORYLATION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=12242293; DOI=10.1128/MCB.22.20.7158-7167.2002;
Jiang Z., Ninomiya-Tsuji J., Qian Y., Matsumoto K., Li X.;
"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.";
Mol. Cell. Biol. 22:7158-7167(2002).
[17]
INTERACTION WITH PELI1 AND PELI2.
PubMed=12804775; DOI=10.1016/S0014-5793(03)00533-7;
Jensen L.E., Whitehead A.S.;
"Pellino2 activates the mitogen activated protein kinase pathway.";
FEBS Lett. 545:199-202(2003).
[18]
INTERACTION WITH PELI3.
PubMed=12874243; DOI=10.4049/jimmunol.171.3.1500;
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).
[19]
FUNCTION, INTERACTION WITH SMAD7; MAP2K3 AND P38 KINASE, MUTAGENESIS
OF LYS-63, AND CATALYTIC ACTIVITY.
PubMed=12589052; DOI=10.1091/mbc.02-03-0037;
Edlund S., Bu S., Schuster N., Aspenstroem P., Heuchel R.,
Heldin N.E., ten Dijke P., Heldin C.H., Landstrom M.;
"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.";
Mol. Biol. Cell 14:529-544(2003).
[20]
INTERACTION WITH TAB3/MAP3K7IP3.
PubMed=14670075; DOI=10.1042/BJ20031794;
Cheung P.C., Nebreda A.R., Cohen P.;
"TAB3, a new binding partner of the protein kinase TAK1.";
Biochem. J. 378:27-34(2004).
[21]
INTERACTION WITH DAB2.
PubMed=15894542; DOI=10.1074/jbc.M501150200;
Hocevar B.A., Prunier C., Howe P.H.;
"Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-
stimulated fibronectin synthesis through TGFbeta-activated kinase 1
and activation of the JNK pathway.";
J. Biol. Chem. 280:25920-25927(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
UBIQUITINATION, PHOSPHORYLATION AT THR-187 BY AUTOCATALYSIS, SUBUNIT,
AND FUNCTION.
PubMed=16845370; DOI=10.1038/sj.embor.7400754;
Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K.,
Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K.,
Kracht M.;
"The Yersinia enterocolitica effector YopP inhibits host cell
signalling by inactivating the protein kinase TAK1 in the IL-1
signalling pathway.";
EMBO Rep. 7:838-844(2006).
[24]
FUNCTION, ENZYME REGULATION, AND INTERACTION WITH TAOK1 AND TAOK2.
PubMed=16893890; DOI=10.1074/jbc.M603627200;
Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J.;
"Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-
mediated NF-kappaB activation: TAO2 regulates TAK1 pathways.";
J. Biol. Chem. 281:28802-28810(2006).
[25]
INTERACTION WITH PP2A AND PPP6C, AND DEPHOSPHORYLATION AT THR-187 BY
PP2A AND PPP6C.
PubMed=17079228; DOI=10.1074/jbc.M608155200;
Kajino T., Ren H., Iemura S., Natsume T., Stefansson B.,
Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J.;
"Protein phosphatase 6 down-regulates TAK1 kinase activation in the
IL-1 signaling pathway.";
J. Biol. Chem. 281:39891-39896(2006).
[26]
INTERACTION WITH RBCK1.
PubMed=17449468; DOI=10.1074/jbc.M701913200;
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.;
"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
J. Biol. Chem. 282:16776-16782(2007).
[27]
UBIQUITINATION, INTERACTION WITH CYLD, AND DEUBIQUITINATION BY CYLD.
PubMed=17548520; DOI=10.1084/jem.20062694;
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.;
"Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-
dependent kinase Tak1 and prevents abnormal T cell responses.";
J. Exp. Med. 204:1475-1485(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[30]
INTERACTION WITH TGFBR1.
PubMed=18758450; DOI=10.1038/ncb1780;
Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V.,
Schuster N., Zhang S., Heldin C.H., Landstrom M.;
"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a
receptor kinase-independent manner.";
Nat. Cell Biol. 10:1199-1207(2008).
[31]
INTERACTION WITH VRK2.
PubMed=18286207; DOI=10.1371/journal.pone.0001660;
Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.;
"Modulation of interleukin-1 transcriptional response by the
interaction between VRK2 and the JIP1 scaffold protein.";
PLoS ONE 3:E1660-E1660(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[34]
INTERACTION WITH WDR34.
PubMed=19521662; DOI=10.1007/s00018-009-0059-6;
Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.;
"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-
induced NF-kappaB activation pathway.";
Cell. Mol. Life Sci. 66:2573-2584(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[36]
INTERACTION WITH TAB2, AND PHOSPHORYLATION AT THR-187.
PubMed=19675569; DOI=10.1038/nature08247;
Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W.,
Chen Z.J.;
"Direct activation of protein kinases by unanchored polyubiquitin
chains.";
Nature 461:114-119(2009).
[37]
REVIEW ON ENZYME REGULATION.
PubMed=17496917; DOI=10.1038/sj.onc.1210413;
Adhikari A., Xu M., Chen Z.J.;
"Ubiquitin-mediated activation of TAK1 and IKK.";
Oncogene 26:3214-3226(2007).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[39]
REVIEW ON ENZYME REGULATION, AND REVIEW ON FUNCTION.
PubMed=20060931; DOI=10.1016/j.biocel.2009.12.023;
Landstrom M.;
"The TAK1-TRAF6 signalling pathway.";
Int. J. Biochem. Cell Biol. 42:585-589(2010).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[42]
FUNCTION, INTERACTION WITH TRIM5, AND PHOSPHORYLATION AT THR-187.
PubMed=21512573; DOI=10.1038/nature09976;
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.;
"TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
Nature 472:361-365(2011).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[44]
UBIQUITINATION AT LYS-72.
PubMed=22406003; DOI=10.1016/j.cellsig.2012.02.017;
Fan Y., Shi Y., Liu S., Mao R., An L., Zhao Y., Zhang H., Zhang F.,
Xu G., Qin J., Yang J.;
"Lys48-linked TAK1 polyubiquitination at lysine-72 downregulates
TNFalpha-induced NF-kappaB activation via mediating TAK1
degradation.";
Cell. Signal. 24:1381-1389(2012).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-389; SER-439
AND SER-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[47]
INTERACTION WITH IFIT5.
PubMed=26334375; DOI=10.1016/j.cellsig.2015.08.018;
Zheng C., Zheng Z., Zhang Z., Meng J., Liu Y., Ke X., Hu Q., Wang H.;
"IFIT5 positively regulates NF-kappaB signaling through synergizing
the recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1
(TAK1).";
Cell. Signal. 27:2343-2354(2015).
[48]
INVOLVEMENT IN FMD2, VARIANTS FMD2 GLN-70; GLU-100; ARG-168 AND
LEU-512, CHARACTERIZATION OF VARIANTS FMD2 LEU-512 AND ARG-168,
SUBUNIT, AND MUTAGENESIS OF PRO-512.
PubMed=27426733; DOI=10.1016/j.ajhg.2016.05.024;
Wade E.M., Daniel P.B., Jenkins Z.A., McInerney-Leo A., Leo P.,
Morgan T., Addor M.C., Ades L.C., Bertola D., Bohring A., Carter E.,
Cho T.J., Duba H.C., Fletcher E., Kim C.A., Krakow D., Morava E.,
Neuhann T., Superti-Furga A., Veenstra-Knol I., Wieczorek D.,
Wilson L.C., Hennekam R.C., Sutherland-Smith A.J., Strom T.M.,
Wilkie A.O., Brown M.A., Duncan E.L., Markie D.M., Robertson S.P.;
"Mutations in MAP3K7 that alter the activity of the TAK1 signaling
complex cause frontometaphyseal dysplasia.";
Am. J. Hum. Genet. 99:392-406(2016).
[49]
INVOLVEMENT IN CSCF, AND VARIANTS CSCF VAL-50 DEL; CYS-110 AND
ARG-241.
PubMed=27426734; DOI=10.1016/j.ajhg.2016.06.005;
Le Goff C., Rogers C., Le Goff W., Pinto G., Bonnet D., Chrabieh M.,
Alibeu O., Nistchke P., Munnich A., Picard C., Cormier-Daire V.;
"Heterozygous mutations in MAP3K7, encoding TGF-beta-activated kinase
1, cause cardiospondylocarpofacial syndrome.";
Am. J. Hum. Genet. 99:407-413(2016).
[50]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-328 IN COMPLEX WITH TAB1
AND ADENOSINE.
PubMed=16289117; DOI=10.1016/j.jmb.2005.09.098;
Brown K., Vial S.C., Dedi N., Long J.M., Dunster N.J.,
Cheetham G.M.T.;
"Structural basis for the interaction of TAK1 kinase with its
activating protein TAB1.";
J. Mol. Biol. 354:1013-1020(2005).
-!- 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.
{ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:11460167,
ECO:0000269|PubMed:12589052, ECO:0000269|PubMed:16845370,
ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:21512573,
ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9079627}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:10838074,
ECO:0000269|PubMed:12589052}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- 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. {ECO:0000269|PubMed:10702308,
ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:12242293,
ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:9079627}.
-!- SUBUNIT: Can form homodimer (PubMed:27426733). Binds both upstream
activators and downstream substrates in multimolecular complexes.
Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3
(PubMed:10838074, PubMed:11460167, PubMed:12242293,
PubMed:14670075, PubMed:16289117, PubMed:19675569,
PubMed:8638164). Identified in the TRIKA2 complex composed of
MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 (PubMed:11460167).
Interacts with PPM1L and PPM1B/PP2CB (PubMed:11104763).
Interaction with PP2A and PPP6C leads to its repressed activity
(PubMed:17079228). Interacts with TRAF6 and TAB1/MAP3K7IP1; during
IL-1 signaling (PubMed:10094049, PubMed:12242293). Interacts with
TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7
interaction with IKKA, thus preventing NF-kappa-B activation
(PubMed:16893890). Interacts with WDR34 (via WD domains)
(PubMed:19521662). Interacts with CYLD and RBCK1 (PubMed:17449468,
PubMed:17548520). Interacts with TGFBR1; induces MAP3K7/TAK1
activation by TRAF6 (PubMed:18758450). Interacts with MAPK8IP1 and
SMAD6 (By similarity). Interacts with isoform 1 of VRK2
(PubMed:18286207). Interacts with DAB2; the interaction is induced
by TGF-beta stimulation and may mediate TGF-beta stimulated JNK
activation (PubMed:15894542). Interacts with TRIM5
(PubMed:21512573). Part of a complex containing ITCH, NDFIP1 and
MAP3K7 (By similarity). Interacts with IFIT5; the interaction
synergizes the recruitment of IKK to MAP3K7 and enhances IKK
phosphorylation (PubMed:26334375). Interacts with PLEKHM1 (via
N- and C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q62073,
ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:10838074,
ECO:0000269|PubMed:11104763, ECO:0000269|PubMed:11460167,
ECO:0000269|PubMed:12242293, ECO:0000269|PubMed:12589052,
ECO:0000269|PubMed:12804775, ECO:0000269|PubMed:12874243,
ECO:0000269|PubMed:14670075, ECO:0000269|PubMed:15894542,
ECO:0000269|PubMed:16289117, ECO:0000269|PubMed:16845370,
ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:17079228,
ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:17548520,
ECO:0000269|PubMed:18286207, ECO:0000269|PubMed:18758450,
ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:19675569,
ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:26334375,
ECO:0000269|PubMed:27426733, ECO:0000269|PubMed:8638164}.
-!- INTERACTION:
B5Z6S0:cagA (xeno); NbExp=4; IntAct=EBI-358684, EBI-7287204;
Q16543:CDC37; NbExp=5; IntAct=EBI-358700, EBI-295634;
P07900:HSP90AA1; NbExp=5; IntAct=EBI-358700, EBI-296047;
O14733:MAP2K7; NbExp=3; IntAct=EBI-358684, EBI-492605;
Q9UQF2:MAPK8IP1; NbExp=11; IntAct=EBI-358684, EBI-78404;
Q9UBE8:NLK; NbExp=3; IntAct=EBI-358684, EBI-366978;
O00743:PPP6C; NbExp=4; IntAct=EBI-358684, EBI-359751;
P40763:STAT3; NbExp=4; IntAct=EBI-358684, EBI-518675;
Q15750:TAB1; NbExp=4; IntAct=EBI-358684, EBI-358643;
Q9NYJ8:TAB2; NbExp=6; IntAct=EBI-358684, EBI-358708;
Q8N5C8:TAB3; NbExp=3; IntAct=EBI-358684, EBI-359964;
Q9UKE5:TNIK; NbExp=3; IntAct=EBI-358684, EBI-1051794;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-358684, EBI-359276;
P0CG48:UBC; NbExp=4; IntAct=EBI-358684, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242293}.
Cell membrane {ECO:0000269|PubMed:12242293}; Peripheral membrane
protein {ECO:0000269|PubMed:12242293}; Cytoplasmic side
{ECO:0000269|PubMed:12242293}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1B;
IsoId=O43318-1; Sequence=Displayed;
Name=1A;
IsoId=O43318-2; Sequence=VSP_004886;
Name=1C;
IsoId=O43318-3; Sequence=VSP_004887, VSP_004888;
Name=1D;
IsoId=O43318-4; Sequence=VSP_004886, VSP_004887, VSP_004888;
-!- 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. {ECO:0000269|PubMed:11118615}.
-!- PTM: 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.
{ECO:0000269|PubMed:10702308, ECO:0000269|PubMed:10838074,
ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:17548520,
ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:21512573}.
-!- PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by
TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-
48'-linked polyubiquitination catalyzed by ITCH (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. {ECO:0000250|UniProtKB:Q62073, ECO:0000269|PubMed:17548520,
ECO:0000269|PubMed:22406003}.
-!- DISEASE: Frontometaphyseal dysplasia 2 (FMD2) [MIM:617137]: A form
of frontometaphyseal dysplasia, a progressive sclerosing skeletal
dysplasia affecting the long bones and skull. Characteristic
features include supraorbital hyperostosis, cranial hyperostosis,
undermodeling of the small bones, flared metaphyses, and digital
anomalies. Extra-skeletal manifestations include hearing loss,
cardiac malformations, and stenosis, particularly of the upper
airway and urinary tract. FMD2 inheritance is autosomal dominant.
{ECO:0000269|PubMed:27426733}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiospondylocarpofacial syndrome (CSCF) [MIM:157800]: A
syndrome characterized by growth retardation, dysmorphic facial
features, brachydactyly with carpal-tarsal fusion and extensive
posterior cervical vertebral synostosis, cardiac septal defects
with valve dysplasia, and deafness with inner ear malformations.
CSCF transmission pattern is consistent with autosomal dominant
inheritance. {ECO:0000269|PubMed:27426734}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAP3K7ID454ch6q15.html";
-----------------------------------------------------------------------
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EMBL; AB009357; BAA25026.1; -; mRNA.
EMBL; AB009356; BAA25025.1; -; mRNA.
EMBL; AB009358; BAA25027.2; -; mRNA.
EMBL; AF218074; AAF27652.1; -; mRNA.
EMBL; DQ314875; ABC40734.1; -; Genomic_DNA.
EMBL; AK315774; BAG38124.1; -; mRNA.
EMBL; AL121964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL121837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48525.1; -; Genomic_DNA.
EMBL; CH471051; EAW48526.1; -; Genomic_DNA.
EMBL; CH471051; EAW48527.1; -; Genomic_DNA.
EMBL; CH471051; EAW48529.1; -; Genomic_DNA.
EMBL; BC017715; AAH17715.1; -; mRNA.
CCDS; CCDS5027.1; -. [O43318-2]
CCDS; CCDS5028.1; -. [O43318-1]
CCDS; CCDS5029.1; -. [O43318-3]
CCDS; CCDS5030.1; -. [O43318-4]
PIR; JC5955; JC5955.
PIR; JC5956; JC5956.
RefSeq; NP_003179.1; NM_003188.3. [O43318-2]
RefSeq; NP_663304.1; NM_145331.2. [O43318-1]
RefSeq; NP_663305.1; NM_145332.2. [O43318-3]
RefSeq; NP_663306.1; NM_145333.2. [O43318-4]
UniGene; Hs.594838; -.
PDB; 2EVA; X-ray; 2.00 A; A=31-412.
PDB; 2YIY; X-ray; 2.49 A; A=31-303.
PDB; 4GS6; X-ray; 2.20 A; A=31-303.
PDB; 4L3P; X-ray; 2.68 A; A=31-303.
PDB; 4L52; X-ray; 2.54 A; A=31-303.
PDB; 4L53; X-ray; 2.55 A; A=31-303.
PDB; 4O91; X-ray; 2.39 A; A=31-303.
PDB; 5E7R; X-ray; 2.11 A; A=31-303.
PDB; 5GJD; X-ray; 2.79 A; A=31-303.
PDB; 5GJF; X-ray; 2.89 A; A=31-303.
PDB; 5GJG; X-ray; 2.61 A; A=31-303.
PDB; 5J7S; X-ray; 2.37 A; A=31-303.
PDB; 5J8I; X-ray; 2.40 A; A=31-303.
PDB; 5J9L; X-ray; 2.75 A; A=31-303.
PDB; 5JGA; X-ray; 2.00 A; A=31-303.
PDB; 5JGB; X-ray; 2.80 A; A=31-303.
PDB; 5JGD; X-ray; 3.10 A; A=31-303.
PDB; 5JH6; X-ray; 2.37 A; A=31-303.
PDB; 5JK3; X-ray; 2.37 A; A=31-303.
PDB; 5V5N; X-ray; 2.01 A; A=31-303.
PDBsum; 2EVA; -.
PDBsum; 2YIY; -.
PDBsum; 4GS6; -.
PDBsum; 4L3P; -.
PDBsum; 4L52; -.
PDBsum; 4L53; -.
PDBsum; 4O91; -.
PDBsum; 5E7R; -.
PDBsum; 5GJD; -.
PDBsum; 5GJF; -.
PDBsum; 5GJG; -.
PDBsum; 5J7S; -.
PDBsum; 5J8I; -.
PDBsum; 5J9L; -.
PDBsum; 5JGA; -.
PDBsum; 5JGB; -.
PDBsum; 5JGD; -.
PDBsum; 5JH6; -.
PDBsum; 5JK3; -.
PDBsum; 5V5N; -.
ProteinModelPortal; O43318; -.
SMR; O43318; -.
BioGrid; 112748; 160.
CORUM; O43318; -.
DIP; DIP-27523N; -.
IntAct; O43318; 53.
MINT; MINT-88554; -.
STRING; 9606.ENSP00000358335; -.
BindingDB; O43318; -.
ChEMBL; CHEMBL5776; -.
GuidetoPHARMACOLOGY; 2082; -.
iPTMnet; O43318; -.
PhosphoSitePlus; O43318; -.
BioMuta; MAP3K7; -.
EPD; O43318; -.
MaxQB; O43318; -.
PaxDb; O43318; -.
PeptideAtlas; O43318; -.
PRIDE; O43318; -.
DNASU; 6885; -.
Ensembl; ENST00000369325; ENSP00000358331; ENSG00000135341. [O43318-3]
Ensembl; ENST00000369327; ENSP00000358333; ENSG00000135341. [O43318-4]
Ensembl; ENST00000369329; ENSP00000358335; ENSG00000135341. [O43318-1]
Ensembl; ENST00000369332; ENSP00000358338; ENSG00000135341. [O43318-2]
GeneID; 6885; -.
KEGG; hsa:6885; -.
UCSC; uc003pnz.3; human. [O43318-1]
CTD; 6885; -.
DisGeNET; 6885; -.
EuPathDB; HostDB:ENSG00000135341.17; -.
GeneCards; MAP3K7; -.
HGNC; HGNC:6859; MAP3K7.
HPA; HPA007633; -.
MalaCards; MAP3K7; -.
MIM; 157800; phenotype.
MIM; 602614; gene.
MIM; 617137; phenotype.
neXtProt; NX_O43318; -.
OpenTargets; ENSG00000135341; -.
PharmGKB; PA30603; -.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140790; -.
HOGENOM; HOG000231735; -.
HOVERGEN; HBG003485; -.
InParanoid; O43318; -.
KO; K04427; -.
OMA; PARSHPW; -.
OrthoDB; EOG091G03QO; -.
PhylomeDB; O43318; -.
TreeFam; TF105116; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-168180; TRAF6 Mediated Induction of proinflammatory cytokines.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SignaLink; O43318; -.
SIGNOR; O43318; -.
ChiTaRS; MAP3K7; human.
EvolutionaryTrace; O43318; -.
GeneWiki; MAP3K7; -.
GenomeRNAi; 6885; -.
PRO; PR:O43318; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000135341; -.
CleanEx; HS_MAP3K7; -.
ExpressionAtlas; O43318; baseline and differential.
Genevisible; O43318; HS.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:Reactome.
GO; GO:0097110; F:scaffold protein binding; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; IDA:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB.
GO; GO:0043276; P:anoikis; ISS:BHF-UCL.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0007252; P:I-kappaB phosphorylation; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:0050870; P:positive regulation of T cell activation; IC:UniProtKB.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017421; MAPKKK7.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR26392:SF74; PTHR26392:SF74; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF038168; MAPKKK7; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Disease mutation;
Isopeptide bond; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 606 Mitogen-activated protein kinase kinase
kinase 7.
/FTId=PRO_0000086252.
DOMAIN 36 291 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 42 50 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 300 Interaction with MAPK8IP1. {ECO:0000250}.
COMPBIAS 8 14 Poly-Ser.
ACT_SITE 156 156 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 63 63 ATP.
MOD_RES 184 184 Phosphothreonine; by autocatalysis.
{ECO:0000305|PubMed:10838074}.
MOD_RES 187 187 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:10838074,
ECO:0000269|PubMed:16845370,
ECO:0000269|PubMed:19675569,
ECO:0000269|PubMed:21512573}.
MOD_RES 192 192 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:10702308,
ECO:0000269|PubMed:10838074}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22406003}.
VAR_SEQ 404 430 Missing (in isoform 1A and isoform 1D).
{ECO:0000303|PubMed:11118615,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9480845}.
/FTId=VSP_004886.
VAR_SEQ 509 518 PLAPCPNSKE -> ARTSCRTGPG (in isoform 1C
and isoform 1D).
{ECO:0000303|PubMed:11118615,
ECO:0000303|PubMed:9480845}.
/FTId=VSP_004887.
VAR_SEQ 519 606 Missing (in isoform 1C and isoform 1D).
{ECO:0000303|PubMed:11118615,
ECO:0000303|PubMed:9480845}.
/FTId=VSP_004888.
VARIANT 50 50 Missing (in CSCF).
{ECO:0000269|PubMed:27426734}.
/FTId=VAR_077341.
VARIANT 70 70 E -> Q (in FMD2).
{ECO:0000269|PubMed:27426733}.
/FTId=VAR_077342.
VARIANT 100 100 V -> E (in FMD2).
{ECO:0000269|PubMed:27426733}.
/FTId=VAR_077343.
VARIANT 110 110 G -> C (in CSCF).
{ECO:0000269|PubMed:27426734}.
/FTId=VAR_077344.
VARIANT 168 168 G -> R (in FMD2; increases
autophosphorylation; no effect on MAPK
signaling; no effect on NF-kappa-B
signaling).
{ECO:0000269|PubMed:27426733}.
/FTId=VAR_077345.
VARIANT 241 241 W -> R (in CSCF).
{ECO:0000269|PubMed:27426734}.
/FTId=VAR_077346.
VARIANT 512 512 P -> L (in FMD2; does not affect
interaction with TAB2; does not affect
homodimerization; increases
autophosphorylation; increases MAPK
signaling; increases NF-kappa-B
signaling).
{ECO:0000269|PubMed:27426733}.
/FTId=VAR_077347.
MUTAGEN 63 63 K->W: Loss of kinase activity.
{ECO:0000269|PubMed:12589052}.
MUTAGEN 512 512 P->R,A: Enhances autophosphorylation;
Alters MAPK signaling.
{ECO:0000269|PubMed:27426733}.
HELIX 33 35 {ECO:0000244|PDB:5JGA}.
STRAND 37 44 {ECO:0000244|PDB:5JGA}.
STRAND 46 55 {ECO:0000244|PDB:5JGA}.
STRAND 58 64 {ECO:0000244|PDB:5JGA}.
HELIX 68 70 {ECO:0000244|PDB:5V5N}.
HELIX 71 83 {ECO:0000244|PDB:5JGA}.
STRAND 92 96 {ECO:0000244|PDB:5JGA}.
TURN 97 100 {ECO:0000244|PDB:5JGA}.
STRAND 101 105 {ECO:0000244|PDB:5JGA}.
HELIX 112 117 {ECO:0000244|PDB:5JGA}.
STRAND 118 123 {ECO:0000244|PDB:5JGA}.
HELIX 127 145 {ECO:0000244|PDB:5JGA}.
STRAND 148 150 {ECO:0000244|PDB:5JGA}.
HELIX 159 161 {ECO:0000244|PDB:5JGA}.
STRAND 162 165 {ECO:0000244|PDB:5JGA}.
TURN 166 169 {ECO:0000244|PDB:5JGA}.
STRAND 170 173 {ECO:0000244|PDB:5JGA}.
HELIX 182 186 {ECO:0000244|PDB:5GJF}.
HELIX 193 195 {ECO:0000244|PDB:5JGA}.
HELIX 198 201 {ECO:0000244|PDB:5JGA}.
HELIX 209 224 {ECO:0000244|PDB:5JGA}.
TURN 228 232 {ECO:0000244|PDB:5JGA}.
HELIX 236 244 {ECO:0000244|PDB:5JGA}.
HELIX 257 266 {ECO:0000244|PDB:5JGA}.
HELIX 271 273 {ECO:0000244|PDB:5JGA}.
HELIX 277 287 {ECO:0000244|PDB:5JGA}.
HELIX 288 290 {ECO:0000244|PDB:5JGA}.
TURN 292 295 {ECO:0000244|PDB:5JGA}.
STRAND 300 302 {ECO:0000244|PDB:5JGA}.
SEQUENCE 606 AA; 67196 MW; 3D8F8147CD174013 CRC64;
MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV
AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE
PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC
DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM
WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ
SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTAYSKPKR GHRKTASFGN
ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPTRSHP
WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI
ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ
KRQGTS


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