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Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)

 M3K20_HUMAN             Reviewed;         800 AA.
Q9NYL2; B3KPG2; Q53SX1; Q580W8; Q59GY5; Q86YW8; Q9HCC4; Q9HCC5; Q9HDD2;
Q9NYE9;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
17-JUN-2020, entry version 179.
RecName: Full=Mitogen-activated protein kinase kinase kinase 20 {ECO:0000312|HGNC:HGNC:17797};
EC=2.7.11.25;
AltName: Full=Human cervical cancer suppressor gene 4 protein;
Short=HCCS-4;
AltName: Full=Leucine zipper- and sterile alpha motif-containing kinase;
AltName: Full=MLK-like mitogen-activated protein triple kinase;
AltName: Full=Mitogen-activated protein kinase kinase kinase MLT;
AltName: Full=Mixed lineage kinase-related kinase;
Short=MLK-related kinase;
Short=MRK;
AltName: Full=Sterile alpha motif- and leucine zipper-containing kinase AZK;
Name=MAP3K20 {ECO:0000312|HGNC:HGNC:17797};
Synonyms=MLTK, ZAK {ECO:0000303|PubMed:10924358}; ORFNames=HCCS4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF63490.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
HOMODIMERIZATION, AND VARIANT LEU-531.
TISSUE=Placenta {ECO:0000269|PubMed:10924358};
PubMed=10924358; DOI=10.1006/bbrc.2000.3236;
Liu T.-C., Huang C.-J., Chu Y.-C., Wei C.-C., Chou C.-C., Chou M.-Y.,
Chou C.-K., Yang J.-J.;
"Cloning and expression of ZAK, a mixed lineage kinase-like protein
containing a leucine-zipper and a sterile-alpha motif.";
Biochem. Biophys. Res. Commun. 274:811-816(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION (ISOFORM 1),
PHOSPHORYLATION AT SER-429 (ISOFORM 2), AND VARIANT LEU-531.
TISSUE=Fetal brain;
PubMed=11042189; DOI=10.1074/jbc.m008595200;
Gotoh I., Adachi M., Nishida E.;
"Identification and characterization of a novel MAP kinase kinase kinase,
MLTK.";
J. Biol. Chem. 276:4276-4286(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=11549352; DOI=10.1006/jmcc.2001.1437;
Bloem L.J., Pickard T.R., Acton S., Donoghue M., Beavis R.C.,
Knierman M.D., Wang X.;
"Tissue distribution and functional expression of a cDNA encoding a novel
mixed lineage kinase.";
J. Mol. Cell. Cardiol. 33:1739-1750(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, MUTAGENESIS OF LYS-45, AND VARIANT LEU-531.
TISSUE=T-cell {ECO:0000269|PubMed:11836244};
PubMed=11836244; DOI=10.1074/jbc.m111994200;
Gross E.A., Callow M.G., Waldbaum L., Thomas S., Ruggieri R.;
"MRK, a mixed lineage kinase-related molecule that plays a role in gamma-
radiation-induced cell cycle arrest.";
J. Biol. Chem. 277:13873-13882(2002).
[5] {ECO:0000305, ECO:0000312|EMBL:BAB12040.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoid tissue;
Abe Y., Ueda N.;
"Placible mixed-lineage kinase derived from LAK cell.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:BAB12040.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-531.
McNee J.J., Frima N., Diamond T.E., Dower S.K., Guesdon F.;
"Cloning and characterisation of AZK, a mixed lineage kinase containing a
sterile-alpha motif.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305, ECO:0000312|EMBL:BAB12040.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kim J.W.;
"Identification of a new tumor suppressor in human cancers.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[9] {ECO:0000305, ECO:0000312|EMBL:BAB12040.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-784.
TISSUE=Brain {ECO:0000312|EMBL:BAD92211.1};
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000312|EMBL:AAX82002.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[11] {ECO:0000305, ECO:0000312|EMBL:BAB12040.1}
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.
[12] {ECO:0000305, ECO:0000312|EMBL:AAH01401.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon {ECO:0000312|EMBL:AAH01401.1};
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).
[13]
INTERACTION WITH ZNF33A.
PubMed=12535642; DOI=10.1016/s0006-291x(02)02980-7;
Yang J.-J.;
"A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the
ZAK-expressing cells re-entering the cell cycle.";
Biochem. Biophys. Res. Commun. 301:71-77(2003).
[14] {ECO:0000305}
PHOSPHORYLATION, AND INTERACTION WITH PKN1.
PubMed=12761180; DOI=10.1093/jb/mvg022;
Takahashi M., Gotoh Y., Isagawa T., Nishimura T., Goyama E., Kim H.-S.,
Mukai H., Ono Y.;
"Regulation of a mitogen-activated protein kinase kinase kinase, MLTK by
PKN.";
J. Biochem. 133:181-187(2003).
[15] {ECO:0000305}
FUNCTION (ISOFORM 1).
PubMed=15172994; DOI=10.1158/0008-5472.can-04-0201;
Cho Y.-Y., Bode A.M., Mizuno H., Choi B.Y., Choi H.S., Dong Z.;
"A novel role for mixed-lineage kinase-like mitogen-activated protein
triple kinase alpha in neoplastic cell transformation and tumor
development.";
Cancer Res. 64:3855-3864(2004).
[16] {ECO:0000305}
FUNCTION IN DNA DAMAGE CHECKPOINTS, FUNCTION IN PHOSPHORYLATION OF CHEK2,
ACTIVITY REGULATION, PHOSPHORYLATION AT THR-161 AND SER-165, AND
MUTAGENESIS OF THR-161; THR-162 AND SER-165.
PubMed=15342622; DOI=10.1074/jbc.m409961200;
Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R.;
"The stress kinase MRK contributes to regulation of DNA damage checkpoints
through a p38gamma-independent pathway.";
J. Biol. Chem. 279:47652-47660(2004).
[17]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3 (ISOFORM 1), AND SUBCELLULAR
LOCATION.
PubMed=15684425; DOI=10.1074/jbc.m410521200;
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
"Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-
like mitogen-activated protein triple kinase alpha.";
J. Biol. Chem. 280:13545-13553(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-302; THR-628;
SER-727 AND SER-733, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339;
SER-434 AND SER-454 (ISOFORM 2), 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; THR-628; SER-633;
SER-727 AND SER-733, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454
(ISOFORM 2), 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).
[20]
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-275; THR-628; SER-633 AND SER-727, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-339; SER-434 AND SER-454 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, 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).
[24]
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).
[25]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH AKAP13; PKN1; MAPK14 AND
MAP2K3.
PubMed=21224381; DOI=10.1074/jbc.m110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38 activation.";
J. Biol. Chem. 286:7925-7937(2011).
[26]
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).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; SER-593; THR-628;
SER-633; SER-637; SER-648; SER-649; SER-685; SER-727 AND SER-733, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, 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).
[30]
VARIANTS [LARGE SCALE ANALYSIS] MET-267; THR-281; VAL-281; LEU-531;
TRP-580; THR-740; HIS-773 AND THR-784.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[31]
INVOLVEMENT IN SFMMP, FUNCTION, SUBUNIT, VARIANT SFMMP CYS-368, AND
CHARACTERIZATION OF VARIANT SFMMP CYS-368.
PubMed=26755636; DOI=10.1101/gr.199430.115;
Spielmann M., Kakar N., Tayebi N., Leettola C., Nuernberg G., Sowada N.,
Lupianez D.G., Harabula I., Floettmann R., Horn D., Chan W.L., Wittler L.,
Yilmaz R., Altmueller J., Thiele H., van Bokhoven H., Schwartz C.E.,
Nuernberg P., Bowie J.U., Ahmad J., Kubisch C., Mundlos S., Borck G.;
"Exome sequencing and CRISPR/Cas genome editing identify mutations of ZAK
as a cause of limb defects in humans and mice.";
Genome Res. 26:183-191(2016).
[32]
INVOLVEMENT IN CNM6, VARIANTS CNM6 95-ASN--PHE-800 DEL AND 172-TRP--PHE-800
DEL, AND CHARACTERIZATION OF VARIANTS CNM6 95-ASN--PHE-800 DEL AND
172-TRP--PHE-800 DEL.
PubMed=27816943; DOI=10.1093/brain/aww257;
Vasli N., Harris E., Karamchandani J., Bareke E., Majewski J., Romero N.B.,
Stojkovic T., Barresi R., Tasfaout H., Charlton R., Malfatti E., Bohm J.,
Marini-Bettolo C., Choquet K., Dicaire M.J., Shao Y.H., Topf A.,
O'Ferrall E., Eymard B., Straub V., Blanco G., Lochmueller H., Brais B.,
Laporte J., Tetreault M.;
"Recessive mutations in the kinase ZAK cause a congenital myopathy with
fibre type disproportion.";
Brain 140:37-48(2017).
[33]
VARIANT CNM6 TRP-250.
PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
"Autozygome and high throughput confirmation of disease genes candidacy.";
Genet. Med. 21:736-742(2019).
-!- FUNCTION: Stress-activated component of a protein kinase signal
transduction cascade. Regulates the JNK and p38 pathways. Part of a
signaling cascade that begins with the activation of the adrenergic
receptor ADRA1B and leads to the activation of MAPK14. Pro-apoptotic.
Role in regulation of S and G2 cell cycle checkpoint by direct
phosphorylation of CHEK2 (PubMed:10924358, PubMed:11836244,
PubMed:15342622, PubMed:21224381). Involved in limb development
(PubMed:26755636). {ECO:0000269|PubMed:10924358,
ECO:0000269|PubMed:11836244, ECO:0000269|PubMed:15342622,
ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:26755636}.
-!- FUNCTION: [Isoform 1]: Phosphorylates histone H3 at 'Ser-28'
(PubMed:15684425). May have role in neoplastic cell transformation and
cancer development (PubMed:15172994). Causes cell shrinkage and
disruption of actin stress fibers (PubMed:11042189).
{ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:15172994,
ECO:0000269|PubMed:15684425}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
Evidence={ECO:0000269|PubMed:11836244};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.25; Evidence={ECO:0000269|PubMed:11836244};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11836244};
-!- ACTIVITY REGULATION: Activated by phosphorylation by PKN1 and
autophosphorylation on Thr-161 and Ser-165.
{ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:12761180,
ECO:0000269|PubMed:15342622}.
-!- SUBUNIT: Homodimer (PubMed:10924358, PubMed:26755636). Interacts with
PKN1 and ZNF33A (PubMed:12535642, PubMed:12761180). Component of a
signaling complex containing at least AKAP13, PKN1, MAPK14, MAP3K20 and
MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which
in turn recruits MAPK14, MAP2K3 and MAP3K20 (PubMed:21224381).
{ECO:0000269|PubMed:10924358, ECO:0000269|PubMed:12535642,
ECO:0000269|PubMed:12761180, ECO:0000269|PubMed:21224381,
ECO:0000269|PubMed:26755636}.
-!- INTERACTION:
Q9NYL2; O75582: RPS6KA5; NbExp=4; IntAct=EBI-602273, EBI-73869;
Q9NYL2; P63104: YWHAZ; NbExp=5; IntAct=EBI-602273, EBI-347088;
Q9NYL2; Q8N184: ZNF567; NbExp=3; IntAct=EBI-602273, EBI-749400;
Q9NYL2-1; Q16512: PKN1; NbExp=2; IntAct=EBI-687346, EBI-602382;
Q9NYL2-2; Q6P2D0: ZFP1; NbExp=4; IntAct=EBI-10255081, EBI-2555749;
Q9NYL2-2; Q6ZN57: ZFP2; NbExp=7; IntAct=EBI-10255081, EBI-7236323;
Q9NYL2-2; P13682: ZNF35; NbExp=3; IntAct=EBI-10255081, EBI-11041653;
Q9NYL2-2; Q8N184: ZNF567; NbExp=7; IntAct=EBI-10255081, EBI-749400;
Q9NYL2-2; Q6AZW8: ZNF660; NbExp=3; IntAct=EBI-10255081, EBI-12376497;
Q9NYL2-2; Q9NQZ8: ZNF71; NbExp=4; IntAct=EBI-10255081, EBI-7138235;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15684425}. Nucleus
{ECO:0000269|PubMed:15684425}. Note=Translocates to the nucleus upon
ultraviolet B irradiation. {ECO:0000269|PubMed:15684425}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:11042189}; Synonyms=Alpha;
IsoId=Q9NYL2-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11042189}; Synonyms=Beta;
IsoId=Q9NYL2-2; Sequence=VSP_051743, VSP_051744;
Name=3; Synonyms=HCCS-4;
IsoId=Q9NYL2-3; Sequence=VSP_051741, VSP_051742;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is the
predominant form in all tissues examined, except for liver, in which
isoform 1 is more highly expressed. {ECO:0000269|PubMed:10924358,
ECO:0000269|PubMed:11836244}.
-!- DISEASE: Split-foot malformation with mesoaxial polydactyly (SFMMP)
[MIM:616890]: An autosomal recessive disorder characterized by a split-
foot defect, mesoaxial polydactyly, nail abnormalities of the hands,
and sensorineural hearing loss. {ECO:0000269|PubMed:26755636}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Myopathy, centronuclear, 6, with fiber-type disproportion
(CNM6) [MIM:617760]: A form of centronuclear myopathy, a congenital
muscle disorder characterized by progressive muscular weakness and
wasting involving mainly limb girdle, trunk, and neck muscles. It may
also affect distal muscles. Weakness may be present during childhood or
adolescence or may not become evident until the third decade of life.
Ptosis is a frequent clinical feature. The most prominent
histopathologic features include high frequency of centrally located
nuclei in muscle fibers not secondary to regeneration, radial
arrangement of sarcoplasmic strands around the central nuclei, and
predominance and hypotrophy of type 1 fibers. CNM6 is an autosomal
recessive, slowly progressive form with onset in infancy or early
childhood. {ECO:0000269|PubMed:27816943, ECO:0000269|PubMed:30237576}.
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}.
-!- SEQUENCE CAUTION:
Sequence=BAD92211.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AF238255; AAF63490.1; -; mRNA.
EMBL; AB049733; BAB16444.1; -; mRNA.
EMBL; AB049734; BAB16445.1; -; mRNA.
EMBL; AF325454; AAK11615.1; -; mRNA.
EMBL; AF480461; AAL85891.1; -; mRNA.
EMBL; AF480462; AAL85892.1; -; mRNA.
EMBL; AB030034; BAB12040.1; -; mRNA.
EMBL; AF251441; AAF65822.1; -; mRNA.
EMBL; AF465843; AAO33376.1; -; mRNA.
EMBL; AK056310; BAG51674.1; -; mRNA.
EMBL; AB208974; BAD92211.1; ALT_INIT; mRNA.
EMBL; AC092573; AAX82002.1; -; Genomic_DNA.
EMBL; AC013461; AAX93067.1; -; Genomic_DNA.
EMBL; AC019046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471058; EAX11164.1; -; Genomic_DNA.
EMBL; BC001401; AAH01401.1; -; mRNA.
CCDS; CCDS2251.1; -. [Q9NYL2-2]
CCDS; CCDS42777.1; -. [Q9NYL2-1]
RefSeq; NP_057737.2; NM_016653.2. [Q9NYL2-1]
RefSeq; NP_598407.1; NM_133646.2. [Q9NYL2-2]
RefSeq; XP_005246697.1; XM_005246640.2. [Q9NYL2-1]
RefSeq; XP_016859812.1; XM_017004323.1. [Q9NYL2-2]
RefSeq; XP_016859813.1; XM_017004324.1. [Q9NYL2-2]
PDB; 5HES; X-ray; 2.14 A; A/B=5-309.
PDB; 5X5O; X-ray; 1.87 A; A=5-309.
PDB; 6JUT; X-ray; 2.10 A; A=5-309.
PDBsum; 5HES; -.
PDBsum; 5X5O; -.
PDBsum; 6JUT; -.
SMR; Q9NYL2; -.
BioGRID; 119725; 47.
CORUM; Q9NYL2; -.
IntAct; Q9NYL2; 47.
MINT; Q9NYL2; -.
STRING; 9606.ENSP00000364361; -.
BindingDB; Q9NYL2; -.
ChEMBL; CHEMBL3886; -.
DrugBank; DB01254; Dasatinib.
DrugBank; DB12010; Fostamatinib.
DrugCentral; Q9NYL2; -.
GuidetoPHARMACOLOGY; 2289; -.
iPTMnet; Q9NYL2; -.
MetOSite; Q9NYL2; -.
PhosphoSitePlus; Q9NYL2; -.
BioMuta; MAP3K20; -.
DMDM; 313104215; -.
EPD; Q9NYL2; -.
jPOST; Q9NYL2; -.
MassIVE; Q9NYL2; -.
MaxQB; Q9NYL2; -.
PaxDb; Q9NYL2; -.
PeptideAtlas; Q9NYL2; -.
PRIDE; Q9NYL2; -.
ProteomicsDB; 83246; -. [Q9NYL2-1]
ProteomicsDB; 83247; -. [Q9NYL2-2]
ProteomicsDB; 83248; -. [Q9NYL2-3]
Antibodypedia; 2065; 291 antibodies.
DNASU; 51776; -.
Ensembl; ENST00000338983; ENSP00000340257; ENSG00000091436. [Q9NYL2-2]
Ensembl; ENST00000375213; ENSP00000364361; ENSG00000091436. [Q9NYL2-1]
Ensembl; ENST00000409176; ENSP00000387259; ENSG00000091436. [Q9NYL2-1]
Ensembl; ENST00000539448; ENSP00000439414; ENSG00000091436. [Q9NYL2-2]
GeneID; 51776; -.
KEGG; hsa:51776; -.
UCSC; uc002uhz.4; human. [Q9NYL2-1]
CTD; 51776; -.
DisGeNET; 51776; -.
EuPathDB; HostDB:ENSG00000091436.16; -.
GeneCards; MAP3K20; -.
HGNC; HGNC:17797; MAP3K20.
HPA; ENSG00000091436; Tissue enhanced (skeletal).
MalaCards; MAP3K20; -.
MIM; 609479; gene.
MIM; 616890; phenotype.
MIM; 617760; phenotype.
neXtProt; NX_Q9NYL2; -.
OpenTargets; ENSG00000091436; -.
Orphanet; 2020; Congenital fiber-type disproportion myopathy.
Orphanet; 488232; Split-foot malformation-mesoaxial polydactyly syndrome.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000161352; -.
HOGENOM; CLU_019131_1_0_1; -.
InParanoid; Q9NYL2; -.
KO; K04424; -.
OMA; KALMMTG; -.
OrthoDB; 938929at2759; -.
PhylomeDB; Q9NYL2; -.
SignaLink; Q9NYL2; -.
SIGNOR; Q9NYL2; -.
BioGRID-ORCS; 51776; 3 hits in 804 CRISPR screens.
ChiTaRS; MAP3K20; human.
GeneWiki; ZAK; -.
GenomeRNAi; 51776; -.
Pharos; Q9NYL2; Tchem.
PRO; PR:Q9NYL2; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q9NYL2; protein.
Bgee; ENSG00000091436; Expressed in heart left ventricle and 220 other tissues.
ExpressionAtlas; Q9NYL2; baseline and differential.
Genevisible; Q9NYL2; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; TAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IMP:UniProtKB.
GO; GO:0008219; P:cell death; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
Gene3D; 1.10.150.50; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032938; MLTK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR23257:SF759; PTHR23257:SF759; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Cytoplasm; Disease mutation; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895"
CHAIN 2..800
/note="Mitogen-activated protein kinase kinase kinase 20"
/id="PRO_0000086338"
DOMAIN 16..277
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
DOMAIN 339..410
/note="SAM"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
NP_BIND 22..30
/note="ATP"
/evidence="ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 287..308
/note="Leucine-zipper"
ACT_SITE 133
/note="Proton acceptor"
/evidence="ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027"
BINDING 45
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:11836244"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895"
MOD_RES 161
/note="Phosphothreonine; by autocatalysis"
/evidence="ECO:0000269|PubMed:15342622"
MOD_RES 165
/note="Phosphoserine; by autocatalysis"
/evidence="ECO:0000269|PubMed:15342622"
MOD_RES 275
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES 302
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976"
MOD_RES 567
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 593
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 599
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 628
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163"
MOD_RES 633
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 637
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 648
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 649
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 685
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 727
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 733
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:23186163"
VAR_SEQ 285..312
/note="CEIEATLERLKKLERDLSFKEQELKERE -> WVAPTAGHSVWLSKTITRLN
EEVNQRSE (in isoform 3)"
/evidence="ECO:0000303|Ref.7"
/id="VSP_051741"
VAR_SEQ 313..800
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|Ref.7"
/id="VSP_051742"
VAR_SEQ 332..455
/note="PSFEIGAWTEDDVYCWVQQLVRKGDSSAEMSVYASLFKENNITGKRLLLLEE
EDLKDMGIVSKGHIIHFKSAIEKLTHDYINLFHFPPLIKDSGGEPEENEEKIVNLELVF
GFHLKPGTGPQDC -> LPLAARMSEESYFESKTEESNSAEMSCQITATSNGEGHGMNP
SLQAMMLMGFGDIFSMNKAGAVMHSGMQINMQAKQNSSKTTSKRRGKKVNMALGFSDFD
LSEGDDDDDDDGEEEDNDMDNSE (in isoform 2)"
/evidence="ECO:0000303|PubMed:11042189,
ECO:0000303|PubMed:11549352, ECO:0000303|PubMed:11836244,
ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
/id="VSP_051743"
VAR_SEQ 456..800
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:11042189,
ECO:0000303|PubMed:11549352, ECO:0000303|PubMed:11836244,
ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
/id="VSP_051744"
VARIANT 95..800
/note="Missing (in CNM6; decrease of protein abundance)"
/evidence="ECO:0000269|PubMed:27816943"
/id="VAR_080563"
VARIANT 172..800
/note="Missing (in CNM6; decrease of protein abundance)"
/evidence="ECO:0000269|PubMed:27816943"
/id="VAR_080564"
VARIANT 250
/note="R -> W (in CNM6; unknown pathological significance;
dbSNP:rs763481300)"
/evidence="ECO:0000269|PubMed:30237576"
/id="VAR_082158"
VARIANT 267
/note="T -> M (in dbSNP:rs6758025)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040806"
VARIANT 281
/note="A -> T (in an ovarian endometrioid sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040807"
VARIANT 281
/note="A -> V (in dbSNP:rs34683477)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040808"
VARIANT 368
/note="F -> C (in SFMMP; produces protein aggregation;
dbSNP:rs863225437)"
/evidence="ECO:0000269|PubMed:26755636"
/id="VAR_076448"
VARIANT 531
/note="S -> L (in dbSNP:rs3769148)"
/evidence="ECO:0000269|PubMed:10924358,
ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:11836244,
ECO:0000269|PubMed:17344846, ECO:0000269|Ref.6"
/id="VAR_022827"
VARIANT 580
/note="R -> W (in dbSNP:rs7593622)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040809"
VARIANT 740
/note="P -> T (in dbSNP:rs56202258)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040810"
VARIANT 773
/note="Y -> H (in dbSNP:rs35608243)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040811"
VARIANT 784
/note="K -> T (in dbSNP:rs55830025)"
/evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.9"
/id="VAR_040812"
MUTAGEN 45
/note="K->M: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:11836244"
MUTAGEN 161
/note="T->A: Loss of autophosphorylation activity."
/evidence="ECO:0000269|PubMed:15342622"
MUTAGEN 162
/note="T->A: Slight loss of autophosphorylation activity."
/evidence="ECO:0000269|PubMed:15342622"
MUTAGEN 165
/note="S->A: Loss of autophosphorylation activity."
/evidence="ECO:0000269|PubMed:15342622"
CONFLICT 346
/note="C -> W (in Ref. 1; AAF63490)"
/evidence="ECO:0000305"
HELIX 13..15
/evidence="ECO:0000244|PDB:5X5O"
STRAND 16..20
/evidence="ECO:0000244|PDB:5X5O"
STRAND 24..26
/evidence="ECO:0000244|PDB:6JUT"
STRAND 30..35
/evidence="ECO:0000244|PDB:5X5O"
TURN 36..39
/evidence="ECO:0000244|PDB:5X5O"
STRAND 40..48
/evidence="ECO:0000244|PDB:5X5O"
HELIX 52..57
/evidence="ECO:0000244|PDB:5X5O"
STRAND 68..74
/evidence="ECO:0000244|PDB:5X5O"
STRAND 77..83
/evidence="ECO:0000244|PDB:5X5O"
HELIX 90..94
/evidence="ECO:0000244|PDB:5X5O"
HELIX 97..101
/evidence="ECO:0000244|PDB:5X5O"
HELIX 104..123
/evidence="ECO:0000244|PDB:5X5O"
STRAND 125..127
/evidence="ECO:0000244|PDB:5X5O"
HELIX 136..138
/evidence="ECO:0000244|PDB:5X5O"
STRAND 139..141
/evidence="ECO:0000244|PDB:5X5O"
STRAND 147..149
/evidence="ECO:0000244|PDB:5X5O"
HELIX 154..157
/evidence="ECO:0000244|PDB:5X5O"
HELIX 159..162
/evidence="ECO:0000244|PDB:5X5O"
HELIX 163..166
/evidence="ECO:0000244|PDB:6JUT"
TURN 167..169
/evidence="ECO:0000244|PDB:5X5O"
HELIX 170..172
/evidence="ECO:0000244|PDB:5X5O"
HELIX 175..178
/evidence="ECO:0000244|PDB:5X5O"
HELIX 186..201
/evidence="ECO:0000244|PDB:5X5O"
TURN 205..208
/evidence="ECO:0000244|PDB:5X5O"
HELIX 211..220
/evidence="ECO:0000244|PDB:5X5O"
HELIX 233..242
/evidence="ECO:0000244|PDB:5X5O"
HELIX 247..249
/evidence="ECO:0000244|PDB:5X5O"
HELIX 253..264
/evidence="ECO:0000244|PDB:5X5O"
HELIX 269..277
/evidence="ECO:0000244|PDB:5X5O"
HELIX 280..298
/evidence="ECO:0000244|PDB:5X5O"
MOD_RES Q9NYL2-2:339
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES Q9NYL2-2:429
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:11042189"
MOD_RES Q9NYL2-2:434
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES Q9NYL2-2:454
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195"
SEQUENCE 800 AA; 91155 MW; B2814509EC54B07A CRC64;
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI EKEAEILSVL
SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE EMDMDHIMTW ATDVAKGMHY
LHMEAPVKVI HRDLKSRNVV IAADGVLKIC DFGASRFHNH TTHMSLVGTF PWMAPEVIQS
LPVSETCDTY SYGVVLWEML TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH
QCWEADAKKR PSFKQIISIL ESMSNDTSLP DKCNSFLHNK AEWRCEIEAT LERLKKLERD
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYCWVQQ LVRKGDSSAE
MSVYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF KSAIEKLTHD YINLFHFPPL
IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT GPQDCKWKMY MEMDGDEIAI TYIKDVTFNT
NLPDAEILKM TKPPFVMEKW IVGIAKSQTV ECTVTYESDV RTPKSTKHVH SIQWSRTKPQ
DEVKAVQLAI QTLFTNSDGN PGSRSDSSAD CQWLDTLRMR QIASNTSLQR SQSNPILGSP
FFSHFDGQDS YAAAVRRPQV PIKYQQITPV NQSRSSSPTQ YGLTKNFSSL HLNSRDSGFS
SGNTDTSSER GRYSDRSRNK YGRGSISLNS SPRGRYSGKS QHSTPSRGRY PGKFYRVSQS
ALNPHQSPDF KRSPRDLHQP NTIPGMPLHP ETDSRASEED SKVSEGGWTK VEYRKKPHRP
SPAKTNKERA RGDHRGWRNF


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Catalog number Product name Quantity
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB24969 HCCS4,HCCS-4,Homo sapiens,Human,Human cervical cancer suppressor gene 4 protein,Leucine zipper- and sterile alpha motif-containing kinase,Mitogen-activated protein kinase kinase kinase MLT,Mixed linea
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
U1358h CLIA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
E1358h ELISA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
E1358h ELISA kit Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
EIAAB24782 B55,GCK family kinase MiNK,Homo sapiens,Human,MAP4K6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,MINK,MINK1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated prote
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.05 mg
18-662-20092 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
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18-662-20090 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 mg
10-782-55048 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
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10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
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Pathways :
WP1493: Carbon assimilation C4 pathway
WP32: Translation Factors
WP1946: Cori Cycle
WP253: Glycolysis
WP1701: Starch and sucrose metabolism
WP1619: Amino sugar and nucleotide sugar metabolism
WP1844: MAP kinase cascade
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1681: Pantothenate and CoA biosynthesis
WP1653: Galactose metabolism
WP1567: Glycolysis and Gluconeogenesis
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1703: Streptomycin biosynthesis
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP1531: Vitamin D synthesis
WP731: Sterol regulatory element binding protein related
WP1566: Citrate cycle (TCA cycle)
WP2292: Chemokine signaling pathway
WP210: Cytoplasmic Ribosomal Proteins
WP1616: ABC transporters
WP1673: Naphthalene and anthracene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1678: Nucleotide excision repair
WP2371: Parkinsons Disease Pathway

Related Genes :
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[MAP3K11 MLK3 PTK1 SPRK] Mitogen-activated protein kinase kinase kinase 11 (EC 2.7.11.25) (Mixed lineage kinase 3) (Src-homology 3 domain-containing proline-rich kinase)
[MAP3K9 MLK1 PRKE1] Mitogen-activated protein kinase kinase kinase 9 (EC 2.7.11.25) (Mixed lineage kinase 1)
[map3k10 mlk2] Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25) (Mixed lineage kinase 2) (xMLK2)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAPK8 JNK1 PRKM8 SAPK1 SAPK1C] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[MAP4K2 GCK RAB8IP] Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (B lymphocyte serine/threonine-protein kinase) (Germinal center kinase) (GC kinase) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein)
[dlk-1 F33E2.2] Mitogen-activated protein kinase kinase kinase dlk-1 (EC 2.7.11.25) (DAP kinase-like kinase) (Death-associated protein kinase-like kinase)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[MAPK8IP1 IB1 JIP1 PRKM8IP] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain 1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[RPS6KA5 MSK1] Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RSKL)
[RPS6KA4 MSK2] Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (Ribosomal protein kinase B) (RSKB)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[MAPK9 JNK2 PRKM9 SAPK1A] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (JNK-55) (Stress-activated protein kinase 1a) (SAPK1a) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP3K1 MAPKKK1 MEKK MEKK1] Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[TAB2 KIAA0733 MAP3K7IP2] TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2)
[Mapk9 Jnk2 Prkm9] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (SAPK-alpha) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) (p54-alpha)

Bibliography :