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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.
05-JUN-2019, entry version 171.
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).
-!- 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:
Q16512:PKN1; NbExp=2; IntAct=EBI-687346, EBI-602382;
O75582:RPS6KA5; NbExp=4; IntAct=EBI-602273, EBI-73869;
P63104:YWHAZ; NbExp=4; IntAct=EBI-602273, EBI-347088;
Q6ZN57:ZFP2; NbExp=5; IntAct=EBI-10255081, EBI-7236323;
Q8N184:ZNF567; NbExp=5; IntAct=EBI-10255081, EBI-749400;
-!- 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;
Note=Contains a phosphoserine at position 429. Contains a
phosphoserine at position 339. Contains a phosphoserine at
position 434. Contains a phosphoserine at position 454.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195, ECO:0000269|PubMed:11042189};
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}. 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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.
PDBsum; 5HES; -.
PDBsum; 5X5O; -.
SMR; Q9NYL2; -.
BioGrid; 119725; 45.
CORUM; Q9NYL2; -.
IntAct; Q9NYL2; 41.
MINT; Q9NYL2; -.
STRING; 9606.ENSP00000364361; -.
BindingDB; Q9NYL2; -.
ChEMBL; CHEMBL3886; -.
GuidetoPHARMACOLOGY; 2289; -.
iPTMnet; Q9NYL2; -.
PhosphoSitePlus; Q9NYL2; -.
BioMuta; MAP3K20; -.
DMDM; 313104215; -.
EPD; Q9NYL2; -.
jPOST; Q9NYL2; -.
MaxQB; Q9NYL2; -.
PaxDb; Q9NYL2; -.
PeptideAtlas; Q9NYL2; -.
PRIDE; Q9NYL2; -.
ProteomicsDB; 83246; -.
ProteomicsDB; 83247; -. [Q9NYL2-2]
ProteomicsDB; 83248; -. [Q9NYL2-3]
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; -.
GeneCards; MAP3K20; -.
H-InvDB; HIX0030332; -.
HGNC; HGNC:17797; MAP3K20.
HPA; HPA017205; -.
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; -.
InParanoid; Q9NYL2; -.
KO; K04424; -.
OMA; FVQIKHE; -.
OrthoDB; 938929at2759; -.
PhylomeDB; Q9NYL2; -.
SignaLink; Q9NYL2; -.
SIGNOR; Q9NYL2; -.
ChiTaRS; ZAK; human.
GeneWiki; ZAK; -.
GenomeRNAi; 51776; -.
PRO; PR:Q9NYL2; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000091436; Expressed in 221 organ(s), highest expression level in heart left ventricle.
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:0008283; P:cell population proliferation; 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; Complete proteome; Cytoplasm; Disease mutation; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895}.
CHAIN 2 800 Mitogen-activated protein kinase kinase
kinase 20.
/FTId=PRO_0000086338.
DOMAIN 16 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 339 410 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 22 30 ATP. {ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 287 308 Leucine-zipper.
ACT_SITE 133 133 Proton acceptor.
{ECO:0000250|UniProtKB:P80192,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 45 45 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:11836244}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895}.
MOD_RES 161 161 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:15342622}.
MOD_RES 165 165 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:15342622}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 599 599 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 637 637 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 685 685 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 727 727 Phosphoserine.
{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 733 733 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 285 312 CEIEATLERLKKLERDLSFKEQELKERE -> WVAPTAGHS
VWLSKTITRLNEEVNQRSE (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_051741.
VAR_SEQ 313 800 Missing (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_051742.
VAR_SEQ 332 455 PSFEIGAWTEDDVYCWVQQLVRKGDSSAEMSVYASLFKENN
ITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYIN
LFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQD
C -> LPLAARMSEESYFESKTEESNSAEMSCQITATSNGE
GHGMNPSLQAMMLMGFGDIFSMNKAGAVMHSGMQINMQAKQ
NSSKTTSKRRGKKVNMALGFSDFDLSEGDDDDDDDGEEEDN
DMDNSE (in isoform 2).
{ECO:0000303|PubMed:11042189,
ECO:0000303|PubMed:11549352,
ECO:0000303|PubMed:11836244,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_051743.
VAR_SEQ 456 800 Missing (in isoform 2).
{ECO:0000303|PubMed:11042189,
ECO:0000303|PubMed:11549352,
ECO:0000303|PubMed:11836244,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_051744.
VARIANT 95 800 Missing (in CNM6; decrease of protein
abundance).
{ECO:0000269|PubMed:27816943}.
/FTId=VAR_080563.
VARIANT 172 800 Missing (in CNM6; decrease of protein
abundance).
{ECO:0000269|PubMed:27816943}.
/FTId=VAR_080564.
VARIANT 267 267 T -> M (in dbSNP:rs6758025).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040806.
VARIANT 281 281 A -> T (in an ovarian endometrioid
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040807.
VARIANT 281 281 A -> V (in dbSNP:rs34683477).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040808.
VARIANT 368 368 F -> C (in SFMMP; produces protein
aggregation; dbSNP:rs863225437).
{ECO:0000269|PubMed:26755636}.
/FTId=VAR_076448.
VARIANT 531 531 S -> L (in dbSNP:rs3769148).
{ECO:0000269|PubMed:10924358,
ECO:0000269|PubMed:11042189,
ECO:0000269|PubMed:11836244,
ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.6}.
/FTId=VAR_022827.
VARIANT 580 580 R -> W (in dbSNP:rs7593622).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040809.
VARIANT 740 740 P -> T (in dbSNP:rs56202258).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040810.
VARIANT 773 773 Y -> H (in dbSNP:rs35608243).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040811.
VARIANT 784 784 K -> T (in dbSNP:rs55830025).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.9}.
/FTId=VAR_040812.
MUTAGEN 45 45 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:11836244}.
MUTAGEN 161 161 T->A: Loss of autophosphorylation
activity. {ECO:0000269|PubMed:15342622}.
MUTAGEN 162 162 T->A: Slight loss of autophosphorylation
activity. {ECO:0000269|PubMed:15342622}.
MUTAGEN 165 165 S->A: Loss of autophosphorylation
activity. {ECO:0000269|PubMed:15342622}.
CONFLICT 346 346 C -> W (in Ref. 1; AAF63490).
{ECO:0000305}.
HELIX 13 15 {ECO:0000244|PDB:5X5O}.
STRAND 16 20 {ECO:0000244|PDB:5X5O}.
HELIX 22 25 {ECO:0000244|PDB:5HES}.
STRAND 30 35 {ECO:0000244|PDB:5X5O}.
TURN 36 39 {ECO:0000244|PDB:5X5O}.
STRAND 40 48 {ECO:0000244|PDB:5X5O}.
HELIX 52 57 {ECO:0000244|PDB:5X5O}.
STRAND 68 74 {ECO:0000244|PDB:5X5O}.
STRAND 77 83 {ECO:0000244|PDB:5X5O}.
HELIX 90 94 {ECO:0000244|PDB:5X5O}.
HELIX 97 101 {ECO:0000244|PDB:5X5O}.
HELIX 104 123 {ECO:0000244|PDB:5X5O}.
STRAND 125 127 {ECO:0000244|PDB:5X5O}.
HELIX 136 138 {ECO:0000244|PDB:5X5O}.
STRAND 139 141 {ECO:0000244|PDB:5X5O}.
STRAND 147 149 {ECO:0000244|PDB:5X5O}.
HELIX 154 157 {ECO:0000244|PDB:5X5O}.
HELIX 159 162 {ECO:0000244|PDB:5X5O}.
TURN 167 169 {ECO:0000244|PDB:5X5O}.
HELIX 170 172 {ECO:0000244|PDB:5X5O}.
HELIX 175 178 {ECO:0000244|PDB:5X5O}.
HELIX 186 201 {ECO:0000244|PDB:5X5O}.
TURN 205 208 {ECO:0000244|PDB:5X5O}.
HELIX 211 220 {ECO:0000244|PDB:5X5O}.
HELIX 233 242 {ECO:0000244|PDB:5X5O}.
HELIX 247 249 {ECO:0000244|PDB:5X5O}.
HELIX 253 264 {ECO:0000244|PDB:5X5O}.
HELIX 269 277 {ECO:0000244|PDB:5X5O}.
HELIX 280 298 {ECO:0000244|PDB:5X5O}.
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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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
18-662-20091 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
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
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 0.05 mg
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
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 0.05 mg
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
WP1531: Vitamin D synthesis
WP731: Sterol regulatory element binding protein related
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP2292: Chemokine signaling pathway
WP210: Cytoplasmic Ribosomal Proteins
WP1673: Naphthalene and anthracene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1616: ABC transporters
WP2371: Parkinsons Disease Pathway
WP1624: Bacterial secretion system

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)
[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)
[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)
[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)
[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) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[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)
[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)
[Mapk13 Serk4] 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)
[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)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (MKK1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)

Bibliography :
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