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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.
25-OCT-2017, entry version 158.
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, ENZYME 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).
-!- 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: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11836244}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11836244};
-!- ENZYME 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=7; 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.
-!- 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-NoDerivs License
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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]
UniGene; Hs.444451; -.
PDB; 5HES; X-ray; 2.14 A; A/B=5-309.
PDBsum; 5HES; -.
ProteinModelPortal; Q9NYL2; -.
SMR; Q9NYL2; -.
BioGrid; 119725; 44.
IntAct; Q9NYL2; 40.
MINT; MINT-1465549; -.
STRING; 9606.ENSP00000364361; -.
BindingDB; Q9NYL2; -.
ChEMBL; CHEMBL3886; -.
GuidetoPHARMACOLOGY; 2289; -.
iPTMnet; Q9NYL2; -.
PhosphoSitePlus; Q9NYL2; -.
BioMuta; MLTK; -.
DMDM; 313104215; -.
EPD; Q9NYL2; -.
MaxQB; Q9NYL2; -.
PaxDb; Q9NYL2; -.
PeptideAtlas; Q9NYL2; -.
PRIDE; Q9NYL2; -.
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; -.
H-InvDB; HIX0030332; -.
HGNC; HGNC:17797; MAP3K20.
HPA; HPA017205; -.
MalaCards; MAP3K20; -.
MIM; 609479; gene.
MIM; 616890; phenotype.
neXtProt; NX_Q9NYL2; -.
OpenTargets; ENSG00000091436; -.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140790; -.
HOVERGEN; HBG080445; -.
InParanoid; Q9NYL2; -.
KO; K04424; -.
OMA; QWRCEIE; -.
OrthoDB; EOG091G037E; -.
PhylomeDB; Q9NYL2; -.
SignaLink; Q9NYL2; -.
SIGNOR; Q9NYL2; -.
ChiTaRS; ZAK; human.
GeneWiki; ZAK; -.
GenomeRNAi; 51776; -.
PRO; PR:Q9NYL2; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000091436; -.
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; IDA: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:0000075; P:cell cycle checkpoint; IDA:UniProtKB.
GO; GO:0008219; P:cell death; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; NAS: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:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
GO; GO:0006950; P:response to stress; NAS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032938; MLTK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR44496; PTHR44496; 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; 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 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:5HES}.
STRAND 16 21 {ECO:0000244|PDB:5HES}.
HELIX 22 25 {ECO:0000244|PDB:5HES}.
STRAND 29 35 {ECO:0000244|PDB:5HES}.
HELIX 36 38 {ECO:0000244|PDB:5HES}.
STRAND 40 48 {ECO:0000244|PDB:5HES}.
HELIX 53 57 {ECO:0000244|PDB:5HES}.
STRAND 68 74 {ECO:0000244|PDB:5HES}.
STRAND 77 83 {ECO:0000244|PDB:5HES}.
HELIX 90 94 {ECO:0000244|PDB:5HES}.
HELIX 97 101 {ECO:0000244|PDB:5HES}.
HELIX 104 123 {ECO:0000244|PDB:5HES}.
STRAND 125 127 {ECO:0000244|PDB:5HES}.
HELIX 136 138 {ECO:0000244|PDB:5HES}.
STRAND 139 141 {ECO:0000244|PDB:5HES}.
STRAND 147 149 {ECO:0000244|PDB:5HES}.
TURN 152 159 {ECO:0000244|PDB:5HES}.
HELIX 170 172 {ECO:0000244|PDB:5HES}.
HELIX 175 178 {ECO:0000244|PDB:5HES}.
HELIX 186 201 {ECO:0000244|PDB:5HES}.
TURN 205 208 {ECO:0000244|PDB:5HES}.
HELIX 211 220 {ECO:0000244|PDB:5HES}.
HELIX 233 242 {ECO:0000244|PDB:5HES}.
HELIX 247 249 {ECO:0000244|PDB:5HES}.
HELIX 253 265 {ECO:0000244|PDB:5HES}.
HELIX 269 278 {ECO:0000244|PDB:5HES}.
HELIX 280 298 {ECO:0000244|PDB:5HES}.
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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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


 

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