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Maternal embryonic leucine zipper kinase (hMELK) (EC 2.7.11.1) (Protein kinase Eg3) (pEg3 kinase) (Protein kinase PK38) (hPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2)

 MELK_HUMAN              Reviewed;         651 AA.
Q14680; A6P3A7; A6P3A8; B1AMQ6; B7Z1E6; B7Z5M5; B7Z6Q7; B7Z6R8;
B7Z6Y0; B7Z7Q1; D3DRP8; F5H0Y0; F5H2R4; F5H689; Q7L3C3;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 3.
28-MAR-2018, entry version 173.
RecName: Full=Maternal embryonic leucine zipper kinase;
Short=hMELK;
EC=2.7.11.1;
AltName: Full=Protein kinase Eg3;
Short=pEg3 kinase;
AltName: Full=Protein kinase PK38;
Short=hPK38;
AltName: Full=Tyrosine-protein kinase MELK;
EC=2.7.10.2;
Name=MELK; Synonyms=KIAA0175;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
Katagiri T., Lin M.;
"Identification of MELK whose expression was highly up-regulated in
breast cancers.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5; 7 AND 8).
TISSUE=Spleen, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[7]
INTERACTION WITH ZNF622, AND FUNCTION IN PHOSPHORYLATION OF ZNF622.
TISSUE=Keratinocyte;
PubMed=11802789; DOI=10.1042/0264-6021:3610597;
Seong H.-A., Gil M., Kim K.-T., Kim S.-J., Ha H.;
"Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine
protein serine/threonine kinase 38 (MPK38).";
Biochem. J. 361:597-604(2002).
[8]
FUNCTION IN PHOSPHORYLATION OF CDC25B.
PubMed=12400006; DOI=10.1038/sj.onc.1205870;
Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.;
"Human pEg3 kinase associates with and phosphorylates CDC25B
phosphatase: a potential role for pEg3 in cell cycle regulation.";
Oncogene 21:7630-7641(2002).
[9]
INTERACTION WITH PPP1R8, AUTOPHOSPHORYLATION, MUTAGENESIS OF ASP-150;
THR-345; THR-387; THR-409; THR-415; THR-428; THR-446; THR-460;
THR-466; THR-478 AND THR-518, PHOSPHORYLATION AT THR-478, AND
FUNCTION.
PubMed=14699119; DOI=10.1074/jbc.M311466200;
Vulsteke V., Beullens M., Boudrez A., Keppens S., Van Eynde A.,
Rider M.H., Stalmans W., Bollen M.;
"Inhibition of spliceosome assembly by the cell cycle-regulated
protein kinase MELK and involvement of splicing factor NIPP1.";
J. Biol. Chem. 279:8642-8647(2004).
[10]
PHOSPHORYLATION AT THR-167, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
THR-167.
PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,
Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,
Alessi D.R.;
"LKB1 is a master kinase that activates 13 kinases of the AMPK
subfamily, including MARK/PAR-1.";
EMBO J. 23:833-843(2004).
[11]
INVOLVEMENT IN CANCER.
PubMed=16266996; DOI=10.1158/0008-5472.CAN-04-4531;
Gray D., Jubb A.M., Hogue D., Dowd P., Kljavin N., Yi S., Bai W.,
Frantz G., Zhang Z., Koeppen H., de Sauvage F.J., Davis D.P.;
"Maternal embryonic leucine zipper kinase/murine protein serine-
threonine kinase 38 is a promising therapeutic target for multiple
cancers.";
Cancer Res. 65:9751-9761(2005).
[12]
FUNCTION IN PHOSPHORYLATION OF CDC25B.
PubMed=15908796; DOI=10.4161/cc.4.6.1716;
Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P.,
Monsarrat B., Tassan J.P., Ducommun B.;
"CDC25B phosphorylated by pEg3 localizes to the centrosome and the
spindle poles at mitosis.";
Cell Cycle 4:806-811(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION AT THR-167; SER-343; SER-356; TYR-367; THR-398;
THR-409; SER-431; THR-494; SER-505 AND SER-529.
PubMed=16628004; DOI=10.4161/cc.5.8.2683;
Badouel C., Korner R., Frank-Vaillant M., Couturier A., Nigg E.A.,
Tassan J.P.;
"M-phase MELK activity is regulated by MPF and MAPK.";
Cell Cycle 5:883-889(2006).
[15]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION,
CALCIUM-BINDING, PHOSPHORYLATION AT THR-56; TYR-163; THR-167; SER-171;
SER-253; SER-336; SER-343; SER-356; SER-391; THR-398; SER-407;
SER-431; THR-494; SER-505; SER-529 AND THR-539, AND MUTAGENESIS OF
CYS-29; CYS-70; CYS-89; ASP-150; CYS-154; TYR-163; CYS-168; CYS-169;
SER-171; CYS-204; 283-ASP--ASP-285; CYS-286 AND CYS-339.
PubMed=16216881; DOI=10.1074/jbc.M507274200;
Beullens M., Vancauwenbergh S., Morrice N., Derua R., Ceulemans H.,
Waelkens E., Bollen M.;
"Substrate specificity and activity regulation of protein kinase
MELK.";
J. Biol. Chem. 280:40003-40011(2005).
[16]
SUBCELLULAR LOCATION.
PubMed=16159311; DOI=10.1042/BC20050041;
Chartrain I., Couturier A., Tassan J.P.;
"Cell-cycle-dependent cortical localization of pEg3 protein kinase in
Xenopus and human cells.";
Biol. Cell 98:253-263(2006).
[17]
FUNCTION IN PHOSPHORYLATION OF BCL2L14, AND MUTAGENESIS OF ASP-150.
PubMed=17280616; DOI=10.1186/bcr1650;
Lin M.L., Park J.H., Nishidate T., Nakamura Y., Katagiri T.;
"Involvement of maternal embryonic leucine zipper kinase (MELK) in
mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic
member of the Bcl-2 family.";
Breast Cancer Res. 9:R17-R17(2007).
[18]
INVOLVEMENT IN CANCER.
PubMed=17960622; DOI=10.1002/ijc.23189;
Marie S.K., Okamoto O.K., Uno M., Hasegawa A.P., Oba-Shinjo S.M.,
Cohen T., Camargo A.A., Kosoy A., Carlotti C.G. Jr., Toledo S.,
Moreira-Filho C.A., Zago M.A., Simpson A.J., Caballero O.L.;
"Maternal embryonic leucine zipper kinase transcript abundance
correlates with malignancy grade in human astrocytomas.";
Int. J. Cancer 122:807-815(2008).
[19]
INVOLVEMENT IN CANCER.
PubMed=17722061; DOI=10.1002/jnr.21471;
Nakano I., Masterman-Smith M., Saigusa K., Paucar A.A., Horvath S.,
Shoemaker L., Watanabe M., Negro A., Bajpai R., Howes A., Lelievre V.,
Waschek J.A., Lazareff J.A., Freije W.A., Liau L.M., Gilbertson R.J.,
Cloughesy T.F., Geschwind D.H., Nelson S.F., Mischel P.S.,
Terskikh A.V., Kornblum H.I.;
"Maternal embryonic leucine zipper kinase is a key regulator of the
proliferation of malignant brain tumors, including brain tumor stem
cells.";
J. Neurosci. Res. 86:48-60(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505;
THR-518 AND SER-529, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 AND SER-505, 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).
[22]
INVOLVEMENT IN CANCER.
PubMed=19671159; DOI=10.1186/bcr2350;
Pickard M.R., Green A.R., Ellis I.O., Caldas C., Hedge V.L.,
Mourtada-Maarabouni M., Williams G.T.;
"Dysregulated expression of Fau and MELK is associated with poor
prognosis in breast cancer.";
Breast Cancer Res. 11:R60-R60(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505
AND SER-529, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, 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).
[25]
INVOLVEMENT IN CANCER.
PubMed=20861186; DOI=10.1158/0008-5472.CAN-10-1295;
Hebbard L.W., Maurer J., Miller A., Lesperance J., Hassell J.,
Oshima R.G., Terskikh A.V.;
"Maternal embryonic leucine zipper kinase is upregulated and required
in mammary tumor-initiating cells in vivo.";
Cancer Res. 70:8863-8873(2010).
[26]
SUBCELLULAR LOCATION.
PubMed=21145462; DOI=10.1016/j.cell.2010.11.028;
Moravcevic K., Mendrola J.M., Schmitz K.R., Wang Y.H., Slochower D.,
Janmey P.A., Lemmon M.A.;
"Kinase associated-1 domains drive MARK/PAR1 kinases to membrane
targets by binding acidic phospholipids.";
Cell 143:966-977(2010).
[27]
DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
PubMed=20420823; DOI=10.1016/j.yexcr.2010.04.019;
Badouel C., Chartrain I., Blot J., Tassan J.P.;
"Maternal embryonic leucine zipper kinase is stabilized in mitosis by
phosphorylation and is partially degraded upon mitotic exit.";
Exp. Cell Res. 316:2166-2173(2010).
[28]
INDUCTION.
PubMed=21806965; DOI=10.1016/j.bbrc.2011.07.060;
Choi S., Ku J.L.;
"Resistance of colorectal cancer cells to radiation and 5-FU is
associated with MELK expression.";
Biochem. Biophys. Res. Commun. 412:207-213(2011).
[29]
INDUCTION.
PubMed=21558073; DOI=10.1093/neuonc/nor023;
Nakano I., Joshi K., Visnyei K., Hu B., Watanabe M., Lam D.,
Wexler E., Saigusa K., Nakamura Y., Laks D.R., Mischel P.S.,
Viapiano M., Kornblum H.I.;
"Siomycin A targets brain tumor stem cells partially through a MELK-
mediated pathway.";
Neuro-oncol. 13:622-634(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505
AND SER-529, 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).
[31]
VARIANTS [LARGE SCALE ANALYSIS] MET-56; ARG-219; LYS-333; ILE-348 AND
MET-460.
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).
-!- FUNCTION: Serine/threonine-protein kinase involved in various
processes such as cell cycle regulation, self-renewal of stem
cells, apoptosis and splicing regulation. Has a broad substrate
specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and
ZNF622. Acts as an activator of apoptosis by phosphorylating and
activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably
by mediating phosphorylation of CDC25B, promoting localization of
CDC25B to the centrosome and the spindle poles during mitosis.
Plays a key role in cell proliferation and carcinogenesis.
Required for proliferation of embryonic and postnatal multipotent
neural progenitors. Phosphorylates and inhibits BCL2L14, possibly
leading to affect mammary carcinogenesis by mediating inhibition
of the pro-apoptotic function of BCL2L14. Also involved in the
inhibition of spliceosome assembly during mitosis by
phosphorylating ZNF622, thereby contributing to its redirection to
the nucleus. May also play a role in primitive hematopoiesis.
{ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006,
ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796,
ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027, ECO:0000269|PubMed:16216881}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:16216881}.
-!- ENZYME REGULATION: Activated by autophosphorylation of the T-loop
at Thr-167 and Ser-171: in contrast to other members of the SNF1
subfamily, phosphorylation at Thr-167 is not mediated by
STK11/LKB1 but via autophosphorylation instead. Inhibited by
calcium-binding. Kinase activity is also regulated by reducing
agents: dithiothreitol (DTT) or reduced glutathione are required
for kinase activity in vitro; such dependence is however not due
to the presence of disulfide bonds. {ECO:0000269|PubMed:16216881}.
-!- SUBUNIT: Monomer. Interacts with ZNF622 and PPP1R8.
{ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:14699119}.
-!- INTERACTION:
Q9BZR8:BCL2L14; NbExp=4; IntAct=EBI-1046702, EBI-1385773;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16159311,
ECO:0000269|PubMed:21145462}; Peripheral membrane protein
{ECO:0000269|PubMed:16159311, ECO:0000269|PubMed:21145462}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=Q14680-1; Sequence=Displayed;
Name=2;
IsoId=Q14680-2; Sequence=VSP_044715;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14680-3; Sequence=VSP_045208;
Name=4;
IsoId=Q14680-4; Sequence=VSP_045209;
Name=5;
IsoId=Q14680-5; Sequence=VSP_045430;
Name=6;
IsoId=Q14680-6; Sequence=VSP_045431;
Name=7;
IsoId=Q14680-7; Sequence=VSP_046760;
Note=No experimental confirmation available.;
Name=8;
IsoId=Q14680-8; Sequence=VSP_046759;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in placenta, kidney, thymus, testis,
ovary and intestine. {ECO:0000269|PubMed:8724849}.
-!- DEVELOPMENTAL STAGE: Increases during G2/M phase compared to
interphase. Protein level decreases when cells exit mitosis,
probably due to degradation. {ECO:0000269|PubMed:20420823}.
-!- INDUCTION: Up-regulated in many cancers cells. Up-regulated upon
treatment with radiation or 5-fluorouracil (5-FU) in colorectal
cancer cells, suggesting that it might be associated with
increased resistance of colorectal cells against radiation and 5-
FU. Down-regulated upon siomycin A, a thiazole antibiotic,
treatment, leading to inhibit tumor growth in vivo.
{ECO:0000269|PubMed:21558073, ECO:0000269|PubMed:21806965}.
-!- DOMAIN: The KA1 domain mediates binding to phospholipids and
targeting to membranes. {ECO:0000250}.
-!- PTM: Autophosphorylated: autophosphorylation of the T-loop at Thr-
167 and Ser-171 is required for activation. Thr-478
phosphorylation during mitosis promotes interaction with PPP1R8
(Probable). {ECO:0000305|PubMed:14699119,
ECO:0000305|PubMed:14976552, ECO:0000305|PubMed:16216881,
ECO:0000305|PubMed:16628004, ECO:0000305|PubMed:20420823}.
-!- DISEASE: Note=Defects in MELK are associated with some cancers,
such as brain or breast cancers. Expression is dramatically
increased in aggressive undifferentiated tumors, correlating with
poor patient outcome in breast and brain cancers, suggesting a
role in tumor-initiating cells and proliferation via its function
in cell proliferation regulation.
-!- MISCELLANEOUS: Potential therapeutic target for treatment of
somatic tumors, such as brain and breast cancers, down-regulation
of MELK inhibiting tumorigenesis (PubMed:17960622,
PubMed:20861186). {ECO:0000305|PubMed:17960622,
ECO:0000305|PubMed:20861186}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA11492.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MELKID43360ch9p13.html";
-----------------------------------------------------------------------
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EMBL; AB183427; BAF73615.1; -; mRNA.
EMBL; AB183428; BAF73616.1; -; mRNA.
EMBL; D79997; BAA11492.2; ALT_INIT; mRNA.
EMBL; AK293284; BAH11482.1; -; mRNA.
EMBL; AK293447; BAH11508.1; -; mRNA.
EMBL; AK299164; BAH12961.1; -; mRNA.
EMBL; AK300761; BAH13343.1; -; mRNA.
EMBL; AK300821; BAH13354.1; -; mRNA.
EMBL; AK301131; BAH13416.1; -; mRNA.
EMBL; AK302374; BAH13687.1; -; mRNA.
EMBL; AL354932; CAI11034.2; -; Genomic_DNA.
EMBL; AL442063; CAI11034.2; JOINED; Genomic_DNA.
EMBL; AL442063; CAI16995.2; -; Genomic_DNA.
EMBL; AL354932; CAI16995.2; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58303.1; -; Genomic_DNA.
EMBL; CH471071; EAW58304.1; -; Genomic_DNA.
EMBL; BC014039; AAH14039.1; -; mRNA.
CCDS; CCDS59123.1; -. [Q14680-7]
CCDS; CCDS59124.1; -. [Q14680-8]
CCDS; CCDS59125.1; -. [Q14680-2]
CCDS; CCDS59126.1; -. [Q14680-6]
CCDS; CCDS59127.1; -. [Q14680-5]
CCDS; CCDS59128.1; -. [Q14680-4]
CCDS; CCDS6606.1; -. [Q14680-1]
RefSeq; NP_001243614.1; NM_001256685.1. [Q14680-7]
RefSeq; NP_001243616.1; NM_001256687.1. [Q14680-8]
RefSeq; NP_001243617.1; NM_001256688.1. [Q14680-2]
RefSeq; NP_001243618.1; NM_001256689.1. [Q14680-6]
RefSeq; NP_001243619.1; NM_001256690.1. [Q14680-5]
RefSeq; NP_001243621.1; NM_001256692.1. [Q14680-4]
RefSeq; NP_001243622.1; NM_001256693.1. [Q14680-3]
RefSeq; NP_055606.1; NM_014791.3. [Q14680-1]
RefSeq; XP_011516378.1; XM_011518076.2. [Q14680-1]
RefSeq; XP_011516379.1; XM_011518077.1. [Q14680-1]
RefSeq; XP_011516380.1; XM_011518078.2. [Q14680-1]
RefSeq; XP_011516381.1; XM_011518079.1. [Q14680-1]
RefSeq; XP_011516383.1; XM_011518081.2. [Q14680-6]
RefSeq; XP_011516384.1; XM_011518082.2. [Q14680-6]
RefSeq; XP_011516385.1; XM_011518083.2. [Q14680-6]
RefSeq; XP_011516386.1; XM_011518084.2. [Q14680-6]
UniGene; Hs.184339; -.
PDB; 4BKY; X-ray; 1.83 A; A=2-340.
PDB; 4BKZ; X-ray; 2.20 A; A=2-340.
PDB; 4BL1; X-ray; 2.60 A; A=2-340.
PDB; 4D2P; X-ray; 2.55 A; A/B/C/D=1-336.
PDB; 4D2T; X-ray; 2.70 A; A/B/C/D=1-336.
PDB; 4D2V; X-ray; 2.45 A; A/B/C/D=1-336.
PDB; 4D2W; X-ray; 1.92 A; A/B/C/D=1-336.
PDB; 4IXP; X-ray; 2.75 A; A=1-340.
PDB; 4UMP; X-ray; 2.30 A; A/B/C/D=1-336.
PDB; 4UMQ; X-ray; 2.60 A; A=1-336.
PDB; 4UMR; X-ray; 3.00 A; A=1-336.
PDB; 4UMT; X-ray; 1.98 A; A=1-336.
PDB; 4UMU; X-ray; 2.02 A; A=1-336.
PDB; 5IH8; X-ray; 1.85 A; A=3-330.
PDB; 5IH9; X-ray; 1.79 A; A=3-330.
PDB; 5IHA; X-ray; 1.96 A; A=3-330.
PDB; 5IHC; X-ray; 2.14 A; A=3-330.
PDB; 5K00; X-ray; 1.77 A; A=3-330.
PDB; 5M5A; X-ray; 1.90 A; A=2-340.
PDB; 5MAF; X-ray; 2.80 A; A=2-340.
PDB; 5MAG; X-ray; 2.35 A; A=2-340.
PDB; 5MAH; X-ray; 2.00 A; A=2-340.
PDB; 5MAI; X-ray; 2.15 A; A=2-340.
PDB; 5TVT; X-ray; 2.28 A; A=2-333.
PDB; 5TWL; X-ray; 2.42 A; A=2-340.
PDB; 5TWU; X-ray; 2.60 A; A/B=1-340.
PDB; 5TWY; X-ray; 2.91 A; A/B=2-340.
PDB; 5TWZ; X-ray; 2.63 A; A=2-340.
PDB; 5TX3; X-ray; 2.90 A; A/B=1-340.
PDBsum; 4BKY; -.
PDBsum; 4BKZ; -.
PDBsum; 4BL1; -.
PDBsum; 4D2P; -.
PDBsum; 4D2T; -.
PDBsum; 4D2V; -.
PDBsum; 4D2W; -.
PDBsum; 4IXP; -.
PDBsum; 4UMP; -.
PDBsum; 4UMQ; -.
PDBsum; 4UMR; -.
PDBsum; 4UMT; -.
PDBsum; 4UMU; -.
PDBsum; 5IH8; -.
PDBsum; 5IH9; -.
PDBsum; 5IHA; -.
PDBsum; 5IHC; -.
PDBsum; 5K00; -.
PDBsum; 5M5A; -.
PDBsum; 5MAF; -.
PDBsum; 5MAG; -.
PDBsum; 5MAH; -.
PDBsum; 5MAI; -.
PDBsum; 5TVT; -.
PDBsum; 5TWL; -.
PDBsum; 5TWU; -.
PDBsum; 5TWY; -.
PDBsum; 5TWZ; -.
PDBsum; 5TX3; -.
ProteinModelPortal; Q14680; -.
SMR; Q14680; -.
BioGrid; 115171; 59.
IntAct; Q14680; 39.
MINT; Q14680; -.
STRING; 9606.ENSP00000298048; -.
BindingDB; Q14680; -.
ChEMBL; CHEMBL4578; -.
GuidetoPHARMACOLOGY; 2102; -.
iPTMnet; Q14680; -.
PhosphoSitePlus; Q14680; -.
BioMuta; MELK; -.
DMDM; 50400857; -.
EPD; Q14680; -.
MaxQB; Q14680; -.
PaxDb; Q14680; -.
PeptideAtlas; Q14680; -.
PRIDE; Q14680; -.
DNASU; 9833; -.
Ensembl; ENST00000298048; ENSP00000298048; ENSG00000165304. [Q14680-1]
Ensembl; ENST00000536329; ENSP00000443550; ENSG00000165304. [Q14680-5]
Ensembl; ENST00000536860; ENSP00000439792; ENSG00000165304. [Q14680-8]
Ensembl; ENST00000536987; ENSP00000439184; ENSG00000165304. [Q14680-4]
Ensembl; ENST00000541717; ENSP00000437804; ENSG00000165304. [Q14680-7]
Ensembl; ENST00000543751; ENSP00000441596; ENSG00000165304. [Q14680-6]
Ensembl; ENST00000545008; ENSP00000445452; ENSG00000165304. [Q14680-2]
GeneID; 9833; -.
KEGG; hsa:9833; -.
UCSC; uc003zzn.5; human. [Q14680-1]
CTD; 9833; -.
DisGeNET; 9833; -.
EuPathDB; HostDB:ENSG00000165304.7; -.
GeneCards; MELK; -.
HGNC; HGNC:16870; MELK.
HPA; HPA017214; -.
MIM; 607025; gene.
neXtProt; NX_Q14680; -.
OpenTargets; ENSG00000165304; -.
PharmGKB; PA134902874; -.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140868; -.
HOGENOM; HOG000233023; -.
HOVERGEN; HBG106273; -.
InParanoid; Q14680; -.
KO; K08799; -.
OMA; YELHETI; -.
OrthoDB; EOG091G05V9; -.
PhylomeDB; Q14680; -.
TreeFam; TF314032; -.
SignaLink; Q14680; -.
SIGNOR; Q14680; -.
ChiTaRS; MELK; human.
GeneWiki; MELK; -.
GenomeRNAi; 9833; -.
PRO; PR:Q14680; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165304; -.
CleanEx; HS_MELK; -.
ExpressionAtlas; Q14680; baseline and differential.
Genevisible; Q14680; HS.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
GO; GO:0061351; P:neural precursor cell proliferation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
CDD; cd14078; STKc_MELK; 1.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR001772; KA1_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034673; MELK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF02149; KA1; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50032; KA1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding; Calcium;
Cell cycle; Cell membrane; Complete proteome; Kinase; Lipid-binding;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 651 Maternal embryonic leucine zipper kinase.
/FTId=PRO_0000086323.
DOMAIN 11 263 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 602 651 KA1. {ECO:0000255|PROSITE-
ProRule:PRU00565}.
NP_BIND 17 25 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 282 321 UBA-like.
REGION 326 651 Autoinhibitory region.
ACT_SITE 132 132 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 56 56 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 163 163 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 167 167 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 171 171 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 253 253 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 336 336 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 343 343 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 356 356 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 367 367 Phosphotyrosine.
{ECO:0000269|PubMed:16628004}.
MOD_RES 391 391 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 398 398 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 407 407 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
MOD_RES 409 409 Phosphothreonine.
{ECO:0000269|PubMed:16628004}.
MOD_RES 431 431 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 478 478 Phosphothreonine.
{ECO:0000269|PubMed:14699119}.
MOD_RES 494 494 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 505 505 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 518 518 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 529 529 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:16628004}.
MOD_RES 539 539 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16216881}.
VAR_SEQ 1 194 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045208.
VAR_SEQ 1 135 MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKI
MDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKI
FMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYV
HSQGYAHRDLKP -> MVLE (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045209.
VAR_SEQ 1 87 MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKI
MDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKI
FMVLE -> MMNFSNIMNYMKLLGQ (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_045430.
VAR_SEQ 1 48 MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKI
MDKNTLG -> MMNFSNIMNYMKLLGQ (in isoform
6). {ECO:0000303|Ref.1}.
/FTId=VSP_045431.
VAR_SEQ 88 158 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044715.
VAR_SEQ 88 135 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046759.
VAR_SEQ 352 392 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046760.
VARIANT 56 56 T -> M (in dbSNP:rs35233455).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040794.
VARIANT 219 219 K -> R (in dbSNP:rs35142210).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040795.
VARIANT 333 333 R -> K (in dbSNP:rs34655121).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040796.
VARIANT 348 348 T -> I (in dbSNP:rs55845414).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040797.
VARIANT 460 460 T -> M (in an ovarian mucinous carcinoma
sample; somatic mutation;
dbSNP:rs144052967).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040798.
MUTAGEN 29 29 C->V: Abolishes dependence to reducing
agents; when associated with V-70; A-89;
A-154; A-168; A-169; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 70 70 C->V: Abolishes dependence to reducing
agents; when associated with V-29; A-89;
A-154; A-168; A-169; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 89 89 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-154; A-168; A-169; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 150 150 D->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:14699119,
ECO:0000269|PubMed:16216881,
ECO:0000269|PubMed:17280616}.
MUTAGEN 154 154 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-168; A-169; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 163 163 Y->F: Abolishes autophosphorylation on
tyrosine but still active on exogenous
substrates.
{ECO:0000269|PubMed:16216881}.
MUTAGEN 167 167 T->A: Abolishes activation of
serine/threonine-protein kinase activity
and has only weak activity.
{ECO:0000269|PubMed:14976552}.
MUTAGEN 167 167 T->D,E: Phosphomimetic mutant that has
similar kinase activity as wild-type.
{ECO:0000269|PubMed:14976552}.
MUTAGEN 168 168 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-154; A-169; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 169 169 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-154; A-168; A-204; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 171 171 S->A: Abolishes activation of
serine/threonine-protein kinase activity
and has only weak activity.
{ECO:0000269|PubMed:16216881}.
MUTAGEN 171 171 S->D: Inactive.
{ECO:0000269|PubMed:16216881}.
MUTAGEN 204 204 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-154; A-168; A-169; A-286 and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 283 285 DDD->KKK: Inactive.
{ECO:0000269|PubMed:16216881}.
MUTAGEN 286 286 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-154; A-168; A-169; A-204; and A-
339. {ECO:0000269|PubMed:16216881}.
MUTAGEN 339 339 C->A: Abolishes dependence to reducing
agents; when associated with V-29; V-70;
A-89; A-154; A-168; A-169; A-204 and A-
286. {ECO:0000269|PubMed:16216881}.
MUTAGEN 345 345 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
MUTAGEN 387 387 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
MUTAGEN 409 409 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
MUTAGEN 415 415 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
MUTAGEN 428 428 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
MUTAGEN 446 446 T->A: Inhibits interaction with PPP1R8.
{ECO:0000269|PubMed:14699119}.
MUTAGEN 460 460 T->A: Inhibits interaction with PPP1R8.
{ECO:0000269|PubMed:14699119}.
MUTAGEN 466 466 T->A: Inhibits interaction with PPP1R8.
{ECO:0000269|PubMed:14699119}.
MUTAGEN 478 478 T->A: Strongly inhibits interaction with
PPP1R8. Enhances enzymatic activity.
{ECO:0000269|PubMed:14699119}.
MUTAGEN 518 518 T->A: No effect on interaction with
PPP1R8. {ECO:0000269|PubMed:14699119}.
CONFLICT 69 69 I -> M (in Ref. 3; BAH12961).
{ECO:0000305}.
CONFLICT 398 398 T -> A (in Ref. 3; BAH12961).
{ECO:0000305}.
CONFLICT 428 428 T -> A (in Ref. 3; BAH11482).
{ECO:0000305}.
CONFLICT 474 474 C -> R (in Ref. 3; BAH13343).
{ECO:0000305}.
CONFLICT 483 483 P -> L (in Ref. 3; BAH13354).
{ECO:0000305}.
TURN 4 6 {ECO:0000244|PDB:4BKY}.
HELIX 7 9 {ECO:0000244|PDB:5K00}.
STRAND 11 19 {ECO:0000244|PDB:5K00}.
STRAND 20 22 {ECO:0000244|PDB:4D2T}.
STRAND 24 30 {ECO:0000244|PDB:5K00}.
TURN 31 33 {ECO:0000244|PDB:5K00}.
STRAND 36 43 {ECO:0000244|PDB:5K00}.
HELIX 44 47 {ECO:0000244|PDB:5K00}.
HELIX 48 50 {ECO:0000244|PDB:5K00}.
HELIX 51 62 {ECO:0000244|PDB:5K00}.
STRAND 72 77 {ECO:0000244|PDB:5K00}.
STRAND 79 87 {ECO:0000244|PDB:5K00}.
HELIX 94 101 {ECO:0000244|PDB:5K00}.
HELIX 106 125 {ECO:0000244|PDB:5K00}.
HELIX 135 137 {ECO:0000244|PDB:5K00}.
STRAND 138 140 {ECO:0000244|PDB:5K00}.
STRAND 146 148 {ECO:0000244|PDB:5K00}.
STRAND 157 159 {ECO:0000244|PDB:4UMP}.
STRAND 163 166 {ECO:0000244|PDB:4IXP}.
HELIX 172 174 {ECO:0000244|PDB:5K00}.
HELIX 177 181 {ECO:0000244|PDB:5K00}.
HELIX 187 204 {ECO:0000244|PDB:5K00}.
HELIX 214 223 {ECO:0000244|PDB:5K00}.
HELIX 234 243 {ECO:0000244|PDB:5K00}.
HELIX 248 250 {ECO:0000244|PDB:5K00}.
HELIX 254 258 {ECO:0000244|PDB:5K00}.
HELIX 261 264 {ECO:0000244|PDB:5K00}.
TURN 265 267 {ECO:0000244|PDB:5K00}.
STRAND 279 281 {ECO:0000244|PDB:4BKZ}.
HELIX 284 291 {ECO:0000244|PDB:5K00}.
STRAND 294 296 {ECO:0000244|PDB:5K00}.
HELIX 298 306 {ECO:0000244|PDB:5K00}.
HELIX 312 326 {ECO:0000244|PDB:5K00}.
SEQUENCE 651 AA; 74642 MW; 57F05CDC6122E570 CRC64;
MKDYDELLKY YELHETIGTG GFAKVKLACH ILTGEMVAIK IMDKNTLGSD LPRIKTEIEA
LKNLRHQHIC QLYHVLETAN KIFMVLEYCP GGELFDYIIS QDRLSEEETR VVFRQIVSAV
AYVHSQGYAH RDLKPENLLF DEYHKLKLID FGLCAKPKGN KDYHLQTCCG SLAYAAPELI
QGKSYLGSEA DVWSMGILLY VLMCGFLPFD DDNVMALYKK IMRGKYDVPK WLSPSSILLL
QQMLQVDPKK RISMKNLLNH PWIMQDYNYP VEWQSKNPFI HLDDDCVTEL SVHHRNNRQT
MEDLISLWQY DHLTATYLLL LAKKARGKPV RLRLSSFSCG QASATPFTDI KSNNWSLEDV
TASDKNYVAG LIDYDWCEDD LSTGAATPRT SQFTKYWTES NGVESKSLTP ALCRTPANKL
KNKENVYTPK SAVKNEEYFM FPEPKTPVNK NQHKREILTT PNRYTTPSKA RNQCLKETPI
KIPVNSTGTD KLMTGVISPE RRCRSVELDL NQAHMEETPK RKGAKVFGSL ERGLDKVITV
LTRSKRKGSA RDGPRRLKLH YNVTTTRLVN PDQLLNEIMS ILPKKHVDFV QKGYTLKCQT
QSDFGKVTMQ FELEVCQLQK PDVVGIRRQR LKGDAWVYKR LVEDILSSCK V


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