Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Maternal embryonic leucine zipper kinase (EC 2.7.11.1) (Protein kinase PK38) (mPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2)

 MELK_MOUSE              Reviewed;         643 AA.
Q61846; Q3TPU1; Q61804; Q6ZQH6;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 161.
RecName: Full=Maternal embryonic leucine zipper kinase;
EC=2.7.11.1;
AltName: Full=Protein kinase PK38;
Short=mPK38;
AltName: Full=Tyrosine-protein kinase MELK;
EC=2.7.10.2;
Name=Melk; Synonyms=Kiaa0175, Pk38;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Keratinocyte;
PubMed=9305775; DOI=10.1016/S0378-1119(97)00181-9;
Gil M., Yang Y., Lee Y., Choi I., Ha H.;
"Cloning and expression of a cDNA encoding a novel protein
serine/threonine kinase predominantly expressed in hematopoietic
cells.";
Gene 195:295-301(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=C57BL/6 X DBA/2;
PubMed=9136115;
DOI=10.1002/(SICI)1098-2795(199706)47:2<148::AID-MRD4>3.0.CO;2-M;
Heyer B.S., Warsowe J., Solter D., Knowles B.B., Ackerman S.L.;
"New member of the Snf1/AMPK kinase family, Melk, is expressed in the
mouse egg and preimplantation embryo.";
Mol. Reprod. Dev. 47:148-156(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16061694; DOI=10.1083/jcb.200412115;
Nakano I., Paucar A.A., Bajpai R., Dougherty J.D., Zewail A.,
Kelly T.K., Kim K.J., Ou J., Groszer M., Imura T., Freije W.A.,
Nelson S.F., Sofroniew M.V., Wu H., Liu X., Terskikh A.V.,
Geschwind D.H., Kornblum H.I.;
"Maternal embryonic leucine zipper kinase (MELK) regulates multipotent
neural progenitor proliferation.";
J. Cell Biol. 170:413-427(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
FUNCTION IN PHOSPHORYLATION OF MAP3K5, AND MUTAGENESIS OF LYS-40.
PubMed=18948261; DOI=10.1074/jbc.M807219200;
Jung H., Seong H.A., Ha H.;
"Murine protein serine/threonine kinase 38 activates apoptosis signal-
regulating kinase 1 via Thr 838 phosphorylation.";
J. Biol. Chem. 283:34541-34553(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. Required for proliferation
of embryonic and postnatal multipotent neural progenitors.
Phosphorylates and inhibits 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:16061694, ECO:0000269|PubMed:18948261}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
-!- 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=2.7.11.1;
-!- 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=2.7.11.1;
-!- ACTIVITY 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Interacts with ZNF622 and PPP1R8 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in testis, ovary, thymus, spleen and
T-cell. Expressed by neural progenitors: highly enriched in
cultures containing multipotent progenitors.
{ECO:0000269|PubMed:16061694, ECO:0000269|PubMed:9136115,
ECO:0000269|PubMed:9305775}.
-!- DEVELOPMENTAL STAGE: Expressed in the 2-cell-stage embryo,
followed by a strong expression at 8-cell-stage.
{ECO:0000269|PubMed:9136115}.
-!- 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L76158; AAB72030.1; -; mRNA.
EMBL; X95351; CAA64641.1; -; mRNA.
EMBL; AK011932; BAB27923.1; -; mRNA.
EMBL; AK145316; BAE26362.1; -; mRNA.
EMBL; AK164138; BAE37644.1; -; mRNA.
EMBL; AK129076; BAC97886.1; -; mRNA.
EMBL; AL805952; CAM14393.1; -; Genomic_DNA.
EMBL; AL807399; CAM14393.1; JOINED; Genomic_DNA.
EMBL; AL807399; CAM22652.1; -; Genomic_DNA.
EMBL; AL805952; CAM22652.1; JOINED; Genomic_DNA.
CCDS; CCDS18124.1; -.
RefSeq; NP_034920.2; NM_010790.2.
UniGene; Mm.268668; -.
PDB; 4BFM; X-ray; 2.35 A; A=1-326.
PDB; 4CQG; X-ray; 2.57 A; A=1-326.
PDBsum; 4BFM; -.
PDBsum; 4CQG; -.
ProteinModelPortal; Q61846; -.
SMR; Q61846; -.
BioGrid; 201390; 9.
STRING; 10090.ENSMUSP00000043806; -.
iPTMnet; Q61846; -.
PhosphoSitePlus; Q61846; -.
EPD; Q61846; -.
MaxQB; Q61846; -.
PaxDb; Q61846; -.
PRIDE; Q61846; -.
Ensembl; ENSMUST00000045607; ENSMUSP00000043806; ENSMUSG00000035683.
GeneID; 17279; -.
KEGG; mmu:17279; -.
UCSC; uc008srv.1; mouse.
CTD; 9833; -.
MGI; MGI:106924; Melk.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000154889; -.
HOGENOM; HOG000233023; -.
HOVERGEN; HBG106273; -.
InParanoid; Q61846; -.
KO; K08799; -.
OrthoDB; EOG091G05V9; -.
TreeFam; TF314032; -.
BRENDA; 2.7.11.1; 3474.
PRO; PR:Q61846; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000035683; Expressed in 260 organ(s), highest expression level in primary oocyte.
CleanEx; MM_MELK; -.
ExpressionAtlas; Q61846; baseline and differential.
Genevisible; Q61846; MM.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; ISS: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; IDA:MGI.
GO; GO:0061351; P:neural precursor cell proliferation; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; Apoptosis; ATP-binding; Calcium; Cell cycle;
Cell membrane; Complete proteome; Kinase; Lipid-binding; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 643 Maternal embryonic leucine zipper kinase.
/FTId=PRO_0000086324.
DOMAIN 11 263 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 594 643 KA1. {ECO:0000255|PROSITE-
ProRule:PRU00565}.
NP_BIND 17 25 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 282 321 UBA-like. {ECO:0000250}.
REGION 326 643 Autoinhibitory region. {ECO:0000250}.
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:0000250|UniProtKB:Q14680}.
MOD_RES 163 163 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 167 167 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 171 171 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 253 253 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 336 336 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 343 343 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 399 399 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 423 423 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 486 486 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 497 497 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 510 510 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14680}.
MOD_RES 521 521 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319}.
MOD_RES 531 531 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q14680}.
MUTAGEN 40 40 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:18948261}.
CONFLICT 335 335 L -> P (in Ref. 2; CAA64641 and 4;
BAC97886). {ECO:0000305}.
HELIX 3 7 {ECO:0000244|PDB:4BFM}.
TURN 8 10 {ECO:0000244|PDB:4BFM}.
STRAND 11 19 {ECO:0000244|PDB:4BFM}.
STRAND 21 30 {ECO:0000244|PDB:4BFM}.
TURN 31 33 {ECO:0000244|PDB:4BFM}.
STRAND 36 43 {ECO:0000244|PDB:4BFM}.
HELIX 44 47 {ECO:0000244|PDB:4BFM}.
HELIX 48 51 {ECO:0000244|PDB:4BFM}.
HELIX 52 62 {ECO:0000244|PDB:4BFM}.
STRAND 72 77 {ECO:0000244|PDB:4BFM}.
STRAND 79 87 {ECO:0000244|PDB:4BFM}.
HELIX 94 101 {ECO:0000244|PDB:4BFM}.
HELIX 106 125 {ECO:0000244|PDB:4BFM}.
HELIX 135 137 {ECO:0000244|PDB:4BFM}.
STRAND 138 140 {ECO:0000244|PDB:4BFM}.
STRAND 146 148 {ECO:0000244|PDB:4BFM}.
HELIX 172 174 {ECO:0000244|PDB:4BFM}.
HELIX 177 179 {ECO:0000244|PDB:4BFM}.
HELIX 188 204 {ECO:0000244|PDB:4BFM}.
HELIX 214 223 {ECO:0000244|PDB:4BFM}.
HELIX 234 243 {ECO:0000244|PDB:4BFM}.
TURN 248 250 {ECO:0000244|PDB:4BFM}.
HELIX 254 258 {ECO:0000244|PDB:4BFM}.
HELIX 261 264 {ECO:0000244|PDB:4BFM}.
HELIX 284 294 {ECO:0000244|PDB:4BFM}.
HELIX 298 305 {ECO:0000244|PDB:4BFM}.
HELIX 312 326 {ECO:0000244|PDB:4BFM}.
SEQUENCE 643 AA; 72729 MW; 5637D2A4E8CFA216 CRC64;
MKDYDELLKY YELYETIGTG GFAKVKLACH VLTGEMVAIK IMDKNALGSD LPRVKTEIDA
LKSLRHQHIC QLYHVLETKN KIFMVLEYCP GGELFDYIIS QDRLSEEETR VVFRQILSAV
AYVHSQGYAH RDLKPENLLF DENHKLKLID FGLCAKPKGN KDYHLQTCCG SLAYAAPELI
QGKSYLGSEA DVWSMGILLY VLMCGFLPFD DDNVMALYKK IMRGKYEVPK WLSPSSILLL
QQMLQVDPKK RISMRNLLNH PWVMQDYSCP VEWQSKTPLT HLDEDCVTEL SVHHRSSRQT
MEDLISSWQY DHLTATYLLL LAKKARGKPA RLQLLSFSCG TASTTPKSKN LSLEDMSTSD
DNCVAGLIDY ELCEDKLLAP KTPQVTKHLA ESNHAASKSP APGVRRAVAN KLMDKENVCT
PKSSVKNEEQ FVFSEPKIPV SKNQYKREIP ASPTRFPTPA KARAQCLREA PVRTPGNSAG
ADTLTTGVIS PERRCRSMDV DLNQAHMEDT PKKKGTNVFG SLERGLDKVL TALTRNKKKG
SARDGPRKRK LHYNVTTTRL VNPDQLLSEI MAILPKKNVD FVQKGYTLKC QTQSDFGKVT
MQFELEVCQL QRPDVVGIRR QRLKGDAWVY KRLVEDILSG CKM


Related products :

Catalog number Product name Quantity
DL-MELK-Hu Human Maternal Embryonic Leucine Zipper Kinase (MELK) ELISA Kit 96T
DL-MELK-Mu Mouse Maternal Embryonic Leucine Zipper Kinase (MELK) ELISA Kit 96T
DL-MELK-Ra Rat Maternal Embryonic Leucine Zipper Kinase (MELK) ELISA Kit 96T
Z02232 Maternal Embryonic Leucine Zipper Kinase(MELK, active) 20ug
MEMO1 MELK Gene maternal embryonic leucine zipper kinase
CSB-EL013692MO Mouse Maternal embryonic leucine zipper kinase(MELK) ELISA kit 96T
CSB-EL013692HU Human Maternal embryonic leucine zipper kinase(MELK) ELISA kit 96T
CSB-EL013692MO Mouse Maternal embryonic leucine zipper kinase(MELK) ELISA kit SpeciesMouse 96T
SEH665Ra ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Rattus norvegicus (Rat) 96T
SEH665Mu ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Mus musculus (Mouse) 96T
CSB-EL013692HU Human Maternal embryonic leucine zipper kinase(MELK) ELISA kit SpeciesHuman 96T
E97665Mu ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Organism: Mus musculus (Mouse) 96T
E97665Ra ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Organism: Rattus norvegicus (Rat) 96T
SEH665Hu ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Homo sapiens (Human) 96T
MELK_MOUSE ELISA Kit FOR Maternal embryonic leucine zipper kinase; organism: Mouse; gene name: Melk 96T
E97665Hu ELISA Kit for Maternal Embryonic Leucine Zipper Kinase (MELK) Organism: Homo sapiens (Human) 96T
CSB-EL013692MO Mouse maternal embryonic leucine zipper kinase (MELK) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL013692HU Human maternal embryonic leucine zipper kinase (MELK) ELISA kit, Species Human, Sample Type serum, plasma 96T
EH1745 Maternal embryonic leucine zipper kinase Elisa Kit 96T
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB33008 CCK4,CCK-4,Colon carcinoma kinase 4,Homo sapiens,Human,Inactive tyrosine-protein kinase 7,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
EIAAB24969 HCCS4,HCCS-4,Homo sapiens,Human,Human cervical cancer suppressor gene 4 protein,Leucine zipper- and sterile alpha motif-containing kinase,Mitogen-activated protein kinase kinase kinase MLT,Mixed linea
EIAAB13106 EK2,Embryonic kinase 2,EPHB3,EPH-like kinase 2,EPH-like tyrosine kinase 2,Ephrin type-B receptor 3,ETK2,hEK2,HEK2,Homo sapiens,Human,TYRO6,Tyrosine-protein kinase TYRO6
E1915m ELISA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur