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MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2)

 MKNK2_MOUSE             Reviewed;         459 AA.
Q8CDB0; O08606; Q75PY0; Q9D893;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 3.
18-JUL-2018, entry version 158.
RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 2;
EC=2.7.11.1;
AltName: Full=MAP kinase signal-integrating kinase 2;
Short=MAPK signal-integrating kinase 2;
Short=Mnk2;
Name=Mknk2; Synonyms=Mnk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:CAA71966.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=15254222; DOI=10.1128/MCB.24.15.6539-6549.2004;
Ueda T., Watanabe-Fukunaga R., Fukuyama H., Nagata S., Fukunaga R.;
"Mnk2 and Mnk1 are essential for constitutive and inducible
phosphorylation of eukaryotic initiation factor 4E but not for cell
growth or development.";
Mol. Cell. Biol. 24:6539-6549(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD;
TISSUE=Dendritic cell, Small intestine, and Thymus;
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).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 20-459 (ISOFORM 1), FUNCTION, AND
INTERACTION WITH MAPK3 AND MAPK1.
TISSUE=Embryo;
PubMed=9155017; DOI=10.1093/emboj/16.8.1909;
Waskiewicz A.J., Flynn A., Proud C.G., Cooper J.A.;
"Mitogen-activated protein kinases activate the serine/threonine
kinases Mnk1 and Mnk2.";
EMBO J. 16:1909-1920(1997).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-459 (ISOFORM 1).
STRAIN=NMRI; TISSUE=Mammary gland;
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).
[5]
FUNCTION AS EIF4E KINASE, PHOSPHORYLATION AT SER-74; SER-431; SER-434;
SER-446 AND THR-450, PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14,
AND INTERACTION WITH EIF4G PROTEINS.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2
is a eukaryotic initiation factor 4E kinase with high levels of basal
activity in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[6]
INTERACTION WITH MAPK3/ERK1 AND MAPK1/ERK2, AND MUTAGENESIS OF
ASP-238; LEU-438; GLN-440; SER-446 AND SER-448.
PubMed=16162500; DOI=10.1074/jbc.M508356200;
Parra J.L., Buxade M., Proud C.G.;
"Features of the catalytic domains and C termini of the MAPK signal-
integrating kinases Mnk1 and Mnk2 determine their differing activities
and regulatory properties.";
J. Biol. Chem. 280:37623-37633(2005).
[7]
FUNCTION IN SERUM-WITHDRAWAL INDUCED APOPTOSIS, AND ENZYME REGULATION.
PubMed=17903173; DOI=10.1111/j.1365-2443.2007.01122.x;
Chrestensen C.A., Eschenroeder A., Ross W.G., Ueda T.,
Watanabe-Fukunaga R., Fukunaga R., Sturgill T.W.;
"Loss of MNK function sensitizes fibroblasts to serum-withdrawal
induced apoptosis.";
Genes Cells 12:1133-1140(2007).
[8]
FUNCTION AS EIF4E KINASE.
PubMed=17689282; DOI=10.1016/j.biocel.2007.05.001;
Shenberger J.S., Zhang L., Hughlock M.K., Ueda T.,
Watanabe-Fukunaga R., Fukunaga R.;
"Roles of mitogen-activated protein kinase signal-integrating kinases
1 and 2 in oxidant-mediated eIF4E phosphorylation.";
Int. J. Biochem. Cell Biol. 39:1828-1842(2007).
[9]
FUNCTION IN MRNA TRANSLATION REGULATION DURING SPERMATOGENESIS.
PubMed=20574055; DOI=10.1095/biolreprod.110.085050;
Messina V., Di Sauro A., Pedrotti S., Adesso L., Latina A.,
Geremia R., Rossi P., Sette C.;
"Differential contribution of the MTOR and MNK pathways to the
regulation of mRNA translation in meiotic and postmeiotic mouse male
germ cells.";
Biol. Reprod. 83:607-615(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue;
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).
[11]
FUNCTION AS EIF4E KINASE, AND INTERACTION WITH EIF4G1.
PubMed=20823271; DOI=10.1128/MCB.00448-10;
Shveygert M., Kaiser C., Bradrick S.S., Gromeier M.;
"Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation
by mitogen-activated protein kinase occurs through modulation of Mnk1-
eIF4G interaction.";
Mol. Cell. Biol. 30:5160-5167(2010).
[12]
FUNCTION IN EIF4E PHOSPHORYLATION REGULATION, DEPHOSPHORYLATION BY
PP2A, AND ENZYME REGULATION.
PubMed=20927323; DOI=10.1593/neo.10704;
Li Y., Yue P., Deng X., Ueda T., Fukunaga R., Khuri F.R., Sun S.-Y.;
"Protein phosphatase 2A negatively regulates eukaryotic initiation
factor 4E phosphorylation and eIF4F assembly through direct
dephosphorylation of Mnk and eIF4E.";
Neoplasia 12:848-855(2010).
-!- FUNCTION: Serine/threonine-protein kinase that phosphorylates
SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to
environmental stress and cytokines. Appears to regulate
translation by phosphorylating EIF4E, thus increasing the affinity
of this protein for the 7-methylguanosine-containing mRNA cap.
Required for mediating PP2A-inhibition-induced EIF4E
phosphorylation. Triggers EIF4E shuttling from cytoplasm to
nucleus. Enhances the formation of EIF4F complex in pachytene
spermatocytes, thus promoting mRNA translation during
spermatogenesis. Displays a high basal kinase activity. Acts as a
mediator of the suppressive effects of IFNgamma on hematopoiesis.
Negative regulator for signals that control generation of arsenic
trioxide As(2)O(3)-dependent apoptosis and anti-leukemic
responses. Involved in anti-apoptotic signaling in response to
serum withdrawal. {ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:17689282, ECO:0000269|PubMed:17903173,
ECO:0000269|PubMed:20574055, ECO:0000269|PubMed:20823271,
ECO:0000269|PubMed:20927323, ECO:0000269|PubMed:9155017}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:9155017}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9155017};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per monomer. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by CGP57380 and staurosporine.
{ECO:0000269|PubMed:17903173, ECO:0000269|PubMed:20927323}.
-!- SUBUNIT: Interacts with ESR2 and EIF4E in the nucleus (By
similarity). Monomer. Interacts with the C-terminal regions of
EIF4G1 and EIF4G2; this interaction is promoted when MAPK pathways
are repressed but repressed upon ERK proteins activation. Also
binds to dephosphorylated MAPK3/ERK1 and MAPK1/ERK2. Interaction
with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects it from
dephosphorylation and inactivation. {ECO:0000250,
ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:16162500,
ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:9155017}.
-!- INTERACTION:
P63085:Mapk1; NbExp=23; IntAct=EBI-646209, EBI-397697;
P63086:Mapk1 (xeno); NbExp=2; IntAct=EBI-646209, EBI-397710;
Q9WUI1:Mapk11; NbExp=2; IntAct=EBI-646209, EBI-645081;
P39429:Traf2; NbExp=3; IntAct=EBI-646209, EBI-520016;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, PML body
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:9155017};
IsoId=Q8CDB0-1; Sequence=Displayed;
Name=2;
IsoId=Q8CDB0-2; Sequence=VSP_007355;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
examined, with high levels in skeletal muscle and low levels in
brain. {ECO:0000269|PubMed:9155017}.
-!- PTM: Dual phosphorylation of Thr-244 and Thr-249 activates the
kinase. Phosphorylation of Thr-379 activates the kinase.
Phosphorylated upon arsenic trioxide As(2)O(3) treatment.
Phosphorylated by MAPK1/ERK2, MAPK11 and MAPK14 (By similarity).
Dephosphorylated by PP2A. {ECO:0000250,
ECO:0000269|PubMed:11154262}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH10256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB25570.2; Type=Frameshift; Positions=439; Evidence={ECO:0000305};
Sequence=CAA71966.1; Type=Frameshift; Positions=31; Evidence={ECO:0000305};
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EMBL; AB164081; BAD18852.1; -; mRNA.
EMBL; AK008277; BAB25570.2; ALT_FRAME; mRNA.
EMBL; AK030830; BAC27151.2; -; mRNA.
EMBL; AK154235; BAE32453.1; -; mRNA.
EMBL; Y11092; CAA71966.1; ALT_FRAME; mRNA.
EMBL; BC010256; AAH10256.1; ALT_INIT; mRNA.
CCDS; CCDS24030.2; -. [Q8CDB0-1]
RefSeq; NP_067437.2; NM_021462.4. [Q8CDB0-1]
RefSeq; XP_006513379.1; XM_006513316.1. [Q8CDB0-1]
RefSeq; XP_017169313.1; XM_017313824.1.
UniGene; Mm.42126; -.
UniGene; Mm.486332; -.
ProteinModelPortal; Q8CDB0; -.
SMR; Q8CDB0; -.
BioGrid; 201432; 2.
IntAct; Q8CDB0; 6.
MINT; Q8CDB0; -.
STRING; 10090.ENSMUSP00000003433; -.
iPTMnet; Q8CDB0; -.
PhosphoSitePlus; Q8CDB0; -.
EPD; Q8CDB0; -.
PaxDb; Q8CDB0; -.
PRIDE; Q8CDB0; -.
Ensembl; ENSMUST00000200082; ENSMUSP00000143508; ENSMUSG00000020190. [Q8CDB0-1]
GeneID; 17347; -.
KEGG; mmu:17347; -.
UCSC; uc007gef.3; mouse. [Q8CDB0-1]
CTD; 2872; -.
MGI; MGI:894279; Mknk2.
eggNOG; KOG0607; Eukaryota.
eggNOG; ENOG410XQA9; LUCA.
GeneTree; ENSGT00900000140876; -.
HOGENOM; HOG000231140; -.
HOVERGEN; HBG106949; -.
InParanoid; Q8CDB0; -.
KO; K04372; -.
OMA; EAIAMNR; -.
OrthoDB; EOG091G0G1X; -.
PhylomeDB; Q8CDB0; -.
TreeFam; TF314050; -.
ChiTaRS; Mknk2; mouse.
PRO; PR:Q8CDB0; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020190; -.
CleanEx; MM_MKNK2; -.
ExpressionAtlas; Q8CDB0; baseline and differential.
Genevisible; Q8CDB0; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0071243; P:cellular response to arsenic-containing substance; ISO:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Translation regulation;
Zinc.
CHAIN 1 459 MAP kinase-interacting serine/threonine-
protein kinase 2.
/FTId=PRO_0000086337.
DOMAIN 84 368 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 90 98 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 160 162 Staurosporine binding. {ECO:0000250}.
MOTIF 60 66 Nuclear localization signal.
{ECO:0000250}.
MOTIF 438 442 MAP kinase binding.
ACT_SITE 205 205 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 299 299 Zinc. {ECO:0000250}.
METAL 311 311 Zinc. {ECO:0000250}.
METAL 314 314 Zinc. {ECO:0000250}.
BINDING 113 113 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 209 209 Staurosporine. {ECO:0000250}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11154262}.
MOD_RES 244 244 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9HBH9}.
MOD_RES 249 249 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9HBH9}.
MOD_RES 379 379 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9HBH9}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000269|PubMed:11154262}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000269|PubMed:11154262}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000269|PubMed:11154262}.
MOD_RES 450 450 Phosphothreonine.
{ECO:0000269|PubMed:11154262}.
VAR_SEQ 48 256 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007355.
MUTAGEN 238 238 D->A: Loss of activity.
{ECO:0000269|PubMed:16162500}.
MUTAGEN 438 438 L->A: Reduced phosphorylation.
{ECO:0000269|PubMed:16162500}.
MUTAGEN 440 440 Q->R: Reduced MAPK3/ERK1 and MAPK1/ERK2-
binding. {ECO:0000269|PubMed:16162500}.
MUTAGEN 446 446 S->A,D: Normal MAPK3/ERK1 and MAPK1/ERK2-
binding. {ECO:0000269|PubMed:16162500}.
MUTAGEN 448 448 S->A: Normal MAPK3/ERK1 and MAPK1/ER2K-
binding. {ECO:0000269|PubMed:16162500}.
MUTAGEN 448 448 S->D: Reduced MAPK3/ERK1 and MAPK1/ER2K-
binding. {ECO:0000269|PubMed:16162500}.
CONFLICT 256 256 Y -> D (in Ref. 2; BAB25570).
{ECO:0000305}.
CONFLICT 349 349 L -> P (in Ref. 2; BAB25570).
{ECO:0000305}.
CONFLICT 454 454 L -> I (in Ref. 2; BAB25570).
{ECO:0000305}.
SEQUENCE 459 AA; 51633 MW; 5252C711AD99729A CRC64;
MVQKRTAELQ GFHRSFKGQN PFELAFSLDL AQHRDSDFSP QCEARPDMPS SQPIDIPDAK
KRGRKKKRCR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT CVNLITNQEY AVKIIEKQLG
HIRSRVFREV EMLYQCQGHR NVLELIEFFE EEDRFYLVFE KMRGGSILSH IHRRRHFNEL
EASVVVQDVA SALDFLHNKG IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS
PISTPELLTP CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGHCG
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWSHISFA AKDLISKLLV RDAKQRLSAA
QVLQHPWVQG CAPENTLPTP LVLQRNSCAK DLTSFAAEAI AMNRQLAQCE EDAGQDQPVV
IRATSRCLQL SPPSQSKLAQ RRQRASLSAT PVVLVGDRA


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E1357r ELISA Erk1,ERK-1,ERT2,Extracellular signal-regulated kinase 1,Insulin-stimulated MAP2 kinase,MAP kinase 1,MAP kinase 3,MAP kinase isoform p44,MAPK 1,MAPK 3,Mapk3,Microtubule-associated protein 2 kinas 96T
E1357m ELISA Erk1,ERK-1,ERT2,Extracellular signal-regulated kinase 1,Insulin-stimulated MAP2 kinase,MAP kinase 1,MAP kinase 3,MAP kinase isoform p44,MAPK 1,MAPK 3,Mapk3,Microtubule-associated protein 2 kinas 96T
E1357h ELISA kit ERK1,ERK-1,ERT2,Extracellular signal-regulated kinase 1,Homo sapiens,Human,Insulin-stimulated MAP2 kinase,MAP kinase 1,MAP kinase 3,MAP kinase isoform p44,MAPK 1,MAPK 3,MAPK3,Microtubule-as 96T
U1357h CLIA ERK1,ERK-1,ERT2,Extracellular signal-regulated kinase 1,Homo sapiens,Human,Insulin-stimulated MAP2 kinase,MAP kinase 1,MAP kinase 3,MAP kinase isoform p44,MAPK 1,MAPK 3,MAPK3,Microtubule-associat 96T
E1357h ELISA ERK1,ERK-1,ERT2,Extracellular signal-regulated kinase 1,Homo sapiens,Human,Insulin-stimulated MAP2 kinase,MAP kinase 1,MAP kinase 3,MAP kinase isoform p44,MAPK 1,MAPK 3,MAPK3,Microtubule-associa 96T
E1206h ELISA kit ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-ac 96T
E1206h ELISA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activat 96T
U1206h CLIA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activate 96T
10-663-45536 ERK2_MAPK1 (p42 MAP Kinase) - Active Enzyme Human - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.001 mg
10-663-45536 ERK2_MAPK1 (p42 MAP Kinase) - Active Enzyme Human - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.005 mg
10-663-45537 ERK2_MAPK1 (p42 MAP Kinase) - Inactive Enzyme Human - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.01 mg
10-663-45537 ERK2_MAPK1 (p42 MAP Kinase) - Inactive Enzyme Human - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.003 mg
10-663-45537 ERK2_MAPK1 (p42 MAP Kinase) - Inactive Enzyme Human - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 N_A 0.02 mg


 

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