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Mitogen-activated protein kinase kinase 2 (AtMAP2Kbeta) (AtMKK2) (MAP kinase kinase 2) (EC 2.7.12.2)

 M2K2_ARATH              Reviewed;         363 AA.
Q9S7U9; O80395;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
12-SEP-2018, entry version 141.
RecName: Full=Mitogen-activated protein kinase kinase 2;
Short=AtMAP2Kbeta;
Short=AtMKK2;
Short=MAP kinase kinase 2;
EC=2.7.12.2 {ECO:0000269|PubMed:15225555};
Name=MKK2; Synonyms=MAP2K, MK1; OrderedLocusNames=At4g29810;
ORFNames=F27B13.50;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY,
INTERACTION WITH MEKK1 AND MPK4, MUTAGENESIS OF LYS-99; THR-220 AND
THR-226, AND PHOSPHORYLATION AT THR-220 AND THR-226.
STRAIN=cv. Columbia;
PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J.,
Matsumoto K., Shinozaki K.;
"Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting
proteins and analysis of a MAP kinase cascade in Arabidopsis.";
Biochem. Biophys. Res. Commun. 253:532-543(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia; TISSUE=Root;
Hamal A., Jouannic S., Leprince A.-S., Kreis M., Henry Y.;
"Molecular characterization and expression of an Arabidopsis thaliana
L. MAP kinase kinase cDNA AtMAP2Kalpha.";
Plant Sci. 140:41-52(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Sherman A., Fink G.R.;
"AMK1, a MAP kinase kinase from Arabidopsis thaliana is a functional
homolog of PBS2, the MAPKK of the osmolarity pathway in yeast
Saccharomyces cerevisiae.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
PHOSPHORYLATION AT THR-220 AND THR-226, AND MUTAGENESIS OF THR-220 AND
THR-226.
PubMed=11875555; DOI=10.1038/415977a;
Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L.,
Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J.;
"MAP kinase signalling cascade in Arabidopsis innate immunity.";
Nature 415:977-983(2002).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12119167; DOI=10.1016/S1360-1385(02)02302-6;
MAPK group;
"Mitogen-activated protein kinase cascades in plants: a new
nomenclature.";
Trends Plant Sci. 7:301-308(2002).
[9]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
MPK4 AND MPK6, PHOSPHORYLATION AT THR-220 AND THR-226, AND MUTAGENESIS
OF THR-220 AND THR-226.
PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
Dangl J.L., Hirt H.;
"The MKK2 pathway mediates cold and salt stress signaling in
Arabidopsis.";
Mol. Cell 15:141-152(2004).
[10]
GENE FAMILY.
PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M.,
Ehlting J., Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G.,
Mundy J., Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S.,
Seguin A., Ellis B.E.;
"Ancient signals: comparative genomics of plant MAPK and MAPKK gene
families.";
Trends Plant Sci. 11:192-198(2006).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17506336; DOI=10.1094/MPMI-20-5-0589;
Brader G., Djamei A., Teige M., Palva E.T., Hirt H.;
"The MAP kinase kinase MKK2 affects disease resistance in
Arabidopsis.";
Mol. Plant Microbe Interact. 20:589-596(2007).
[12]
FUNCTION, INTERACTION WITH MEKK1 AND MPK4, AND DISRUPTION PHENOTYPE.
PubMed=18982020; DOI=10.1038/cr.2008.300;
Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
"MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated
protein kinase cascade to regulate innate immunity in plants.";
Cell Res. 18:1190-1198(2008).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18599650; DOI=10.1104/pp.108.120006;
Qiu J.L., Zhou L., Yun B.W., Nielsen H.B., Fiil B.K., Petersen K.,
Mackinlay J., Loake G.J., Mundy J., Morris P.C.;
"Arabidopsis mitogen-activated protein kinase kinases MKK1 and MKK2
have overlapping functions in defense signaling mediated by MEKK1,
MPK4, and MKS1.";
Plant Physiol. 148:212-222(2008).
[14]
INTERACTION WITH MPK4; MPK6; MPK10 AND MPK11.
PubMed=19513235; DOI=10.4161/psb.3.12.6848;
Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
"Comprehensive analysis of protein-protein interactions between
Arabidopsis MAPKs and MAPK kinases helps define potential MAPK
signalling modules.";
Plant Signal. Behav. 3:1037-1041(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[16]
ACTIVITY REGULATION, AND PHOSPHORYLATION.
STRAIN=cv. Columbia;
PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
Furuya T., Matsuoka D., Nanmori T.;
"Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as
a part of the cold stress response.";
J. Plant Res. 126:833-840(2013).
[17]
INTERACTION WITH MAPKKK5, PHOSPHORYLATION BY MAPKKK5, AND MUTAGENESIS
OF LYS-99; THR-220 AND THR-226.
STRAIN=cv. Columbia;
PubMed=27679653; DOI=10.15252/embj.201694248;
Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A.,
Ishikawa K., Fujiwara M., Narusaka M., Narusaka Y., Ichimura K.,
Kobayashi Y., Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y.,
Fukamizo T., Tsuda K., Shirasu K., Shibuya N., Kawasaki T.;
"The Arabidopsis CERK1-associated kinase PBL27 connects chitin
perception to MAPK activation.";
EMBO J. 35:2468-2483(2016).
-!- FUNCTION: MEKK1, MKK1/MKK2 and MPK4 function in a signaling
pathway that modulates the expression of genes responding to
biotic and abiotic stresses and also plays an important role in
pathogen defense by negatively regulating innate immunity. Plays a
role in abiotic stress tolerance and plant disease resistance
through activation of MPK4 and MPK6 by phosphorylation. Acts
redundantly with MKK1. {ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:17506336, ECO:0000269|PubMed:18599650,
ECO:0000269|PubMed:18982020}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15225555}.
-!- ACTIVITY REGULATION: Activated in response to cold and salt
stresses through serine and threonine phosphorylation by MEKK1.
{ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:23857079}.
-!- SUBUNIT: Interacts with MEKK1, MPK4 and MPK6. May form a ternary
complex composed of MEKK1 and MKK1/MKK2 and MPK4. Interacts with
MPK10 and MPK11. Interacts with MAPKKK5 mainly in the cytosol
(PubMed:27679653). {ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:19513235,
ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:9878570}.
-!- INTERACTION:
Q9M1Z5:MPK10; NbExp=2; IntAct=EBI-994350, EBI-2358527;
Q9LMM5:MPK11; NbExp=2; IntAct=EBI-994350, EBI-2358699;
Q9LQQ9:MPK13; NbExp=2; IntAct=EBI-994350, EBI-2358762;
Q39024:MPK4; NbExp=5; IntAct=EBI-994350, EBI-994375;
Q39026:MPK6; NbExp=5; IntAct=EBI-994350, EBI-349548;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9S7U9-1; Sequence=Displayed;
Name=2;
IsoId=Q9S7U9-2; Sequence=VSP_019784;
Note=May be due to intron retention. No experimental
confirmation available.;
-!- PTM: Phosphorylation at Thr-220 and Thr-226 by MAP kinase kinase
kinases positively regulates kinase activity. Phosphorylated by
MEKK1 in response to cold (PubMed:23857079). Phosphorylated by
MAPKKK5 (PubMed:27679653). {ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:23857079,
ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:9878570}.
-!- DISRUPTION PHENOTYPE: No obvious developmental defects under
normal growth conditions. Simultaneous knockdown of MKK1 and MKK2
results in dwarf and small plants exhibiting a seedling-lethality
phenotype. {ECO:0000269|PubMed:17506336,
ECO:0000269|PubMed:18599650, ECO:0000269|PubMed:18982020}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; AB015313; BAA28828.1; -; mRNA.
EMBL; AJ006871; CAA07281.1; -; mRNA.
EMBL; AF067792; AAC72754.1; -; mRNA.
EMBL; AL050352; CAB43656.1; -; Genomic_DNA.
EMBL; AL161575; CAB79739.1; -; Genomic_DNA.
EMBL; CP002687; AEE85679.1; -; Genomic_DNA.
EMBL; CP002687; AEE85680.1; -; Genomic_DNA.
EMBL; AF385688; AAK60281.1; -; mRNA.
EMBL; AY078009; AAL77710.1; -; mRNA.
PIR; T08542; T08542.
PIR; T51735; T51735.
RefSeq; NP_001031751.1; NM_001036674.2. [Q9S7U9-2]
RefSeq; NP_194710.1; NM_119127.4. [Q9S7U9-1]
UniGene; At.1001; -.
UniGene; At.24272; -.
ProteinModelPortal; Q9S7U9; -.
SMR; Q9S7U9; -.
BioGrid; 14390; 7.
IntAct; Q9S7U9; 8.
STRING; 3702.AT4G29810.2; -.
iPTMnet; Q9S7U9; -.
PaxDb; Q9S7U9; -.
PRIDE; Q9S7U9; -.
EnsemblPlants; AT4G29810.1; AT4G29810.1; AT4G29810. [Q9S7U9-1]
EnsemblPlants; AT4G29810.2; AT4G29810.2; AT4G29810. [Q9S7U9-2]
GeneID; 829103; -.
Gramene; AT4G29810.1; AT4G29810.1; AT4G29810. [Q9S7U9-1]
Gramene; AT4G29810.2; AT4G29810.2; AT4G29810. [Q9S7U9-2]
KEGG; ath:AT4G29810; -.
Araport; AT4G29810; -.
TAIR; locus:2123909; AT4G29810.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
HOGENOM; HOG000234206; -.
InParanoid; Q9S7U9; -.
KO; K20603; -.
OMA; WGTPFEQ; -.
PhylomeDB; Q9S7U9; -.
Reactome; R-ATH-110056; MAPK3 (ERK1) activation.
Reactome; R-ATH-2559580; Oxidative Stress Induced Senescence.
Reactome; R-ATH-2871796; FCERI mediated MAPK activation.
Reactome; R-ATH-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-ATH-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
PRO; PR:Q9S7U9; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9S7U9; baseline and differential.
Genevisible; Q9S7U9; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0060918; P:auxin transport; IMP:TAIR.
GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
GO; GO:0009814; P:defense response, incompatible interaction; IGI:TAIR.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IDA:UniProtKB.
GO; GO:0009651; P:response to salt stress; IDA:TAIR.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
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; ATP-binding; Complete proteome; Immunity;
Innate immunity; Kinase; Nucleotide-binding; Phosphoprotein;
Plant defense; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase.
CHAIN 1 363 Mitogen-activated protein kinase kinase
2.
/FTId=PRO_0000245822.
DOMAIN 70 330 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 76 84 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 192 192 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 99 99 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:9878570}.
MOD_RES 226 226 Phosphothreonine.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:9878570}.
MOD_RES 230 230 Phosphothreonine.
{ECO:0000250|UniProtKB:O80397}.
VAR_SEQ 26 26 L -> LRKGFGSLCR (in isoform 2).
{ECO:0000305}.
/FTId=VSP_019784.
MUTAGEN 99 99 K->R: Loss of interaction with MEKK1.
Phosphorylated by MAPKKK5.
{ECO:0000269|PubMed:27679653,
ECO:0000269|PubMed:9878570}.
MUTAGEN 220 220 T->A: Loss of interaction with MEKK1.
Normal phosphorylation by MAPKKK5; when
associated with A-226.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:27679653,
ECO:0000269|PubMed:9878570}.
MUTAGEN 220 220 T->E: Constitutively active; when
associated with E-226.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:9878570}.
MUTAGEN 226 226 T->A: Loss of interaction with MEKK1.
Normal phosphorylation by MAPKKK5; when
associated with A-220.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:27679653,
ECO:0000269|PubMed:9878570}.
MUTAGEN 226 226 T->E: Constitutively active; when
associated with E-220.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:9878570}.
CONFLICT 314 314 D -> E (in Ref. 2; CAA07281 and 3;
AAC72754). {ECO:0000305}.
SEQUENCE 363 AA; 39848 MW; 3E7EFC6D3A831D93 CRC64;
MKKGGFSNNL KLAIPVAGEQ SITKFLTQSG TFKDGDLRVN KDGVRIISQL EPEVLSPIKP
ADDQLSLSDL DMVKVIGKGS SGVVQLVQHK WTGQFFALKV IQLNIDEAIR KAIAQELKIN
QSSQCPNLVT SYQSFYDNGA ISLILEYMDG GSLADFLKSV KAIPDSYLSA IFRQVLQGLI
YLHHDRHIIH RDLKPSNLLI NHRGEVKITD FGVSTVMTNT AGLANTFVGT YNYMSPERIV
GNKYGNKSDI WSLGLVVLEC ATGKFPYAPP NQEETWTSVF ELMEAIVDQP PPALPSGNFS
PELSSFISTC LQKDPNSRSS AKELMEHPFL NKYDYSGINL ASYFTDAGSP LATLGNLSGT
FSV


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EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
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
E1358h ELISA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
U1358h CLIA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
E1358h ELISA kit Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
18-662-20091 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
18-662-20090 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
18-662-20092 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 mg
15-288-21068 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.05 mg
10-782-55048 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
10-782-55048 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.05 mg
10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.05 mg
10-782-55047 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 N_A 0.02 mg
EIAAB25228 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,Map2k1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,Mek1,Prkmk1,Rat,Rattus norvegicus
EIAAB25230 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,Map2k1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,Mek1,Mouse,Mus musculus,Prkmk1


 

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