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Mitogen-activated protein kinase kinase 1 (AtMKK1) (MAP kinase kinase 1) (EC 2.7.12.2) (AtMEK1) (NMAPKK)

 M2K1_ARATH              Reviewed;         354 AA.
Q94A06; O04440; O04661;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
23-MAY-2018, entry version 136.
RecName: Full=Mitogen-activated protein kinase kinase 1;
Short=AtMKK1;
Short=MAP kinase kinase 1;
EC=2.7.12.2;
AltName: Full=AtMEK1;
AltName: Full=NMAPKK;
Name=MKK1; Synonyms=MEK1; OrderedLocusNames=At4g26070;
ORFNames=F20B18.180;
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), TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=cv. Columbia;
PubMed=9426629; DOI=10.1023/A:1005963222768;
Morris P.C., Guerrier D., Leung J., Giraudat J.;
"Cloning and characterisation of MEK1, an Arabidopsis gene encoding a
homologue of MAP kinase kinase.";
Plant Mol. Biol. 35:1057-1064(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Nanmori T., Matsuoka D., Deguchi M., Ariga H.;
"Nucleotide sequence of plant mapkk subfamily.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
SUBUNIT, AND INTERACTION WITH MEKK1 AND MPK4.
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).
[8]
FUNCTION.
PubMed=10759527; DOI=10.1104/pp.122.4.1301;
Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.;
"ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase,
is activated in vitro by AtMEK1 through threonine phosphorylation.";
Plant Physiol. 122:1301-1310(2000).
[9]
PHOSPHORYLATION AT THR-218 AND SER-224, AND MUTAGENESIS OF THR-218 AND
SER-224.
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).
[10]
ENZYME REGULATION, PHOSPHORYLATION AT THR-218, AND MUTAGENESIS OF
THR-218; SER-220 AND SER-224.
PubMed=11874576; DOI=10.1046/j.0960-7412.2001.01246.x;
Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T.;
"Activation of AtMEK1, an Arabidopsis mitogen-activated protein kinase
kinase, in vitro and in vivo: analysis of active mutants expressed in
E. coli and generation of the active form in stress response in
seedlings.";
Plant J. 29:637-647(2002).
[11]
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).
[12]
ENZYME REGULATION.
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).
[13]
ENZYME REGULATION, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17059410; DOI=10.1111/j.1365-313X.2006.02888.x;
Meszaros T., Helfer A., Hatzimasoura E., Magyar Z., Serazetdinova L.,
Rios G., Bardoczy V., Teige M., Koncz C., Peck S., Bogre L.;
"The Arabidopsis MAP kinase kinase MKK1 participates in defence
responses to the bacterial elicitor flagellin.";
Plant J. 48:485-498(2006).
[14]
INTERACTION WITH MEKK1, PHOSPHORYLATION AT THR-218 AND SER-224, AND
MUTAGENESIS OF LYS-97; THR-218 AND SER-224.
PubMed=16211390; DOI=10.1007/s00425-005-0126-7;
Hadiarto T., Nanmori T., Matsuoka D., Iwasaki T., Sato K., Fukami Y.,
Azuma T., Yasuda T.;
"Activation of Arabidopsis MAPK kinase kinase (AtMEKK1) and induction
of AtMEKK1-AtMEK1 pathway by wounding.";
Planta 223:708-713(2006).
[15]
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).
[16]
FUNCTION, AND ENZYME REGULATION.
PubMed=17728292; DOI=10.1093/jxb/erm144;
Xing Y., Jia W., Zhang J.;
"AtMEK1 mediates stress-induced gene expression of CAT1 catalase by
triggering H2O2 production in Arabidopsis.";
J. Exp. Bot. 58:2969-2981(2007).
[17]
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).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18248592; DOI=10.1111/j.1365-313X.2008.03433.x;
Xing Y., Jia W., Zhang J.;
"AtMKK1 mediates ABA-induced CAT1 expression and H2O2 production via
AtMPK6-coupled signaling in Arabidopsis.";
Plant J. 54:440-451(2008).
[19]
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).
[20]
INTERACTION WITH MPK4 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).
[21]
FUNCTION.
PubMed=19484493; DOI=10.1007/s11103-009-9503-0;
Xing Y., Jia W., Zhang J.;
"AtMKK1 and AtMPK6 are involved in abscisic acid and sugar signaling
in Arabidopsis seed germination.";
Plant Mol. Biol. 70:725-736(2009).
[22]
INTERACTION WITH P.SYRINGAE HOPF2.
PubMed=20571112; DOI=10.1105/tpc.110.075697;
Wang Y., Li J., Hou S., Wang X., Li Y., Ren D., Chen S., Tang X.,
Zhou J.M.;
"A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis
mitogen-activated protein kinase kinases.";
Plant Cell 22:2033-2044(2010).
-!- FUNCTION: MEKK1, MKK1/MKK2 and MPK4/MPK6 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.
Activates by phosphorylation the downstream MPK4. Acts redundantly
with MKK2. MKK1-MPK6 module mediates abscisic acid (ABA)-dependent
CAT1 expression with H(2)O(2) production and response to drought
and salt stress. MKK1-MPK6 module is also involved in sugar
signaling during the process of seed germination.
{ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:17059410,
ECO:0000269|PubMed:17728292, ECO:0000269|PubMed:18248592,
ECO:0000269|PubMed:18599650, ECO:0000269|PubMed:18982020,
ECO:0000269|PubMed:19484493}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated through serine and threonine
phosphorylation in response to wounding, cold, drought, salt
stresses, abscisic acid (ABA), hydrogen peroxide, bacterial
flagellin and laminarin beta-glucan. {ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:17059410,
ECO:0000269|PubMed:17728292}.
-!- SUBUNIT: Interacts with MEKK1 and MPK4. May form a ternary complex
composed of MEKK1 and MKK1/MKK2 and MPK4. Interacts with
P.syringae type III effector HopF2. Interacts with MPK11.
{ECO:0000269|PubMed:16211390, ECO:0000269|PubMed:18982020,
ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20571112,
ECO:0000269|PubMed:9878570}.
-!- INTERACTION:
Q39008:MEKK1; NbExp=4; IntAct=EBI-994464, EBI-994439;
Q9LMM5:MPK11; NbExp=2; IntAct=EBI-994464, EBI-2358699;
Q8GYQ5:MPK12; NbExp=2; IntAct=EBI-994464, EBI-2128461;
Q39024:MPK4; NbExp=6; IntAct=EBI-994464, EBI-994375;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q94A06-1; Sequence=Displayed;
Name=2;
IsoId=Q94A06-2; Sequence=VSP_019782, VSP_019783;
Note=May be due to an intron retention. No experimental
confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in roots, stem, flowers and
siliques. {ECO:0000269|PubMed:9426629}.
-!- INDUCTION: By wounding. {ECO:0000269|PubMed:9426629}.
-!- PTM: Phosphorylation at Thr-218 and Ser-224 by MAP kinase kinase
kinases positively regulates kinase activity.
{ECO:0000269|PubMed:11874576, ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
-!- DISRUPTION PHENOTYPE: No obvious developmental defects under
normal growth conditions. Compromised in resistance to both
virulent and avirulent Pseudomonas syringae strains. Reduced
sensitivity to abscisic acid (ABA) during germination and reduced
drought tolerance of seedlings. Simultaneous knockdown of MKK1 and
MKK2 results in dwarf and small plants exhibiting a seedling-
lethality phenotype. {ECO:0000269|PubMed:17059410,
ECO:0000269|PubMed:18248592, 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; AF000977; AAB97145.1; -; mRNA.
EMBL; AB004796; BAA24079.1; -; mRNA.
EMBL; AL049483; CAB39672.1; -; Genomic_DNA.
EMBL; AL161564; CAB79462.1; -; Genomic_DNA.
EMBL; CP002687; AEE85152.1; -; Genomic_DNA.
EMBL; CP002687; AEE85153.1; -; Genomic_DNA.
EMBL; CP002687; AEE85154.1; -; Genomic_DNA.
EMBL; AY050774; AAK92709.1; -; mRNA.
EMBL; BT001935; AAN71934.1; -; mRNA.
EMBL; AY087065; AAM64626.1; -; mRNA.
PIR; T04262; T04262.
RefSeq; NP_194337.1; NM_118740.3. [Q94A06-1]
RefSeq; NP_849446.1; NM_179115.2. [Q94A06-2]
RefSeq; NP_974619.1; NM_202890.2. [Q94A06-1]
UniGene; At.21332; -.
UniGene; At.223; -.
ProteinModelPortal; Q94A06; -.
SMR; Q94A06; -.
BioGrid; 14000; 2.
IntAct; Q94A06; 4.
STRING; 3702.AT4G26070.2; -.
iPTMnet; Q94A06; -.
PaxDb; Q94A06; -.
PRIDE; Q94A06; -.
EnsemblPlants; AT4G26070.1; AT4G26070.1; AT4G26070. [Q94A06-2]
EnsemblPlants; AT4G26070.2; AT4G26070.2; AT4G26070. [Q94A06-1]
EnsemblPlants; AT4G26070.3; AT4G26070.3; AT4G26070. [Q94A06-1]
GeneID; 828713; -.
Gramene; AT4G26070.1; AT4G26070.1; AT4G26070. [Q94A06-2]
Gramene; AT4G26070.2; AT4G26070.2; AT4G26070. [Q94A06-1]
Gramene; AT4G26070.3; AT4G26070.3; AT4G26070. [Q94A06-1]
KEGG; ath:AT4G26070; -.
Araport; AT4G26070; -.
TAIR; locus:2120855; AT4G26070.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
HOGENOM; HOG000234206; -.
InParanoid; Q94A06; -.
KO; K20602; -.
OMA; VMKSNDC; -.
OrthoDB; EOG09360FLW; -.
PhylomeDB; Q94A06; -.
BRENDA; 2.7.12.2; 399.
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:Q94A06; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q94A06; baseline and differential.
Genevisible; Q94A06; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0042742; P:defense response to bacterium; IDA:TAIR.
GO; GO:0009814; P:defense response, incompatible interaction; IGI:TAIR.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
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 1 354 Mitogen-activated protein kinase kinase
1.
/FTId=PRO_0000245821.
DOMAIN 68 328 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 190 190 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 97 97 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 218 218 Phosphothreonine.
{ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:O80397}.
VAR_SEQ 308 308 C -> W (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_019782.
VAR_SEQ 309 354 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_019783.
MUTAGEN 97 97 K->R: Loss of kinase activity in vitro.
{ECO:0000269|PubMed:16211390}.
MUTAGEN 218 218 T->A: Loss of kinase activity in vitro;
when associated with E-224.
{ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
MUTAGEN 218 218 T->E: Constitutively active; when
associated with D-224. Increases kinase
activity in vitro; when associated with
E-224. {ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
MUTAGEN 220 220 S->E: Increases kinase activity in vitro;
when associated with E-224.
{ECO:0000269|PubMed:11874576}.
MUTAGEN 224 224 S->D: Constitutively active; when
associated with E-218.
{ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
MUTAGEN 224 224 S->E: Increases kinase activity in vitro;
when associated with E-218 or E-220.
{ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:11875555,
ECO:0000269|PubMed:16211390}.
SEQUENCE 354 AA; 39210 MW; D889CFBB97653B8E CRC64;
MNRGSLCPNP ICLPPLEQSI SKFLTQSGTF KDGDLRVNKD GIQTVSLSEP GAPPPIEPLD
NQLSLADLEV IKVIGKGSSG NVQLVKHKLT QQFFALKVIQ LNTEESTCRA ISQELRINLS
SQCPYLVSCY QSFYHNGLVS IILEFMDGGS LADLLKKVGK VPENMLSAIC KRVLRGLCYI
HHERRIIHRD LKPSNLLINH RGEVKITDFG VSKILTSTSS LANSFVGTYP YMSPERISGS
LYSNKSDIWS LGLVLLECAT GKFPYTPPEH KKGWSSVYEL VDAIVENPPP CAPSNLFSPE
FCSFISQCVQ KDPRDRKSAK ELLEHKFVKM FEDSDTNLSA YFTDAGSLIP PLAN


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