(data stored in ACNUC8465 zone)

SWISSPROT: M2K4_ARATH

ID   M2K4_ARATH              Reviewed;         366 AA.
AC   O80397;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   11-DEC-2019, entry version 148.
DE   RecName: Full=Mitogen-activated protein kinase kinase 4;
DE            Short=AtMKK4;
DE            Short=MAP kinase kinase 4;
DE            EC=2.7.12.2;
GN   Name=MKK4; OrderedLocusNames=At1g51660; ORFNames=F19C24.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10048483; DOI=10.1093/dnares/5.6.341;
RA   Ichimura K., Mizoguchi T., Hayashida N., Seki M., Shinozaki K.;
RT   "Molecular cloning and characterization of three cDNAs encoding putative
RT   mitogen-activated protein kinase kinases (MAPKKs) in Arabidopsis
RT   thaliana.";
RL   DNA Res. 5:341-348(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF LYS-108; THR-224 AND SER-230.
RX   PubMed=11687590; DOI=10.1074/jbc.m109495200;
RA   Ren D., Yang H., Zhang S.;
RT   "Cell death mediated by MAPK is associated with hydrogen peroxide
RT   production in Arabidopsis.";
RL   J. Biol. Chem. 277:559-565(2002).
RN   [6]
RP   FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-224 AND SER-230, AND
RP   MUTAGENESIS OF LYS-108; THR-224 AND SER-230.
RX   PubMed=11875555; DOI=10.1038/415977a;
RA   Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA   Boller T., Ausubel F.M., Sheen J.;
RT   "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL   Nature 415:977-983(2002).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG   MAPK group;
RT   "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL   Trends Plant Sci. 7:301-308(2002).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA   Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA   Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA   Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT   "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT   families.";
RL   Trends Plant Sci. 11:192-198(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=17259259; DOI=10.1105/tpc.106.048298;
RA   Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S.;
RT   "Stomatal development and patterning are regulated by environmentally
RT   responsive mitogen-activated protein kinases in Arabidopsis.";
RL   Plant Cell 19:63-73(2007).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19516975; DOI=10.4161/psb.3.1.4856;
RA   Samuel M.A., Chaal B.K., Lampard G., Green B.R., Ellis B.E.;
RT   "Surviving the passage: Non-canonical stromal targeting of an Arabidopsis
RT   mitogen-activated protein kinase kinase.";
RL   Plant Signal. Behav. 3:6-12(2008).
RN   [11]
RP   INTERACTION WITH MPK6.
RX   PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA   Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT   "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT   MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL   Plant Signal. Behav. 3:1037-1041(2008).
RN   [12]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18809915; DOI=10.1073/pnas.0805539105;
RA   Cho S.K., Larue C.T., Chevalier D., Wang H., Jinn T.-L., Zhang S.,
RA   Walker J.C.;
RT   "Regulation of floral organ abscission in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15629-15634(2008).
RN   [13]
RP   INTERACTION WITH P.SYRINGAE HOPF2.
RX   PubMed=20571112; DOI=10.1105/tpc.110.075697;
RA   Wang Y., Li J., Hou S., Wang X., Li Y., Ren D., Chen S., Tang X.,
RA   Zhou J.M.;
RT   "A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis
RT   mitogen-activated protein kinase kinases.";
RL   Plant Cell 22:2033-2044(2010).
RN   [14]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=21806969; DOI=10.1016/j.bbrc.2011.07.064;
RA   Kim S.H., Woo D.H., Kim J.M., Lee S.Y., Chung W.S., Moon Y.H.;
RT   "Arabidopsis MKK4 mediates osmotic-stress response via its regulation of
RT   MPK3 activity.";
RL   Biochem. Biophys. Res. Commun. 412:150-154(2011).
RN   [15]
RP   FUNCTION.
RX   PubMed=23263767; DOI=10.1105/tpc.112.104695;
RA   Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S.;
RT   "A MAPK cascade downstream of ERECTA receptor-like protein kinase regulates
RT   Arabidopsis inflorescence architecture by promoting localized cell
RT   proliferation.";
RL   Plant Cell 24:4948-4960(2012).
RN   [16]
RP   FUNCTION, ACTIVITY REGULATION, INTERACTION WITH ASK7/BIN2, MUTAGENESIS OF
RP   SER-230 AND THR-234, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION
RP   AT SER-6; SER-230 AND THR-234, AND SUBCELLULAR LOCATION.
RX   PubMed=23341468; DOI=10.1074/jbc.m112.384453;
RA   Khan M., Rozhon W., Bigeard J., Pflieger D., Husar S., Pitzschke A.,
RA   Teige M., Jonak C., Hirt H., Poppenberger B.;
RT   "Brassinosteroid-regulated GSK3/Shaggy-like kinases phosphorylate mitogen-
RT   activated protein (MAP) kinase kinases, which control stomata development
RT   in Arabidopsis thaliana.";
RL   J. Biol. Chem. 288:7519-7527(2013).
RN   [17]
RP   INTERACTION WITH RACK1A; RACK1B AND RACK1C.
RX   PubMed=25731164; DOI=10.1038/nature14243;
RA   Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S.,
RA   Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.;
RT   "Pathogen-secreted proteases activate a novel plant immune pathway.";
RL   Nature 521:213-216(2015).
RN   [18]
RP   INTERACTION WITH MAPKKK5, PHOSPHORYLATION BY MAPKKK5, AND MUTAGENESIS OF
RP   LYS-108; THR-224 AND SER-230.
RC   STRAIN=cv. Columbia;
RX   PubMed=27679653; DOI=10.15252/embj.201694248;
RA   Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA   Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA   Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA   Shirasu K., Shibuya N., Kawasaki T.;
RT   "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT   to MAPK activation.";
RL   EMBO J. 35:2468-2483(2016).
CC   -!- FUNCTION: Involved in the second phase of hydrogen peroxide generation
CC       during hypersensitive response-like cell death. Involved in the innate
CC       immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6)
CC       downstream of bacterial flagellin receptor FLS2. Activates by
CC       phosphorylation the downstream MPK3 and MPK6. YDA-MKK4/MKK5-MPK3/MPK6
CC       module regulates stomatal cell fate before the guard mother cell (GMC)
CC       is specified. This MAPK cascade also functions downstream of the ER
CC       receptor in regulating coordinated local cell proliferation, which
CC       shapes the morphology of plant organs. MKK4 and MKK5 participate in the
CC       regulation of floral organ abscission. Mediates osmotic-stress response
CC       via its regulation of MPK3 activity. Target of the Pseudomonas syringae
CC       type III effector HopF2. {ECO:0000269|PubMed:11687590,
CC       ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:17259259,
CC       ECO:0000269|PubMed:18809915, ECO:0000269|PubMed:21806969,
CC       ECO:0000269|PubMed:23263767, ECO:0000269|PubMed:23341468}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- ACTIVITY REGULATION: Activated through serine and threonine
CC       phosphorylation by MEKK1. Inhibited through phosphorylation by
CC       GSK3/Shaggy-like kinase ASKs. {ECO:0000269|PubMed:11875555,
CC       ECO:0000269|PubMed:23341468}.
CC   -!- SUBUNIT: Interacts with ASK7/BIN2 (PubMed:23341468). Interacts with
CC       P.syringae type III effector HopF2 (PubMed:20571112). Interacts with
CC       MPK6 (PubMed:19513235). Interacts with RACK1A, RACK1B and RACK1C
CC       (PubMed:25731164). Interacts with MAPKKK5 mainly in the cytosol
CC       (PubMed:27679653). {ECO:0000269|PubMed:19513235,
CC       ECO:0000269|PubMed:20571112, ECO:0000269|PubMed:23341468,
CC       ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:27679653}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Plastid, chloroplast stroma.
CC   -!- TISSUE SPECIFICITY: Expressed higher in stems and leaves than in
CC       flowers and roots. {ECO:0000269|PubMed:10048483,
CC       ECO:0000269|PubMed:21806969}.
CC   -!- PTM: Phosphorylation at Thr-224 and Ser-230 by MAP kinase kinase
CC       kinases positively regulates kinase activity. Phosphorylation at Ser-
CC       230 and Thr-234 by GSK3/Shaggy-like kinase ASKs negatively regulates
CC       kinase activity. Phosphorylated by MAPKKK5 (PubMed:27679653).
CC       {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:23341468,
CC       ECO:0000269|PubMed:27679653}.
CC   -!- DISRUPTION PHENOTYPE: RNAi double mutants MKK4 and MKK5 have a strong
CC       abscission defect. Higher sensitivity to high salt and drought
CC       stresses. {ECO:0000269|PubMed:18809915, ECO:0000269|PubMed:21806969}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
DR   EMBL; AB015315; BAA28830.1; -; mRNA.
DR   EMBL; AC025294; AAG50863.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32696.1; -; Genomic_DNA.
DR   EMBL; AF324667; AAG40018.1; -; mRNA.
DR   EMBL; AF326878; AAG41460.1; -; mRNA.
DR   EMBL; AF349517; AAK15564.1; -; mRNA.
DR   EMBL; AF375398; AAK52982.1; -; mRNA.
DR   EMBL; AY129469; AAM91055.1; -; mRNA.
DR   PIR; T51339; T51339.
DR   RefSeq; NP_175577.1; NM_104044.3.
DR   SMR; O80397; -.
DR   BioGrid; 26816; 15.
DR   IntAct; O80397; 10.
DR   STRING; 3702.AT1G51660.1; -.
DR   iPTMnet; O80397; -.
DR   PaxDb; O80397; -.
DR   PRIDE; O80397; -.
DR   EnsemblPlants; AT1G51660.1; AT1G51660.1; AT1G51660.
DR   GeneID; 841591; -.
DR   Gramene; AT1G51660.1; AT1G51660.1; AT1G51660.
DR   KEGG; ath:AT1G51660; -.
DR   Araport; AT1G51660; -.
DR   TAIR; locus:2017662; AT1G51660.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; O80397; -.
DR   KO; K13413; -.
DR   OMA; CHDMYER; -.
DR   OrthoDB; 688282at2759; -.
DR   PhylomeDB; O80397; -.
DR   PRO; PR:O80397; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80397; baseline and differential.
DR   Genevisible; O80397; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0009814; P:defense response, incompatible interaction; IMP:TAIR.
DR   GO; GO:0010227; P:floral organ abscission; IMP:TAIR.
DR   GO; GO:0010229; P:inflorescence development; IGI:TAIR.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O80397.
DR   SWISS-2DPAGE; O80397.
KW   ATP-binding; Chloroplast; Cytoplasm; Hypersensitive response; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense; Plastid;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..366
FT                   /note="Mitogen-activated protein kinase kinase 4"
FT                   /id="PRO_0000245823"
FT   DOMAIN          79..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         85..93
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         108
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         6
FT                   /note="Phosphoserine; by ASK7"
FT                   /evidence="ECO:0000269|PubMed:23341468"
FT   MOD_RES         224
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:11875555"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11875555,
FT                   ECO:0000269|PubMed:23341468"
FT   MOD_RES         230
FT                   /note="Phosphoserine; by ASK7"
FT                   /evidence="ECO:0000269|PubMed:11875555,
FT                   ECO:0000269|PubMed:23341468"
FT   MOD_RES         234
FT                   /note="Phosphothreonine; by ASK7"
FT                   /evidence="ECO:0000269|PubMed:23341468"
FT   MUTAGEN         108
FT                   /note="K->M: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555"
FT   MUTAGEN         108
FT                   /note="K->R: Loss of activity. Phosphorylated by MAPKKK5."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:27679653"
FT   MUTAGEN         224
FT                   /note="T->A: Impaired phosphorylation by MAPKKK5; when
FT                   associated with A-230."
FT                   /evidence="ECO:0000269|PubMed:27679653"
FT   MUTAGEN         224
FT                   /note="T->D: Constitutively active; when associated with D-
FT                   230 or E-230."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555"
FT   MUTAGEN         230
FT                   /note="S->A: Abolishes phosphorylation by ASK7/BIN2.
FT                   Impaired phosphorylation by MAPKKK5; when associated with
FT                   A-224."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:23341468,
FT                   ECO:0000269|PubMed:27679653"
FT   MUTAGEN         230
FT                   /note="S->D: Constitutively active; when associated with D-
FT                   224."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:23341468"
FT   MUTAGEN         230
FT                   /note="S->E: Constitutively active; when associated with D-
FT                   224."
FT                   /evidence="ECO:0000269|PubMed:11687590,
FT                   ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:23341468"
FT   MUTAGEN         234
FT                   /note="T->A: Abolishes phosphorylation by ASK7/BIN2."
FT                   /evidence="ECO:0000269|PubMed:23341468"
FT   MUTAGEN         234
FT                   /note="T->D,E: Abolishes activity of MKK4 against MPK6."
FT                   /evidence="ECO:0000269|PubMed:23341468"
SQ   SEQUENCE   366 AA;  40117 MW;  34C1CA3EEA19D07C CRC64;
     MRPIQSPPGV SVPVKSRPRR RPDLTLPLPQ RDVSLAVPLP LPPTSGGSGG SSGSAPSSGG
     SASSTNTNSS IEAKNYSDLV RGNRIGSGAG GTVYKVIHRP SSRLYALKVI YGNHEETVRR
     QICREIEILR DVNHPNVVKC HEMFDQNGEI QVLLEFMDKG SLEGAHVWKE QQLADLSRQI
     LSGLAYLHSR HIVHRDIKPS NLLINSAKNV KIADFGVSRI LAQTMDPCNS SVGTIAYMSP
     ERINTDLNQG KYDGYAGDIW SLGVSILEFY LGRFPFPVSR QGDWASLMCA ICMSQPPEAP
     ATASPEFRHF ISCCLQREPG KRRSAMQLLQ HPFILRASPS QNRSPQNLHQ LLPPPRPLSS
     SSSPTT
//

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