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Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)

 AHK4_ARATH              Reviewed;        1080 AA.
Q9C5U0; A5YY60; A5YY75; Q9C5T8; Q9C5T9; Q9FDZ3; Q9SIT0;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 122.
RecName: Full=Histidine kinase 4;
EC=2.7.13.3;
AltName: Full=Arabidopsis histidine kinase 4;
Short=AtHK4;
AltName: Full=Cytokinin receptor CYTOKININ RESPONSE 1;
Short=AtCRE1;
Short=Cytokinin receptor CRE1;
AltName: Full=Phosphoprotein phosphatase AHK4;
EC=3.1.3.16;
AltName: Full=Protein AUTHENTIC HIS-KINASE 4;
AltName: Full=Protein ROOT AS IN WOL 1;
AltName: Full=Protein WOODEN LEG;
Name=AHK4; Synonyms=CRE1, RAW1, WOL; OrderedLocusNames=At2g01830;
ORFNames=T23K3.2;
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 2), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, FUNCTION, AND MUTAGENESIS OF THR-301.
STRAIN=cv. Columbia; TISSUE=Root;
PubMed=11114883; DOI=10.1101/gad.189200;
Maehoenen A.P., Bonke M., Kauppinen L., Riikonen M., Benfey P.N.,
Helariutta Y.;
"A novel two-component hybrid molecule regulates vascular
morphogenesis of the Arabidopsis root.";
Genes Dev. 14:2938-2943(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME
REGULATION, AND MUTAGENESIS OF HIS-482; GLY-490 AND ASP-996.
STRAIN=cv. Wassilewskija; TISSUE=Seedling;
PubMed=11234017; DOI=10.1038/35059117;
Inoue T., Higuchi M., Hashimoto Y., Seki M., Kobayashi M., Kato T.,
Tabata S., Shinozaki K., Kakimoto T.;
"Identification of CRE1 as a cytokinin receptor from Arabidopsis.";
Nature 409:1060-1063(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=11230578; DOI=10.1093/pcp/pce015;
Ueguchi C., Koizumi H., Suzuki T., Mizuno T.;
"Novel family of sensor histidine kinase genes in Arabidopsis
thaliana.";
Plant Cell Physiol. 42:231-235(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 722-983, AND VARIANT ASN-765.
STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta,
cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0,
cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and
cv. Wassilewskija;
PubMed=17435248; DOI=10.1534/genetics.107.071928;
Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
"The genetic architecture of shoot branching in Arabidopsis thaliana:
a comparative assessment of candidate gene associations vs.
quantitative trait locus mapping.";
Genetics 176:1223-1236(2007).
[7]
FUNCTION, AND INTERACTION WITH AHP1; AHP2; AHP3 AND AHP5.
PubMed=11230563; DOI=10.1093/pcp/pce037;
Suzuki T., Miwa K., Ishikawa K., Yamada H., Aiba H., Mizuno T.;
"The Arabidopsis sensor His-kinase, AHk4, can respond to cytokinins.";
Plant Cell Physiol. 42:107-113(2001).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11479382; DOI=10.1093/pcp/pce094;
Ueguchi C., Sato S., Kato T., Tabata S.;
"The AHK4 gene involved in the cytokinin-signaling pathway as a direct
receptor molecule in Arabidopsis thaliana.";
Plant Cell Physiol. 42:751-755(2001).
[9]
FUNCTION, ACTIVATION BY CYTOKININS, AND MUTAGENESIS OF THR-301.
PubMed=11577198; DOI=10.1093/pcp/pce127;
Yamada H., Suzuki T., Terada K., Takei K., Ishikawa K., Miwa K.,
Yamashino T., Mizuno T.;
"The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor
that transduces cytokinin signals across the membrane.";
Plant Cell Physiol. 42:1017-1023(2001).
[10]
REVIEW.
PubMed=11435149; DOI=10.1016/S1360-1385(01)02011-8;
Schmuelling T.;
"CREam of cytokinin signalling: receptor identified.";
Trends Plant Sci. 6:281-284(2001).
[11]
REVIEW.
PubMed=12589073; DOI=10.1266/ggs.77.383;
Oka A., Sakai H., Iwakoshi S.;
"His-Asp phosphorelay signal transduction in higher plants: receptors
and response regulators for cytokinin signaling in Arabidopsis
thaliana.";
Genes Genet. Syst. 77:383-391(2002).
[12]
FUNCTION, AND MUTAGENESIS OF GLY-490.
PubMed=12354925; DOI=10.1093/pcp/pcf121;
Kiba T., Yamada H., Mizuno T.;
"Characterization of the ARR15 and ARR16 response regulators with
special reference to the cytokinin signaling pathway mediated by the
AHK4 histidine kinase in roots of Arabidopsis thaliana.";
Plant Cell Physiol. 43:1059-1066(2002).
[13]
FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND MUTAGENESIS OF GLY-493;
THR-1008 AND ALA-1032.
PubMed=12410813; DOI=10.1046/j.1365-313X.2002.01431.x;
Franco-Zorrilla J.M., Martin A.C., Solano R., Rubio V., Leyva A.,
Paz-Ares J.;
"Mutations at CRE1 impair cytokinin-induced repression of phosphate
starvation responses in Arabidopsis.";
Plant J. 32:353-360(2002).
[14]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12068096; DOI=10.1104/pp.005504;
Hwang I., Chen H.-C., Sheen J.;
"Two-component signal transduction pathways in Arabidopsis.";
Plant Physiol. 129:500-515(2002).
[15]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15155880; DOI=10.1105/tpc.021477;
Nishimura C., Ohashi Y., Sato S., Kato T., Tabata S., Ueguchi C.;
"Histidine kinase homologs that act as cytokinin receptors possess
overlapping functions in the regulation of shoot and root growth in
Arabidopsis.";
Plant Cell 16:1365-1377(2004).
[16]
FUNCTION.
PubMed=15509853; DOI=10.1093/pcp/pch132;
Spichal L., Rakova N.Y., Riefler M., Mizuno T., Romanov G.A.,
Strnad M., Schmuelling T.;
"Two cytokinin receptors of Arabidopsis thaliana, CRE1/AHK4 and AHK3,
differ in their ligand specificity in a bacterial assay.";
Plant Cell Physiol. 45:1299-1305(2004).
[17]
FUNCTION, AND MUTAGENESIS OF THR-301 AND LEU-529.
PubMed=15053761; DOI=10.1111/j.1365-313X.2004.02023.x;
de Leon B.G.-P., Zorrilla J.M.F., Rubio V., Dahiya P., Paz-Ares J.,
Leyva A.;
"Interallelic complementation at the Arabidopsis CRE1 locus uncovers
independent pathways for the proliferation of vascular initials and
canonical cytokinin signalling.";
Plant J. 38:70-79(2004).
[18]
FUNCTION, AND MUTAGENESIS OF GLY-490.
PubMed=15144379; DOI=10.1111/j.1365-313X.2004.02079.x;
Maruyama-Nakashita A., Nakamura Y., Yamaya T., Takahashi H.;
"A novel regulatory pathway of sulfate uptake in Arabidopsis roots:
implication of CRE1/WOL/AHK4-mediated cytokinin-dependent
regulation.";
Plant J. 38:779-789(2004).
[19]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15166290; DOI=10.1073/pnas.0402887101;
Higuchi M., Pischke M.S., Maehoenen A.P., Miyawaki K., Hashimoto Y.,
Seki M., Kobayashi M., Shinozaki K., Kato T., Tabata S.,
Helariutta Y., Sussman M.R., Kakimoto T.;
"In planta functions of the Arabidopsis cytokinin receptor family.";
Proc. Natl. Acad. Sci. U.S.A. 101:8821-8826(2004).
[20]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16246292; DOI=10.1016/j.ab.2005.09.012;
Romanov G.A., Spichal L., Lomin S.N., Strnad M., Schmuelling T.;
"A live cell hormone-binding assay on transgenic bacteria expressing a
eukaryotic receptor protein.";
Anal. Biochem. 347:129-134(2005).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15923327; DOI=10.1104/pp.105.060517;
Franco-Zorrilla J.M., Martin A.C., Leyva A., Paz-Ares J.;
"Interaction between phosphate-starvation, sugar, and cytokinin
signaling in Arabidopsis and the roles of cytokinin receptors
CRE1/AHK4 and AHK3.";
Plant Physiol. 138:847-857(2005).
[22]
FUNCTION.
PubMed=15728338; DOI=10.1104/pp.104.057174;
Mok M.C., Martin R.C., Dobrev P.I., Vankova R., Ho P.S.,
Yonekura-Sakakibara K., Sakakibara H., Mok D.W.;
"Topolins and hydroxylated thidiazuron derivatives are substrates of
cytokinin O-glucosyltransferase with position specificity related to
receptor recognition.";
Plant Physiol. 137:1057-1066(2005).
[23]
FUNCTION, PHOSPHORYLATION AT HIS-482, MUTAGENESIS OF THR-301; HIS-482;
PHE-708 AND ASP-996, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=16753566; DOI=10.1016/j.cub.2006.04.030;
Maehoenen A.P., Higuchi M., Toermaekangas K., Miyawaki K.,
Pischke M.S., Sussman M.R., Helariutta Y., Kakimoto T.;
"Cytokinins regulate a bidirectional phosphorelay network in
Arabidopsis.";
Curr. Biol. 16:1116-1122(2006).
[24]
INTERACTION WITH AHP1; AHP2; AHP3; AHP5 AND AHK3.
PubMed=16965536; DOI=10.1111/j.1742-4658.2006.05467.x;
Dortay H., Mehnert N., Buerkle L., Schmuelling T., Heyl A.;
"Analysis of protein interactions within the cytokinin-signaling
pathway of Arabidopsis thaliana.";
FEBS J. 273:4631-4644(2006).
[25]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17075078; DOI=10.1093/jxb/erl179;
Romanov G.A., Lomin S.N., Schmuelling T.;
"Biochemical characteristics and ligand-binding properties of
Arabidopsis cytokinin receptor AHK3 compared to CRE1/AHK4 as revealed
by a direct binding assay.";
J. Exp. Bot. 57:4051-4058(2006).
[26]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16361392; DOI=10.1105/tpc.105.037796;
Riefler M., Novak O., Strnad M., Schmuelling T.;
"Arabidopsis cytokinin receptor mutants reveal functions in shoot
growth, leaf senescence, seed size, germination, root development, and
cytokinin metabolism.";
Plant Cell 18:40-54(2006).
[27]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-459 AND
GLY-490.
PubMed=16357038; DOI=10.1093/pcp/pci240;
Kuroha T., Ueguchi C., Sakakibara H., Satoh S.;
"Cytokinin receptors are required for normal development of auxin-
transporting vascular tissues in the hypocotyl but not in adventitious
roots.";
Plant Cell Physiol. 47:234-243(2006).
[28]
FUNCTION.
PubMed=17216481; DOI=10.1007/s00425-006-0464-0;
Horiuchi J., Badri D.V., Kimball B.A., Negre F., Dudareva N.,
Paschke M.W., Vivanco J.M.;
"The floral volatile, methyl benzoate, from snapdragon (Antirrhinum
majus) triggers phytotoxic effects in Arabidopsis thaliana.";
Planta 226:1-10(2007).
[29]
FUNCTION, AND MUTAGENESIS OF THR-301; GLY-435; PHE-436; MET-447;
VAL-471 AND MET-494.
PubMed=17956858; DOI=10.1093/pcp/pcm145;
Miwa K., Ishikawa K., Terada K., Yamada H., Suzuki T., Yamashino T.,
Mizuno T.;
"Identification of amino acid substitutions that render the
Arabidopsis cytokinin receptor histidine kinase AHK4 constitutively
active.";
Plant Cell Physiol. 48:1809-1814(2007).
[30]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=18077346; DOI=10.1073/pnas.0706547105;
Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K.,
Yamaguchi-Shinozaki K.;
"Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine
kinases in response to abscisic acid, drought, and salt stress in
Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007).
[31]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17965178; DOI=10.1104/pp.107.107953;
Lopez-Bucio J., Millan-Godinez M., Mendez-Bravo A.,
Morquecho-Contreras A., Ramirez-Chavez E., Molina-Torres J.,
Perez-Torres A., Higuchi M., Kakimoto T., Herrera-Estrella L.;
"Cytokinin receptors are involved in alkamide regulation of root and
shoot development in Arabidopsis.";
Plant Physiol. 145:1703-1713(2007).
[32]
FUNCTION.
PubMed=18571199; DOI=10.1016/j.jmb.2008.05.044;
Kopecny D., Sebela M., Briozzo P., Spichal L., Houba-Herin N.,
Masek V., Joly N., Madzak C., Anzenbacher P., Laloue M.;
"Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack
FAD cofactor.";
J. Mol. Biol. 380:886-899(2008).
[33]
INTERACTION WITH AHP2; AMPD; WNK5 AND AT4G15630.
PubMed=18642946; DOI=10.1021/pr0703831;
Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T.,
Heyl A.;
"Toward an interaction map of the two-component signaling pathway of
Arabidopsis thaliana.";
J. Proteome Res. 7:3649-3660(2008).
[34]
FUNCTION.
PubMed=18785832; DOI=10.1094/MPMI-21-10-1371;
Vadassery J., Ritter C., Venus Y., Camehl I., Varma A., Shahollari B.,
Novak O., Strnad M., Ludwig-Mueller J., Oelmueller R.;
"The role of auxins and cytokinins in the mutualistic interaction
between Arabidopsis and Piriformospora indica.";
Mol. Plant Microbe Interact. 21:1371-1383(2008).
[35]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18397377; DOI=10.1111/j.1365-313X.2008.03502.x;
Seguela M., Briat J.-F., Vert G., Curie C.;
"Cytokinins negatively regulate the root iron uptake machinery in
Arabidopsis through a growth-dependent pathway.";
Plant J. 55:289-300(2008).
[36]
FUNCTION, AND ENZYME REGULATION.
PubMed=19032596; DOI=10.1111/j.1742-4658.2008.06777.x;
Spichal L., Werner T., Popa I., Riefler M., Schmuelling T., Strnad M.;
"The purine derivative PI-55 blocks cytokinin action via receptor
inhibition.";
FEBS J. 276:244-253(2009).
[37]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20110319; DOI=10.1242/dev.041426;
Skylar A., Hong F., Chory J., Weigel D., Wu X.;
"STIMPY mediates cytokinin signaling during shoot meristem
establishment in Arabidopsis seedlings.";
Development 137:541-549(2010).
[38]
ENZYME REGULATION.
PubMed=20189204; DOI=10.1016/j.phytochem.2010.01.018;
Nisler J., Zatloukal M., Popa I., Dolezal K., Strnad M., Spichal L.;
"Cytokinin receptor antagonists derived from 6-benzylaminopurine.";
Phytochemistry 71:823-830(2010).
[39]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=21709172; DOI=10.1104/pp.111.180539;
Wulfetange K., Lomin S.N., Romanov G.A., Stolz A., Heyl A.,
Schmuelling T.;
"The cytokinin receptors of Arabidopsis are located mainly to the
endoplasmic reticulum.";
Plant Physiol. 156:1808-1818(2011).
[40]
INTERACTION WITH FBR12 AND AHP1.
PubMed=24163315; DOI=10.1105/tpc.113.116236;
Ren B., Chen Q., Hong S., Zhao W., Feng J., Feng H., Zuo J.;
"The Arabidopsis eukaryotic translation initiation factor eIF5A-2
regulates root protoxylem development by modulating cytokinin
signaling.";
Plant Cell 25:3841-3857(2013).
[41]
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 149-418 IN COMPLEX WITH
CYTOKININS OR THIADIAZURON, SUBUNIT, AND MUTAGENESIS OF ALA-225;
ALA-227; TYR-273; MET-279; ASP-285; THR-301; PRO-303; PHE-304;
LEU-306; LEU-307; THR-317 AND GLY-343.
PubMed=21964459; DOI=10.1038/nchembio.667;
Hothorn M., Dabi T., Chory J.;
"Structural basis for cytokinin recognition by Arabidopsis thaliana
histidine kinase 4.";
Nat. Chem. Biol. 7:766-768(2011).
-!- FUNCTION: Cytokinins (CK) receptor related to bacterial two-
component regulators. Binds also the synthetic urea-type cytokinin
thiadiazuron, a potent defoliant and herbicide. Functions as a
histidine kinase and transmits the stress signal to a downstream
MAPK cascade. This protein undergoes an ATP-dependent
autophosphorylation at a conserved histidine residue in the kinase
core, and a phosphoryl group is then transferred to a conserved
aspartate residue in the receiver domain. In the presence of
cytokinin, feeds phosphate to phosphorelay-integrating histidine
phosphotransfer protein (HPt) and activates subsequent cascade. In
the absence of cytokinin, removes phosphate from HPt proteins,
decreasing the system phosphoload. Involved in meristems
establishment in seedlings. Acts as a redundant negative regulator
of drought and salt stress responses, and abscisic acid (ABA)
signaling in a cytokinin-dependent manner. Required to set
vascular asymmetric cell divisions that establish phloem and
procambium cell lines. Redundant positive regulator of cytokinin
signaling that regulates many developmental processes including
seed germination, cell division, seed size, chlorophyll retention
during leaf senescence, root repression and shoot promotion. Can
interact with isoprenoid-type cytokinins trans-zeatin (tZ and
tZR), isopentenyladenine (iP), and isopentenyladenosine (iPR), the
meta hydroxylated derivative of benzyladenine m-topolin, buta-2,3-
dienyladenine (HA-8), penta-2,3-dienyladenine (HA-1), 4-methyl-
penta-2,3-dienyladenine (HA-10), 4-hydroxy-2-butynyladenine (RM1),
2-butynyladenine (RM6), and to a lower extent, with cis-zeatin
(cZ), zeatin riboside and dihydrozeatin (DZ). Together with AHK3,
involved in the cytokinin-dependent responses to Pi starvation and
sucrose stresses. Required for the formation of auxin-transporting
vascular tissues in the hypocotyl, and primary and lateral roots,
but not in adventitious roots, thus leading to auxin basipetal
transport that regulates root development and branching. Involved
in alkamides (e.g. N-isobutyl decanamide) and N-acylethanolamides
(NAE) signaling that control meristematic activity and
differentiation processes during plant development. Prevents the
uptake of sulfate by mediating cytokinin-dependent down-regulation
of high-affinity sulfate transporters (e.g. SULTR1;1 and SULTR1;2)
expression in roots. Together with AHK2, required for growth and
reproduction promotion stimulated by the endophytic fungus
Piriformospora indica in a trans-zeatin-dependent manner. Required
to trigger the phytotoxic effect of the snapdragon (Antirrhinum
majus) flowers volatile organic compound (VOC) methyl benzoate
(MB). Plays a role in the cytokinin-mediated repression of the
iron uptake pathway. {ECO:0000269|PubMed:11114883,
ECO:0000269|PubMed:11230563, ECO:0000269|PubMed:11234017,
ECO:0000269|PubMed:11479382, ECO:0000269|PubMed:11577198,
ECO:0000269|PubMed:12354925, ECO:0000269|PubMed:12410813,
ECO:0000269|PubMed:15053761, ECO:0000269|PubMed:15144379,
ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
ECO:0000269|PubMed:15509853, ECO:0000269|PubMed:15728338,
ECO:0000269|PubMed:15923327, ECO:0000269|PubMed:16246292,
ECO:0000269|PubMed:16357038, ECO:0000269|PubMed:16361392,
ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17075078,
ECO:0000269|PubMed:17216481, ECO:0000269|PubMed:17956858,
ECO:0000269|PubMed:17965178, ECO:0000269|PubMed:18077346,
ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:18571199,
ECO:0000269|PubMed:18785832, ECO:0000269|PubMed:19032596,
ECO:0000269|PubMed:20110319}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- ENZYME REGULATION: Activated by cytokinins to initiate
phosphorelay signaling. This cytokinin-mediated activation is
repressed by the trans-zeatin antagonists 6-(2-hydroxy-3-
methylbenzylamino)purine (PI-55) and 6-(2,5-
Dihydroxybenzylamino)purine (LGR-991).
{ECO:0000269|PubMed:11234017, ECO:0000269|PubMed:19032596,
ECO:0000269|PubMed:20189204}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH to bind cytokinin is about 7-8.5 at 0 degrees
Celsius. {ECO:0000269|PubMed:16246292,
ECO:0000269|PubMed:17075078};
Temperature dependence:
Cytokinin-binding is more stable at 0 degrees Celsius than at 20
and 37 degrees Celsius. {ECO:0000269|PubMed:16246292,
ECO:0000269|PubMed:17075078};
-!- SUBUNIT: Homodimer. Interacts with AHP1, AHP2, AHP3, AHP5, AHK3,
AMPD, FBR12, WNK5 and At4g15630. {ECO:0000269|PubMed:11230563,
ECO:0000269|PubMed:16965536, ECO:0000269|PubMed:18642946,
ECO:0000269|PubMed:21964459, ECO:0000269|PubMed:24163315}.
-!- INTERACTION:
Q9C5U1:AHK3; NbExp=2; IntAct=EBI-1100775, EBI-1100653;
O80452:AMPD; NbExp=2; IntAct=EBI-1100775, EBI-1807679;
Q67XQ1:At1g03430; NbExp=3; IntAct=EBI-1100775, EBI-1100725;
Q8L8Z1:At4g15630; NbExp=2; IntAct=EBI-1100775, EBI-1807704;
Q9SCU5:WNK5; NbExp=2; IntAct=EBI-1100775, EBI-1807651;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:21709172}; Multi-pass membrane protein
{ECO:0000269|PubMed:21709172}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CRE1b;
IsoId=Q9C5U0-1; Sequence=Displayed;
Name=2; Synonyms=CRE1a;
IsoId=Q9C5U0-2; Sequence=VSP_039770;
-!- TISSUE SPECIFICITY: Mostly expressed in roots, specifically in the
vascular cylinder and pericycle, and, to a lower extent, in leaves
and flowers. Present in seedlings. {ECO:0000269|PubMed:11114883,
ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:15155880,
ECO:0000269|PubMed:15166290}.
-!- DEVELOPMENTAL STAGE: Expressed specifically in the vasculature
since the early stages of embryogenesis. At the globular stage of
embryogenesis, detected in the four innermost cells, which are the
precursors of the vascular tissue. During the heart, torpedo, and
nearly mature stages, expressed in the procambium of the cotyledon
shoulders, prospective hypocotyl, and embryonic root. In
seedlings, mainly localized in meristematic tissues (e.g. shoot
apical meristem SAM, root tips, and growing leaf and lateral root
primordia), especially in vasculature. Present in all the
vasculature and the shoot apical meristem (SAM) of the adult
plant. In flowers, localized in carpels and developing ovules. In
the root tips, expressed in the central cylinder.
{ECO:0000269|PubMed:11114883, ECO:0000269|PubMed:15155880,
ECO:0000269|PubMed:16753566}.
-!- INDUCTION: Rapidly induced by dehydration. Down-regulated by Pi
starvation and induced by cytokinins.
{ECO:0000269|PubMed:12410813, ECO:0000269|PubMed:18077346}.
-!- PTM: Autophosphorylated predominantly on His residues. Activation
probably requires a transfer of a phosphate group between a His in
the transmitter domain and an Asp of the receiver domain.
{ECO:0000269|PubMed:16753566}.
-!- DISRUPTION PHENOTYPE: Reduced sensitivity to cytokinin (mostly in
shoots). Narrow vascular cylinder composed mainly of protoxylem
cell files, with no apparent metaxylem or phloem. Hypersensitivity
to ABA. Strong drought and salinity tolerance only in the presence
of CK. Reduced cytokinin repression of several Pi starvation-
responsive genes and increased sucrose sensitivity. More rapid
germination, reduced requirement for light, and decreased far-red
light sensitivity. Reduced sensitivity to N-isobutyl decanamide.
Impaired benzyladenine (6-BA)-mediated repression of the iron
uptake pathway. Impaired meristematic development in seedlings.
{ECO:0000269|PubMed:11479382, ECO:0000269|PubMed:12410813,
ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
ECO:0000269|PubMed:15923327, ECO:0000269|PubMed:16357038,
ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16753566,
ECO:0000269|PubMed:17965178, ECO:0000269|PubMed:18077346,
ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:20110319}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ278528; CAC18521.1; -; mRNA.
EMBL; AJ278529; CAC18522.1; -; mRNA.
EMBL; AJ278530; CAC18523.1; -; mRNA.
EMBL; AB049934; BAB33310.1; -; mRNA.
EMBL; AB049935; BAB33311.1; -; mRNA.
EMBL; AB046871; BAB40776.1; -; mRNA.
EMBL; AC007069; AAD21777.2; -; Genomic_DNA.
EMBL; CP002685; AEC05505.1; -; Genomic_DNA.
EMBL; CP002685; AEC05506.1; -; Genomic_DNA.
EMBL; CP002685; AEC05507.1; -; Genomic_DNA.
EMBL; CP002685; ANM62256.1; -; Genomic_DNA.
EMBL; CP002685; ANM62257.1; -; Genomic_DNA.
EMBL; EF598292; ABQ85264.1; -; Genomic_DNA.
EMBL; EF598293; ABQ85265.1; -; Genomic_DNA.
EMBL; EF598294; ABQ85266.1; -; Genomic_DNA.
EMBL; EF598295; ABQ85267.1; -; Genomic_DNA.
EMBL; EF598296; ABQ85268.1; -; Genomic_DNA.
EMBL; EF598297; ABQ85269.1; -; Genomic_DNA.
EMBL; EF598298; ABQ85270.1; -; Genomic_DNA.
EMBL; EF598299; ABQ85271.1; -; Genomic_DNA.
EMBL; EF598300; ABQ85272.1; -; Genomic_DNA.
EMBL; EF598301; ABQ85273.1; -; Genomic_DNA.
EMBL; EF598302; ABQ85274.1; -; Genomic_DNA.
EMBL; EF598303; ABQ85275.1; -; Genomic_DNA.
EMBL; EF598304; ABQ85276.1; -; Genomic_DNA.
EMBL; EF598305; ABQ85277.1; -; Genomic_DNA.
EMBL; EF598306; ABQ85278.1; -; Genomic_DNA.
EMBL; EF598307; ABQ85279.1; -; Genomic_DNA.
EMBL; EF598308; ABQ85280.1; -; Genomic_DNA.
EMBL; EF598309; ABQ85281.1; -; Genomic_DNA.
EMBL; EF598310; ABQ85282.1; -; Genomic_DNA.
EMBL; EF598311; ABQ85283.1; -; Genomic_DNA.
EMBL; EF598312; ABQ85284.1; -; Genomic_DNA.
EMBL; EF598313; ABQ85285.1; -; Genomic_DNA.
EMBL; EF598314; ABQ85286.1; -; Genomic_DNA.
EMBL; EF598315; ABQ85287.1; -; Genomic_DNA.
PIR; F84429; F84429.
RefSeq; NP_001324428.1; NM_001335080.1. [Q9C5U0-2]
RefSeq; NP_001324429.1; NM_001335082.1. [Q9C5U0-2]
RefSeq; NP_565277.1; NM_126244.3. [Q9C5U0-2]
RefSeq; NP_849925.1; NM_179594.2. [Q9C5U0-1]
RefSeq; NP_973396.1; NM_201667.1. [Q9C5U0-2]
UniGene; At.10485; -.
PDB; 3T4J; X-ray; 1.65 A; A/B=149-418.
PDB; 3T4K; X-ray; 1.77 A; A/B=149-418.
PDB; 3T4L; X-ray; 1.53 A; A/B=149-418.
PDB; 3T4O; X-ray; 1.75 A; A/B=149-418.
PDB; 3T4Q; X-ray; 2.30 A; A/B=149-418.
PDB; 3T4S; X-ray; 1.60 A; A/B=149-418.
PDB; 3T4T; X-ray; 1.70 A; A/B=149-418.
PDBsum; 3T4J; -.
PDBsum; 3T4K; -.
PDBsum; 3T4L; -.
PDBsum; 3T4O; -.
PDBsum; 3T4Q; -.
PDBsum; 3T4S; -.
PDBsum; 3T4T; -.
ProteinModelPortal; Q9C5U0; -.
SMR; Q9C5U0; -.
BioGrid; 117; 32.
IntAct; Q9C5U0; 29.
STRING; 3702.AT2G01830.2; -.
BindingDB; Q9C5U0; -.
ChEMBL; CHEMBL6124; -.
iPTMnet; Q9C5U0; -.
PaxDb; Q9C5U0; -.
EnsemblPlants; AT2G01830.1; AT2G01830.1; AT2G01830. [Q9C5U0-2]
EnsemblPlants; AT2G01830.2; AT2G01830.2; AT2G01830. [Q9C5U0-1]
EnsemblPlants; AT2G01830.3; AT2G01830.3; AT2G01830. [Q9C5U0-2]
EnsemblPlants; AT2G01830.4; AT2G01830.4; AT2G01830. [Q9C5U0-2]
EnsemblPlants; AT2G01830.6; AT2G01830.6; AT2G01830. [Q9C5U0-2]
GeneID; 814714; -.
Gramene; AT2G01830.1; AT2G01830.1; AT2G01830.
Gramene; AT2G01830.2; AT2G01830.2; AT2G01830.
Gramene; AT2G01830.3; AT2G01830.3; AT2G01830.
Gramene; AT2G01830.4; AT2G01830.4; AT2G01830.
Gramene; AT2G01830.6; AT2G01830.6; AT2G01830.
KEGG; ath:AT2G01830; -.
Araport; AT2G01830; -.
TAIR; locus:2059718; AT2G01830.
eggNOG; KOG0519; Eukaryota.
eggNOG; COG0642; LUCA.
InParanoid; Q9C5U0; -.
KO; K14489; -.
OMA; FNITHEL; -.
OrthoDB; EOG093601CR; -.
PhylomeDB; Q9C5U0; -.
EvolutionaryTrace; Q9C5U0; -.
PRO; PR:Q9C5U0; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9C5U0; baseline and differential.
Genevisible; Q9C5U0; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0019955; F:cytokine binding; IDA:TAIR.
GO; GO:0009884; F:cytokinin receptor activity; TAS:TAIR.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0004673; F:protein histidine kinase activity; IDA:TAIR.
GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0009885; F:transmembrane histidine kinase cytokinin receptor activity; IDA:UniProtKB.
GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
GO; GO:0016036; P:cellular response to phosphate starvation; IMP:UniProtKB.
GO; GO:0071329; P:cellular response to sucrose stimulus; IMP:UniProtKB.
GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
GO; GO:0010086; P:embryonic root morphogenesis; IMP:TAIR.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IGI:TAIR.
GO; GO:0048509; P:regulation of meristem development; IMP:UniProtKB.
GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
GO; GO:0048831; P:regulation of shoot system development; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
GO; GO:0008272; P:sulfate transport; IMP:UniProtKB.
CDD; cd00082; HisKA; 1.
CDD; cd06223; PRTases_typeI; 1.
CDD; cd00156; REC; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR006189; CHASE_dom.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR003594; HATPase_C.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
Pfam; PF03924; CHASE; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00512; HisKA; 1.
Pfam; PF00072; Response_reg; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM01079; CHASE; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SMART; SM00448; REC; 1.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF52172; SSF52172; 2.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS50839; CHASE; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Cytokinin signaling pathway; Developmental protein;
Endoplasmic reticulum; Hydrolase; Kinase; Membrane; Phosphoprotein;
Protein phosphatase; Reference proteome; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 1080 Histidine kinase 4.
/FTId=PRO_0000398589.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.
TRANSMEM 125 145 Helical. {ECO:0000255}.
TOPO_DOM 146 429 Extracellular. {ECO:0000255}.
TRANSMEM 430 450 Helical. {ECO:0000255}.
TOPO_DOM 451 1080 Cytoplasmic. {ECO:0000255}.
DOMAIN 198 411 CHASE. {ECO:0000255|PROSITE-
ProRule:PRU00049}.
DOMAIN 479 760 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
DOMAIN 786 920 Response regulatory 1.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 946 1071 Response regulatory 2.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
COMPBIAS 823 826 Poly-Ala.
BINDING 285 285 Cytokinin.
BINDING 307 307 Cytokinin; via amide nitrogen.
BINDING 317 317 Cytokinin.
MOD_RES 482 482 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107,
ECO:0000269|PubMed:16753566}.
MOD_RES 996 996 4-aspartylphosphate.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
VAR_SEQ 1 23 Missing (in isoform 2).
{ECO:0000303|PubMed:11114883,
ECO:0000303|PubMed:11230578,
ECO:0000303|PubMed:11234017}.
/FTId=VSP_039770.
VARIANT 765 765 S -> N (in strain: cv. Se-0).
{ECO:0000269|PubMed:17435248}.
MUTAGEN 225 225 A->L: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 227 227 A->L: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 273 273 Y->E: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 279 279 M->A: No effect on activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 285 285 D->A,E,R: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 301 301 T->I: In wol-1; locked in the
phosphoprotein phosphatase active form,
retardation of the primary root growth
with reduced cell number and exclusive
xylem differentiation within the vascular
tissue associated with abnormal vascular
asymmetric cell divisions, impaired
metaxylem and phloem differentiation, and
reduced cytokinin-binding ability leading
to impaired kinase activity and cyokinin-
mediated activation.
{ECO:0000269|PubMed:11114883,
ECO:0000269|PubMed:11577198,
ECO:0000269|PubMed:15053761,
ECO:0000269|PubMed:16753566,
ECO:0000269|PubMed:17956858,
ECO:0000269|PubMed:21964459}.
MUTAGEN 303 303 P->V: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 304 304 F->A: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 306 306 L->A: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 307 307 L->A: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 317 317 T->A: No effect on activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 343 343 G->L: Loss of activity.
{ECO:0000269|PubMed:21964459}.
MUTAGEN 435 435 G->C: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 436 436 F->S: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 447 447 M->T: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 459 459 M->I: In wol-3; retardation of the
primary root growth, no production of
lateral roots and enhanced formation of
adventitious roots associated with
impaired auxin basipetal transport.
{ECO:0000269|PubMed:16357038}.
MUTAGEN 471 471 V->A: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 482 482 H->Q: Reduced phosphoprotein phosphatase
activity. {ECO:0000269|PubMed:11234017,
ECO:0000269|PubMed:16753566}.
MUTAGEN 490 490 G->D: In cre1-1; impaired histidine-
kinase receptor activity and reduced
responses to cytokinins, including rapid
cell proliferation and shoot formation in
tissue culture, repression of sulfate
uptake, retardation of the primary root
growth, no production of lateral roots
and enhanced formation of adventitious
roots associated with impaired auxin
basipetal transport, as well as reduced
cell number within the vascular tissues
in roots. {ECO:0000269|PubMed:11234017,
ECO:0000269|PubMed:12354925,
ECO:0000269|PubMed:15144379,
ECO:0000269|PubMed:16357038}.
MUTAGEN 493 493 G->R: In cre1-6; reduced sensitivity to
cytokinin. {ECO:0000269|PubMed:12410813}.
MUTAGEN 494 494 M->L: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 529 529 L->F: In wol-2/raw1; impaired metaxylem
and phloem differentiation, and reduced
sensitivity to cytokinins.
{ECO:0000269|PubMed:15053761}.
MUTAGEN 529 529 L->F: In wol-2; retardation of the
primary root growth with reduced cell
number and exclusive xylem
differentiation within the vascular
tissue associated with abnormal vascular
asymmetric cell divisions, and impaired
cytokinin-binding ability.
{ECO:0000269|PubMed:15053761}.
MUTAGEN 708 708 F->L: No histidine kinase activity, but
normal phosphoprotein phosphatase
activity. {ECO:0000269|PubMed:16753566}.
MUTAGEN 996 996 D->N: Cytokinin-mediated
autophosphorylation but impaired
phosphotransfer to an HPt, abolished
phosphoprotein phosphatase activity.
{ECO:0000269|PubMed:11234017,
ECO:0000269|PubMed:16753566}.
MUTAGEN 1008 1008 T->I: In cre1-4; slightly reduced
sensitivity to cytokinin, and impaired
cytokinin repression of several Pi
starvation-responses.
{ECO:0000269|PubMed:12410813}.
MUTAGEN 1032 1032 A->T: In cre1-9; impaired cytokinin
repression of several Pi starvation-
responses. {ECO:0000269|PubMed:12410813}.
CONFLICT 567 567 S -> G (in Ref. 2; BAB33311).
{ECO:0000305}.
CONFLICT 1018 1018 T -> A (in Ref. 2; BAB33311).
{ECO:0000305}.
HELIX 151 193 {ECO:0000244|PDB:3T4L}.
TURN 194 196 {ECO:0000244|PDB:3T4L}.
STRAND 197 199 {ECO:0000244|PDB:3T4L}.
HELIX 204 213 {ECO:0000244|PDB:3T4L}.
HELIX 215 217 {ECO:0000244|PDB:3T4L}.
STRAND 221 228 {ECO:0000244|PDB:3T4L}.
HELIX 232 234 {ECO:0000244|PDB:3T4L}.
HELIX 235 242 {ECO:0000244|PDB:3T4L}.
TURN 249 251 {ECO:0000244|PDB:3T4L}.
STRAND 259 261 {ECO:0000244|PDB:3T4L}.
STRAND 263 267 {ECO:0000244|PDB:3T4L}.
HELIX 269 274 {ECO:0000244|PDB:3T4L}.
HELIX 279 281 {ECO:0000244|PDB:3T4L}.
HELIX 283 295 {ECO:0000244|PDB:3T4L}.
TURN 307 309 {ECO:0000244|PDB:3T4L}.
STRAND 312 321 {ECO:0000244|PDB:3T4L}.
HELIX 331 336 {ECO:0000244|PDB:3T4L}.
STRAND 338 346 {ECO:0000244|PDB:3T4L}.
HELIX 348 357 {ECO:0000244|PDB:3T4L}.
HELIX 362 364 {ECO:0000244|PDB:3T4L}.
STRAND 365 371 {ECO:0000244|PDB:3T4L}.
STRAND 379 382 {ECO:0000244|PDB:3T4L}.
STRAND 385 387 {ECO:0000244|PDB:3T4T}.
STRAND 395 399 {ECO:0000244|PDB:3T4L}.
STRAND 408 414 {ECO:0000244|PDB:3T4L}.
SEQUENCE 1080 AA; 120731 MW; 5950DB968B529401 CRC64;
MRRDFVYNNN AMFNPLTTHY SSDMNWALNN HQEEEEEPRR IEISDSESLE NLKSSDFYQL
GGGGALNSSE KPRKIDFWRS GLMGFAKMQQ QQQLQHSVAV KMNNNNNNDL MGNKKGSTFI
QEHRALLPKA LILWIIIVGF ISSGIYQWMD DANKIRREEV LVSMCDQRAR MLQDQFSVSV
NHVHALAILV STFHYHKNPS AIDQETFAEY TARTAFERPL LSGVAYAEKV VNFEREMFER
QHNWVIKTMD RGEPSPVRDE YAPVIFSQDS VSYLESLDMM SGEEDRENIL RARETGKAVL
TSPFRLLETH HLGVVLTFPV YKSSLPENPT VEERIAATAG YLGGAFDVES LVENLLGQLA
GNQAIVVHVY DITNASDPLV MYGNQDEEAD RSLSHESKLD FGDPFRKHKM ICRYHQKAPI
PLNVLTTVPL FFAIGFLVGY ILYGAAMHIV KVEDDFHEMQ ELKVRAEAAD VAKSQFLATV
SHEIRTPMNG ILGMLAMLLD TELSSTQRDY AQTAQVCGKA LIALINEVLD RAKIEAGKLE
LESVPFDIRS ILDDVLSLFS EESRNKSIEL AVFVSDKVPE IVKGDSGRFR QIIINLVGNS
VKFTEKGHIF VKVHLAEQSK DESEPKNALN GGVSEEMIVV SKQSSYNTLS GYEAADGRNS
WDSFKHLVSE EQSLSEFDIS SNVRLMVSIE DTGIGIPLVA QGRVFMPFMQ ADSSTSRNYG
GTGIGLSISK CLVELMRGQI NFISRPHIGS TFWFTAVLEK CDKCSAINHM KKPNVEHLPS
TFKGMKAIVV DAKPVRAAVT RYHMKRLGIN VDVVTSLKTA VVAAAAFERN GSPLPTKPQL
DMILVEKDSW ISTEDNDSEI RLLNSRTNGN VHHKSPKLAL FATNITNSEF DRAKSAGFAD
TVIMKPLRAS MIGACLQQVL ELRKTRQQHP EGSSPATLKS LLTGKKILVV DDNIVNRRVA
AGALKKFGAE VVCAESGQVA LGLLQIPHTF DACFMDIQMP QMDGFEATRQ IRMMEKETKE
KTNLEWHLPI LAMTADVIHA TYEECLKSGM DGYVSKPFEE ENLYKSVAKS FKPNPISPSS


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EIAAB45788 Bos taurus,Bovine,Diphosphoinositol pentakisphosphate kinase 1,HISPPD2A,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB34873 Ankrd3,Ankyrin repeat domain-containing protein 3,Mouse,Mus musculus,PKC-associated protein kinase,PKC-regulated protein kinase,Pkk,Receptor-interacting serine_threonine-protein kinase 4,Ripk4
EIAAB42378 Angiopoietin-1 receptor,Homo sapiens,hTIE2,Human,p140 TEK,TEK,TIE2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB42377 Angiopoietin-1 receptor,HYK,Hyk,Mouse,mTIE2,Mus musculus,p140 TEK,STK1,Tek,Tie2,Tie-2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
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
EIAAB26650 Canis familiaris,Canis lupus familiaris,Dog,Histidine protein kinase NDKB,NDK B,NDP kinase B,NM23B,nm23-C2,NME2,Nucleoside diphosphate kinase B
EIAAB40306 Homo sapiens,Human,Serine_threonine-protein kinase 25,SOK1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,STK25,YSK1
EIAAB40307 Mouse,Mus musculus,Serine_threonine-protein kinase 25,Sok1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,Stk25
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4


 

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