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Q9C5U0 (AHK4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine kinase 4

EC=2.7.13.3
Alternative name(s):
Arabidopsis histidine kinase 4
Short name=AtHK4
Cytokinin receptor CYTOKININ RESPONSE 1
Short name=AtCRE1
Short name=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
Gene names
Name:AHK4
Synonyms:CRE1, RAW1, WOL
Ordered Locus Names:At2g01830
ORF Names:T23K3.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1080 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokinins (CK) receptor related to bacterial two-component regulators. 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, feed 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 development process 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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

[a protein]-serine/threonine phosphate + H2O = [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). Ref.2 Ref.36 Ref.38

Subunit structure

Interacts with AHP1, AHP2, AHP3, AHP5, AHK3, AMPD, WNK5 and At4g15630. Ref.7 Ref.24 Ref.33

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

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. Ref.1 Ref.3 Ref.15 Ref.19

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. Ref.1 Ref.15 Ref.23

Induction

Rapidly induced by dehydration. Down-regulated by Pi starvation and induced by cytokinins. Ref.2 Ref.13 Ref.30 Ref.36 Ref.38

Post-translational modification

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. Ref.23

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. Ref.8 Ref.13 Ref.15 Ref.19 Ref.21 Ref.23 Ref.26 Ref.27 Ref.30 Ref.31 Ref.35 Ref.37

Sequence similarities

Contains 1 CHASE domain.

Contains 1 histidine kinase domain.

Contains 1 response regulatory domain.

Biophysicochemical properties

pH dependence:

Optimum pH to bind cytokinin is about 7-8.5 at 0 degrees Celsius. Ref.20 Ref.25

Temperature dependence:

Cytokinin-binding is more stable at 0 degrees Celsius than at 20 and 37 degrees Celsius.

Ontologies

Keywords
   Biological processCytokinin signaling pathway
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Hydrolase
Kinase
Protein phosphatase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate homeostasis

Inferred from mutant phenotype PubMed 22422940. Source: TAIR

cellular response to phosphate starvation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

cellular response to sucrose stimulus

Inferred from mutant phenotype Ref.21. Source: UniProtKB

cytokinin-activated signaling pathway

Traceable author statement Ref.14. Source: TAIR

defense response to bacterium

Inferred from direct assay PubMed 19129491. Source: TAIR

dephosphorylation

Inferred from direct assay Ref.23. Source: GOC

embryonic root morphogenesis

Inferred from mutant phenotype Ref.1. Source: TAIR

osmosensory signaling pathway

Inferred from mutant phenotype PubMed 22422940. Source: TAIR

peptidyl-histidine phosphorylation

Inferred from direct assay Ref.23. Source: GOC

phosphorelay signal transduction system

Inferred from direct assay Ref.7. Source: UniProtKB

protein phosphorylation

Inferred from genetic interaction Ref.23. Source: TAIR

regulation of meristem development

Inferred from mutant phenotype Ref.37. Source: UniProtKB

regulation of seed germination

Inferred from mutant phenotype Ref.26. Source: TAIR

regulation of shoot system development

Inferred from mutant phenotype Ref.26. Source: TAIR

response to water deprivation

Inferred from expression pattern Ref.30. Source: TAIR

sulfate transport

Inferred from mutant phenotype Ref.18. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 22923678. Source: TAIR

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

cytokine binding

Inferred from direct assay Ref.20. Source: TAIR

cytokinin receptor activity

Traceable author statement PubMed 14503005Ref.26. Source: TAIR

enzyme binding

Inferred from physical interaction Ref.33. Source: UniProtKB

osmosensor activity

Inferred from genetic interaction Ref.30. Source: TAIR

phosphoprotein phosphatase activity

Inferred from direct assay Ref.23. Source: TAIR

phosphorelay response regulator activity

Inferred from electronic annotation. Source: InterPro

phosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

protein histidine kinase activity

Inferred from direct assay Ref.23. Source: TAIR

protein histidine kinase binding

Inferred from physical interaction Ref.24. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.33. Source: UniProtKB

transmembrane histidine kinase cytokinin receptor activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C5U0-1)

Also known as: CRE1b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9C5U0-2)

Also known as: CRE1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10801080Histidine kinase 4
PRO_0000398589

Regions

Topological domain1 – 124124Cytoplasmic Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 429284Extracellular Potential
Transmembrane430 – 45021Helical; Potential
Topological domain451 – 1080630Cytoplasmic Potential
Domain198 – 411214CHASE
Domain479 – 760282Histidine kinase
Domain946 – 1071126Response regulatory
Compositional bias823 – 8264Poly-Ala

Amino acid modifications

Modified residue4821Phosphohistidine; by autocatalysis By similarity
Modified residue99614-aspartylphosphate By similarity

Natural variations

Alternative sequence1 – 2323Missing in isoform 2.
VSP_039770
Natural variant7651S → N in strain: cv. Se-0. Ref.6

Experimental info

Mutagenesis3011T → 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. Ref.1 Ref.9 Ref.17 Ref.23 Ref.29
Mutagenesis4351G → C: Constitutively activated independently of cytokinin. Ref.29
Mutagenesis4361F → S: Constitutively activated independently of cytokinin. Ref.29
Mutagenesis4471M → T: Constitutively activated independently of cytokinin. Ref.29
Mutagenesis4591M → 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. Ref.27
Mutagenesis4711V → A: Constitutively activated independently of cytokinin. Ref.29
Mutagenesis4821H → Q: Reduced phosphoprotein phosphatase activity. Ref.2 Ref.23
Mutagenesis4901G → 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. Ref.2 Ref.12 Ref.18 Ref.27
Mutagenesis4931G → R in cre1-6; reduced sensitivity to cytokinin. Ref.13
Mutagenesis4941M → L: Constitutively activated independently of cytokinin. Ref.29
Mutagenesis5291L → F in wol-2/raw1; impaired metaxylem and phloem differentiation, and reduced sensitivity to cytokinins. Ref.17
Mutagenesis5291L → 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. Ref.17
Mutagenesis7081F → L: No histidine kinase activity, but normal phosphoprotein phosphatase activity. Ref.23
Mutagenesis9961D → N: Cytokinin-mediated autophosphorylation but impaired phosphotransfer to an HPt, abolished phosphoprotein phosphatase activity. Ref.2 Ref.23
Mutagenesis10081T → I in cre1-4; slightly reduced sensitivity to cytokinin, and impaired cytokinin repression of several Pi starvation-responses. Ref.13
Mutagenesis10321A → T in cre1-9; impaired cytokinin repression of several Pi starvation-responses. Ref.13
Sequence conflict5671S → G in BAB33311. Ref.2
Sequence conflict10181T → A in BAB33311. Ref.2

Secondary structure

............................................... 1080
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CRE1b) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5950DB968B529401

FASTA1,080120,731
        10         20         30         40         50         60 
MRRDFVYNNN AMFNPLTTHY SSDMNWALNN HQEEEEEPRR IEISDSESLE NLKSSDFYQL 

        70         80         90        100        110        120 
GGGGALNSSE KPRKIDFWRS GLMGFAKMQQ QQQLQHSVAV KMNNNNNNDL MGNKKGSTFI 

       130        140        150        160        170        180 
QEHRALLPKA LILWIIIVGF ISSGIYQWMD DANKIRREEV LVSMCDQRAR MLQDQFSVSV 

       190        200        210        220        230        240 
NHVHALAILV STFHYHKNPS AIDQETFAEY TARTAFERPL LSGVAYAEKV VNFEREMFER 

       250        260        270        280        290        300 
QHNWVIKTMD RGEPSPVRDE YAPVIFSQDS VSYLESLDMM SGEEDRENIL RARETGKAVL 

       310        320        330        340        350        360 
TSPFRLLETH HLGVVLTFPV YKSSLPENPT VEERIAATAG YLGGAFDVES LVENLLGQLA 

       370        380        390        400        410        420 
GNQAIVVHVY DITNASDPLV MYGNQDEEAD RSLSHESKLD FGDPFRKHKM ICRYHQKAPI 

       430        440        450        460        470        480 
PLNVLTTVPL FFAIGFLVGY ILYGAAMHIV KVEDDFHEMQ ELKVRAEAAD VAKSQFLATV 

       490        500        510        520        530        540 
SHEIRTPMNG ILGMLAMLLD TELSSTQRDY AQTAQVCGKA LIALINEVLD RAKIEAGKLE 

       550        560        570        580        590        600 
LESVPFDIRS ILDDVLSLFS EESRNKSIEL AVFVSDKVPE IVKGDSGRFR QIIINLVGNS 

       610        620        630        640        650        660 
VKFTEKGHIF VKVHLAEQSK DESEPKNALN GGVSEEMIVV SKQSSYNTLS GYEAADGRNS 

       670        680        690        700        710        720 
WDSFKHLVSE EQSLSEFDIS SNVRLMVSIE DTGIGIPLVA QGRVFMPFMQ ADSSTSRNYG 

       730        740        750        760        770        780 
GTGIGLSISK CLVELMRGQI NFISRPHIGS TFWFTAVLEK CDKCSAINHM KKPNVEHLPS 

       790        800        810        820        830        840 
TFKGMKAIVV DAKPVRAAVT RYHMKRLGIN VDVVTSLKTA VVAAAAFERN GSPLPTKPQL 

       850        860        870        880        890        900 
DMILVEKDSW ISTEDNDSEI RLLNSRTNGN VHHKSPKLAL FATNITNSEF DRAKSAGFAD 

       910        920        930        940        950        960 
TVIMKPLRAS MIGACLQQVL ELRKTRQQHP EGSSPATLKS LLTGKKILVV DDNIVNRRVA 

       970        980        990       1000       1010       1020 
AGALKKFGAE VVCAESGQVA LGLLQIPHTF DACFMDIQMP QMDGFEATRQ IRMMEKETKE 

      1030       1040       1050       1060       1070       1080 
KTNLEWHLPI LAMTADVIHA TYEECLKSGM DGYVSKPFEE ENLYKSVAKS FKPNPISPSS 

« Hide

Isoform 2 (CRE1a) [UniParc].

Checksum: E1381C8685F0D787
Show »

FASTA1,057117,955

References

« Hide 'large scale' references
[1]"A novel two-component hybrid molecule regulates vascular morphogenesis of the Arabidopsis root."
Maehoenen A.P., Bonke M., Kauppinen L., Riikonen M., Benfey P.N., Helariutta Y.
Genes Dev. 14:2938-2943(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION, MUTAGENESIS OF THR-301.
Strain: cv. Columbia.
Tissue: Root.
[2]"Identification of CRE1 as a cytokinin receptor from Arabidopsis."
Inoue T., Higuchi M., Hashimoto Y., Seki M., Kobayashi M., Kato T., Tabata S., Shinozaki K., Kakimoto T.
Nature 409:1060-1063(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-482; GLY-490 AND ASP-996.
Strain: cv. Wassilewskija.
Tissue: Seedling.
[3]"Novel family of sensor histidine kinase genes in Arabidopsis thaliana."
Ueguchi C., Koizumi H., Suzuki T., Mizuno T.
Plant Cell Physiol. 42:231-235(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[4]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"The genetic architecture of shoot branching in Arabidopsis thaliana: a comparative assessment of candidate gene associations vs. quantitative trait locus mapping."
Ehrenreich I.M., Stafford P.A., Purugganan M.D.
Genetics 176:1223-1236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 722-983, 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.
[7]"The Arabidopsis sensor His-kinase, AHk4, can respond to cytokinins."
Suzuki T., Miwa K., Ishikawa K., Yamada H., Aiba H., Mizuno T.
Plant Cell Physiol. 42:107-113(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AHP1; AHP2; AHP3 AND AHP5.
[8]"The AHK4 gene involved in the cytokinin-signaling pathway as a direct receptor molecule in Arabidopsis thaliana."
Ueguchi C., Sato S., Kato T., Tabata S.
Plant Cell Physiol. 42:751-755(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that transduces cytokinin signals across the membrane."
Yamada H., Suzuki T., Terada K., Takei K., Ishikawa K., Miwa K., Yamashino T., Mizuno T.
Plant Cell Physiol. 42:1017-1023(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIVATION BY CYTOKININS, MUTAGENESIS OF THR-301.
[10]"CREam of cytokinin signalling: receptor identified."
Schmuelling T.
Trends Plant Sci. 6:281-284(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"His-Asp phosphorelay signal transduction in higher plants: receptors and response regulators for cytokinin signaling in Arabidopsis thaliana."
Oka A., Sakai H., Iwakoshi S.
Genes Genet. Syst. 77:383-391(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"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."
Kiba T., Yamada H., Mizuno T.
Plant Cell Physiol. 43:1059-1066(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-490.
[13]"Mutations at CRE1 impair cytokinin-induced repression of phosphate starvation responses in Arabidopsis."
Franco-Zorrilla J.M., Martin A.C., Solano R., Rubio V., Leyva A., Paz-Ares J.
Plant J. 32:353-360(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF GLY-493; THR-1008 AND ALA-1032.
[14]"Two-component signal transduction pathways in Arabidopsis."
Hwang I., Chen H.-C., Sheen J.
Plant Physiol. 129:500-515(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[15]"Histidine kinase homologs that act as cytokinin receptors possess overlapping functions in the regulation of shoot and root growth in Arabidopsis."
Nishimura C., Ohashi Y., Sato S., Kato T., Tabata S., Ueguchi C.
Plant Cell 16:1365-1377(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[16]"Two cytokinin receptors of Arabidopsis thaliana, CRE1/AHK4 and AHK3, differ in their ligand specificity in a bacterial assay."
Spichal L., Rakova N.Y., Riefler M., Mizuno T., Romanov G.A., Strnad M., Schmuelling T.
Plant Cell Physiol. 45:1299-1305(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Interallelic complementation at the Arabidopsis CRE1 locus uncovers independent pathways for the proliferation of vascular initials and canonical cytokinin signalling."
de Leon B.G.-P., Zorrilla J.M.F., Rubio V., Dahiya P., Paz-Ares J., Leyva A.
Plant J. 38:70-79(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-301 AND LEU-529.
[18]"A novel regulatory pathway of sulfate uptake in Arabidopsis roots: implication of CRE1/WOL/AHK4-mediated cytokinin-dependent regulation."
Maruyama-Nakashita A., Nakamura Y., Yamaya T., Takahashi H.
Plant J. 38:779-789(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-490.
[19]"In planta functions of the Arabidopsis cytokinin receptor family."
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.
Proc. Natl. Acad. Sci. U.S.A. 101:8821-8826(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[20]"A live cell hormone-binding assay on transgenic bacteria expressing a eukaryotic receptor protein."
Romanov G.A., Spichal L., Lomin S.N., Strnad M., Schmuelling T.
Anal. Biochem. 347:129-134(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[21]"Interaction between phosphate-starvation, sugar, and cytokinin signaling in Arabidopsis and the roles of cytokinin receptors CRE1/AHK4 and AHK3."
Franco-Zorrilla J.M., Martin A.C., Leyva A., Paz-Ares J.
Plant Physiol. 138:847-857(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[22]"Topolins and hydroxylated thidiazuron derivatives are substrates of cytokinin O-glucosyltransferase with position specificity related to receptor recognition."
Mok M.C., Martin R.C., Dobrev P.I., Vankova R., Ho P.S., Yonekura-Sakakibara K., Sakakibara H., Mok D.W.
Plant Physiol. 137:1057-1066(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Cytokinins regulate a bidirectional phosphorelay network in Arabidopsis."
Maehoenen A.P., Higuchi M., Toermaekangas K., Miyawaki K., Pischke M.S., Sussman M.R., Helariutta Y., Kakimoto T.
Curr. Biol. 16:1116-1122(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION AT HIS-482, MUTAGENESIS OF THR-301; HIS-482; PHE-708 AND ASP-996, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[24]"Analysis of protein interactions within the cytokinin-signaling pathway of Arabidopsis thaliana."
Dortay H., Mehnert N., Buerkle L., Schmuelling T., Heyl A.
FEBS J. 273:4631-4644(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AHP1; AHP2; AHP3; AHP5 AND AHK3.
[25]"Biochemical characteristics and ligand-binding properties of Arabidopsis cytokinin receptor AHK3 compared to CRE1/AHK4 as revealed by a direct binding assay."
Romanov G.A., Lomin S.N., Schmuelling T.
J. Exp. Bot. 57:4051-4058(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[26]"Arabidopsis cytokinin receptor mutants reveal functions in shoot growth, leaf senescence, seed size, germination, root development, and cytokinin metabolism."
Riefler M., Novak O., Strnad M., Schmuelling T.
Plant Cell 18:40-54(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[27]"Cytokinin receptors are required for normal development of auxin-transporting vascular tissues in the hypocotyl but not in adventitious roots."
Kuroha T., Ueguchi C., Sakakibara H., Satoh S.
Plant Cell Physiol. 47:234-243(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF MET-459 AND GLY-490.
[28]"The floral volatile, methyl benzoate, from snapdragon (Antirrhinum majus) triggers phytotoxic effects in Arabidopsis thaliana."
Horiuchi J., Badri D.V., Kimball B.A., Negre F., Dudareva N., Paschke M.W., Vivanco J.M.
Planta 226:1-10(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Identification of amino acid substitutions that render the Arabidopsis cytokinin receptor histidine kinase AHK4 constitutively active."
Miwa K., Ishikawa K., Terada K., Yamada H., Suzuki T., Yamashino T., Mizuno T.
Plant Cell Physiol. 48:1809-1814(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-301; GLY-435; PHE-436; MET-447; VAL-471 AND MET-494.
[30]"Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases in response to abscisic acid, drought, and salt stress in Arabidopsis."
Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K., Yamaguchi-Shinozaki K.
Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
[31]"Cytokinin receptors are involved in alkamide regulation of root and shoot development in Arabidopsis."
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.
Plant Physiol. 145:1703-1713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[32]"Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor."
Kopecny D., Sebela M., Briozzo P., Spichal L., Houba-Herin N., Masek V., Joly N., Madzak C., Anzenbacher P., Laloue M.
J. Mol. Biol. 380:886-899(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"Toward an interaction map of the two-component signaling pathway of Arabidopsis thaliana."
Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.
J. Proteome Res. 7:3649-3660(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AHP2; AMPD; WNK5 AND AT4G15630.
[34]"The role of auxins and cytokinins in the mutualistic interaction between Arabidopsis and Piriformospora indica."
Vadassery J., Ritter C., Venus Y., Camehl I., Varma A., Shahollari B., Novak O., Strnad M., Ludwig-Mueller J., Oelmueller R.
Mol. Plant Microbe Interact. 21:1371-1383(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[35]"Cytokinins negatively regulate the root iron uptake machinery in Arabidopsis through a growth-dependent pathway."
Seguela M., Briat J.-F., Vert G., Curie C.
Plant J. 55:289-300(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[36]"The purine derivative PI-55 blocks cytokinin action via receptor inhibition."
Spichal L., Werner T., Popa I., Riefler M., Schmuelling T., Strnad M.
FEBS J. 276:244-253(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[37]"STIMPY mediates cytokinin signaling during shoot meristem establishment in Arabidopsis seedlings."
Skylar A., Hong F., Chory J., Weigel D., Wu X.
Development 137:541-549(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[38]"Cytokinin receptor antagonists derived from 6-benzylaminopurine."
Nisler J., Zatloukal M., Popa I., Dolezal K., Strnad M., Spichal L.
Phytochemistry 71:823-830(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278528 mRNA. Translation: CAC18521.1.
AJ278529 mRNA. Translation: CAC18522.1.
AJ278530 mRNA. Translation: CAC18523.1.
AB049934 mRNA. Translation: BAB33310.1.
AB049935 mRNA. Translation: BAB33311.1.
AB046871 mRNA. Translation: BAB40776.1.
AC007069 Genomic DNA. Translation: AAD21777.2.
CP002685 Genomic DNA. Translation: AEC05505.1.
CP002685 Genomic DNA. Translation: AEC05506.1.
CP002685 Genomic DNA. Translation: AEC05507.1.
EF598292 Genomic DNA. Translation: ABQ85264.1.
EF598293 Genomic DNA. Translation: ABQ85265.1.
EF598294 Genomic DNA. Translation: ABQ85266.1.
EF598295 Genomic DNA. Translation: ABQ85267.1.
EF598296 Genomic DNA. Translation: ABQ85268.1.
EF598297 Genomic DNA. Translation: ABQ85269.1.
EF598298 Genomic DNA. Translation: ABQ85270.1.
EF598299 Genomic DNA. Translation: ABQ85271.1.
EF598300 Genomic DNA. Translation: ABQ85272.1.
EF598301 Genomic DNA. Translation: ABQ85273.1.
EF598302 Genomic DNA. Translation: ABQ85274.1.
EF598303 Genomic DNA. Translation: ABQ85275.1.
EF598304 Genomic DNA. Translation: ABQ85276.1.
EF598305 Genomic DNA. Translation: ABQ85277.1.
EF598306 Genomic DNA. Translation: ABQ85278.1.
EF598307 Genomic DNA. Translation: ABQ85279.1.
EF598308 Genomic DNA. Translation: ABQ85280.1.
EF598309 Genomic DNA. Translation: ABQ85281.1.
EF598310 Genomic DNA. Translation: ABQ85282.1.
EF598311 Genomic DNA. Translation: ABQ85283.1.
EF598312 Genomic DNA. Translation: ABQ85284.1.
EF598313 Genomic DNA. Translation: ABQ85285.1.
EF598314 Genomic DNA. Translation: ABQ85286.1.
EF598315 Genomic DNA. Translation: ABQ85287.1.
PIRF84429.
RefSeqNP_565277.1. NM_126244.2.
NP_849925.1. NM_179594.1.
NP_973396.1. NM_201667.1.
UniGeneAt.10485.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T4JX-ray1.65A/B149-418[»]
3T4KX-ray1.77A/B149-418[»]
3T4LX-ray1.53A/B149-418[»]
3T4OX-ray1.75A/B149-418[»]
3T4QX-ray2.30A/B149-418[»]
3T4SX-ray1.60A/B149-418[»]
3T4TX-ray1.70A/B149-418[»]
ProteinModelPortalQ9C5U0.
SMRQ9C5U0. Positions 150-416, 465-752, 780-923, 941-1060.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117. 30 interactions.
IntActQ9C5U0. 29 interactions.
STRING3702.AT2G01830.2-P.

Chemistry

BindingDBQ9C5U0.
ChEMBLCHEMBL6124.

Proteomic databases

PaxDbQ9C5U0.
PRIDEQ9C5U0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G01830.2; AT2G01830.2; AT2G01830. [Q9C5U0-1]
GeneID814714.
KEGGath:AT2G01830.

Organism-specific databases

TAIRAT2G01830.

Phylogenomic databases

eggNOGCOG0784.
InParanoidQ9C5U0.
KOK14489.
OMAADTVIMK.
PhylomeDBQ9C5U0.
ProtClustDBCLSN2687668.

Enzyme and pathway databases

BioCycARA:AT2G01830-MONOMER.
ARA:GQT-91-MONOMER.
ARA:GQT-92-MONOMER.

Gene expression databases

GenevestigatorQ9C5U0.

Family and domain databases

Gene3D1.10.287.130. 1 hit.
3.30.565.10. 2 hits.
InterProIPR006189. CHASE.
IPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF03924. CHASE. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55874. SSF55874. 2 hits.
PROSITEPS50839. CHASE. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9C5U0.

Entry information

Entry nameAHK4_ARATH
AccessionPrimary (citable) accession number: Q9C5U0
Secondary accession number(s): A5YY60 expand/collapse secondary AC list , A5YY75, Q9C5T8, Q9C5T9, Q9FDZ3, Q9SIT0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names