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Protein

Histidine kinase 3

Gene

AHK3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Involved in meristems establishment in seedlings. Redundant negative regulator of drought and salt stress responses and abscisic acid (ABA) signaling. Together with AHK2, plays a negative regulatory role in cold stress signaling via inhibition of ABA response, occurring independently of the cold acclimation pathway. 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), cis-zeatin (cZ), dihydrozeatin (DZ), 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-propynyladenine (RM3), 2-butynyladenine (RM6), and cytokinin ribosides and ribotides. Together with AHK4, involved in the cytokinin-dependent responses to Pi starvation and sucrose stresses. Promotes cytokinin-mediated leaf longevity through a specific phosphorylation of the response regulator ARR2. Involved in alkamides (e.g. N-isobutyl decanamide) and N-acylethanolamides (NAE) signaling that control meristematic activity and differentiation processes during plant development. Contributes to vascular bundle formation and secondary growth in a cytokinin-dependent manner, probably by promoting the maintenance of mitotic activity and/or identity of procambial cells. Plays a role in the cytokinin-mediated repression of the iron uptake pathway. Required by the cytokinin-dependent flower development regulation pathway.19 Publications

Catalytic activityi

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

Enzyme regulationi

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).2 Publications

pH dependencei

Optimum pH to bind cytokinin is about 8.5 at 0 degrees Celsius.1 Publication

Temperature dependencei

Cytokinin-binding is stable at 0 degrees Celsius but transient at 37 degrees Celsius.1 Publication

GO - Molecular functioni

  • cytokinin receptor activity Source: TAIR
  • phosphorelay sensor kinase activity Source: InterPro
  • protein histidine kinase activity Source: UniProtKB
  • protein histidine kinase binding Source: UniProtKB

GO - Biological processi

  • cellular response to abscisic acid stimulus Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to phosphate starvation Source: UniProtKB
  • cellular response to sucrose stimulus Source: UniProtKB
  • cytokinin-activated signaling pathway Source: TAIR
  • defense response to bacterium Source: TAIR
  • leaf senescence Source: TAIR
  • negative regulation of iron ion transport Source: UniProtKB
  • peptidyl-histidine phosphorylation Source: GOC
  • phloem or xylem histogenesis Source: UniProtKB
  • regulation of chlorophyll catabolic process Source: TAIR
  • regulation of flower development Source: UniProtKB
  • regulation of meristem development Source: UniProtKB
  • regulation of seed germination Source: TAIR
  • regulation of shoot system development Source: TAIR
  • response to cold Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to water deprivation Source: TAIR
  • secondary growth Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase

Keywords - Biological processi

Cytokinin signaling pathway

Enzyme and pathway databases

BioCyciARA:AT1G27320-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine kinase 3 (EC:2.7.13.3)
Alternative name(s):
Arabidopsis histidine kinase 3
Short name:
AtHK3
Protein AUTHENTIC HIS-KINASE 3
Protein ORESARA 12
Gene namesi
Name:AHK3
Synonyms:ORE12
Ordered Locus Names:At1g27320
ORF Names:F17L21.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G27320.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88ExtracellularSequence analysis
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Topological domaini30 – 9465CytoplasmicSequence analysisAdd
BLAST
Transmembranei95 – 11521HelicalSequence analysisAdd
BLAST
Topological domaini116 – 399284ExtracellularSequence analysisAdd
BLAST
Transmembranei400 – 42021HelicalSequence analysisAdd
BLAST
Topological domaini421 – 1036616CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Hypersensitivity to ABA, and strong drought and salinity tolerance. Reduced sensitivity to cytokinin (mostly in roots). More rapid germination, reduced requirement for light, and decreased far-red light sensitivity. Early senescence promoted by darkness. Reduced sensitivity to N-isobutyl decanamide. Defects in procambium proliferation and absence of secondary growth. Enhanced freezing tolerance. Impaired benzyladenine (6-BA)-mediated repression of the iron uptake pathway. Disturbed cytokinin-mediated flower development abnormality. Impaired meristematic development in seedlings.11 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi243 – 2431P → S in ore12-1; delayed leaf senescence and abolished cytokinin-dependent phosphorylation activity toward ARR2. 1 Publication
Mutagenesisi281 – 2811T → I: Loss of cyokinin-mediated activation. 1 Publication
Mutagenesisi448 – 4481D → N: Delayed leaf senescence. 1 Publication
Mutagenesisi449 – 4491V → A: Constitutively activated independently of cytokinin. 1 Publication
Mutagenesisi713 – 7131S → F in ahk3-4; reduced sensitivity to cytokinin (mostly in roots), and impaired cytokinin repression of several Pi starvation-responsive genes and increased sucrose sensitivity. 1 Publication

Chemistry

ChEMBLiCHEMBL6125.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10361036Histidine kinase 3PRO_0000398588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei460 – 4601Phosphohistidine; by autocatalysisPROSITE-ProRule annotation
Modified residuei941 – 94114-aspartylphosphatePROSITE-ProRule annotation

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9C5U1.
PRIDEiQ9C5U1.

Expressioni

Tissue specificityi

Mostly expressed in leaves and flowers, and, to a lower extent, in roots, stems, and siliques, especially in the vascular tissues. Present in seedlings.3 Publications

Developmental stagei

In seedlings, mainly localized in meristematic tissues (e.g. shoot apical meristem SAM, root tips, and growing leaf and lateral root primordia). Present in all the vasculature and the shoot apical meristem (SAM) of the adult plant. In the root tips, strongest expression in the procambium.2 Publications

Inductioni

Rapidly induced by dehydration, high salinity and cold stresses.1 Publication

Gene expression databases

GenevisibleiQ9C5U1. AT.

Interactioni

Subunit structurei

Interacts with AHK2, AHK4, AHP1, AHP2, AHP3, AHP5 and At5g43560.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AHK2Q9C5U22EBI-1100653,EBI-1100634
AHK4Q9C5U02EBI-1100653,EBI-1100775
AHP1Q9ZNV92EBI-1100653,EBI-1100673
AHP2Q9ZNV82EBI-1100653,EBI-1100687
AHP3Q9SAZ52EBI-1100653,EBI-1100711
At1g03430Q67XQ13EBI-1100653,EBI-1100725

GO - Molecular functioni

  • protein histidine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi24856. 7 interactions.
IntActiQ9C5U1. 7 interactions.
STRINGi3702.AT1G27320.1.

Chemistry

BindingDBiQ9C5U1.

Structurei

3D structure databases

ProteinModelPortaliQ9C5U1.
SMRiQ9C5U1. Positions 121-394, 447-716, 891-1029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 389227CHASEPROSITE-ProRule annotationAdd
BLAST
Domaini457 – 723267Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini746 – 865120Response regulatory 1PROSITE-ProRule annotationAdd
BLAST
Domaini891 – 1028138Response regulatory 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CHASE domain.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 2 response regulatory domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
COG0642. LUCA.
HOGENOMiHOG000116474.
InParanoidiQ9C5U1.
KOiK14489.
OMAiMILIEQE.
PhylomeDBiQ9C5U1.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 2 hits.
InterProiIPR006189. CHASE_dom.
IPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF03924. CHASE. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 2 hits.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55874. SSF55874. 2 hits.
PROSITEiPS50839. CHASE. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C5U1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFHVLGFG VKIGHLFWML CCWFVSWFVD NGIEDKSGLL VGSVGDLEKT
60 70 80 90 100
KMTTLKKKNK MWFWNKISSS GLKIPSFSYQ FLGSVKFNKA WWRKLVVVWV
110 120 130 140 150
VFWVLVSIWT FWYFSSQAME KRKETLASMC DERARMLQDQ FNVSMNHVQA
160 170 180 190 200
MSILISTFHH GKIPSAIDQR TFSEYTDRTS FERPLTSGVA YAMRVLHSER
210 220 230 240 250
EEFERQQGWT IRKMYSLEQN PVHKDDYDLE ALEPSPVQEE YAPVIFAQDT
260 270 280 290 300
VSHVVSLDML SGKEDRENVL RARSSGKGVL TAPFPLIKTN RLGVILTFAV
310 320 330 340 350
YKRDLPSNAT PKERIEATNG YLGGVFDIES LVENLLQQLA SKQTILVNVY
360 370 380 390 400
DITNHSQPIS MYGTNVSADG LERVSPLIFG DPLRKHEMRC RFKQKPPWPV
410 420 430 440 450
LSMVTSFGIL VIALLVAHII HATVSRIHKV EEDCDKMKQL KKKAEAADVA
460 470 480 490 500
KSQFLATVSH EIRTPMNGVL GMLHMLMDTE LDVTQQDYVR TAQASGKALV
510 520 530 540 550
SLINEVLDQA KIESGKLELE EVRFDLRGIL DDVLSLFSSK SQQKGVELAV
560 570 580 590 600
YISDRVPDML IGDPGRFRQI LTNLMGNSIK FTEKGHIFVT VHLVDELFES
610 620 630 640 650
IDGETASSPE STLSGLPVAD RQRSWENFKA FSSNGHRSFE PSPPDINLIV
660 670 680 690 700
SVEDTGVGIP VEAQSRIFTP FMQVGPSISR THGGTGIGLS ISKCLVGLMK
710 720 730 740 750
GEIGFSSTPK VGSTFTFTAV FSNGMQPAER KNDNNQPIFS EFRGMKAVVV
760 770 780 790 800
DHRPARAKVS WYHFQRLGIR VEVVPRVEQA LHYLKIGTTT VNMILIEQEI
810 820 830 840 850
WNREADDFIK KLQKDPLFLS PKLILLANSV ESSISEALCT GIDPPIVIVK
860 870 880 890 900
PLRASMLAAT LQRGLGIGIR EPPQHKGPPA LILRNLLLGR KILIVDDNNV
910 920 930 940 950
NLRVAAGALK KYGADVVCAE SGIKAISLLK PPHEFDACFM DIQMPEMDGF
960 970 980 990 1000
EATRRIRDME EEMNKRIKNG EALIVENGNK TSWHLPVLAM TADVIQATHE
1010 1020 1030
ECLKCGMDGY VSKPFEAEQL YREVSRFFNS PSDTES
Length:1,036
Mass (Da):116,373
Last modified:June 1, 2001 - v1
Checksum:i03F23DEE4B44C40B
GO

Sequence cautioni

The sequence AAF99730.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046870 mRNA. Translation: BAB40775.1.
AC004557 Genomic DNA. Translation: AAF99730.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30806.1.
RefSeqiNP_564276.1. NM_102494.3.
UniGeneiAt.24547.

Genome annotation databases

EnsemblPlantsiAT1G27320.1; AT1G27320.1; AT1G27320.
GeneIDi839621.
GrameneiAT1G27320.1; AT1G27320.1; AT1G27320.
KEGGiath:AT1G27320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046870 mRNA. Translation: BAB40775.1.
AC004557 Genomic DNA. Translation: AAF99730.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30806.1.
RefSeqiNP_564276.1. NM_102494.3.
UniGeneiAt.24547.

3D structure databases

ProteinModelPortaliQ9C5U1.
SMRiQ9C5U1. Positions 121-394, 447-716, 891-1029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24856. 7 interactions.
IntActiQ9C5U1. 7 interactions.
STRINGi3702.AT1G27320.1.

Chemistry

BindingDBiQ9C5U1.
ChEMBLiCHEMBL6125.

Proteomic databases

PaxDbiQ9C5U1.
PRIDEiQ9C5U1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G27320.1; AT1G27320.1; AT1G27320.
GeneIDi839621.
GrameneiAT1G27320.1; AT1G27320.1; AT1G27320.
KEGGiath:AT1G27320.

Organism-specific databases

TAIRiAT1G27320.

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
COG0642. LUCA.
HOGENOMiHOG000116474.
InParanoidiQ9C5U1.
KOiK14489.
OMAiMILIEQE.
PhylomeDBiQ9C5U1.

Enzyme and pathway databases

BioCyciARA:AT1G27320-MONOMER.

Miscellaneous databases

PROiQ9C5U1.

Gene expression databases

GenevisibleiQ9C5U1. AT.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 2 hits.
InterProiIPR006189. CHASE_dom.
IPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF03924. CHASE. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 2 hits.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55874. SSF55874. 2 hits.
PROSITEiPS50839. CHASE. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], FUNCTION, TISSUE SPECIFICITY.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  10. "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, MUTAGENESIS OF SER-713.
  11. Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  12. "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; AHK2 AND AHK4.
  13. "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.
  14. "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.
  15. "Cytokinin-mediated control of leaf longevity by AHK3 through phosphorylation of ARR2 in Arabidopsis."
    Kim H.J., Ryu H., Hong S.H., Woo H.R., Lim P.O., Lee I.C., Sheen J., Nam H.G., Hwang I.
    Proc. Natl. Acad. Sci. U.S.A. 103:814-819(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PRO-243 AND ASP-448, SUBCELLULAR LOCATION.
  16. "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-281 AND VAL-449.
  17. "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.
  18. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  19. "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.
  20. "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 AT5G43560.
  21. "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.
  22. "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: ENZYME REGULATION.
  23. "The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS HISTIDINE KINASE2 and 3 regulate vascular tissue development in Arabidopsis shoots."
    Hejatko J., Ryu H., Kim G.-T., Dobesova R., Choi S., Choi S.M., Soucek P., Horak J., Pekarova B., Palme K., Brzobohaty B., Hwang I.
    Plant Cell 21:2008-2021(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  24. "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.
  25. "Cytokinin overproduction-caused alteration of flower development is partially mediated by CUC2 and CUC3 in Arabidopsis."
    Li X.G., Su Y.H., Zhao X.Y., Li W., Gao X.Q., Zhang X.S.
    Gene 450:109-120(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  26. "A subset of cytokinin two-component signaling system plays a role in cold temperature stress response in Arabidopsis."
    Jeon J., Kim N.Y., Kim S., Kang N.Y., Novak O., Ku S.-J., Cho C., Lee D.J., Lee E.-J., Strnad M., Kim J.
    J. Biol. Chem. 285:23371-23386(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  27. "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.
  28. "The cytokinin receptors of Arabidopsis are located mainly to the endoplasmic reticulum."
    Wulfetange K., Lomin S.N., Romanov G.A., Stolz A., Heyl A., Schmuelling T.
    Plant Physiol. 156:1808-1818(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiAHK3_ARATH
AccessioniPrimary (citable) accession number: Q9C5U1
Secondary accession number(s): Q9FZK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

'Oresara' means 'long living' in Korean.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.