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Protein

Histidine kinase 2

Gene

AHK2

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 AHK3, 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. 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. Together with AHK4, required for growth and reproduction promotion stimulated by the endophytic fungus Piriformospora indica in a trans-zeatin-dependent manner. Required by the cytokinin-dependent flower development regulation pathway.12 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by cytokinins to initiate phosphorelay signaling.By similarity

GO - Molecular functioni

  • cytokinin receptor activity Source: TAIR
  • identical protein binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • 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
  • cytokinin-activated signaling pathway Source: TAIR
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of iron ion transport Source: UniProtKB
  • 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 abscisic acid Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to toxic substance Source: UniProtKB
  • 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:AT5G35750-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine kinase 2 (EC:2.7.13.3)
Alternative name(s):
Arabidopsis histidine kinase 2
Short name:
AtHK2
Protein AUTHENTIC HIS-KINASE 2
Gene namesi
Name:AHK2
Ordered Locus Names:At5g35750
ORF Names:MXH1.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G35750.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929CytoplasmicSequence analysisAdd
BLAST
Transmembranei30 – 5021HelicalSequence analysisAdd
BLAST
Topological domaini51 – 174124ExtracellularSequence analysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence analysisAdd
BLAST
Topological domaini196 – 23237CytoplasmicSequence analysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence analysisAdd
BLAST
Topological domaini254 – 536283ExtracellularSequence analysisAdd
BLAST
Transmembranei537 – 55721HelicalSequence analysisAdd
BLAST
Topological domaini558 – 1176619CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Hypersensitivity to ABA, and strong drought and salinity tolerance. Slightly reduced sensitivity to cytokinin. More rapid germination, reduced requirement for light, and decreased far-red light sensitivity. Reduced sensitivity to N-isobutyl decanamide. Defects in procambium proliferation and absence of secondary growth. Enhanced freezing tolerance. Impaired meristematic development in seedlings. Disturbed cytokinin-mediated flower development abnormality.10 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi418 – 4181T → I: Loss of cyokinin-mediated activation. 1 Publication
Mutagenesisi586 – 5861I → A: Constitutively activated independently of cytokinin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11761176Histidine kinase 2PRO_0000398587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei597 – 5971Phosphohistidine; by autocatalysisPROSITE-ProRule annotation
Modified residuei942 – 94214-aspartylphosphatePROSITE-ProRule annotation
Modified residuei1086 – 108614-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

PaxDbiQ9C5U2.
PRIDEiQ9C5U2.

PTM databases

iPTMnetiQ9C5U2.

Expressioni

Tissue specificityi

Expressed in roots, leaves and flowers, mostly 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 flowers, localized in carpels and developing ovules. In the root tips, expressed in and near the vascular initial cells.2 Publications

Inductioni

Rapidly induced by dehydration, slightly induced by high salinity and abscisic acid (ABA).1 Publication

Gene expression databases

GenevisibleiQ9C5U2. AT.

Interactioni

Subunit structurei

Self-interacts. Interacts with AHK3, AHP1, AHP2, AHP3, AHP5, ATAF2, AT2S3, BETAA-AD, CYP20-2, DRP1A, HIR1, HIR2, PI4KB1, PI4KG5 and At4g12060.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1100634,EBI-1100634
AHK3Q9C5U12EBI-1100634,EBI-1100653
AHP1Q9ZNV92EBI-1100634,EBI-1100673
AHP2Q9ZNV83EBI-1100634,EBI-1100687
AHP3Q9SAZ53EBI-1100634,EBI-1100711
ARR14Q8L9Y33EBI-1100634,EBI-1100737
At1g03430Q67XQ13EBI-1100634,EBI-1100725
AT2S3P154592EBI-1100634,EBI-1807552
DRP1AP426973EBI-1100634,EBI-994234
HIR1Q9FM192EBI-1100634,EBI-1807466
HIR2Q9CAR72EBI-1100634,EBI-1807580
PI4KB1Q9FMJ02EBI-1100634,EBI-1807432
PNSL5Q9ASS62EBI-1100634,EBI-1807485

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • protein histidine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi18805. 44 interactions.
IntActiQ9C5U2. 45 interactions.
STRINGi3702.AT5G35750.1.

Structurei

3D structure databases

ProteinModelPortaliQ9C5U2.
SMRiQ9C5U2. Positions 259-529, 579-860, 1037-1169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini302 – 526225CHASEPROSITE-ProRule annotationAdd
BLAST
Domaini594 – 867274Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini891 – 1013123Response regulatory 1PROSITE-ProRule annotationAdd
BLAST
Domaini1036 – 1173138Response 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

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
COG0642. LUCA.
HOGENOMiHOG000116474.
InParanoidiQ9C5U2.
KOiK14489.
OMAiGNSMKFT.
PhylomeDBiQ9C5U2.

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. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C5U2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITCELLNL TSKKAKKSSS SDKKWLKKPL FFLILCGSLV IVLVMFLRLG
60 70 80 90 100
RSQKEETDSC NGEEKVLYRH QNVTRSEIHD LVSLFSDSDQ VTSFECHKES
110 120 130 140 150
SPGMWTNYGI TCSLSVRSDK QETRGLPWNL GLGHSISSTS CMCGNLEPIL
160 170 180 190 200
QQPENLEEEN HEEGLEQGLS SYLRNAWWCL ILGVLVCHKI YVSHSKARGE
210 220 230 240 250
RKEKVHLQEA LAPKKQQQRA QTSSRGAGRW RKNILLLGIL GGVSFSVWWF
260 270 280 290 300
WDTNEEIIMK RRETLANMCD ERARVLQDQF NVSLNHVHAL SILVSTFHHG
310 320 330 340 350
KIPSAIDQRT FEEYTERTNF ERPLTSGVAY ALKVPHSERE KFEKEHGWAI
360 370 380 390 400
KKMETEDQTV VQDCVPENFD PAPIQDEYAP VIFAQETVSH IVSVDMMSGE
410 420 430 440 450
EDRENILRAR ASGKGVLTSP FKLLKSNHLG VVLTFAVYDT SLPPDATEEQ
460 470 480 490 500
RVEATIGYLG ASYDMPSLVE KLLHQLASKQ TIAVDVYDTT NTSGLIKMYG
510 520 530 540 550
SEIGDISEQH ISSLDFGDPS RNHEMHCRFK HKLPIPWTAI TPSILVLVIT
560 570 580 590 600
FLVGYILYEA INRIATVEED CQKMRELKAR AEAADIAKSQ FLATVSHEIR
610 620 630 640 650
TPMNGVLGML KMLMDTDLDA KQMDYAQTAH GSGKDLTSLI NEVLDQAKIE
660 670 680 690 700
SGRLELENVP FDMRFILDNV SSLLSGKANE KGIELAVYVS SQVPDVVVGD
710 720 730 740 750
PSRFRQIITN LVGNSIKFTQ ERGHIFISVH LADEVKEPLT IEDAVLKQRL
760 770 780 790 800
ALGCSESGET VSGFPAVNAW GSWKNFKTCY STESQNSDQI KLLVTVEDTG
810 820 830 840 850
VGIPVDAQGR IFTPFMQADS STSRTYGGTG IGLSISKRLV ELMQGEMGFV
860 870 880 890 900
SEPGIGSTFS FTGVFGKAET NTSITKLERF DLAIQEFTGL RALVIDNRNI
910 920 930 940 950
RAEVTRYELR RLGISADIVS SLRMACTCCI SKLENLAMIL IDKDAWNKEE
960 970 980 990 1000
FSVLDELFTR SKVTFTRVPK IFLLATSATL TERSEMKSTG LIDEVVIKPL
1010 1020 1030 1040 1050
RMSVLICCLQ ETLVNGKKRQ PNRQRRNLGH LLREKQILVV DDNLVNRRVA
1060 1070 1080 1090 1100
EGALKKYGAI VTCVESGKAA LAMLKPPHNF DACFMDLQMP EMDGFEATRR
1110 1120 1130 1140 1150
VRELEREINK KIASGEVSAE MFCKFSSWHV PILAMTADVI QATHEECMKC
1160 1170
GMDGYVSKPF EEEVLYTAVA RFFEPC
Length:1,176
Mass (Da):131,860
Last modified:June 1, 2001 - v1
Checksum:iAC0019CC612361BC
GO

Sequence cautioni

The sequence AAO00890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB09274.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAD43496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1103 – 11031E → K in BAD43496 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046869 mRNA. Translation: BAB40774.1.
AB011485 Genomic DNA. Translation: BAB09274.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED94014.1.
BT002530 mRNA. Translation: AAO00890.1. Different initiation.
BT008407 mRNA. Translation: AAP37766.1.
AK175733 mRNA. Translation: BAD43496.1. Different initiation.
RefSeqiNP_568532.1. NM_122966.2.
UniGeneiAt.23233.

Genome annotation databases

EnsemblPlantsiAT5G35750.1; AT5G35750.1; AT5G35750.
GeneIDi833552.
GrameneiAT5G35750.1; AT5G35750.1; AT5G35750.
KEGGiath:AT5G35750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046869 mRNA. Translation: BAB40774.1.
AB011485 Genomic DNA. Translation: BAB09274.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED94014.1.
BT002530 mRNA. Translation: AAO00890.1. Different initiation.
BT008407 mRNA. Translation: AAP37766.1.
AK175733 mRNA. Translation: BAD43496.1. Different initiation.
RefSeqiNP_568532.1. NM_122966.2.
UniGeneiAt.23233.

3D structure databases

ProteinModelPortaliQ9C5U2.
SMRiQ9C5U2. Positions 259-529, 579-860, 1037-1169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi18805. 44 interactions.
IntActiQ9C5U2. 45 interactions.
STRINGi3702.AT5G35750.1.

PTM databases

iPTMnetiQ9C5U2.

Proteomic databases

PaxDbiQ9C5U2.
PRIDEiQ9C5U2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G35750.1; AT5G35750.1; AT5G35750.
GeneIDi833552.
GrameneiAT5G35750.1; AT5G35750.1; AT5G35750.
KEGGiath:AT5G35750.

Organism-specific databases

TAIRiAT5G35750.

Phylogenomic databases

eggNOGiKOG0519. Eukaryota.
COG0642. LUCA.
HOGENOMiHOG000116474.
InParanoidiQ9C5U2.
KOiK14489.
OMAiGNSMKFT.
PhylomeDBiQ9C5U2.

Enzyme and pathway databases

BioCyciARA:AT5G35750-MONOMER.

Miscellaneous databases

PROiQ9C5U2.

Gene expression databases

GenevisibleiQ9C5U2. 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. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM01079. CHASE. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[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. 2 hits.
[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], TISSUE SPECIFICITY.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
    Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:131-145(1998) [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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 519-1176.
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1095-1176.
    Strain: cv. Columbia.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  10. Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  11. "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: HOMODIMERIZATION, INTERACTION WITH AHK3; AHP1; AHP2; AHP3 AND AHP5.
  12. "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.
  13. "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-418 AND ILE-586.
  14. "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.
  15. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. "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 AT2S3; ATAF2; BETAA-AD; CYP20-2; DRP1A; HIR1; HIR2; PI4KB1; PI4KG5; AT4G12060; AHP3 AND AHP2.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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 nameiAHK2_ARATH
AccessioniPrimary (citable) accession number: Q9C5U2
Secondary accession number(s): Q680Y4, Q8GUG0, Q9FKH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.