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Q05609

- CTR1_ARATH

UniProt

Q05609 - CTR1_ARATH

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Protein

Serine/threonine-protein kinase CTR1

Gene

CTR1

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

Functioni

Acts as a negative regulator in the ethylene response pathway.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei578 – 5781ATPPROSITE-ProRule annotation
Active sitei676 – 6761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi557 – 5659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine/tyrosine kinase activity Source: TAIR
  3. protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  1. cellular response to iron ion Source: TAIR
  2. ethylene-activated signaling pathway Source: UniProtKB-KW
  3. gibberellin biosynthetic process Source: TAIR
  4. negative regulation of ethylene-activated signaling pathway Source: TAIR
  5. protein autophosphorylation Source: TAIR
  6. regulation of post-embryonic root development Source: TAIR
  7. regulation of stem cell division Source: TAIR
  8. regulation of timing of transition from vegetative to reproductive phase Source: TAIR
  9. response to ethylene Source: TAIR
  10. response to fructose Source: TAIR
  11. response to sucrose Source: TAIR
  12. sugar mediated signaling pathway Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Ethylene signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G03730-MONOMER.
ARA:GQT-223-MONOMER.
BRENDAi2.7.11.1. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase CTR1 (EC:2.7.11.1)
Gene namesi
Name:CTR1
Ordered Locus Names:At5g03730
ORF Names:F17C15_150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G03730.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutants display ethylene-treated phenotypes, resulting in plants with small, unexpanded leaves and whose seed cotyledon growth is impaired.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi596 – 5961E → K in ctr1-4; exhibits ethylene-treated phenotype.
Mutagenesisi694 – 6941D → E in ctr1-1; exhibits ethylene-treated phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 821821Serine/threonine-protein kinase CTR1PRO_0000085907Add
BLAST

Proteomic databases

PaxDbiQ05609.
PRIDEiQ05609.

Expressioni

Tissue specificityi

Expressed in both seedlings and adult plants.1 Publication

Gene expression databases

ExpressionAtlasiQ05609. baseline and differential.
GenevestigatoriQ05609.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ERS1Q388462EBI-1606697,EBI-1606754
ETR1P493336EBI-1606697,EBI-1606682
ETR2Q0WPQ22EBI-1606697,EBI-1787533

Protein-protein interaction databases

BioGridi17024. 6 interactions.
IntActiQ05609. 4 interactions.
STRINGi3702.AT5G03730.1-P.

Structurei

Secondary structure

1
821
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi548 – 5503
Beta strandi551 – 5599
Beta strandi561 – 57010
Beta strandi573 – 5808
Helixi587 – 60216
Beta strandi611 – 6155
Beta strandi617 – 6193
Beta strandi622 – 6265
Helixi633 – 6386
Helixi642 – 6454
Helixi648 – 66619
Beta strandi668 – 6703
Helixi679 – 6813
Beta strandi682 – 6843
Beta strandi690 – 6923
Beta strandi703 – 7053
Turni715 – 7173
Helixi720 – 7234
Helixi732 – 74615
Turni750 – 7534
Helixi756 – 76510
Helixi778 – 78710
Helixi792 – 7943
Helixi798 – 80912

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P86X-ray2.50A/B540-821[»]
3PPZX-ray2.99A/B540-821[»]
ProteinModelPortaliQ05609.
SMRiQ05609. Positions 540-810.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini551 – 809259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 695Poly-Gly
Compositional biasi135 – 1417Poly-Gly

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000239752.
InParanoidiQ05609.
KOiK14510.
OMAiPSFATIM.
PhylomeDBiQ05609.

Family and domain databases

InterProiIPR028324. CTR1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR23257:SF384. PTHR23257:SF384. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05609-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEMPGRRSNY TLLSQFSDDQ VSVSVTGAPP PHYDSLSSEN RSNHNSGNTG
60 70 80 90 100
KAKAERGGFD WDPSGGGGGD HRLNNQPNRV GNNMYASSLG LQRQSSGSSF
110 120 130 140 150
GESSLSGDYY MPTLSAAANE IESVGFPQDD GFRLGFGGGG GDLRIQMAAD
160 170 180 190 200
SAGGSSSGKS WAQQTEESYQ LQLALALRLS SEATCADDPN FLDPVPDESA
210 220 230 240 250
LRTSPSSAET VSHRFWVNGC LSYYDKVPDG FYMMNGLDPY IWTLCIDLHE
260 270 280 290 300
SGRIPSIESL RAVDSGVDSS LEAIIVDRRS DPAFKELHNR VHDISCSCIT
310 320 330 340 350
TKEVVDQLAK LICNRMGGPV IMGEDELVPM WKECIDGLKE IFKVVVPIGS
360 370 380 390 400
LSVGLCRHRA LLFKVLADII DLPCRIAKGC KYCNRDDAAS CLVRFGLDRE
410 420 430 440 450
YLVDLVGKPG HLWEPDSLLN GPSSISISSP LRFPRPKPVE PAVDFRLLAK
460 470 480 490 500
QYFSDSQSLN LVFDPASDDM GFSMFHRQYD NPGGENDALA ENGGGSLPPS
510 520 530 540 550
ANMPPQNMMR ASNQIEAAPM NAPPISQPVP NRANRELGLD GDDMDIPWCD
560 570 580 590 600
LNIKEKIGAG SFGTVHRAEW HGSDVAVKIL MEQDFHAERV NEFLREVAIM
610 620 630 640 650
KRLRHPNIVL FMGAVTQPPN LSIVTEYLSR GSLYRLLHKS GAREQLDERR
660 670 680 690 700
RLSMAYDVAK GMNYLHNRNP PIVHRDLKSP NLLVDKKYTV KVCDFGLSRL
710 720 730 740 750
KASTFLSSKS AAGTPEWMAP EVLRDEPSNE KSDVYSFGVI LWELATLQQP
760 770 780 790 800
WGNLNPAQVV AAVGFKCKRL EIPRNLNPQV AAIIEGCWTN EPWKRPSFAT
810 820
IMDLLRPLIK SAVPPPNRSD L
Length:821
Mass (Da):90,306
Last modified:November 1, 1995 - v1
Checksum:i2922D3DCD0CC15BC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08789 mRNA. Translation: AAA32779.1.
L08790 Genomic DNA. Translation: AAA32780.1.
AL162506 Genomic DNA. Translation: CAB82938.1.
CP002688 Genomic DNA. Translation: AED90647.1.
CP002688 Genomic DNA. Translation: AED90648.1.
PIRiT48400.
RefSeqiNP_195993.1. NM_120454.3.
NP_850760.1. NM_180429.3.
UniGeneiAt.300.

Genome annotation databases

EnsemblPlantsiAT5G03730.1; AT5G03730.1; AT5G03730.
AT5G03730.2; AT5G03730.2; AT5G03730.
GeneIDi831748.
KEGGiath:AT5G03730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08789 mRNA. Translation: AAA32779.1 .
L08790 Genomic DNA. Translation: AAA32780.1 .
AL162506 Genomic DNA. Translation: CAB82938.1 .
CP002688 Genomic DNA. Translation: AED90647.1 .
CP002688 Genomic DNA. Translation: AED90648.1 .
PIRi T48400.
RefSeqi NP_195993.1. NM_120454.3.
NP_850760.1. NM_180429.3.
UniGenei At.300.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P86 X-ray 2.50 A/B 540-821 [» ]
3PPZ X-ray 2.99 A/B 540-821 [» ]
ProteinModelPortali Q05609.
SMRi Q05609. Positions 540-810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 17024. 6 interactions.
IntActi Q05609. 4 interactions.
STRINGi 3702.AT5G03730.1-P.

Proteomic databases

PaxDbi Q05609.
PRIDEi Q05609.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G03730.1 ; AT5G03730.1 ; AT5G03730 .
AT5G03730.2 ; AT5G03730.2 ; AT5G03730 .
GeneIDi 831748.
KEGGi ath:AT5G03730.

Organism-specific databases

GeneFarmi 884.
TAIRi AT5G03730.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000239752.
InParanoidi Q05609.
KOi K14510.
OMAi PSFATIM.
PhylomeDBi Q05609.

Enzyme and pathway databases

BioCyci ARA:AT5G03730-MONOMER.
ARA:GQT-223-MONOMER.
BRENDAi 2.7.11.1. 399.

Gene expression databases

ExpressionAtlasi Q05609. baseline and differential.
Genevestigatori Q05609.

Family and domain databases

InterProi IPR028324. CTR1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR23257:SF384. PTHR23257:SF384. 1 hit.
Pfami PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "CTR1, a negative regulator of the ethylene response pathway in Arabidopsis, encodes a member of the raf family of protein kinases."
    Kieber J.J., Rothenberg M., Roman G., Feldmann K.A., Ecker J.R.
    Cell 72:427-441(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(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.

Entry informationi

Entry nameiCTR1_ARATH
AccessioniPrimary (citable) accession number: Q05609
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 124 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3