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Protein

Probable choline kinase 3

Gene

At4g09760

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity).By similarity

Catalytic activityi

ATP + choline = ADP + phosphocholine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATPBy similarity
Binding sitei207 – 2071ATPBy similarity
Binding sitei224 – 2241ATPBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G09760-MONOMER.
ARA:GQT-1965-MONOMER.
ReactomeiREACT_279011. Synthesis of PE.
REACT_348151. Synthesis of PC.
UniPathwayiUPA00753; UER00737.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable choline kinase 3 (EC:2.7.1.32)
Gene namesi
Ordered Locus Names:At4g09760
ORF Names:F17A8.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G09760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Probable choline kinase 3PRO_0000423348Add
BLAST

Proteomic databases

PRIDEiQ9SZ92.

Expressioni

Inductioni

By wounding, and salt and osmotic stresses.1 Publication

Gene expression databases

ExpressionAtlasiQ9SZ92. baseline and differential.
GenevestigatoriQ9SZ92.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G09760.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SZ92.
SMRiQ9SZ92. Positions 36-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the choline/ethanolamine kinase family.Curated

Phylogenomic databases

HOGENOMiHOG000041274.
InParanoidiQ9SZ92.
KOiK14156.
OMAiERRRFIC.
PhylomeDBiQ9SZ92.

Family and domain databases

InterProiIPR026712. Cho/Etha_kinase.
IPR011009. Kinase-like_dom.
[Graphical view]
PANTHERiPTHR22603:SF32. PTHR22603:SF32. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SZ92-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAVGIFGLIP SSSPDELRKI LQALSTKWGD VVEDFESLEV KPMKGAMTNE
60 70 80 90 100
VFMVSWPRKE TNLRCRKLLV RVYGEGVELF FNRDDEIRTF EYVARHGHGP
110 120 130 140 150
TLLGRFAGGR VEEFIHARTL SATDLRDPNI SALVASKLRR FHSIHIPGDR
160 170 180 190 200
IMLIWDRMRT WVGQAKNLCS NEHSTEFGLD DIEDEINLLE QEVNNEQEIG
210 220 230 240 250
FCHNDLQYGN IMIDEETNAI TIIDYEYASY NPIAYDIANH FCEMAADYHS
260 270 280 290 300
NTPHILDYTL YPGEEERRRF ICNYLTSSGE EAREEDIEQL LDDIEKYTLA
310 320 330 340
SHLFWGLWGI ISGYVNKIEF DYIEYSRQRF KQYWLRKPKL LSFFPS
Length:346
Mass (Da):40,351
Last modified:May 1, 2000 - v1
Checksum:iCF5CCA7CF80F5FF7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 674RCRK → QCRN in AAM66047 (Ref. 3) Curated
Sequence conflicti151 – 1511I → T in AAM61617 (Ref. 3) Curated
Sequence conflicti175 – 1751T → S in AAM61617 (Ref. 3) Curated
Sequence conflicti181 – 1833DIE → CID in AAM61617 (Ref. 3) Curated
Sequence conflicti219 – 2191A → T in AAM66047 (Ref. 3) Curated
Sequence conflicti288 – 2881E → D in AAM61617 (Ref. 3) Curated
Sequence conflicti344 – 3441F → Y in AAM61617 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049482 Genomic DNA. Translation: CAB39643.1.
AL161515 Genomic DNA. Translation: CAB78099.1.
CP002687 Genomic DNA. Translation: AEE82792.1.
CP002687 Genomic DNA. Translation: AEE82793.1.
AY085061 mRNA. Translation: AAM61617.1.
AY088512 mRNA. Translation: AAM66047.1.
PIRiT04023.
RefSeqiNP_192714.1. NM_117044.3. [Q9SZ92-1]
NP_849350.1. NM_179019.1. [Q9SZ92-1]
UniGeneiAt.27989.
At.33676.

Genome annotation databases

EnsemblPlantsiAT4G09760.1; AT4G09760.1; AT4G09760. [Q9SZ92-1]
AT4G09760.2; AT4G09760.2; AT4G09760. [Q9SZ92-1]
GeneIDi826564.
KEGGiath:AT4G09760.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049482 Genomic DNA. Translation: CAB39643.1.
AL161515 Genomic DNA. Translation: CAB78099.1.
CP002687 Genomic DNA. Translation: AEE82792.1.
CP002687 Genomic DNA. Translation: AEE82793.1.
AY085061 mRNA. Translation: AAM61617.1.
AY088512 mRNA. Translation: AAM66047.1.
PIRiT04023.
RefSeqiNP_192714.1. NM_117044.3. [Q9SZ92-1]
NP_849350.1. NM_179019.1. [Q9SZ92-1]
UniGeneiAt.27989.
At.33676.

3D structure databases

ProteinModelPortaliQ9SZ92.
SMRiQ9SZ92. Positions 36-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G09760.1-P.

Proteomic databases

PRIDEiQ9SZ92.

Protocols and materials databases

DNASUi826564.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G09760.1; AT4G09760.1; AT4G09760. [Q9SZ92-1]
AT4G09760.2; AT4G09760.2; AT4G09760. [Q9SZ92-1]
GeneIDi826564.
KEGGiath:AT4G09760.

Organism-specific databases

TAIRiAT4G09760.

Phylogenomic databases

HOGENOMiHOG000041274.
InParanoidiQ9SZ92.
KOiK14156.
OMAiERRRFIC.
PhylomeDBiQ9SZ92.

Enzyme and pathway databases

UniPathwayiUPA00753; UER00737.
BioCyciARA:AT4G09760-MONOMER.
ARA:GQT-1965-MONOMER.
ReactomeiREACT_279011. Synthesis of PE.
REACT_348151. Synthesis of PC.

Miscellaneous databases

PROiQ9SZ92.

Gene expression databases

ExpressionAtlasiQ9SZ92. baseline and differential.
GenevestigatoriQ9SZ92.

Family and domain databases

InterProiIPR026712. Cho/Etha_kinase.
IPR011009. Kinase-like_dom.
[Graphical view]
PANTHERiPTHR22603:SF32. PTHR22603:SF32. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Regulation of phosphatidylcholine biosynthesis under salt stress involves choline kinases in Arabidopsis thaliana."
    Tasseva G., Richard L., Zachowski A.
    FEBS Lett. 566:115-120(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiCK3_ARATH
AccessioniPrimary (citable) accession number: Q9SZ92
Secondary accession number(s): Q8L9C6, Q8LF42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 104 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.