Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SZ92

- CK3_ARATH

UniProt

Q9SZ92 - CK3_ARATH

Protein

Probable choline kinase 3

Gene

At4g09760

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATP binding Source: UniProtKB-KW
    2. choline kinase activity Source: UniProtKB-EC

    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.
    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: 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

    ArrayExpressiQ9SZ92.
    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

    InParanoidiQ9SZ92.
    KOiK14156.
    OMAiVSHESID.
    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. Align

    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

    MAVGIFGLIP SSSPDELRKI LQALSTKWGD VVEDFESLEV KPMKGAMTNE    50
    VFMVSWPRKE TNLRCRKLLV RVYGEGVELF FNRDDEIRTF EYVARHGHGP 100
    TLLGRFAGGR VEEFIHARTL SATDLRDPNI SALVASKLRR FHSIHIPGDR 150
    IMLIWDRMRT WVGQAKNLCS NEHSTEFGLD DIEDEINLLE QEVNNEQEIG 200
    FCHNDLQYGN IMIDEETNAI TIIDYEYASY NPIAYDIANH FCEMAADYHS 250
    NTPHILDYTL YPGEEERRRF ICNYLTSSGE EAREEDIEQL LDDIEKYTLA 300
    SHLFWGLWGI ISGYVNKIEF DYIEYSRQRF KQYWLRKPKL LSFFPS 346
    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. 1 PublicationCurated
    Sequence conflicti151 – 1511I → T in AAM61617. 1 PublicationCurated
    Sequence conflicti175 – 1751T → S in AAM61617. 1 PublicationCurated
    Sequence conflicti181 – 1833DIE → CID in AAM61617. 1 PublicationCurated
    Sequence conflicti219 – 2191A → T in AAM66047. 1 PublicationCurated
    Sequence conflicti288 – 2881E → D in AAM61617. 1 PublicationCurated
    Sequence conflicti344 – 3441F → Y in AAM61617. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T04023.
    RefSeqi NP_192714.1. NM_117044.3. [Q9SZ92-1 ]
    NP_849350.1. NM_179019.1. [Q9SZ92-1 ]
    UniGenei At.27989.
    At.33676.

    3D structure databases

    ProteinModelPortali Q9SZ92.
    SMRi Q9SZ92. Positions 36-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G09760.1-P.

    Proteomic databases

    PRIDEi Q9SZ92.

    Protocols and materials databases

    DNASUi 826564.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G09760.1 ; AT4G09760.1 ; AT4G09760 . [Q9SZ92-1 ]
    AT4G09760.2 ; AT4G09760.2 ; AT4G09760 . [Q9SZ92-1 ]
    GeneIDi 826564.
    KEGGi ath:AT4G09760.

    Organism-specific databases

    TAIRi AT4G09760.

    Phylogenomic databases

    InParanoidi Q9SZ92.
    KOi K14156.
    OMAi VSHESID.
    PhylomeDBi Q9SZ92.

    Enzyme and pathway databases

    UniPathwayi UPA00753 ; UER00737 .
    BioCyci ARA:AT4G09760-MONOMER.
    ARA:GQT-1965-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SZ92.
    Genevestigatori Q9SZ92.

    Family and domain databases

    InterProi IPR026712. Cho/Etha_kinase.
    IPR011009. Kinase-like_dom.
    [Graphical view ]
    PANTHERi PTHR22603:SF32. PTHR22603:SF32. 1 hit.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 99 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