Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SZ92 (CK3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable choline kinase 3

EC=2.7.1.32
Gene names
Ordered Locus Names:At4g09760
ORF Names:F17A8.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

ATP + choline = ADP + phosphocholine.

Pathway

Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1.

Induction

By wounding, and salt and osmotic stresses. Ref.4

Sequence similarities

Belongs to the choline/ethanolamine kinase family.

Ontologies

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SZ92-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Probable choline kinase 3
PRO_0000423348

Sites

Binding site711ATP By similarity
Binding site2071ATP By similarity
Binding site2241ATP By similarity

Experimental info

Sequence conflict64 – 674RCRK → QCRN in AAM66047. Ref.3
Sequence conflict1511I → T in AAM61617. Ref.3
Sequence conflict1751T → S in AAM61617. Ref.3
Sequence conflict181 – 1833DIE → CID in AAM61617. Ref.3
Sequence conflict2191A → T in AAM66047. Ref.3
Sequence conflict2881E → D in AAM61617. Ref.3
Sequence conflict3441F → Y in AAM61617. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CF5CCA7CF80F5FF7

FASTA34640,351
        10         20         30         40         50         60 
MAVGIFGLIP SSSPDELRKI LQALSTKWGD VVEDFESLEV KPMKGAMTNE VFMVSWPRKE 

        70         80         90        100        110        120 
TNLRCRKLLV RVYGEGVELF FNRDDEIRTF EYVARHGHGP TLLGRFAGGR VEEFIHARTL 

       130        140        150        160        170        180 
SATDLRDPNI SALVASKLRR FHSIHIPGDR IMLIWDRMRT WVGQAKNLCS NEHSTEFGLD 

       190        200        210        220        230        240 
DIEDEINLLE QEVNNEQEIG FCHNDLQYGN IMIDEETNAI TIIDYEYASY NPIAYDIANH 

       250        260        270        280        290        300 
FCEMAADYHS NTPHILDYTL YPGEEERRRF ICNYLTSSGE EAREEDIEQL LDDIEKYTLA 

       310        320        330        340 
SHLFWGLWGI ISGYVNKIEF DYIEYSRQRF KQYWLRKPKL LSFFPS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04023.
RefSeqNP_192714.1. NM_117044.3.
NP_849350.1. NM_179019.1.
UniGeneAt.27989.
At.33676.

3D structure databases

ProteinModelPortalQ9SZ92.
SMRQ9SZ92. Positions 36-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G09760.1-P.

Proteomic databases

PRIDEQ9SZ92.

Protocols and materials databases

DNASU826564.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G09760.1; AT4G09760.1; AT4G09760. [Q9SZ92-1]
AT4G09760.2; AT4G09760.2; AT4G09760. [Q9SZ92-1]
GeneID826564.
KEGGath:AT4G09760.

Organism-specific databases

TAIRAT4G09760.

Phylogenomic databases

InParanoidQ9SZ92.
KOK14156.
OMARIPREAR.
PhylomeDBQ9SZ92.
ProtClustDBPLN02236.

Enzyme and pathway databases

BioCycARA:AT4G09760-MONOMER.
ARA:GQT-1965-MONOMER.
UniPathwayUPA00753; UER00737.

Gene expression databases

ArrayExpressQ9SZ92.
GenevestigatorQ9SZ92.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCK3_ARATH
AccessionPrimary (citable) accession number: Q9SZ92
Secondary accession number(s): Q8L9C6, Q8LF42
Entry history
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names