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UniProtKB/Swiss-Prot entry Q9M149


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PI5KB_ARATH
Primary accession number Q9M149
Secondary accession number O04613
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 41)
Name and origin of the protein
Protein name Putative phosphatidylinositol-4-phosphate 5-kinase 11
Synonyms AtPIP5K11
EC 2.7.1.68
1-phosphatidylinositol-4-phosphate kinase 11
PtdIns(4)P-5-kinase 11
Diphosphoinositide kinase 11
Gene name
Name: PIP5K11
OrderedLocusNames: At4g01190
ORFNames: F2N1.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
GENE FAMILY, AND NOMENCLATURE.
DOI=10.1104/pp.004770; PubMed=12226484 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller-Roeber B., Pical C.;
"Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C.";
Plant Physiol. 130:22-46(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF007269; AAB61030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161491; CAB80928.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F85015; F85015.
T01723; T01723.
RefSeq NP_192028.1; -.
UniGene At.54072
3D structure databases
HSSP P78356; 1BO1. [HSSP ENTRY / PDB]
ModBase Q9M149.
Organism-specific databases
TAIR At4g01190; -.
Gene expression databases
ArrayExpress Q9M149; -.
GermOnline AT4G01190; Arabidopsis thaliana.
Ontologies
GO
GO:0016308; Molecular function: 1-phosphatidylinositol-4-phosphate 5-kinase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR002498; PIP5K_core.
IPR016034; PIP5K_core_sub.
Graphical view of domain structure.
PANTHER PTHR23086; PIP5K; 1.
Pfam PF01504; PIP5K; 1.
Pfam graphical view of domain structure.
SMART SM00330; PIPKc; 1.
SMART graphical view of domain structure.
BLOCKS Q9M149.
ProtoNet Q9M149.
Genome annotation databases
GeneID 828066; -.
GenomeReviews CT486007_GR; AT4G01190.
KEGG ath:AT4G01190; -.
NMPDR fig|3702.1.peg.17902; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   401  401     Putative phosphatidylinositol-4-phosphate 5-kinase 11. PRO_0000185483
DOMAIN   55   390  336     PI5K. 
REGION   350   371  22     Activation loop (By similarity). 
COMPBIAS   241   293  53     Ser-rich. 
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 45659 Da [This is the MW of the unprocessed precursor] CRC64: 8A12D10DA2DED4CA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELRATVENR IRYSTKHIKH LPPGSITEFD WKDYCPVGFG LIQELEGIDH DDYLLSICTD 

        70         80         90        100        110        120 
ETLKKISSGK IGNVFHISND NRFLIKILRK SEIKVTLEML PRYYRHINYH RSSLFTRIFG 

       130        140        150        160        170        180 
AHSVKPLGGV KTYFAVMSNM LHSTIFVNKL YDLKGSPKGR SNKKIEVRNT TVLKDIDFDF 

       190        200        210        220        230        240 
CFYVDPLARQ RIIKQTKLDC ELLEEEGIMD YSLLVGLQSK GSCQGSLDGL NPVYGSFAPP 

       250        260        270        280        290        300 
SSFKSNSTKS MKTASSSPDR SSVAMYSCSP DRDSVENEMS MTIQSVTSNS ASSETNILAT 

       310        320        330        340        350        360 
TLSDLFHNSS NINFGMKIPA RARRVTRETG EEEWYNVVLY IGIVDTFQDY GMKKRIEHCY 

       370        380        390        400 
KSIQYNSNSI STVHPKIYSS RFQDFVSNIF LPHDDDLSSK Y 

Q9M149 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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