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Q9M149 (PI5KB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative phosphatidylinositol 4-phosphate 5-kinase 11

Short name=AtPIP5K11
EC=2.7.1.68
Alternative name(s):
1-phosphatidylinositol 4-phosphate kinase 11
Diphosphoinositide kinase 11
PtdIns(4)P-5-kinase 11
Gene names
Name:PIP5K11
Ordered Locus Names:At4g01190
ORF Names:F2N1.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Sequence similarities

Contains 1 PIPK domain.

Sequence caution

The sequence AAB61030.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Putative phosphatidylinositol 4-phosphate 5-kinase 11
PRO_0000185483

Regions

Domain1 – 390390PIPK
Region350 – 37122Activation loop By similarity
Compositional bias241 – 29353Ser-rich

Sequences

Sequence LengthMass (Da)Tools
Q9M149 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8A12D10DA2DED4CA

FASTA40145,659
        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 

« 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]"Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C."
Mueller-Roeber B., Pical C.
Plant Physiol. 130:22-46(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007269 Genomic DNA. Translation: AAB61030.1. Sequence problems.
AL161491 Genomic DNA. Translation: CAB80928.1.
CP002687 Genomic DNA. Translation: AEE81992.1.
PIRF85015.
T01723.
RefSeqNP_192028.1. NM_116349.1.
UniGeneAt.54072.

3D structure databases

ProteinModelPortalQ9M149.
SMRQ9M149. Positions 27-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13357. 4 interactions.

Proteomic databases

PRIDEQ9M149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G01190.1; AT4G01190.1; AT4G01190.
GeneID828066.
KEGGath:AT4G01190.

Organism-specific databases

TAIRAT4G01190.

Phylogenomic databases

eggNOGCOG5253.
HOGENOMHOG000193875.
InParanoidQ9M149.
KOK00889.
OMANRIRYST.
PhylomeDBQ9M149.
ProtClustDBCLSN2685476.

Enzyme and pathway databases

BioCycARA:AT4G01190-MONOMER.

Gene expression databases

GenevestigatorQ9M149.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
InterProIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERPTHR23086. PTHR23086. 1 hit.
PfamPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9M149.

Entry information

Entry namePI5KB_ARATH
AccessionPrimary (citable) accession number: Q9M149
Secondary accession number(s): O04613
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 82 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names