Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylinositol 4-phosphate 5-kinase 9

Gene

PIP5K9

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

Functioni

Plays a role in sugar-mediated root development. Interaction with CINV1 induces repression of CINV1 activity and negative regulation of sugar-mediated root cell elongation.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: TAIR
  2. cellular amino acid metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G09920-MONOMER.
ARA:GQT-1409-MONOMER.
ARA:GQT-2574-MONOMER.
BRENDAi2.7.1.68. 399.
ReactomeiREACT_345128. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase 9 (EC:2.7.1.68)
Short name:
AtPIP5K9
Alternative name(s):
1-phosphatidylinositol 4-phosphate kinase 9
Diphosphoinositide kinase 9
PtdIns(4)P-5-kinase 9
Gene namesi
Name:PIP5K9
Ordered Locus Names:At3g09920
ORF Names:F8A24.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G09920.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. membrane Source: TAIR
  3. nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 815815Phosphatidylinositol 4-phosphate 5-kinase 9PRO_0000185481Add
BLAST

Proteomic databases

PaxDbiQ8L850.
PRIDEiQ8L850.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Transiently down-regulated by cold.1 Publication

Gene expression databases

GenevestigatoriQ8L850.

Interactioni

Subunit structurei

Interacts with CINV1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CINV1Q9LQF26EBI-2008013,EBI-2008033

Protein-protein interaction databases

BioGridi5485. 1 interaction.
IntActiQ8L850. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8L850.
SMRiQ8L850. Positions 451-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati58 – 8023MORN 1Add
BLAST
Repeati81 – 10323MORN 2Add
BLAST
Repeati104 – 12623MORN 3Add
BLAST
Repeati127 – 14923MORN 4Add
BLAST
Repeati150 – 17223MORN 5Add
BLAST
Repeati173 – 19523MORN 6Add
BLAST
Repeati196 – 21823MORN 7Add
BLAST
Repeati219 – 24022MORN 8Add
BLAST
Domaini391 – 809419PIPKPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni769 – 79022Activation loopBy similarityAdd
BLAST

Sequence similaritiesi

Contains 8 MORN repeats.Curated
Contains 1 PIPK domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG4642.
HOGENOMiHOG000193875.
InParanoidiQ8L850.
KOiK00889.
OMAiWIQGEIE.
PhylomeDBiQ8L850.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
InterProiIPR003409. MORN.
IPR017163. PIno-4-P-5_kinase_pln.
IPR023610. 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]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF02493. MORN. 8 hits.
PF01504. PIP5K. 1 hit.
[Graphical view]
PIRSFiPIRSF037274. PIP5K_plant_prd. 1 hit.
SMARTiSM00698. MORN. 8 hits.
SM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8L850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLDVRGAV SFAERTKSVD ALTKKEILSA LNSGEVSETS EDARFRVREL
60 70 80 90 100
VLPDGESYSG SLLGNVPEGP GKYIWSDGCV YDGEWRRGMR HGIGNMRWAS
110 120 130 140 150
GASYDGEFSG GYMHGSGTYV DANKLTYKGR WRLNLKHGLG YQVYPNGDVF
160 170 180 190 200
EGSWIQGLGE GPGKYTWANK NVYLGDMKGG KMSGKGTLTW VTGDSYEGSW
210 220 230 240 250
LNGMMHGVGV YTWSDGGCYV GTWTRGLKDG KGSFYSAGTR VPVVQEFYLN
260 270 280 290 300
ALRKRGVLPD MRRQNQVASS VNMENLRVGV NRNKLSKGSL INLEQSRNGR
310 320 330 340 350
VSLERRWSLE VSIEKVIGHG YSDLSTAVLD SGSSVQYKAN IPILEREYMQ
360 370 380 390 400
GVLISELVVN NGFSRTSRRA KRKHKRLVKE AKKPGEVVIK GHRSYDLMLS
410 420 430 440 450
LQLGIRYTVG KITPIQRRQV RTADFGPRAS FWMTFPRAGS TMTPPHHSED
460 470 480 490 500
FKWKDYCPMV FRNLREMFKI DAADYMMSIC GNDTLRELSS PGKSGSVFFL
510 520 530 540 550
SQDDRFMIKT LRKSEVKVLL RMLPDYHHHV KTYENTLITK FFGLHRIKPS
560 570 580 590 600
SGQKFRFVVM GNMFFTDLRI HRRFDLKGSS LGRSADKVEI DENTILKDLD
610 620 630 640 650
LNYSFFLETS WREGLLRQLE IDSKFLEAQN IMDYSLLLGV HHRAPQHLRS
660 670 680 690 700
QLVRSQSITT DALESVAEDD TIEDDMLSYH EGLVLVPRGS ENTVTGPHIR
710 720 730 740 750
GSRLRASAVG DEEVDLLLPG TARLQIQQGV NMPARAELIP GREDKEKQIL
760 770 780 790 800
HDCCDVVLYL GIIDILQEYN MTKKIEHAYK SLHFDSLSIS AVDPTFYSQR
810
FLEFIKKVFP QNNKS
Length:815
Mass (Da):92,092
Last modified:October 25, 2005 - v2
Checksum:i3194F009D2C50130
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti482 – 4821N → K in AAM53300 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ810853 mRNA. Translation: CAH18644.1.
AC015985 Genomic DNA. Translation: AAF23244.1.
CP002686 Genomic DNA. Translation: AEE74832.1.
CP002686 Genomic DNA. Translation: AEE74833.1.
CP002686 Genomic DNA. Translation: AEE74834.1.
AY120742 mRNA. Translation: AAM53300.1.
AK229815 mRNA. Translation: BAF01646.1.
RefSeqiNP_001030666.1. NM_001035589.2.
NP_001189852.1. NM_001202923.1.
NP_187603.1. NM_111827.2.
UniGeneiAt.40019.

Genome annotation databases

EnsemblPlantsiAT3G09920.1; AT3G09920.1; AT3G09920.
AT3G09920.2; AT3G09920.2; AT3G09920.
AT3G09920.3; AT3G09920.3; AT3G09920.
GeneIDi820151.
KEGGiath:AT3G09920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ810853 mRNA. Translation: CAH18644.1.
AC015985 Genomic DNA. Translation: AAF23244.1.
CP002686 Genomic DNA. Translation: AEE74832.1.
CP002686 Genomic DNA. Translation: AEE74833.1.
CP002686 Genomic DNA. Translation: AEE74834.1.
AY120742 mRNA. Translation: AAM53300.1.
AK229815 mRNA. Translation: BAF01646.1.
RefSeqiNP_001030666.1. NM_001035589.2.
NP_001189852.1. NM_001202923.1.
NP_187603.1. NM_111827.2.
UniGeneiAt.40019.

3D structure databases

ProteinModelPortaliQ8L850.
SMRiQ8L850. Positions 451-641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5485. 1 interaction.
IntActiQ8L850. 1 interaction.

Proteomic databases

PaxDbiQ8L850.
PRIDEiQ8L850.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G09920.1; AT3G09920.1; AT3G09920.
AT3G09920.2; AT3G09920.2; AT3G09920.
AT3G09920.3; AT3G09920.3; AT3G09920.
GeneIDi820151.
KEGGiath:AT3G09920.

Organism-specific databases

TAIRiAT3G09920.

Phylogenomic databases

eggNOGiCOG4642.
HOGENOMiHOG000193875.
InParanoidiQ8L850.
KOiK00889.
OMAiWIQGEIE.
PhylomeDBiQ8L850.

Enzyme and pathway databases

BioCyciARA:AT3G09920-MONOMER.
ARA:GQT-1409-MONOMER.
ARA:GQT-2574-MONOMER.
BRENDAi2.7.1.68. 399.
ReactomeiREACT_345128. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

PROiQ8L850.

Gene expression databases

GenevestigatoriQ8L850.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
InterProiIPR003409. MORN.
IPR017163. PIno-4-P-5_kinase_pln.
IPR023610. 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]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF02493. MORN. 8 hits.
PF01504. PIP5K. 1 hit.
[Graphical view]
PIRSFiPIRSF037274. PIP5K_plant_prd. 1 hit.
SMARTiSM00698. MORN. 8 hits.
SM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana putative phosphatidylinositol-4-phosphate 5-kinase."
    Lou Y.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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.
  7. "PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase, interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth."
    Lou Y., Gou J.Y., Xue H.W.
    Plant Cell 19:163-181(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CINV1, TISSUE SPECIFICITY, INDUCTION BY COLD.
    Strain: cv. Columbia.

Entry informationi

Entry nameiPI5K9_ARATH
AccessioniPrimary (citable) accession number: Q8L850
Secondary accession number(s): Q0WMK5, Q9SF93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: April 29, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The gain-of-function mutant pip5k9-d (T-DNA insertion line) has reduced primary root length.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.