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Q56YP2

- PI5K1_ARATH

UniProt

Q56YP2 - PI5K1_ARATH

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Protein

Phosphatidylinositol 4-phosphate 5-kinase 1

Gene

PIP5K1

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

Functioni

Catalyzes the synthesis of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate.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: TAIR
  2. actin filament binding Source: TAIR
  3. actin monomer binding Source: TAIR
  4. ATP binding Source: UniProtKB-KW
  5. phosphatidylinositol phosphate kinase activity Source: TAIR

GO - Biological processi

  1. phosphatidylinositol phosphorylation Source: GOC
  2. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G21980-MONOMER.
ReactomeiREACT_187642. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase 1 (EC:2.7.1.68)
Short name:
AtPIP5K1
Alternative name(s):
1-phosphatidylinositol 4-phosphate kinase 1
Diphosphoinositide kinase 1
PtdIns(4)P-5-kinase 1
Gene namesi
Name:PIP5K1
Synonyms:P5K1
Ordered Locus Names:At1g21980
ORF Names:F2E2.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G21980.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Phosphatidylinositol 4-phosphate 5-kinase 1PRO_0000185473Add
BLAST

Post-translational modificationi

Phosphorylation inactivates the enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ56YP2.

Expressioni

Tissue specificityi

Expressed in the whole plant, preferentially in roots. Strongly expressed in meristematic tissues, namely procambial cell layers.2 Publications

Inductioni

By abscisic acid (ABA), drought and salt treatment.1 Publication

Gene expression databases

ExpressionAtlasiQ56YP2. baseline and differential.
GenevestigatoriQ56YP2.

Interactioni

Protein-protein interaction databases

BioGridi24040. 6 interactions.
MINTiMINT-8067725.
STRINGi3702.AT1G21980.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ56YP2.
SMRiQ56YP2. Positions 410-602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati81 – 10323MORN 1Add
BLAST
Repeati104 – 12623MORN 2Add
BLAST
Repeati127 – 14923MORN 3Add
BLAST
Repeati150 – 17223MORN 4Add
BLAST
Repeati173 – 19523MORN 5Add
BLAST
Repeati196 – 21823MORN 6Add
BLAST
Repeati219 – 24123MORN 7Add
BLAST
Domaini349 – 748400PIPKPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni708 – 72922Activation loopBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 128Poly-Glu

Sequence similaritiesi

Contains 7 MORN repeats.Curated
Contains 1 PIPK domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG4642.
HOGENOMiHOG000193875.
InParanoidiQ56YP2.
KOiK00889.
OMAiDNTGEKM.
PhylomeDBiQ56YP2.

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. 7 hits.
PF01504. PIP5K. 1 hit.
[Graphical view]
PIRSFiPIRSF037274. PIP5K_plant_prd. 1 hit.
SMARTiSM00698. MORN. 7 hits.
SM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56YP2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDSEEDEEE EEASEVILSS VVQKKKKKNL RFGEEVERRD GLVLLAQSTP
60 70 80 90 100
MVRSRSQGTT RRVTPTPLVD VEKPLPNGDL YIGSFSGGFP HGSGKYLWKD
110 120 130 140 150
GCMYEGDWKR GKASGKGKFS WPSGATYEGE FKSGRMEGFG TFTGADGDTY
160 170 180 190 200
RGTWVADRKH GHGQKRYANG DFYEGTWRRN LQDGRGRYVW RNGNQYTGEW
210 220 230 240 250
RSGVISGKGL LVWPNGNRYE GLWENGIPKG NGVFTWSDGS SCVGAWNESN
260 270 280 290 300
IMRSFFNGVE KNDLIVGNRK RSSVDSGAGS LGGEKVFPRI CIWESDGEAG
310 320 330 340 350
DITCDIIDNV EASMIYRDRI SVDRDGFRQF KKNPCWFNGE AKKPGQTISK
360 370 380 390 400
GHKKYDLMLN LQLGIRYSVG KHASIVRDLK QTDFDPKEKF WTRFPPEGTK
410 420 430 440 450
TTPPHQSVDF RWKDYCPLVF RRLRELFQVD PAKYMLAICG NDALRELSSP
460 470 480 490 500
GKSGSFFYLT QDDRFMIKTV KKSEVKVLLR MLPSYYKHVC QYENSLVTRF
510 520 530 540 550
YGVHCVKPVG GQKTRFIVMG NLFCSEYRIQ RRFDLKGSSH GRSTAKPEGE
560 570 580 590 600
IDETTTLKDL DLNFSFRLQR NWYQELMKQI KRDCEFLEAE RIMDYSLLVG
610 620 630 640 650
VHFRDDNTGE KMGLSPFVLR SGRIDSYQNE KFMRGCRFLE AELQDMDRIL
660 670 680 690 700
AGRKPSIRLG ANMPAKAERM ARRSDFDQYS SGGASYPSHG EMYEVVLYFG
710 720 730 740 750
VIDILQDYDI TKKIEHAYKS LQADPASISA VDPKLYSKRF RDFISRIFIE

EG
Length:752
Mass (Da):85,945
Last modified:May 10, 2005 - v1
Checksum:i8A9E7D10A32CBF53
GO

Sequence cautioni

The sequence AAF86542.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA33501.1 differs from that shown. Reason: Frameshift at position 91. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821Q → P in AAB82658. 1 PublicationCurated
Sequence conflicti186 – 1861G → S in AAB82658. 1 PublicationCurated
Sequence conflicti202 – 2021S → I in BAA33501. (PubMed:9753781)Curated
Sequence conflicti416 – 4161C → Y in BAA33501. (PubMed:9753781)Curated
Sequence conflicti419 – 4191V → M in BAA33501. (PubMed:9753781)Curated
Sequence conflicti456 – 4561F → L in BAA33501. (PubMed:9753781)Curated
Sequence conflicti588 – 5881E → D in BAA33501. (PubMed:9753781)Curated
Sequence conflicti602 – 6021H → P in BAA33501. (PubMed:9753781)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019380 mRNA. Translation: AAB82658.1.
AB005902 mRNA. Translation: BAA33501.1. Frameshift.
AC069252 Genomic DNA. Translation: AAF86542.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30181.1.
AK221279 mRNA. Translation: BAD93975.1.
PIRiT51821.
RefSeqiNP_173617.1. NM_102047.3.
UniGeneiAt.22532.

Genome annotation databases

EnsemblPlantsiAT1G21980.1; AT1G21980.1; AT1G21980.
GeneIDi838801.
KEGGiath:AT1G21980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019380 mRNA. Translation: AAB82658.1 .
AB005902 mRNA. Translation: BAA33501.1 . Frameshift.
AC069252 Genomic DNA. Translation: AAF86542.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE30181.1 .
AK221279 mRNA. Translation: BAD93975.1 .
PIRi T51821.
RefSeqi NP_173617.1. NM_102047.3.
UniGenei At.22532.

3D structure databases

ProteinModelPortali Q56YP2.
SMRi Q56YP2. Positions 410-602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 24040. 6 interactions.
MINTi MINT-8067725.
STRINGi 3702.AT1G21980.1-P.

Proteomic databases

PRIDEi Q56YP2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G21980.1 ; AT1G21980.1 ; AT1G21980 .
GeneIDi 838801.
KEGGi ath:AT1G21980.

Organism-specific databases

GeneFarmi 5099.
TAIRi AT1G21980.

Phylogenomic databases

eggNOGi COG4642.
HOGENOMi HOG000193875.
InParanoidi Q56YP2.
KOi K00889.
OMAi DNTGEKM.
PhylomeDBi Q56YP2.

Enzyme and pathway databases

BioCyci ARA:AT1G21980-MONOMER.
Reactomei REACT_187642. Synthesis of PIPs at the plasma membrane.

Gene expression databases

ExpressionAtlasi Q56YP2. baseline and differential.
Genevestigatori Q56YP2.

Family and domain databases

Gene3Di 3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
InterProi IPR003409. 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 ]
PANTHERi PTHR23086. PTHR23086. 1 hit.
Pfami PF02493. MORN. 7 hits.
PF01504. PIP5K. 1 hit.
[Graphical view ]
PIRSFi PIRSF037274. PIP5K_plant_prd. 1 hit.
SMARTi SM00698. MORN. 7 hits.
SM00330. PIPKc. 1 hit.
[Graphical view ]
PROSITEi PS51455. PIPK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "An Arabidopsis phosphatidylinositol-4-phosphate 5-kinase homolog with seven novel repeats rich in aromatic and glycine residues."
    Satterlee J.S., Sussman M.R.
    Plant Gene Register PGR97-150
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana."
    Mikami K., Katagiri T., Iuchi S., Yamaguchi-Shinozaki K., Shinozaki K.
    Plant J. 15:563-568(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "AtPIP5K1, an Arabidopsis thaliana phosphatidylinositol phosphate kinase, synthesizes PtdIns(3,4)P(2) and PtdIns(4,5)P(2) in vitro and is inhibited by phosphorylation."
    Westergren T., Dove S.K., Sommarin M., Pical C.
    Biochem. J. 359:583-589(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  7. "An Arabidopsis inositol phospholipid kinase strongly expressed in procambial cells: synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 in insect cells by 5-phosphorylation of precursors."
    Elge S., Brearley C., Xia H.J., Kehr J., Xue H.W., Mueller-Roeber B.
    Plant J. 26:561-571(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  8. "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.

Entry informationi

Entry nameiPI5K1_ARATH
AccessioniPrimary (citable) accession number: Q56YP2
Secondary accession number(s): O22503, O82120, Q9LM65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 80 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3