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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 beta

Gene

Pip5k1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion.3 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by phosphatidic acid.2 Publications

Kineticsi

  1. KM=34 µM for PtdIns4P1 Publication
  2. KM=27 µM for ATP1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. phosphatidylinositol metabolic process Source: MGI
  2. phosphatidylinositol phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_337993. WNT mediated activation of DVL.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 beta (EC:2.7.1.68)
Short name:
PIP5K1-beta
Short name:
PtdIns(4)P-5-kinase 1 beta
Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I alpha
Short name:
PIP5KIalpha
Phosphatidylinositol 4-phosphate 5-kinase type I beta
Short name:
PIP5KIbeta
Gene namesi
Name:Pip5k1b
Synonyms:Pip5k1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:107930. Pip5k1b.

Subcellular locationi

  1. Endomembrane system By similarity

  2. Note: Associated with membranes.By similarity

GO - Cellular componenti

  1. endomembrane system Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB-KW
  3. uropod Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381K → A: Almost complete loss of kinase activity. 1 Publication
Mutagenesisi227 – 2271D → A: Reduces kinase activity by 98%. Loss of actin-remodeling activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Phosphatidylinositol 4-phosphate 5-kinase type-1 betaPRO_0000185459Add
BLAST

Proteomic databases

MaxQBiP70181.
PaxDbiP70181.
PRIDEiP70181.

PTM databases

PhosphoSiteiP70181.

Expressioni

Tissue specificityi

Highly expressed in brain and testis. Barely detectable in liver and skeletal muscle.1 Publication

Gene expression databases

BgeeiP70181.
GenevestigatoriP70181.

Interactioni

Subunit structurei

Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Clic4Q9QYB14EBI-645167,EBI-645175

Protein-protein interaction databases

IntActiP70181. 3 interactions.
MINTiMINT-1651965.
STRINGi10090.ENSMUSP00000025800.

Structurei

3D structure databases

ProteinModelPortaliP70181.
SMRiP70181. Positions 25-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 395371PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiP70181.
KOiK00889.
OMAiEHYPHDR.
OrthoDBiEOG70W3DM.
PhylomeDBiP70181.
TreeFamiTF319618.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. 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.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P70181-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER
60 70 80 90 100
DVLMQDFYVV ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI
110 120 130 140 150
KPDDYLYSIC SEPLIELSNP GASGSLFFLT SDDEFIIKTV QHKEAEFLQK
160 170 180 190 200
LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG INIRIVVMNN VLPRAMRMHL
210 220 230 240 250
TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF DTETYNALMK
260 270 280 290 300
TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN VPDAKRPGMQ
310 320 330 340 350
KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID
360 370 380 390 400
ILQSYRLMKK LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ
410 420 430 440 450
ALKASPSKKR CNSIAALKAT SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD
460 470 480 490 500
EEALGSRHRP DLVPSTPSLF EAASLATTIS SSSLYVGEHY PHDRTTLYSN
510 520 530
SKGLPSSSTF TLEEGTIYLT AEPNTLDLQD DASVLDVYL
Length:539
Mass (Da):60,803
Last modified:February 1, 1997 - v1
Checksum:iA8478C9E21546AC3
GO
Isoform 2 (identifier: P70181-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-452: Missing.

Note: No experimental confirmation available.

Show »
Length:487
Mass (Da):55,080
Checksum:i41ADCD8B56419DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911V → A in AAC05374 (Ref. 2) Curated
Sequence conflicti425 – 4251V → L in AAC05374 (Ref. 2) Curated
Sequence conflicti437 – 4371R → Q in AAC05374 (Ref. 2) Curated
Sequence conflicti525 – 5284TLDL → ALET in AAC05374 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei401 – 45252Missing in isoform 2. 1 PublicationVSP_016012Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86176 mRNA. Translation: BAA13030.1.
AF048695 mRNA. Translation: AAC05374.1.
AK149354 mRNA. Translation: BAE28830.1.
AK164552 mRNA. Translation: BAE37836.1.
AK146100 mRNA. Translation: BAE26901.1.
BC034864 mRNA. Translation: AAH34864.1.
CCDSiCCDS37940.1. [P70181-1]
RefSeqiNP_032872.1. NM_008846.2. [P70181-1]
XP_006526826.1. XM_006526763.2. [P70181-1]
UniGeneiMm.217214.

Genome annotation databases

EnsembliENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867. [P70181-1]
ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867. [P70181-2]
GeneIDi18719.
KEGGimmu:18719.
UCSCiuc008hap.1. mouse. [P70181-1]
uc012bjs.1. mouse. [P70181-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86176 mRNA. Translation: BAA13030.1.
AF048695 mRNA. Translation: AAC05374.1.
AK149354 mRNA. Translation: BAE28830.1.
AK164552 mRNA. Translation: BAE37836.1.
AK146100 mRNA. Translation: BAE26901.1.
BC034864 mRNA. Translation: AAH34864.1.
CCDSiCCDS37940.1. [P70181-1]
RefSeqiNP_032872.1. NM_008846.2. [P70181-1]
XP_006526826.1. XM_006526763.2. [P70181-1]
UniGeneiMm.217214.

3D structure databases

ProteinModelPortaliP70181.
SMRiP70181. Positions 25-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70181. 3 interactions.
MINTiMINT-1651965.
STRINGi10090.ENSMUSP00000025800.

PTM databases

PhosphoSiteiP70181.

Proteomic databases

MaxQBiP70181.
PaxDbiP70181.
PRIDEiP70181.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867. [P70181-1]
ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867. [P70181-2]
GeneIDi18719.
KEGGimmu:18719.
UCSCiuc008hap.1. mouse. [P70181-1]
uc012bjs.1. mouse. [P70181-2]

Organism-specific databases

CTDi8395.
MGIiMGI:107930. Pip5k1b.

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiP70181.
KOiK00889.
OMAiEHYPHDR.
OrthoDBiEOG70W3DM.
PhylomeDBiP70181.
TreeFamiTF319618.

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_337993. WNT mediated activation of DVL.

Miscellaneous databases

NextBioi294817.
PROiP70181.
SOURCEiSearch...

Gene expression databases

BgeeiP70181.
GenevestigatoriP70181.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. 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.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol 4-phosphate 5-kinase."
    Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T., Oka Y.
    J. Biol. Chem. 271:23611-23614(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Insulinoma.
  2. Machesky L.M.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Amnion, Heart and Retina.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family."
    Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y.
    J. Biol. Chem. 273:8741-8748(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-138, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly."
    Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.
    Curr. Biol. 10:153-156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF ASP-227.
  7. "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity."
    Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M., Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.
    EMBO J. 19:5440-5449(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLD1 AND PLD2, SUBCELLULAR LOCATION.
  8. "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi compartment."
    Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F., Cockcroft S.
    J. Biol. Chem. 275:13962-13966(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF1.
  9. "The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha."
    Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.
    Mol. Cell. Biol. 25:3956-3966(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AJUBA.
  10. "Loss of PIP5KIbeta demonstrates that PIP5KI isoform-specific PIP2 synthesis is required for IP3 formation."
    Wang Y., Chen X., Lian L., Tang T., Stalker T.J., Sasaki T., Kanaho Y., Brass L.F., Choi J.K., Hartwig J.H., Abrams C.S.
    Proc. Natl. Acad. Sci. U.S.A. 105:14064-14069(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELETS.

Entry informationi

Entry nameiPI51B_MOUSE
AccessioniPrimary (citable) accession number: P70181
Secondary accession number(s): O70335, Q8JZY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: February 1, 1997
Last modified: April 1, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

There is confusion in the literature with phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due to the fact that frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-kinase type I alpha.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.