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 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-phosphatidylinositol-4-phosphate 5-kinase activity Source: MGI
    • ATP binding Source: UniProtKB-KW

    GO - Biological processi

    • phosphatidylinositol metabolic process Source: MGI
    • 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

    GO - Cellular componenti

    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.
    GenevisibleiP70181. MM.

    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 25-288.
    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.
    OMAiHYPHDRT.
    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 25-288.
    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.
    OMAiHYPHDRT.
    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.
    GenevisibleiP70181. MM.

    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: July 22, 2015
    This is version 115 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.