Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70181

- PI51B_MOUSE

UniProt

P70181 - PI51B_MOUSE

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 beta

Gene

Pip5k1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    3. protein binding Source: IntAct

    GO - Biological processi

    1. phosphatidylinositol metabolic process Source: MGI
    2. phosphatidylinositol phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_225118. 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: Chromosome 19

    Organism-specific databases

    MGIiMGI:107930. Pip5k1b.

    Subcellular locationi

    Endomembrane system By similarity
    Note: Associated with membranes.By similarity

    GO - Cellular componenti

    1. endomembrane system Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-KW
    3. uropod Source: Ensembl

    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 25-288.
    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.
    GeneTreeiENSGT00690000101870.
    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. Align

    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

    MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER    50
    DVLMQDFYVV ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI 100
    KPDDYLYSIC SEPLIELSNP GASGSLFFLT SDDEFIIKTV QHKEAEFLQK 150
    LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG INIRIVVMNN VLPRAMRMHL 200
    TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF DTETYNALMK 250
    TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN VPDAKRPGMQ 300
    KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID 350
    ILQSYRLMKK LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ 400
    ALKASPSKKR CNSIAALKAT SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD 450
    EEALGSRHRP DLVPSTPSLF EAASLATTIS SSSLYVGEHY PHDRTTLYSN 500
    SKGLPSSSTF TLEEGTIYLT AEPNTLDLQD DASVLDVYL 539
    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. 1 PublicationCurated
    Sequence conflicti425 – 4251V → L in AAC05374. 1 PublicationCurated
    Sequence conflicti437 – 4371R → Q in AAC05374. 1 PublicationCurated
    Sequence conflicti525 – 5284TLDL → ALET in AAC05374. 1 PublicationCurated

    Alternative sequence

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006526763.1. [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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS37940.1. [P70181-1 ]
    RefSeqi NP_032872.1. NM_008846.2. [P70181-1 ]
    XP_006526826.1. XM_006526763.1. [P70181-1 ]
    UniGenei Mm.217214.

    3D structure databases

    ProteinModelPortali P70181.
    SMRi P70181. Positions 25-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P70181. 3 interactions.
    MINTi MINT-1651965.
    STRINGi 10090.ENSMUSP00000025800.

    PTM databases

    PhosphoSitei P70181.

    Proteomic databases

    MaxQBi P70181.
    PaxDbi P70181.
    PRIDEi P70181.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025800 ; ENSMUSP00000025800 ; ENSMUSG00000024867 . [P70181-1 ]
    ENSMUST00000112673 ; ENSMUSP00000108292 ; ENSMUSG00000024867 . [P70181-2 ]
    GeneIDi 18719.
    KEGGi mmu:18719.
    UCSCi uc008hap.1. mouse. [P70181-1 ]
    uc012bjs.1. mouse. [P70181-2 ]

    Organism-specific databases

    CTDi 8395.
    MGIi MGI:107930. Pip5k1b.

    Phylogenomic databases

    eggNOGi COG5253.
    GeneTreei ENSGT00690000101870.
    HOGENOMi HOG000193876.
    HOVERGENi HBG052818.
    InParanoidi P70181.
    KOi K00889.
    OMAi EHYPHDR.
    OrthoDBi EOG70W3DM.
    PhylomeDBi P70181.
    TreeFami TF319618.

    Enzyme and pathway databases

    Reactomei REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_225118. WNT mediated activation of DVL.

    Miscellaneous databases

    NextBioi 294817.
    PROi P70181.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70181.
    Genevestigatori P70181.

    Family and domain databases

    Gene3Di 3.30.800.10. 1 hit.
    3.30.810.10. 1 hit.
    InterProi 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 PF01504. PIP5K. 1 hit.
    [Graphical view ]
    SMARTi SM00330. PIPKc. 1 hit.
    [Graphical view ]
    PROSITEi PS51455. PIPK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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