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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

Pip5k1c

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

Functioni

Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth.10 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.1 Publication

Kineticsi

  1. KM=37 µM for PtdIns4P
  2. KM=39 µM for ATP

    GO - Molecular functioni

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

    GO - Biological processi

    • axonogenesis Source: MGI
    • chemotaxis Source: UniProtKB-KW
    • cytoskeletal anchoring at plasma membrane Source: MGI
    • exocytosis Source: UniProtKB-KW
    • phagocytosis Source: UniProtKB-KW
    • phosphatidylinositol metabolic process Source: MGI
    • phosphatidylinositol phosphorylation Source: GOC
    • platelet aggregation Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Cell adhesion, Chemotaxis, Endocytosis, Exocytosis, Phagocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
    REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (EC:2.7.1.68)
    Short name:
    PIP5K1-gamma
    Short name:
    PtdIns(4)P-5-kinase 1 gamma
    Alternative name(s):
    Phosphatidylinositol 4-phosphate 5-kinase type I gamma
    Short name:
    PIP5KIgamma
    Gene namesi
    Name:Pip5k1c
    Synonyms:Kiaa0589
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 10

    Organism-specific databases

    MGIiMGI:1298224. Pip5k1c.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    According to some authors, mutants die within hours after birth and are unable to feed after birth (PubMed:15386003). According to another report, mutants are embryonically lethal at organogenesis stage, and display cardiovascular and neuronal defects (PubMed:15386003). PIP5K1C and PIP5K1B double mutant mice die within minutes after birth. PIP5K1C and PIP5K1A double mutant mice are embryonic lethal. Bone marrow-derived macrophages are defective in phagocytosis, attachment to IgG-opsonized particles and Fc-gamma-R clustering, and display highly polymerized actin cytoskeleton. Neurons display defects in synaptic transmission due to defects in synaptic vesicle trafficking at different levels. T-cells mutant for isoform 1 display increase adhesion and polarization.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi253 – 2531D → A: Abolishes lipid kinase activity. Does not affect targeting of TLN1 to plasma membrane. Affects assembly of TLN1 into focal adhesions. Affects uropodium formation and retraction of the cell rear. 2 Publications
    Mutagenesisi634 – 6341Y → F: Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Does not affect lipid kinase activity. Does not alter binding to tailin. Decreased tailin assembly into focal adhesions. Increased interaction with PLCG1. 1 Publication
    Mutagenesisi635 – 6351F → A: Abolishes interaction with AP2B1. 1 Publication
    Mutagenesisi642 – 6421W → A: Abolishes interaction with AP2B1. 1 Publication
    Mutagenesisi644 – 6441Y → F: Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. 4 Publications
    Mutagenesisi645 – 6451S → F: Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions. 1 Publication
    Mutagenesisi646 – 6461P → F: Abolishes interaction with AP-2 complex. 1 Publication
    Mutagenesisi647 – 6471L → V: Abolishes interaction with AP-2 complex. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 661661Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPRO_0000185463Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei268 – 2681N6-acetyllysineBy similarity
    Modified residuei634 – 6341Phosphotyrosine; by EGFR1 Publication
    Modified residuei644 – 6441Phosphotyrosine; by CSK1 Publication
    Modified residuei645 – 6451Phosphoserine; by CDK5, MAPK1 and CDK1By similarity

    Post-translational modificationi

    Phosphorylation on Ser-645 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-644 is necessary for targeting to focal adhesions. Phosphorylation on Ser-645 and Tyr-644 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-634 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-644 enhances binding to tailins (TLN1 and TLN2); others that phosphorylation at Tyr-644 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-645.5 Publications
    Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells (By similarity).By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO70161.
    PaxDbiO70161.
    PRIDEiO70161.

    PTM databases

    PhosphoSiteiO70161.

    Expressioni

    Tissue specificityi

    High expression in brain. Also detected in lung, thymus, heart, testicle, kidney and embryo. Highly expressed in forebrain, in particular in cerebellum, hippocampus and cerebral cortex.3 Publications

    Developmental stagei

    Expression increases during embryonic development and continued to steadily increase postnatally.1 Publication

    Gene expression databases

    BgeeiO70161.
    ExpressionAtlasiO70161. baseline and differential.
    GenevisibleiO70161. MM.

    Interactioni

    Subunit structurei

    Isoform 1 interacts with TLN1. Interacts with TLN2; interaction stimulates lipid kinase activity. May compete with beta-integrins for the same binding site on TLN1 and TLN2. Interacts with ARF6 (By similarity). Interacts with AP2B1. Isoform 1 interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C. Interacts with CDH1 (By similarity). Interacts with CSK. Interacts with PLCG1; interaction is abolished upon EGF stimulation.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ap2b1Q9DBG3-13EBI-773657,EBI-775239
    Ap2b1Q9DBG3-28EBI-773657,EBI-7257021

    Protein-protein interaction databases

    IntActiO70161. 8 interactions.
    MINTiMINT-4105231.
    STRINGi10090.ENSMUSP00000100964.

    Structurei

    Secondary structure

    1
    661
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi642 – 6443Combined sources
    Helixi646 – 6483Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y19X-ray2.60A/C/E/G/I/K638-651[»]
    2H7DNMR-B643-652[»]
    2H7ENMR-B643-652[»]
    ProteinModelPortaliO70161.
    SMRiO70161. Positions 76-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO70161.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini75 – 443369PIPKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni636 – 66126Mediates interaction with TLN2Add
    BLAST

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5253.
    GeneTreeiENSGT00760000119184.
    HOGENOMiHOG000193876.
    HOVERGENiHBG052818.
    InParanoidiO70161.
    KOiK00889.
    OrthoDBiEOG70W3DM.
    PhylomeDBiO70161.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O70161-1) [UniParc]FASTAAdd to basket

    Also known as: PIPKIgamma661

    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
    MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP
    60 70 80 90 100
    GPGHGKKLGH RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER
    110 120 130 140 150
    DVLMQDFYVV ESIFFPSEGS NLTPAHHFQD FRFKTYAPVA FRYFRELFGI
    160 170 180 190 200
    RPDDYLYSLC NEPLIELSNP GASGSVFYVT SDDEFIIKTV MHKEAEFLQK
    210 220 230 240 250
    LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN VLPRVVKMHL
    260 270 280 290 300
    KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK
    310 320 330 340 350
    TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ
    360 370 380 390 400
    KALYSTAMES IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL
    410 420 430 440 450
    QSYRFIKKLE HTWKALVHDG DTVSVHRPSF YAERFFKFMS STVFRKSSSL
    460 470 480 490 500
    KSSPSKKGRG ALLAVKPLGP TAAFSASQIP SEREDVQYDL RGARSYPTLE
    510 520 530 540 550
    DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS DTSEQPRYRR
    560 570 580 590 600
    RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG
    610 620 630 640 650
    ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFPTDER SWVYSPLHYS
    660
    ARPASDGESD T
    Length:661
    Mass (Da):72,408
    Last modified:October 25, 2005 - v2
    Checksum:i4A3B71E4465B83C3
    GO
    Isoform 2 (identifier: O70161-2) [UniParc]FASTAAdd to basket

    Also known as: PIPKIgamma627

    The sequence of this isoform differs from the canonical sequence as follows:
         343-402: Missing.
         635-635: F → FFAHGRYWLFSPRRRQLRAVTPNHTGT

    Note: No experimental confirmation available.
    Show »
    Length:627
    Mass (Da):69,199
    Checksum:iC40D860D3F3419BD
    GO
    Isoform 3 (identifier: O70161-3) [UniParc]FASTAAdd to basket

    Also known as: PIPKIgamma635

    The sequence of this isoform differs from the canonical sequence as follows:
         636-661: Missing.

    Show »
    Length:635
    Mass (Da):69,502
    Checksum:i781F012CC868250A
    GO

    Sequence cautioni

    The sequence BAC65601.2 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101V → M in BAA25664 (PubMed:9535851).Curated
    Sequence conflicti122 – 1221L → F in BAA25664 (PubMed:9535851).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei343 – 40260Missing in isoform 2. 1 PublicationVSP_016013Add
    BLAST
    Alternative sequencei635 – 6351F → FFAHGRYWLFSPRRRQLRAV TPNHTGT in isoform 2. 1 PublicationVSP_016014
    Alternative sequencei636 – 66126Missing in isoform 3. 2 PublicationsVSP_016015Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB006916 mRNA. Translation: BAA25664.1.
    AK122319 mRNA. Translation: BAC65601.2. Different initiation.
    AK154816 mRNA. Translation: BAE32849.1.
    AK171576 mRNA. Translation: BAE42536.1.
    BC019138 mRNA. Translation: AAH19138.1.
    BC094665 mRNA. Translation: AAH94665.1.
    CCDSiCCDS35994.1. [O70161-1]
    CCDS48643.1. [O70161-3]
    RefSeqiNP_001140159.1. NM_001146687.2. [O70161-3]
    NP_001280575.1. NM_001293646.1.
    NP_001280576.1. NM_001293647.1.
    NP_032870.2. NM_008844.3. [O70161-1]
    UniGeneiMm.29836.
    Mm.471109.

    Genome annotation databases

    EnsembliENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902. [O70161-1]
    ENSMUST00000163075; ENSMUSP00000124155; ENSMUSG00000034902. [O70161-3]
    GeneIDi18717.
    KEGGimmu:18717.
    UCSCiuc007ghc.2. mouse. [O70161-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB006916 mRNA. Translation: BAA25664.1.
    AK122319 mRNA. Translation: BAC65601.2. Different initiation.
    AK154816 mRNA. Translation: BAE32849.1.
    AK171576 mRNA. Translation: BAE42536.1.
    BC019138 mRNA. Translation: AAH19138.1.
    BC094665 mRNA. Translation: AAH94665.1.
    CCDSiCCDS35994.1. [O70161-1]
    CCDS48643.1. [O70161-3]
    RefSeqiNP_001140159.1. NM_001146687.2. [O70161-3]
    NP_001280575.1. NM_001293646.1.
    NP_001280576.1. NM_001293647.1.
    NP_032870.2. NM_008844.3. [O70161-1]
    UniGeneiMm.29836.
    Mm.471109.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y19X-ray2.60A/C/E/G/I/K638-651[»]
    2H7DNMR-B643-652[»]
    2H7ENMR-B643-652[»]
    ProteinModelPortaliO70161.
    SMRiO70161. Positions 76-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiO70161. 8 interactions.
    MINTiMINT-4105231.
    STRINGi10090.ENSMUSP00000100964.

    PTM databases

    PhosphoSiteiO70161.

    Proteomic databases

    MaxQBiO70161.
    PaxDbiO70161.
    PRIDEiO70161.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902. [O70161-1]
    ENSMUST00000163075; ENSMUSP00000124155; ENSMUSG00000034902. [O70161-3]
    GeneIDi18717.
    KEGGimmu:18717.
    UCSCiuc007ghc.2. mouse. [O70161-1]

    Organism-specific databases

    CTDi23396.
    MGIiMGI:1298224. Pip5k1c.
    RougeiSearch...

    Phylogenomic databases

    eggNOGiCOG5253.
    GeneTreeiENSGT00760000119184.
    HOGENOMiHOG000193876.
    HOVERGENiHBG052818.
    InParanoidiO70161.
    KOiK00889.
    OrthoDBiEOG70W3DM.
    PhylomeDBiO70161.
    TreeFamiTF319618.

    Enzyme and pathway databases

    ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
    REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

    Miscellaneous databases

    ChiTaRSiPip5k1c. mouse.
    EvolutionaryTraceiO70161.
    NextBioi294809.
    PROiO70161.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO70161.
    ExpressionAtlasiO70161. baseline and differential.
    GenevisibleiO70161. 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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    3. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "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 3).
      Strain: C57BL/6J and NOD.
    5. "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 3).
      Strain: FVB/N.
      Tissue: Brain and Kidney.
    6. "Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions."
      Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.
      Nature 420:89-93(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FOCAL ADHESION DYNAMIC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH TLN1, MUTAGENESIS OF ASP-253.
    7. "Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch."
      Ling K., Doughman R.L., Iyer V.V., Firestone A.J., Bairstow S.F., Mosher D.F., Schaller M.D., Anderson R.A.
      J. Cell Biol. 163:1339-1349(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLN1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-644, MUTAGENESIS OF TYR-644.
    8. "A novel neuronal-specific splice variant of Type I phosphatidylinositol 4-phosphate 5-kinase isoform gamma."
      Giudici M.-L., Emson P.C., Irvine R.F.
      Biochem. J. 379:489-496(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking."
      Di Paolo G., Moskowitz H.S., Gipson K., Wenk M.R., Voronov S., Obayashi M., Flavell R., Fitzsimonds R.M., Ryan T.A., De Camilli P.
      Nature 431:415-422(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SYNAPTIC VESICLE TRAFFICKING, DISRUPTION PHENOTYPE.
    10. "Type Igamma661 phosphatidylinositol phosphate kinase directly interacts with AP2 and regulates endocytosis."
      Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C., Anderson R.A.
      J. Biol. Chem. 281:20632-20642(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH AP2M1 AND TLN1, PHOSPHORYLATION, MUTAGENESIS OF TYR-644; PRO-646 AND LEU-647.
    11. "Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration."
      Sun Y., Ling K., Wagoner M.P., Anderson R.A.
      J. Cell Biol. 178:297-308(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION AND ADHESION, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-634, MUTAGENESIS OF TYR-634; TYR-644 AND SER-645.
    12. "Type Igamma PIP kinase is a novel uropod component that regulates rear retraction during neutrophil chemotaxis."
      Lokuta M.A., Senetar M.A., Bennin D.A., Nuzzi P.A., Chan K.T., Ott V.L., Huttenlocher A.
      Mol. Biol. Cell 18:5069-5080(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEUTROPHIL CHEMOTAXIS, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-253.
    13. "PIP5KI gamma is required for cardiovascular and neuronal development."
      Wang Y., Lian L., Golden J.A., Morrisey E.E., Abrams C.S.
      Proc. Natl. Acad. Sci. U.S.A. 104:11748-11753(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EMBRYOGENESIS, DISRUPTION PHENOTYPE.
    14. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Clathrin regulates the association of PIPKIgamma661 with the AP-2 adaptor beta2 appendage."
      Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A., Traub L.M.
      J. Biol. Chem. 284:13924-13939(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2B1, MUTAGENESIS OF PHE-635; TRP-642 AND TYR-644.
    16. "Essential and unique roles of PIP5K-gamma and -alpha in Fcgamma receptor-mediated phagocytosis."
      Mao Y.S., Yamaga M., Zhu X., Wei Y., Sun H.-Q., Wang J., Yun M., Wang Y., Di Paolo G., Bennett M., Mellman I., Abrams C.S., De Camilli P., Lu C.Y., Yin H.L.
      J. Cell Biol. 184:281-296(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHAGOCYTOSIS, SUBCELLULAR LOCATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE.
    17. "Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5-bisphosphate synthesis in the brain."
      Volpicelli-Daley L.A., Lucast L., Gong L.-W., Liu L., Sasaki J., Sasaki T., Abrams C.S., Kanaho Y., De Camilli P.
      J. Biol. Chem. 285:28708-28714(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EMBRYOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    18. "PIPKI gamma 90 negatively regulates LFA-1-mediated adhesion and activation in antigen-induced CD4+ T cells."
      Wernimont S.A., Legate K.R., Simonson W.T.N., Fassler R., Huttenlocher A.
      J. Immunol. 185:4714-4723(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL ADHESION, DISRUPTION PHENOTYPE.
    19. "Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions."
      de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H., Critchley D.R., Campbell I.D., Liddington R.C.
      J. Biol. Chem. 280:8381-8386(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 636-652 IN COMPLEX WITH TLN1.

    Entry informationi

    Entry nameiPI51C_MOUSE
    AccessioniPrimary (citable) accession number: O70161
    Secondary accession number(s): Q505A1, Q80TW9, Q8VCU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: June 24, 2015
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.