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O60331

- PI51C_HUMAN

UniProt

O60331 - PI51C_HUMAN

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

PIP5K1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (25 Oct 2005)
      Previous versions | rss
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    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.4 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by interaction with TLN2.1 Publication

    GO - Molecular functioni

    1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. adherens junction assembly Source: UniProtKB
    3. axon guidance Source: Reactome
    4. clathrin-mediated endocytosis Source: UniProtKB
    5. cytoskeletal anchoring at plasma membrane Source: Ensembl
    6. neutrophil chemotaxis Source: UniProtKB
    7. phagocytosis Source: UniProtKB
    8. phosphatidylinositol biosynthetic process Source: Reactome
    9. phospholipid metabolic process Source: Reactome
    10. platelet aggregation Source: Ensembl
    11. single organismal cell-cell adhesion Source: UniProtKB
    12. small molecule metabolic process Source: Reactome
    13. synaptic vesicle endocytosis Source: UniProtKB
    14. synaptic vesicle exocytosis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Cell adhesion, Chemotaxis, Endocytosis, Exocytosis, Phagocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02710-MONOMER.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_19279. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:8996. PIP5K1C.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junctionfocal adhesion. Cell junctionadherens junction. Cell projectionruffle membrane. Cell projectionphagocytic cup. Cell projectionuropodium
    Note: Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endomembrane system Source: UniProtKB-SubCell
    3. focal adhesion Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. phagocytic cup Source: UniProtKB-SubCell
    6. ruffle membrane Source: UniProtKB-SubCell
    7. uropod Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Lethal congenital contracture syndrome 3 (LCCS3) [MIM:611369]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS3 patients present at birth with severe multiple joint contractures and severe muscle wasting and atrophy, mainly in the legs. Death occurs minutes to hours after birth due to respiratory insufficiency. The phenotype can be distinguished from that of LCCS1 by the absence of hydrops, fractures and multiple pterygia, and from LCCS2 by the absence of neurogenic bladder defect.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti253 – 2531D → N in LCCS3; loss of activity. 1 Publication
    VAR_036996

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi650 – 6501S → D: Abolishes binding to TLN2. Affects localization to focal adhesions. 1 Publication
    Mutagenesisi650 – 6501S → N: Does not affect binding to TLN2 and localization to focal adhesions. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi611369. phenotype.
    Orphaneti137783. Lethal congenital contracture syndrome type 3.
    PharmGKBiPA33329.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 668668Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPRO_0000185462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-acetyllysine1 Publication
    Modified residuei268 – 2681N6-acetyllysine1 Publication
    Modified residuei639 – 6391Phosphotyrosine; by EGFRBy similarity
    Modified residuei649 – 6491Phosphotyrosine; by CSK1 Publication
    Modified residuei650 – 6501Phosphoserine; by CDK5, MAPK1 and CDK11 Publication

    Post-translational modificationi

    Phosphorylation on Ser-650 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-649 is necessary for targeting to focal adhesions. Phosphorylation on Ser-650 and Tyr-649 are mutually exclusive. Phosphorylated by SYK and CSK By similarity. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-639 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-649 enhances binding to tailins (TLN1 and TLN2). According to PubMed:15738269 phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650.By similarity1 Publication
    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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60331.
    PaxDbiO60331.
    PRIDEiO60331.

    PTM databases

    PhosphoSiteiO60331.

    Expressioni

    Tissue specificityi

    Isoform 1 is strongly expressed in brain and also detected in heart and lung. Isoform 2 is strongly expressed in pancreas and liver and in lesser quantities in brain, heart, lung and kidney. Isoform 3 is detected in large amounts in heart and large intestine, is also present in lung, pancreas and thyroid, and to a lesser extent in brain, stomach and kidney.1 Publication

    Gene expression databases

    ArrayExpressiO60331.
    BgeeiO60331.
    CleanExiHS_PIP5K1C.
    GenevestigatoriO60331.

    Organism-specific databases

    HPAiHPA017168.

    Interactioni

    Subunit structurei

    Interacts with TLN1 By similarity. 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. Interacts with AP2B1. Interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C By similarity. Interacts with CDH1. Interacts with CSK By similarity. Interacts with PLCG1; interaction is abolished upon EGF stimulation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IQGAP1P469406EBI-8838062,EBI-297509

    Protein-protein interaction databases

    BioGridi116969. 7 interactions.
    DIPiDIP-39809N.
    IntActiO60331. 1 interaction.
    STRINGi9606.ENSP00000335333.

    Structurei

    Secondary structure

    1
    668
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi644 – 6463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G35NMR-B646-653[»]
    3H1ZX-ray1.83P639-653[»]
    3H85X-ray2.60P646-653[»]
    ProteinModelPortaliO60331.
    SMRiO60331. Positions 76-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60331.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni641 – 66828Mediates interaction with TLN2Add
    BLAST

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5253.
    HOGENOMiHOG000193876.
    HOVERGENiHBG052818.
    InParanoidiO60331.
    KOiK00889.
    OMAiPTDERSW.
    OrthoDBiEOG70W3DM.
    PhylomeDBiO60331.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60331-1) [UniParc]FASTAAdd to Basket

    Also known as: PIPKIgamma-90, PIPKIgamma-668, PIPkinIgamma-a, PIPKIgamma_i2

    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

    MELEVPDEAE SAEAGAVPSE AAWAAESGAA AGLAQKKAAP TEVLSMTAQP    50
    GPGHGKKLGH RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGHLSSKPER 100
    DVLMQDFYVV ESIFFPSEGS NLTPAHHFQD FRFKTYAPVA FRYFRELFGI 150
    RPDDYLYSLC NEPLIELSNP GASGSLFYVT SDDEFIIKTV MHKEAEFLQK 200
    LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN ILPRVVKMHL 250
    KFDLKGSTYK RRASKKEKEK SFPTYKDLDF MQDMPEGLLL DADTFSALVK 300
    TLQRDCLVLE SFKIMDYSLL LGVHNIDQHE RERQAQGAQS TSDEKRPVGQ 350
    KALYSTAMES IQGGAARGEA IESDDTMGGI PAVNGRGERL LLHIGIIDIL 400
    QSYRFIKKLE HTWKALVHDG DTVSVHRPSF YAERFFKFMS NTVFRKNSSL 450
    KSSPSKKGRG GALLAVKPLG PTAAFSASQI PSEREEAQYD LRGARSYPTL 500
    EDEGRPDLLP CTPPSFEEAT TASIATTLSS TSLSIPERSP SETSEQPRYR 550
    RRTQSSGQDG RPQEEPPAEE DLQQITVQVE PACSVEIVVP KEEDAGVEAS 600
    PAGASAAVEV ETASQASDEE GAPASQASDE EDAPATDIYF PTDERSWVYS 650
    PLHYSAQAPP ASDGESDT 668
    Length:668
    Mass (Da):73,260
    Last modified:October 25, 2005 - v2
    Checksum:i45A9FB32B4E43083
    GO
    Isoform 2 (identifier: O60331-2) [UniParc]FASTAAdd to Basket

    Also known as: variant 700, PIPKIgamma-700, PIPKIgamma_i4

    The sequence of this isoform differs from the canonical sequence as follows:
         640-668: FPTDERSWVYSPLHYSAQAPPASDGESDT → FWRLWGPHAP...GAMSCCVSVS

    Show »
    Length:700
    Mass (Da):76,620
    Checksum:iD3E3DC89BDF2E868
    GO
    Isoform 3 (identifier: O60331-3) [UniParc]FASTAAdd to Basket

    Also known as: variant 707, PIPKIgamma-707, PIPKIgamma_i5

    The sequence of this isoform differs from the canonical sequence as follows:
         641-668: PTDERSWVYSPLHYSAQAPPASDGESDT → FTDGRYWIYS...TSVVFQKGFG

    Show »
    Length:707
    Mass (Da):77,484
    Checksum:i42BC87A1C20A5037
    GO
    Isoform 4 (identifier: O60331-4) [UniParc]FASTAAdd to Basket

    Also known as: PIPKIgamma-87, PIPKIgamma-640, PIPkinIgamma-b, PIPKIgamma_i1

    The sequence of this isoform differs from the canonical sequence as follows:
         641-668: Missing.

    Show »
    Length:640
    Mass (Da):70,214
    Checksum:i197B427BF16392C8
    GO

    Sequence cautioni

    The sequence BAA25515.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361V → M in BAH14283. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti253 – 2531D → N in LCCS3; loss of activity. 1 Publication
    VAR_036996

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei640 – 66829FPTDE…GESDT → FWRLWGPHAPTWPWRREGRA ACLCPYPPHVVTPFPGTGLC ASWSPDGTGGLGAMSCCVSV S in isoform 2. 1 PublicationVSP_042078Add
    BLAST
    Alternative sequencei641 – 66828PTDER…GESDT → FTDGRYWIYSPRHRRLRAVT LSASGTVSDRSRPPWGEGAV PLGQQGAAGPRPEAQCLTSV VFQKGFG in isoform 3. 1 PublicationVSP_042080Add
    BLAST
    Alternative sequencei641 – 66828Missing in isoform 4. 1 PublicationVSP_042079Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ965536 mRNA. Translation: ACS73483.1.
    FJ965537 mRNA. Translation: ACS73484.1.
    AB011161 mRNA. Translation: BAA25515.1. Different initiation.
    AK315912 mRNA. Translation: BAH14283.1.
    AC005542 Genomic DNA. Translation: AAC32904.1.
    AC093071 Genomic DNA. No translation available.
    AC004637 Genomic DNA. No translation available.
    CCDSiCCDS32872.1. [O60331-1]
    CCDS56074.1. [O60331-4]
    RefSeqiNP_001182662.1. NM_001195733.1. [O60331-4]
    NP_036530.1. NM_012398.2. [O60331-1]
    XP_005259580.1. XM_005259523.2. [O60331-3]
    UniGeneiHs.282177.

    Genome annotation databases

    EnsembliENST00000335312; ENSP00000335333; ENSG00000186111. [O60331-1]
    ENST00000537021; ENSP00000444779; ENSG00000186111. [O60331-2]
    ENST00000539785; ENSP00000445992; ENSG00000186111. [O60331-4]
    ENST00000589578; ENSP00000466363; ENSG00000186111. [O60331-3]
    GeneIDi23396.
    KEGGihsa:23396.
    UCSCiuc002lyj.2. human. [O60331-1]
    uc010xhr.2. human. [O60331-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ965536 mRNA. Translation: ACS73483.1 .
    FJ965537 mRNA. Translation: ACS73484.1 .
    AB011161 mRNA. Translation: BAA25515.1 . Different initiation.
    AK315912 mRNA. Translation: BAH14283.1 .
    AC005542 Genomic DNA. Translation: AAC32904.1 .
    AC093071 Genomic DNA. No translation available.
    AC004637 Genomic DNA. No translation available.
    CCDSi CCDS32872.1. [O60331-1 ]
    CCDS56074.1. [O60331-4 ]
    RefSeqi NP_001182662.1. NM_001195733.1. [O60331-4 ]
    NP_036530.1. NM_012398.2. [O60331-1 ]
    XP_005259580.1. XM_005259523.2. [O60331-3 ]
    UniGenei Hs.282177.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G35 NMR - B 646-653 [» ]
    3H1Z X-ray 1.83 P 639-653 [» ]
    3H85 X-ray 2.60 P 646-653 [» ]
    ProteinModelPortali O60331.
    SMRi O60331. Positions 76-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116969. 7 interactions.
    DIPi DIP-39809N.
    IntActi O60331. 1 interaction.
    STRINGi 9606.ENSP00000335333.

    Chemistry

    BindingDBi O60331.
    ChEMBLi CHEMBL1908383.
    GuidetoPHARMACOLOGYi 2165.

    PTM databases

    PhosphoSitei O60331.

    Proteomic databases

    MaxQBi O60331.
    PaxDbi O60331.
    PRIDEi O60331.

    Protocols and materials databases

    DNASUi 23396.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335312 ; ENSP00000335333 ; ENSG00000186111 . [O60331-1 ]
    ENST00000537021 ; ENSP00000444779 ; ENSG00000186111 . [O60331-2 ]
    ENST00000539785 ; ENSP00000445992 ; ENSG00000186111 . [O60331-4 ]
    ENST00000589578 ; ENSP00000466363 ; ENSG00000186111 . [O60331-3 ]
    GeneIDi 23396.
    KEGGi hsa:23396.
    UCSCi uc002lyj.2. human. [O60331-1 ]
    uc010xhr.2. human. [O60331-3 ]

    Organism-specific databases

    CTDi 23396.
    GeneCardsi GC19M003631.
    HGNCi HGNC:8996. PIP5K1C.
    HPAi HPA017168.
    MIMi 606102. gene.
    611369. phenotype.
    neXtProti NX_O60331.
    Orphaneti 137783. Lethal congenital contracture syndrome type 3.
    PharmGKBi PA33329.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5253.
    HOGENOMi HOG000193876.
    HOVERGENi HBG052818.
    InParanoidi O60331.
    KOi K00889.
    OMAi PTDERSW.
    OrthoDBi EOG70W3DM.
    PhylomeDBi O60331.
    TreeFami TF319618.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02710-MONOMER.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

    Miscellaneous databases

    ChiTaRSi PIP5K1C. human.
    EvolutionaryTracei O60331.
    GeneWikii PIP5K1C.
    GenomeRNAii 23396.
    NextBioi 45537.
    PROi O60331.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60331.
    Bgeei O60331.
    CleanExi HS_PIP5K1C.
    Genevestigatori O60331.

    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. "Two novel phosphatidylinositol-4-phosphate 5-kinase type Igamma splice variants expressed in human cells display distinctive cellular targeting."
      Schill N.J., Anderson R.A.
      Biochem. J. 422:473-482(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin."
      Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R., Voronov S., Chang S., Guo J., Wenk M.R., De Camilli P.
      Nature 420:85-89(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TLN2, SUBCELLULAR LOCATION, ENZYME REGULATION.
    6. "ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma."
      Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.
      J. Cell Biol. 162:113-124(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARF6, SUBCELLULAR LOCATION.
    7. "Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases."
      Lee S.Y., Voronov S., Letinic K., Nairn A.C., Di Paolo G., De Camilli P.
      J. Cell Biol. 168:789-799(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-649 AND SER-650, MUTAGENESIS OF SER-650.
    8. "Type I gamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin."
      Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., Anderson R.A.
      J. Cell Biol. 176:343-353(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDH1.
    9. "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.
    10. Cited for: ACETYLATION AT LYS-265 AND LYS-268, DEACETYLATION BY SIRT1.
    11. "PIP5K-driven PtdIns(4,5)P2 synthesis: regulation and cellular functions."
      van den Bout I., Divecha N.
      J. Cell Sci. 122:3837-3850(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    12. "Lethal contractural syndrome type 3 (LCCS3) is caused by a mutation in PIP5K1C, which encodes PIPKI gamma of the phophatidylinositol pathway."
      Narkis G., Ofir R., Landau D., Manor E., Volokita M., Hershkowitz R., Elbedour K., Birk O.S.
      Am. J. Hum. Genet. 81:530-539(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LCCS3 ASN-253, CHARACTERIZATION OF VARIANT LCCS3 ASN-253.

    Entry informationi

    Entry nameiPI51C_HUMAN
    AccessioniPrimary (citable) accession number: O60331
    Secondary accession number(s): B7Z9E7
    , C6GIJ7, C6GIJ8, Q7LE07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3