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Q5I6B8

- PI51C_RAT

UniProt

Q5I6B8 - PI51C_RAT

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

Pip5k1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (15 Feb 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 By similarity.By similarity

    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 ARF6.

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. chemotaxis Source: UniProtKB-KW
    3. exocytosis Source: UniProtKB-KW
    4. phagocytosis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Cell adhesion, Chemotaxis, Endocytosis, Exocytosis, Phagocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1309938. Pip5k1c.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Endomembrane system 1 Publication. Cytoplasm 1 Publication. Cell junctionfocal adhesion 1 Publication. Cell junctionadherens junction 1 Publication. Cell projectionruffle membrane 1 Publication. Cell projectionphagocytic cup 1 Publication. Cell projectionuropodium 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi188 – 1881K → A: Reduces activity by over 99%. 1 Publication
    Mutagenesisi316 – 3161D → K: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 688688Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPRO_0000185464Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei268 – 2681N6-acetyllysineBy similarity
    Modified residuei635 – 6351Phosphotyrosine; by EGFRBy similarity
    Modified residuei671 – 6711Phosphotyrosine; by CSKBy similarity
    Modified residuei672 – 6721Phosphoserine; by CDK5, MAPK1 and CDK1By similarity

    Post-translational modificationi

    Phosphorylation on Ser-672 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-671 is necessary for targeting to focal adhesions. Phosphorylation on Ser-672 and Tyr-671 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-635 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-671 enhances binding to tailins (TLN1 and TLN2) By similarity; others that phosphorylation at Tyr-671 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-672.By similarity
    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

    PaxDbiQ5I6B8.
    PRIDEiQ5I6B8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ5I6B8.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ5I6B8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5253.
    HOGENOMiHOG000193876.
    HOVERGENiHBG052818.
    InParanoidiQ5I6B8.
    KOiK00889.
    PhylomeDBiQ5I6B8.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q5I6B8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAIL AEAPLVTGQP    50
    GPGHGKKLGH RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER 100
    DVLMQDFYVV ESIFFPSEGS NLTPAHHFQD FRFKTYAPVA FRYFRELFGI 150
    RPDDYLYSLC NEPLIELSNP GASGSVFYVT SDDEFIIKTV MHKEAEFLQK 200
    LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN VLPRVVKMHL 250
    KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK 300
    TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ 350
    KALYSTARES IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL 400
    QSYRFIKKLE HTWKALVHDG DTVSVHRPSF YAERFFKFMS STVFRKSSSL 450
    KSSPSKKGRG ALLAVKPLGP TAAFSASQIP SEREDVQYDL RGARSYPTLE 500
    DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS DTSEQPRYRR 550
    RTQSSGQDGR PQEELHAEDL QKITVQVEPV CGVGVVVPKE QGAGVEVPPS 600
    GASAAATVEV DAASQASEPA SQASDEEDAP STDIYFFAHG RYWLFSPRRR 650
    RLRAVTPSHT GAPTDGRSWV YSPLHYSARP ASDGESDT 688
    Length:688
    Mass (Da):75,594
    Last modified:February 15, 2005 - v1
    Checksum:iF34E175EFFF54D5D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY850259 mRNA. Translation: AAW34235.1.
    RefSeqiNP_001009967.2. NM_001009967.2.
    NP_001029142.1. NM_001033970.1.
    UniGeneiRn.2928.

    Genome annotation databases

    GeneIDi314641.
    KEGGirno:314641.
    UCSCiRGD:1309938. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY850259 mRNA. Translation: AAW34235.1 .
    RefSeqi NP_001009967.2. NM_001009967.2.
    NP_001029142.1. NM_001033970.1.
    UniGenei Rn.2928.

    3D structure databases

    ProteinModelPortali Q5I6B8.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q5I6B8.
    PRIDEi Q5I6B8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 314641.
    KEGGi rno:314641.
    UCSCi RGD:1309938. rat.

    Organism-specific databases

    CTDi 23396.
    RGDi 1309938. Pip5k1c.

    Phylogenomic databases

    eggNOGi COG5253.
    HOGENOMi HOG000193876.
    HOVERGENi HBG052818.
    InParanoidi Q5I6B8.
    KOi K00889.
    PhylomeDBi Q5I6B8.

    Miscellaneous databases

    NextBioi 668018.

    Gene expression databases

    Genevestigatori Q5I6B8.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-188 AND ASP-316, TISSUE SPECIFICITY.
      Tissue: Hippocampus.
    2. "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.

    Entry informationi

    Entry nameiPI51C_RAT
    AccessioniPrimary (citable) accession number: Q5I6B8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 74 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3