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Q5I6B8

- PI51C_RAT

UniProt

Q5I6B8 - PI51C_RAT

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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

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.1 Publication

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
Complete GO annotation...

GO - Biological processi

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

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; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junctionfocal adhesion. Cell junctionadherens junction. Cell projectionruffle membrane. Cell projectionphagocytic cup. 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
Complete GO annotation...

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 gamma
PRO_0000185464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-acetyllysine By similarity
Modified residuei268 – 2681N6-acetyllysine By similarity
Modified residuei635 – 6351Phosphotyrosine; by EGFR By similarity
Modified residuei671 – 6711Phosphotyrosine; by CSK By similarity
Modified residuei672 – 6721Phosphoserine; by CDK5, MAPK1 and CDK1 By similarity

Post-translational modificationi

Phosphorylation on Ser-672 negatively regulates binding to TLN2 and is strongly stimulated in mitosis By similarity. Phosphorylation on Tyr-671 is necessary for targeting to focal adhesions By similarity. Phosphorylation on Ser-672 and Tyr-671 are mutually exclusive By similarity. Phosphorylated by SYK and CSK By similarity. Tyrosine phosphorylation is enhanced by PTK2 signaling By similarity. Phosphorylated at Tyr-635 upon EGF stimulation By similarity. 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.

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ5I6B8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 443369PIPK
Add
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.

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

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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...

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: April 16, 2014
This is version 73 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

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