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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

Pip5k1c

Organism
Rattus norvegicus (Rat)
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 (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

GO - Biological processi

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 Componenti: Unplaced

Organism-specific databases

RGDi1309938. Pip5k1c.

Subcellular locationi

GO - Cellular componenti

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 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

        10         20         30         40         50
MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAIL 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
KALYSTARES 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 PQEELHAEDL QKITVQVEPV CGVGVVVPKE QGAGVEVPPS
610 620 630 640 650
GASAAATVEV DAASQASEPA SQASDEEDAP STDIYFFAHG RYWLFSPRRR
660 670 680
RLRAVTPSHT GAPTDGRSWV YSPLHYSARP ASDGESDT
Length:688
Mass (Da):75,594
Last modified:February 15, 2005 - v1
Checksum:iF34E175EFFF54D5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY850259 mRNA. Translation: AAW34235.1.
RefSeqiNP_001009967.2. NM_001009967.2.
NP_001029142.1. NM_001033970.1.
UniGeneiRn.2928.

3D structure databases

ProteinModelPortaliQ5I6B8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ5I6B8.
PRIDEiQ5I6B8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23396.
RGDi1309938. Pip5k1c.

Phylogenomic databases

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

Miscellaneous databases

NextBioi668018.
PROiQ5I6B8.

Gene expression databases

GenevestigatoriQ5I6B8.

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

  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 29, 2015
This is version 78 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

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.