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Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1-gamma) (PtdIns(4)P-5-kinase 1 gamma) (EC 2.7.1.68) (Phosphatidylinositol 4-phosphate 5-kinase type I gamma) (PIP5KIgamma)

 PI51C_MOUSE             Reviewed;         661 AA.
O70161; Q505A1; Q80TW9; Q8VCU5;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
22-NOV-2017, entry version 142.
RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma;
Short=PIP5K1-gamma;
Short=PtdIns(4)P-5-kinase 1 gamma;
EC=2.7.1.68;
AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I gamma;
Short=PIP5KIgamma;
Name=Pip5k1c; Synonyms=Kiaa0589;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=9535851; DOI=10.1074/jbc.273.15.8741;
Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T.,
Oka Y.;
"Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the
third isoform and deletion/substitution analysis of members of this
novel lipid kinase family.";
J. Biol. Chem. 273:8741-8748(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"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.";
DNA Res. 10:35-48(2003).
[3]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J, and NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Brain, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION IN FOCAL ADHESION DYNAMIC, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH TLN1, AND
MUTAGENESIS OF ASP-253.
PubMed=12422220; DOI=10.1038/nature01082;
Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.;
"Type I gamma phosphatidylinositol phosphate kinase targets and
regulates focal adhesions.";
Nature 420:89-93(2002).
[7]
INTERACTION WITH TLN1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
TYR-644, AND MUTAGENESIS OF TYR-644.
PubMed=14691141; DOI=10.1083/jcb.200310067;
Ling K., Doughman R.L., Iyer V.V., Firestone A.J., Bairstow S.F.,
Mosher D.F., Schaller M.D., Anderson R.A.;
"Tyrosine phosphorylation of type Igamma phosphatidylinositol
phosphate kinase by Src regulates an integrin-talin switch.";
J. Cell Biol. 163:1339-1349(2003).
[8]
TISSUE SPECIFICITY.
PubMed=14741049; DOI=10.1042/BJ20031394;
Giudici M.-L., Emson P.C., Irvine R.F.;
"A novel neuronal-specific splice variant of Type I
phosphatidylinositol 4-phosphate 5-kinase isoform gamma.";
Biochem. J. 379:489-496(2004).
[9]
FUNCTION IN SYNAPTIC VESICLE TRAFFICKING, AND DISRUPTION PHENOTYPE.
PubMed=15386003; DOI=10.1038/nature02896;
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.;
"Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects
in synaptic vesicle trafficking.";
Nature 431:415-422(2004).
[10]
FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH AP2M1 AND
TLN1, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-644; PRO-646 AND
LEU-647.
PubMed=16707488; DOI=10.1074/jbc.M601465200;
Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C.,
Anderson R.A.;
"Type Igamma661 phosphatidylinositol phosphate kinase directly
interacts with AP2 and regulates endocytosis.";
J. Biol. Chem. 281:20632-20642(2006).
[11]
FUNCTION IN CELL MIGRATION AND ADHESION, INTERACTION WITH PLCG1,
PHOSPHORYLATION AT TYR-634, AND MUTAGENESIS OF TYR-634; TYR-644 AND
SER-645.
PubMed=17635937; DOI=10.1083/jcb.200701078;
Sun Y., Ling K., Wagoner M.P., Anderson R.A.;
"Type I gamma phosphatidylinositol phosphate kinase is required for
EGF-stimulated directional cell migration.";
J. Cell Biol. 178:297-308(2007).
[12]
FUNCTION IN NEUTROPHIL CHEMOTAXIS, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ASP-253.
PubMed=17928408; DOI=10.1091/mbc.E07-05-0428;
Lokuta M.A., Senetar M.A., Bennin D.A., Nuzzi P.A., Chan K.T.,
Ott V.L., Huttenlocher A.;
"Type Igamma PIP kinase is a novel uropod component that regulates
rear retraction during neutrophil chemotaxis.";
Mol. Biol. Cell 18:5069-5080(2007).
[13]
FUNCTION IN EMBRYOGENESIS, AND DISRUPTION PHENOTYPE.
PubMed=17609388; DOI=10.1073/pnas.0700019104;
Wang Y., Lian L., Golden J.A., Morrisey E.E., Abrams C.S.;
"PIP5KI gamma is required for cardiovascular and neuronal
development.";
Proc. Natl. Acad. Sci. U.S.A. 104:11748-11753(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
INTERACTION WITH AP2B1, AND MUTAGENESIS OF PHE-635; TRP-642 AND
TYR-644.
PubMed=19287005; DOI=10.1074/jbc.M901017200;
Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A.,
Traub L.M.;
"Clathrin regulates the association of PIPKIgamma661 with the AP-2
adaptor beta2 appendage.";
J. Biol. Chem. 284:13924-13939(2009).
[16]
FUNCTION IN PHAGOCYTOSIS, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
DISRUPTION PHENOTYPE.
PubMed=19153220; DOI=10.1083/jcb.200806121;
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.;
"Essential and unique roles of PIP5K-gamma and -alpha in Fcgamma
receptor-mediated phagocytosis.";
J. Cell Biol. 184:281-296(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION IN EMBRYOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=20622009; DOI=10.1074/jbc.M110.132191;
Volpicelli-Daley L.A., Lucast L., Gong L.-W., Liu L., Sasaki J.,
Sasaki T., Abrams C.S., Kanaho Y., De Camilli P.;
"Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol
4,5-bisphosphate synthesis in the brain.";
J. Biol. Chem. 285:28708-28714(2010).
[19]
FUNCTION IN CELL ADHESION, AND DISRUPTION PHENOTYPE.
PubMed=20855869; DOI=10.4049/jimmunol.1001445;
Wernimont S.A., Legate K.R., Simonson W.T.N., Fassler R.,
Huttenlocher A.;
"PIPKI gamma 90 negatively regulates LFA-1-mediated adhesion and
activation in antigen-induced CD4+ T cells.";
J. Immunol. 185:4714-4723(2010).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-459, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 636-652 IN COMPLEX WITH TLN1.
PubMed=15623515; DOI=10.1074/jbc.M413180200;
de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H.,
Critchley D.R., Campbell I.D., Liddington R.C.;
"Structural basis for phosphatidylinositol phosphate kinase type
Igamma binding to talin at focal adhesions.";
J. Biol. Chem. 280:8381-8386(2005).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12422220,
ECO:0000269|PubMed:15386003, ECO:0000269|PubMed:16707488,
ECO:0000269|PubMed:17609388, ECO:0000269|PubMed:17635937,
ECO:0000269|PubMed:17928408, ECO:0000269|PubMed:19153220,
ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:20855869,
ECO:0000269|PubMed:9535851}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
-!- ENZYME REGULATION: Activated by phosphatidic acid.
{ECO:0000269|PubMed:9535851}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=37 uM for PtdIns(4)P;
KM=39 uM for ATP;
-!- SUBUNIT: 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. Interacts with
LAPTM4B; promotes SNX5 association with LAPTM4B; kinase activity
of PIP5K1C is required; interaction is regulated by
phosphatidylinositol 4,5-bisphosphate generated by PIP5K1C (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O60331,
ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141,
ECO:0000269|PubMed:15623515, ECO:0000269|PubMed:16707488,
ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19287005}.
-!- INTERACTION:
Q9DBG3-1:Ap2b1; NbExp=3; IntAct=EBI-773657, EBI-775239;
Q9DBG3-2:Ap2b1; NbExp=8; IntAct=EBI-773657, EBI-7257021;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction,
focal adhesion. Cell junction, adherens junction. Cell projection,
ruffle membrane. Cell projection, phagocytic cup. Cell projection,
uropodium. Note=During directional migration isoform 1 localized
at the uropodium, and isoform 3 localized all along cell membrane
including the uropodium and the leading edge.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=PIPKIgamma661;
IsoId=O70161-1; Sequence=Displayed;
Name=2; Synonyms=PIPKIgamma627;
IsoId=O70161-2; Sequence=VSP_016013, VSP_016014;
Note=No experimental confirmation available.;
Name=3; Synonyms=PIPKIgamma635;
IsoId=O70161-3; Sequence=VSP_016015;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:14741049,
ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:9535851}.
-!- DEVELOPMENTAL STAGE: Expression increases during embryonic
development and continued to steadily increase postnatally.
{ECO:0000269|PubMed:20622009}.
-!- PTM: 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. {ECO:0000269|PubMed:12422220,
ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:16707488,
ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19153220}.
-!- PTM: 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). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:15386003, ECO:0000269|PubMed:17609388,
ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009,
ECO:0000269|PubMed:20855869}.
-!- SEQUENCE CAUTION:
Sequence=BAC65601.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB006916; BAA25664.1; -; mRNA.
EMBL; AK122319; BAC65601.2; ALT_INIT; mRNA.
EMBL; AK154816; BAE32849.1; -; mRNA.
EMBL; AK171576; BAE42536.1; -; mRNA.
EMBL; BC019138; AAH19138.1; -; mRNA.
EMBL; BC094665; AAH94665.1; -; mRNA.
CCDS; CCDS35994.1; -. [O70161-1]
CCDS; CCDS48643.1; -. [O70161-3]
RefSeq; NP_001140159.1; NM_001146687.2. [O70161-3]
RefSeq; NP_001280575.1; NM_001293646.1.
RefSeq; NP_001280576.1; NM_001293647.1.
RefSeq; NP_032870.2; NM_008844.3. [O70161-1]
UniGene; Mm.24222; -.
UniGene; Mm.29836; -.
UniGene; Mm.471109; -.
PDB; 1Y19; X-ray; 2.60 A; A/C/E/G/I/K=638-651.
PDB; 2H7D; NMR; -; B=643-652.
PDB; 2H7E; NMR; -; B=643-652.
PDBsum; 1Y19; -.
PDBsum; 2H7D; -.
PDBsum; 2H7E; -.
ProteinModelPortal; O70161; -.
SMR; O70161; -.
BioGrid; 202169; 1.
IntAct; O70161; 8.
MINT; MINT-4105231; -.
STRING; 10090.ENSMUSP00000100964; -.
iPTMnet; O70161; -.
PhosphoSitePlus; O70161; -.
MaxQB; O70161; -.
PaxDb; O70161; -.
PeptideAtlas; O70161; -.
PRIDE; O70161; -.
Ensembl; ENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902. [O70161-1]
Ensembl; ENSMUST00000163075; ENSMUSP00000124155; ENSMUSG00000034902. [O70161-3]
GeneID; 18717; -.
KEGG; mmu:18717; -.
UCSC; uc007ghc.3; mouse. [O70161-1]
CTD; 23396; -.
MGI; MGI:1298224; Pip5k1c.
eggNOG; KOG0229; Eukaryota.
eggNOG; COG5253; LUCA.
GeneTree; ENSGT00760000119184; -.
HOGENOM; HOG000193876; -.
HOVERGEN; HBG052818; -.
InParanoid; O70161; -.
KO; K00889; -.
PhylomeDB; O70161; -.
TreeFam; TF319618; -.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
ChiTaRS; Pip5k1c; mouse.
EvolutionaryTrace; O70161; -.
PRO; PR:O70161; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000034902; -.
ExpressionAtlas; O70161; baseline and differential.
Genevisible; O70161; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001931; C:uropod; IEA:UniProtKB-SubCell.
GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1990147; F:talin binding; IDA:MGI.
GO; GO:0007409; P:axonogenesis; IDA:MGI.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IMP:MGI.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:MGI.
GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
GO; GO:0070527; P:platelet aggregation; IMP:MGI.
Gene3D; 3.30.800.10; -; 1.
Gene3D; 3.30.810.10; -; 1.
InterPro; IPR023610; PInositol-4-P-5-kinase.
InterPro; IPR027483; PInositol-4-P-5-kinase_C.
InterPro; IPR002498; PInositol-4-P-5-kinase_core.
InterPro; IPR027484; PInositol-4-P-5-kinase_N.
PANTHER; PTHR23086; PTHR23086; 1.
Pfam; PF01504; PIP5K; 1.
SMART; SM00330; PIPKc; 1.
PROSITE; PS51455; PIPK; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Chemotaxis; Complete proteome; Cytoplasm; Endocytosis; Exocytosis;
Kinase; Membrane; Methylation; Nucleotide-binding; Phagocytosis;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 661 Phosphatidylinositol 4-phosphate 5-kinase
type-1 gamma.
/FTId=PRO_0000185463.
DOMAIN 75 443 PIPK. {ECO:0000255|PROSITE-
ProRule:PRU00781}.
REGION 636 661 Mediates interaction with TLN2.
MOD_RES 265 265 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60331}.
MOD_RES 268 268 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60331}.
MOD_RES 459 459 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 459 459 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q5I6B8}.
MOD_RES 634 634 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:17635937}.
MOD_RES 644 644 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:14691141}.
MOD_RES 645 645 Phosphoserine; by CDK5, MAPK1 and CDK1.
{ECO:0000250|UniProtKB:O60331}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:Q5I6B8}.
MOD_RES 661 661 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5I6B8}.
VAR_SEQ 343 402 Missing (in isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_016013.
VAR_SEQ 635 635 F -> FFAHGRYWLFSPRRRQLRAVTPNHTGT (in
isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_016014.
VAR_SEQ 636 661 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_016015.
MUTAGEN 253 253 D->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. {ECO:0000269|PubMed:12422220,
ECO:0000269|PubMed:17928408}.
MUTAGEN 634 634 Y->F: Cannot 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.
{ECO:0000269|PubMed:17635937}.
MUTAGEN 635 635 F->A: Abolishes interaction with AP2B1.
{ECO:0000269|PubMed:19287005}.
MUTAGEN 642 642 W->A: Abolishes interaction with AP2B1.
{ECO:0000269|PubMed:19287005}.
MUTAGEN 644 644 Y->F: Loss of phosphorylation by CSK.
Abolishes interaction with AP-2 complex.
Cannot rescue the effect PIP5K1C
knockdown on EGF-stimulated cell
migration. {ECO:0000269|PubMed:14691141,
ECO:0000269|PubMed:16707488,
ECO:0000269|PubMed:17635937,
ECO:0000269|PubMed:19287005}.
MUTAGEN 645 645 S->F: Cannot rescue the effect PIP5K1C
knockdown on EGF-stimulated cell
migration. Decreased tailin assembly into
focal adhesions.
{ECO:0000269|PubMed:17635937}.
MUTAGEN 646 646 P->F: Abolishes interaction with AP-2
complex. {ECO:0000269|PubMed:16707488}.
MUTAGEN 647 647 L->V: Abolishes interaction with AP-2
complex. {ECO:0000269|PubMed:16707488}.
CONFLICT 110 110 V -> M (in Ref. 1; BAA25664).
{ECO:0000305}.
CONFLICT 122 122 L -> F (in Ref. 1; BAA25664).
{ECO:0000305}.
STRAND 642 644 {ECO:0000244|PDB:1Y19}.
HELIX 646 648 {ECO:0000244|PDB:1Y19}.
SEQUENCE 661 AA; 72408 MW; 4A3B71E4465B83C3 CRC64;
MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP GPGHGKKLGH
RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS
NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT
SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN
VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK
TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTAMES
IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG
DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP
SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS
DTSEQPRYRR RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG
ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFPTDER SWVYSPLHYS ARPASDGESD
T


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