O70161 (PI51C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
Short name=PIP5K1-gamma
Short name=PtdIns(4)P-5-kinase 1 gamma
EC=2.7.1.68

Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I gamma
Short name=PIP5KIgamma

Gene names

Name:	Pip5k1c
Synonyms:	Kiaa0589

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	661 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17
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. Ref.1
Subunit structure	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. Ref.6 Ref.7 Ref.10 Ref.11 Ref.14
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. Ref.6 Ref.7 Ref.12 Ref.15 Ref.16
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. Ref.1 Ref.8 Ref.16
Developmental stage	Expression increases during embryonic development and continued to steadily increase postnatally. Ref.16
Post-translational modification	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. Ref.6 Ref.7 Ref.10 Ref.11 Ref.15 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.
Disruption phenotype	According to some authors, mutants die within hours after birth and are unable to feed after birth (Ref.9). According to another report, mutants are embryonically lethal at organogenesis stage, and display cardiovascular and neuronal defects (Ref.9). Double mutant mice carrying both PIP5K1B and PIP5K1C mutations die within minutes after birth. Double mutant mice carrying both PIP5K1A and PIP5K1C mutations are embryonic lethal. Bone marrow-derived macrophages (BMM) 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. Ref.9 Ref.13 Ref.15 Ref.16 Ref.17
Sequence similarities	Contains 1 PIPK domain.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for PtdIns4P KM=39 µM for ATP
Sequence caution	The sequence BAC65601.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion Chemotaxis Endocytosis Exocytosis Phagocytosis
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from direct assay Ref.8. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW exocytosis Inferred from electronic annotation. Source: UniProtKB-KW phagocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic cup Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell uropod Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from direct assay Ref.8Ref.1. Source: MGI ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O70161-1)

Also known as: PIPKIgamma661;

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.

Isoform 2 (identifier: O70161-2)

Also known as: PIPKIgamma627;

The sequence of this isoform differs from the canonical sequence as follows:
     343-402: Missing.
     635-635: F → FFAHGRYWLFSPRRRQLRAVTPNHTGT

Note: No experimental confirmation available.

Isoform 3 (identifier: O70161-3)

Also known as: PIPKIgamma635;

The sequence of this isoform differs from the canonical sequence as follows:
     636-661: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 661

661

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

PRO_0000185463

Regions

Domain

75 – 443

369

PIPK

Region

636 – 661

26

Mediates interaction with TLN2

Amino acid modifications

Modified residue

265

1

N6-acetyllysine By similarity

Modified residue

268

1

N6-acetyllysine By similarity

Modified residue

634

1

Phosphotyrosine; by EGFR Ref.6 Ref.11

Modified residue

644

1

Phosphotyrosine; by CSK Ref.6 Ref.7

Modified residue

645

1

Phosphoserine; by CDK5, MAPK1 and CDK1 By similarity

Natural variations

Alternative sequence

343 – 402

60

Missing in isoform 2.

VSP_016013

Alternative sequence

635

1

F → FFAHGRYWLFSPRRRQLRAV TPNHTGT in isoform 2.

VSP_016014

Alternative sequence

636 – 661

26

Missing in isoform 3.

VSP_016015

Experimental info

Mutagenesis

253

1

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. Ref.6 Ref.12

Mutagenesis

634

1

Y → F: Can not 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. Ref.11

Mutagenesis

635

1

F → A: Abolishes interaction with AP2B1. Ref.14

Mutagenesis

642

1

W → A: Abolishes interaction with AP2B1. Ref.14

Mutagenesis

644

1

Y → F: Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Ref.7 Ref.10 Ref.11 Ref.14

Mutagenesis

645

1

S → F: Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions. Ref.11

Mutagenesis

646

1

P → F: Abolishes interaction with AP-2 complex. Ref.10

Mutagenesis

647

1

L → V: Abolishes interaction with AP-2 complex. Ref.10

Sequence conflict

110

1

V → M in BAA25664. Ref.1

Sequence conflict

122

1

L → F in BAA25664. Ref.1

Secondary structure

1

.

.

.

.

.

661

Helix Strand Turn

Details...

Beta strand

642 – 644

3

Helix

646 – 648

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PIPKIgamma661) [UniParc]. Last modified October 25, 2005. Version 2. Checksum: 4A3B71E4465B83C3	FASTA	661	72,408
	10 20 30 40 50 60 MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP GPGHGKKLGH 70 80 90 100 110 120 RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS 130 140 150 160 170 180 NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT 190 200 210 220 230 240 SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN 250 260 270 280 290 300 VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK 310 320 330 340 350 360 TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTAMES 370 380 390 400 410 420 IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG 430 440 450 460 470 480 DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP 490 500 510 520 530 540 SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS 550 560 570 580 590 600 DTSEQPRYRR RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG 610 620 630 640 650 660 ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFPTDER SWVYSPLHYS ARPASDGESD T
	Isoform 2 (PIPKIgamma627) [UniParc]. Checksum: C40D860D3F3419BD	FASTA	627	69,199
	10 20 30 40 50 60 MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP GPGHGKKLGH 70 80 90 100 110 120 RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS 130 140 150 160 170 180 NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT 190 200 210 220 230 240 SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN 250 260 270 280 290 300 VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK 310 320 330 340 350 360 TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KAYRFIKKLE HTWKALVHDG 370 380 390 400 410 420 DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP 430 440 450 460 470 480 SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS 490 500 510 520 530 540 DTSEQPRYRR RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG 550 560 570 580 590 600 ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFFAHGR YWLFSPRRRQ LRAVTPNHTG 610 620 TPTDERSWVY SPLHYSARPA SDGESDT
	Isoform 3 (PIPKIgamma635) [UniParc]. Checksum: 781F012CC868250A	FASTA	635	69,502
	10 20 30 40 50 60 MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP GPGHGKKLGH 70 80 90 100 110 120 RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS 130 140 150 160 170 180 NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT 190 200 210 220 230 240 SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN 250 260 270 280 290 300 VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK 310 320 330 340 350 360 TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTAMES 370 380 390 400 410 420 IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG 430 440 450 460 470 480 DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP 490 500 510 520 530 540 SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS 550 560 570 580 590 600 DTSEQPRYRR RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG 610 620 630 ASAAASVEID AASQASEPAS QASDEEDAPS TDIYF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family." Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y. J. Biol. Chem. 273:8741-8748(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[2]	"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." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal brain.
[3]	Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Strain: C57BL/6J and NOD.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Strain: FVB/N. Tissue: Brain and Kidney.
[6]	"Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions." Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A. Nature 420:89-93(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN FOCAL ADHESION DYNAMIC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH TLN1, MUTAGENESIS OF ASP-253.
[7]	"Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch." Ling K., Doughman R.L., Iyer V.V., Firestone A.J., Bairstow S.F., Mosher D.F., Schaller M.D., Anderson R.A. J. Cell Biol. 163:1339-1349(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TLN1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-644, MUTAGENESIS OF TYR-644.
[8]	"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: TISSUE SPECIFICITY.
[9]	"Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking." 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. Nature 431:415-422(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SYNAPTIC VESICLE TRAFFICKING, DISRUPTION PHENOTYPE.
[10]	"Type Igamma661 phosphatidylinositol phosphate kinase directly interacts with AP2 and regulates endocytosis." Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C., Anderson R.A. J. Biol. Chem. 281:20632-20642(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH AP2M1 AND TLN1, PHOSPHORYLATION, MUTAGENESIS OF TYR-644; PRO-646 AND LEU-647.
[11]	"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, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-634, MUTAGENESIS OF TYR-634; TYR-644 AND SER-645.
[12]	"Type Igamma PIP kinase is a novel uropod component that regulates rear retraction during neutrophil chemotaxis." Lokuta M.A., Senetar M.A., Bennin D.A., Nuzzi P.A., Chan K.T., Ott V.L., Huttenlocher A. Mol. Biol. Cell 18:5069-5080(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEUTROPHIL CHEMOTAXIS, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-253.
[13]	"PIP5KI gamma is required for cardiovascular and neuronal development." Wang Y., Lian L., Golden J.A., Morrisey E.E., Abrams C.S. Proc. Natl. Acad. Sci. U.S.A. 104:11748-11753(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EMBRYOGENESIS, DISRUPTION PHENOTYPE.
[14]	"Clathrin regulates the association of PIPKIgamma661 with the AP-2 adaptor beta2 appendage." Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A., Traub L.M. J. Biol. Chem. 284:13924-13939(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AP2B1, MUTAGENESIS OF PHE-635; TRP-642 AND TYR-644.
[15]	"Essential and unique roles of PIP5K-gamma and -alpha in Fcgamma receptor-mediated phagocytosis." 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. J. Cell Biol. 184:281-296(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHAGOCYTOSIS, SUBCELLULAR LOCATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE.
[16]	"Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5-bisphosphate synthesis in the brain." Volpicelli-Daley L.A., Lucast L., Gong L.-W., Liu L., Sasaki J., Sasaki T., Abrams C.S., Kanaho Y., De Camilli P. J. Biol. Chem. 285:28708-28714(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EMBRYOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[17]	"PIPKI gamma 90 negatively regulates LFA-1-mediated adhesion and activation in antigen-induced CD4+ T cells." Wernimont S.A., Legate K.R., Simonson W.T.N., Fassler R., Huttenlocher A. J. Immunol. 185:4714-4723(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL ADHESION, DISRUPTION PHENOTYPE.
[18]	"Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions." de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H., Critchley D.R., Campbell I.D., Liddington R.C. J. Biol. Chem. 280:8381-8386(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 636-652 IN COMPLEX WITH TLN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB006916 mRNA. Translation: BAA25664.1.
AK122319 mRNA. Translation: BAC65601.2. Different initiation.
AK154816 mRNA. Translation: BAE32849.1.
AK171576 mRNA. Translation: BAE42536.1.
BC019138 mRNA. Translation: AAH19138.1.
BC094665 mRNA. Translation: AAH94665.1.

IPI

IPI00403328.
IPI00655177.
IPI00655218.

RefSeq

NP_001140159.1. NM_001146687.1.
NP_032870.2. NM_008844.2.

UniGene

Mm.29836.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y19	X-ray	2.60	A/C/E/G/I/K	638-651	[»]
2H7D	NMR	-	B	642-652	[»]
2H7E	NMR	-	B	642-652	[»]

ProteinModelPortal

O70161.

SMR

O70161. Positions 76-328.

ModBase

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Protein-protein interaction databases

IntAct

O70161. 2 interactions.

MINT

MINT-4105231.

PTM databases

PhosphoSite

O70161.

Proteomic databases

PaxDb

O70161.

PRIDE

O70161.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902.
ENSMUST00000163075; ENSMUSP00000124155; ENSMUSG00000034902.

GeneID

18717.

KEGG

mmu:18717.

UCSC

uc007ghc.2. mouse.

Organism-specific databases

CTD

23396.

MGI

MGI:1298224. Pip5k1c.

Rouge

Search...

Phylogenomic databases

eggNOG

COG5253.

GeneTree

ENSGT00690000101870.

HOGENOM

HOG000193876.

HOVERGEN

HBG052818.

InParanoid

O70161.

KO

K00889.

OrthoDB

EOG4JQ3Z0.

Gene expression databases

ArrayExpress

O70161.

Bgee

O70161.

Genevestigator

O70161.

GermOnline

ENSMUSG00000034902. Mus musculus.

Family and domain databases

Gene3D

3.30.800.10. 1 hit.
3.30.810.10. 1 hit.

InterPro

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]

PANTHER

PTHR23086. PTHR23086. 1 hit.

Pfam

PF01504. PIP5K. 1 hit.
[Graphical view]

SMART

SM00330. PIPKc. 1 hit.
[Graphical view]

PROSITE

PS51455. PIPK. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

PIP5K1C. mouse.

EvolutionaryTrace

O70161.

NextBio

294809.

SOURCE

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Entry information

Entry name

PI51C_MOUSE

Accession

Primary (citable) accession number: O70161
Secondary accession number(s): Q505A1, Q80TW9, Q8VCU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 29, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program