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O70161

- PI51C_MOUSE

UniProt

O70161 - PI51C_MOUSE

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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

Pip5k1c

Organism
Mus musculus (Mouse)
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.10 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Enzyme regulationi

Activated by phosphatidic acid.1 Publication

Kineticsi

  1. KM=37 µM for PtdIns4P
  2. KM=39 µM for ATP

GO - Molecular functioni

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

GO - Biological processi

  1. axonogenesis Source: MGI
  2. chemotaxis Source: UniProtKB-KW
  3. cytoskeletal anchoring at plasma membrane Source: MGI
  4. exocytosis Source: UniProtKB-KW
  5. phagocytosis Source: UniProtKB-KW
  6. phosphatidylinositol metabolic process Source: MGI
  7. phosphatidylinositol phosphorylation Source: GOC
  8. platelet aggregation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cell adhesion, Chemotaxis, Endocytosis, Exocytosis, Phagocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

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
Synonyms:Kiaa0589
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1298224. 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
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.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531D → 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. 2 Publications
Mutagenesisi634 – 6341Y → 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. 1 Publication
Mutagenesisi635 – 6351F → A: Abolishes interaction with AP2B1. 1 Publication
Mutagenesisi642 – 6421W → A: Abolishes interaction with AP2B1. 1 Publication
Mutagenesisi644 – 6441Y → F: Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. 4 Publications
Mutagenesisi645 – 6451S → F: Can not rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions. 1 Publication
Mutagenesisi646 – 6461P → F: Abolishes interaction with AP-2 complex. 1 Publication
Mutagenesisi647 – 6471L → V: Abolishes interaction with AP-2 complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPRO_0000185463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei268 – 2681N6-acetyllysineBy similarity
Modified residuei634 – 6341Phosphotyrosine; by EGFR1 Publication
Modified residuei644 – 6441Phosphotyrosine; by CSK1 Publication
Modified residuei645 – 6451Phosphoserine; by CDK5, MAPK1 and CDK1By similarity

Post-translational modificationi

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-645.5 Publications
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

MaxQBiO70161.
PaxDbiO70161.
PRIDEiO70161.

PTM databases

PhosphoSiteiO70161.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

Expression increases during embryonic development and continued to steadily increase postnatally.1 Publication

Gene expression databases

BgeeiO70161.
ExpressionAtlasiO70161. baseline and differential.
GenevestigatoriO70161.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ap2b1Q9DBG3-13EBI-773657,EBI-775239
Ap2b1Q9DBG3-28EBI-773657,EBI-7257021

Protein-protein interaction databases

IntActiO70161. 8 interactions.
MINTiMINT-4105231.

Structurei

Secondary structure

1
661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi642 – 6443Combined sources
Helixi646 – 6483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y19X-ray2.60A/C/E/G/I/K638-651[»]
2H7DNMR-B643-652[»]
2H7ENMR-B643-652[»]
ProteinModelPortaliO70161.
SMRiO70161. Positions 76-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70161.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni636 – 66126Mediates interaction with TLN2Add
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiO70161.
KOiK00889.
OrthoDBiEOG70W3DM.
PhylomeDBiO70161.
TreeFamiTF319618.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O70161-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL 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
KALYSTAMES 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 PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG
610 620 630 640 650
ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFPTDER SWVYSPLHYS
660
ARPASDGESD T
Length:661
Mass (Da):72,408
Last modified:October 25, 2005 - v2
Checksum:i4A3B71E4465B83C3
GO
Isoform 2 (identifier: O70161-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:627
Mass (Da):69,199
Checksum:iC40D860D3F3419BD
GO
Isoform 3 (identifier: O70161-3) [UniParc]FASTAAdd to Basket

Also known as: PIPKIgamma635

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

Show »
Length:635
Mass (Da):69,502
Checksum:i781F012CC868250A
GO

Sequence cautioni

The sequence BAC65601.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101V → M in BAA25664. (PubMed:9535851)Curated
Sequence conflicti122 – 1221L → F in BAA25664. (PubMed:9535851)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei343 – 40260Missing in isoform 2. 1 PublicationVSP_016013Add
BLAST
Alternative sequencei635 – 6351F → FFAHGRYWLFSPRRRQLRAV TPNHTGT in isoform 2. 1 PublicationVSP_016014
Alternative sequencei636 – 66126Missing in isoform 3. 2 PublicationsVSP_016015Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35994.1. [O70161-1]
CCDS48643.1. [O70161-3]
RefSeqiNP_001140159.1. NM_001146687.2. [O70161-3]
NP_001280575.1. NM_001293646.1.
NP_001280576.1. NM_001293647.1.
NP_032870.2. NM_008844.3. [O70161-1]
UniGeneiMm.29836.
Mm.471109.

Genome annotation databases

EnsembliENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902. [O70161-1]
ENSMUST00000163075; ENSMUSP00000124155; ENSMUSG00000034902. [O70161-3]
GeneIDi18717.
KEGGimmu:18717.
UCSCiuc007ghc.2. mouse. [O70161-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS35994.1. [O70161-1 ]
CCDS48643.1. [O70161-3 ]
RefSeqi NP_001140159.1. NM_001146687.2. [O70161-3 ]
NP_001280575.1. NM_001293646.1.
NP_001280576.1. NM_001293647.1.
NP_032870.2. NM_008844.3. [O70161-1 ]
UniGenei Mm.29836.
Mm.471109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y19 X-ray 2.60 A/C/E/G/I/K 638-651 [» ]
2H7D NMR - B 643-652 [» ]
2H7E NMR - B 643-652 [» ]
ProteinModelPortali O70161.
SMRi O70161. Positions 76-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O70161. 8 interactions.
MINTi MINT-4105231.

PTM databases

PhosphoSitei O70161.

Proteomic databases

MaxQBi O70161.
PaxDbi O70161.
PRIDEi O70161.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000105327 ; ENSMUSP00000100964 ; ENSMUSG00000034902 . [O70161-1 ]
ENSMUST00000163075 ; ENSMUSP00000124155 ; ENSMUSG00000034902 . [O70161-3 ]
GeneIDi 18717.
KEGGi mmu:18717.
UCSCi uc007ghc.2. mouse. [O70161-1 ]

Organism-specific databases

CTDi 23396.
MGIi MGI:1298224. Pip5k1c.
Rougei Search...

Phylogenomic databases

eggNOGi COG5253.
GeneTreei ENSGT00760000119184.
HOGENOMi HOG000193876.
HOVERGENi HBG052818.
InParanoidi O70161.
KOi K00889.
OrthoDBi EOG70W3DM.
PhylomeDBi O70161.
TreeFami TF319618.

Enzyme and pathway databases

Reactomei REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Miscellaneous databases

ChiTaRSi Pip5k1c. mouse.
EvolutionaryTracei O70161.
NextBioi 294809.
PROi O70161.
SOURCEi Search...

Gene expression databases

Bgeei O70161.
ExpressionAtlasi O70161. baseline and differential.
Genevestigatori O70161.

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

« Hide 'large scale' publications
  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. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.

Entry informationi

Entry nameiPI51C_MOUSE
AccessioniPrimary (citable) accession number: O70161
Secondary accession number(s): Q505A1, Q80TW9, Q8VCU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3