PI42C_HUMAN
ID PI42C_HUMAN Reviewed; 421 AA.
AC Q8TBX8; B2RDL3; B4DM11; B4DY44; Q9H6N2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma {ECO:0000305};
DE EC=2.7.1.149 {ECO:0000305|PubMed:26774281};
DE AltName: Full=Phosphatidylinositol 5-phosphate 4-kinase type II gamma;
DE Short=PI(5)P 4-kinase type II gamma;
DE Short=PIP4KII-gamma;
GN Name=PIP4K2C {ECO:0000312|HGNC:HGNC:23786}; Synonyms=PIP5K2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-241.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-349, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26774281; DOI=10.1016/j.molcel.2015.12.011;
RA Sumita K., Lo Y.H., Takeuchi K., Senda M., Kofuji S., Ikeda Y.,
RA Terakawa J., Sasaki M., Yoshino H., Majd N., Zheng Y., Kahoud E.R.,
RA Yokota T., Emerling B.M., Asara J.M., Ishida T., Locasale J.W., Daikoku T.,
RA Anastasiou D., Senda T., Sasaki A.T.;
RT "The Lipid Kinase PI5P4Kbeta Is an Intracellular GTP Sensor for Metabolism
RT and Tumorigenesis.";
RL Mol. Cell 61:187-198(2016).
RN [9]
RP FUNCTION, INTERACTION WITH PIP5K1A, AND MUTAGENESIS OF 69-VAL--ASP-75.
RX PubMed=31091439; DOI=10.1016/j.celrep.2019.04.070;
RA Wang D.G., Paddock M.N., Lundquist M.R., Sun J.Y., Mashadova O.,
RA Amadiume S., Bumpus T.W., Hodakoski C., Hopkins B.D., Fine M., Hill A.,
RA Yang T.J., Baskin J.M., Dow L.E., Cantley L.C.;
RT "PIP4Ks Suppress Insulin Signaling through a Catalytic-Independent
RT Mechanism.";
RL Cell Rep. 27:1991.e5-2001.e5(2019).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-421.
RG Structural genomics consortium (SGC);
RT "Structure of human phosphatidylinositol-4-phosphate 5-kinase, type II,
RT gamma.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic
CC activity. May be a GTP sensor, has higher GTP-dependent kinase activity
CC than ATP-dependent kinase activity. PIP4Ks negatively regulate insulin
CC signaling through a catalytic-independent mechanism. They interact with
CC PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-
CC dependent conversion to PtdIns(3,4,5)P3 (PubMed:31091439).
CC {ECO:0000269|PubMed:26774281, ECO:0000269|PubMed:31091439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149;
CC Evidence={ECO:0000305|PubMed:26774281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281;
CC Evidence={ECO:0000305|PubMed:26774281};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423,
CC ChEBI:CHEBI:84968, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:26774281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993;
CC Evidence={ECO:0000305|PubMed:26774281};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:83423, ChEBI:CHEBI:84968;
CC Evidence={ECO:0000269|PubMed:26774281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965;
CC Evidence={ECO:0000305|PubMed:26774281};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for ATP {ECO:0000269|PubMed:26774281};
CC KM=389 uM for GTP {ECO:0000269|PubMed:26774281};
CC -!- SUBUNIT: Interacts with PIP5K1A; the interaction inhibits PIP5K1A
CC kinase activity. {ECO:0000269|PubMed:31091439}.
CC -!- INTERACTION:
CC Q8TBX8; Q8TBX8: PIP4K2C; NbExp=2; IntAct=EBI-1383637, EBI-1383637;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O88370}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88370}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TBX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBX8-2; Sequence=VSP_042929;
CC Name=3;
CC IsoId=Q8TBX8-3; Sequence=VSP_043369;
CC -!- PTM: Phosphorylated, phosphorylation is induced by EGF.
CC {ECO:0000250|UniProtKB:O88370}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15223.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK025708; BAB15223.1; ALT_INIT; mRNA.
DR EMBL; AK297243; BAG59723.1; -; mRNA.
DR EMBL; AK302254; BAG63606.1; -; mRNA.
DR EMBL; AK315588; BAG37960.1; -; mRNA.
DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97031.1; -; Genomic_DNA.
DR EMBL; BC028596; AAH28596.1; -; mRNA.
DR CCDS; CCDS53808.1; -. [Q8TBX8-2]
DR CCDS; CCDS55839.1; -. [Q8TBX8-3]
DR CCDS; CCDS8946.1; -. [Q8TBX8-1]
DR RefSeq; NP_001139730.1; NM_001146258.1. [Q8TBX8-1]
DR RefSeq; NP_001139731.1; NM_001146259.1. [Q8TBX8-3]
DR RefSeq; NP_001139732.1; NM_001146260.1. [Q8TBX8-2]
DR RefSeq; NP_079055.3; NM_024779.4. [Q8TBX8-1]
DR PDB; 2GK9; X-ray; 2.80 A; A/B/C/D=32-421.
DR PDBsum; 2GK9; -.
DR AlphaFoldDB; Q8TBX8; -.
DR SMR; Q8TBX8; -.
DR BioGRID; 122928; 114.
DR IntAct; Q8TBX8; 27.
DR MINT; Q8TBX8; -.
DR STRING; 9606.ENSP00000347032; -.
DR BindingDB; Q8TBX8; -.
DR ChEMBL; CHEMBL1770034; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8TBX8; -.
DR GlyGen; Q8TBX8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TBX8; -.
DR PhosphoSitePlus; Q8TBX8; -.
DR BioMuta; PIP4K2C; -.
DR DMDM; 317373532; -.
DR EPD; Q8TBX8; -.
DR jPOST; Q8TBX8; -.
DR MassIVE; Q8TBX8; -.
DR MaxQB; Q8TBX8; -.
DR PaxDb; Q8TBX8; -.
DR PeptideAtlas; Q8TBX8; -.
DR PRIDE; Q8TBX8; -.
DR ProteomicsDB; 74044; -. [Q8TBX8-1]
DR ProteomicsDB; 74045; -. [Q8TBX8-2]
DR ProteomicsDB; 74046; -. [Q8TBX8-3]
DR Antibodypedia; 28802; 114 antibodies from 25 providers.
DR DNASU; 79837; -.
DR Ensembl; ENST00000354947.10; ENSP00000347032.5; ENSG00000166908.18. [Q8TBX8-1]
DR Ensembl; ENST00000422156.7; ENSP00000412035.3; ENSG00000166908.18. [Q8TBX8-2]
DR Ensembl; ENST00000540759.6; ENSP00000439878.2; ENSG00000166908.18. [Q8TBX8-1]
DR Ensembl; ENST00000550465.5; ENSP00000447390.1; ENSG00000166908.18. [Q8TBX8-3]
DR GeneID; 79837; -.
DR KEGG; hsa:79837; -.
DR MANE-Select; ENST00000354947.10; ENSP00000347032.5; NM_024779.5; NP_079055.3.
DR UCSC; uc001sot.4; human. [Q8TBX8-1]
DR CTD; 79837; -.
DR DisGeNET; 79837; -.
DR GeneCards; PIP4K2C; -.
DR HGNC; HGNC:23786; PIP4K2C.
DR HPA; ENSG00000166908; Low tissue specificity.
DR neXtProt; NX_Q8TBX8; -.
DR OpenTargets; ENSG00000166908; -.
DR PharmGKB; PA162399665; -.
DR VEuPathDB; HostDB:ENSG00000166908; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000156890; -.
DR HOGENOM; CLU_004312_7_0_1; -.
DR InParanoid; Q8TBX8; -.
DR OMA; SEWDGDC; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q8TBX8; -.
DR TreeFam; TF354315; -.
DR BRENDA; 2.7.1.149; 2681.
DR PathwayCommons; Q8TBX8; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8847453; Synthesis of PIPs in the nucleus.
DR SignaLink; Q8TBX8; -.
DR BioGRID-ORCS; 79837; 19 hits in 1083 CRISPR screens.
DR ChiTaRS; PIP4K2C; human.
DR EvolutionaryTrace; Q8TBX8; -.
DR GenomeRNAi; 79837; -.
DR Pharos; Q8TBX8; Tchem.
DR PRO; PR:Q8TBX8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TBX8; protein.
DR Bgee; ENSG00000166908; Expressed in corpus epididymis and 202 other tissues.
DR ExpressionAtlas; Q8TBX8; baseline and differential.
DR Genevisible; Q8TBX8; HS.
DR GO; GO:0005776; C:autophagosome; IMP:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043229; C:intracellular organelle; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:UniProtKB.
DR GO; GO:0016309; F:1-phosphatidylinositol-5-phosphate 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1902635; P:1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0090217; P:negative regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Endoplasmic reticulum; Kinase; Lipid metabolism; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..421
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT gamma"
FT /id="PRO_0000285750"
FT DOMAIN 43..420
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 69..75
FT /note="Required for interaction with PIP5K1A"
FT /evidence="ECO:0000269|PubMed:31091439"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 83..100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043369"
FT VAR_SEQ 124..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042929"
FT VARIANT 84
FT /note="V -> A (in dbSNP:rs17550713)"
FT /id="VAR_032049"
FT VARIANT 241
FT /note="K -> R (in dbSNP:rs17852569)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032050"
FT VARIANT 300
FT /note="A -> G (in dbSNP:rs2277319)"
FT /id="VAR_032051"
FT MUTAGEN 69..75
FT /note="VMLLPDD->EIFLPNN: Loss of interaction with PIP5K1A.
FT Loss of inhibition of PIP5K1A activity."
FT /evidence="ECO:0000269|PubMed:31091439"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:2GK9"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2GK9"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 260..275
FT /evidence="ECO:0007829|PDB:2GK9"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:2GK9"
SQ SEQUENCE 421 AA; 47300 MW; 65D1CBCF0826D476 CRC64;
MASSSVPPAT VSAATAGPGP GFGFASKTKK KHFVQQKVKV FRAADPLVGV FLWGVAHSIN
ELSQVPPPVM LLPDDFKASS KIKVNNHLFH RENLPSHFKF KEYCPQVFRN LRDRFGIDDQ
DYLVSLTRNP PSESEGSDGR FLISYDRTLV IKEVSSEDIA DMHSNLSNYH QYIVKCHGNT
LLPQFLGMYR VSVDNEDSYM LVMRNMFSHR LPVHRKYDLK GSLVSREASD KEKVKELPTL
KDMDFLNKNQ KVYIGEEEKK IFLEKLKRDV EFLVQLKIMD YSLLLGIHDI IRGSEPEEEA
PVREDESEVD GDCSLTGPPA LVGSYGTSPE GIGGYIHSHR PLGPGEFESF IDVYAIRSAE
GAPQKEVYFM GLIDILTQYD AKKKAAHAAK TVKHGAGAEI STVHPEQYAK RFLDFITNIF
A
