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 27-MAR-2024, entry version 168. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QIE; X-ray; 2.39 A; A/B/C/D=32-421. DR PDB; 7QPN; X-ray; 1.95 A; A/B=32-421. DR PDB; 8BQ4; X-ray; 2.42 A; A/B=32-421. DR PDBsum; 2GK9; -. DR PDBsum; 7QIE; -. DR PDBsum; 7QPN; -. DR PDBsum; 8BQ4; -. DR AlphaFoldDB; Q8TBX8; -. DR SMR; Q8TBX8; -. DR BioGRID; 122928; 154. DR IntAct; Q8TBX8; 29. 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 CPTAC; non-CPTAC-3021; -. DR EPD; Q8TBX8; -. DR jPOST; Q8TBX8; -. DR MassIVE; Q8TBX8; -. DR MaxQB; Q8TBX8; -. DR PaxDb; 9606-ENSP00000347032; -. DR PeptideAtlas; Q8TBX8; -. DR ProteomicsDB; 74044; -. [Q8TBX8-1] DR ProteomicsDB; 74045; -. [Q8TBX8-2] DR ProteomicsDB; 74046; -. [Q8TBX8-3] DR Pumba; Q8TBX8; -. DR Antibodypedia; 28802; 125 antibodies from 26 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 AGR; HGNC:23786; -. 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; REDESEW; -. DR OrthoDB; 5481504at2759; -. 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 SIGNOR; Q8TBX8; -. DR BioGRID-ORCS; 79837; 30 hits in 1161 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 204 other cell types or tissues. DR ExpressionAtlas; Q8TBX8; baseline and differential. 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; IBA:GO_Central. 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: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 CDD; cd17311; PIPKc_PIP5K2C; 1. DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 2. DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1. DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf. DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core. DR InterPro; IPR027484; PInositol-4-P-5-kinase_N. DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase. DR PANTHER; PTHR23086:SF35; PHOSPHATIDYLINOSITOL 5-PHOSPHATE 4-KINASE TYPE-2 GAMMA; 1. DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1. DR Pfam; PF01504; PIP5K; 1. DR SMART; SM00330; PIPKc; 1. DR SUPFAM; SSF56104; SAICAR synthase-like; 1. DR PROSITE; PS51455; PIPK; 1. DR Genevisible; Q8TBX8; HS. 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:7QPN" FT HELIX 73..77 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 79..88 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 105..114 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 119..127 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 156..176 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:2GK9" FT STRAND 185..193 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 196..204 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 214..219 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 230..233 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:8BQ4" FT HELIX 242..247 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 256..275 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 282..289 FT /evidence="ECO:0007829|PDB:7QPN" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:7QPN" FT STRAND 366..373 FT /evidence="ECO:0007829|PDB:7QPN" FT TURN 375..377 FT /evidence="ECO:0007829|PDB:7QPN" FT HELIX 405..417 FT /evidence="ECO:0007829|PDB:7QPN" 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 //