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Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-alpha)

 P4K2A_HUMAN             Reviewed;         479 AA.
Q9BTU6; D3DR59; Q9NSG8;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=Phosphatidylinositol 4-kinase type 2-alpha;
EC=2.7.1.67 {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678};
AltName: Full=Phosphatidylinositol 4-kinase type II-alpha;
Name=PI4K2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=11279162; DOI=10.1074/jbc.M100982200;
Minogue S., Anderson J.S., Waugh M.G., dos Santos M., Corless S.,
Cramer R., Hsuan J.J.;
"Cloning of a human type II phosphatidylinositol 4-kinase reveals a
novel lipid kinase family.";
J. Biol. Chem. 276:16635-16640(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-479.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16443754; DOI=10.1242/jcs.02752;
Minogue S., Waugh M.G., De Matteis M.A., Stephens D.J.,
Berditchevski F., Hsuan J.J.;
"Phosphatidylinositol 4-kinase is required for endosomal trafficking
and degradation of the EGF receptor.";
J. Cell Sci. 119:571-581(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=20388919; DOI=10.1194/jlr.M005751;
Minogue S., Chu K.M., Westover E.J., Covey D.F., Hsuan J.J.,
Waugh M.G.;
"Relationship between phosphatidylinositol 4-phosphate synthesis,
membrane organization, and lateral diffusion of PI4KIIalpha at the
trans-Golgi network.";
J. Lipid Res. 51:2314-2324(2010).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
INTERACTION WITH BLOC1S5 AND DTNBP1.
PubMed=21998198; DOI=10.1091/mbc.E11-07-0592;
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A.,
Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
"The schizophrenia susceptibility factor dysbindin and its associated
complex sort cargoes from cell bodies to the synapse.";
Mol. Biol. Cell 22:4854-4867(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, AND
FUNCTION.
PubMed=23146885; DOI=10.1038/embor.2012.164;
Mossinger J., Wieffer M., Krause E., Freund C., Gerth F., Krauss M.,
Haucke V.;
"Phosphatidylinositol 4-kinase IIalpha function at endosomes is
regulated by the ubiquitin ligase Itch.";
EMBO Rep. 13:1087-1094(2012).
[17]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND
CYS-178, AND MUTAGENESIS OF 174-CYS--CYS-178.
PubMed=22535966; DOI=10.1074/jbc.M112.348094;
Lu D., Sun H.Q., Wang H., Barylko B., Fukata Y., Fukata M.,
Albanesi J.P., Yin H.L.;
"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-
localized palmitoyltransferases in cholesterol-dependent manner.";
J. Biol. Chem. 287:21856-21865(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND
SER-51, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47 AND SER-51,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 76-172 AND 180-468 IN
COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445.
PubMed=25168678; DOI=10.15252/embr.201438841;
Baumlova A., Chalupska D., Rozycki B., Jovic M., Wisniewski E.,
Klima M., Dubankova A., Kloer D.P., Nencka R., Balla T., Boura E.;
"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.";
EMBO Rep. 15:1085-1092(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 78-453 IN COMPLEX WITH ADP,
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168;
LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275;
ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.
PubMed=24675427; DOI=10.1038/ncomms4552;
Zhou Q., Li J., Yu H., Zhai Y., Gao Z., Liu Y., Pang X., Zhang L.,
Schulten K., Sun F., Chen C.;
"Molecular insights into the membrane-associated phosphatidylinositol
4-kinase IIalpha.";
Nat. Commun. 5:3552-3552(2014).
-!- FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4-
kinase) that catalyzes the phosphorylation of phosphatidylinositol
(PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that
plays important roles in endocytosis, Golgi function, protein
sorting and membrane trafficking and is required for prolonged
survival of neurons. Besides, phosphorylation of
phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate
(PI4P) is the first committed step in the generation of
phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the
second messenger inositol 1,4,5-trisphosphate (InsP3).
{ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754,
ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:23146885,
ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
1-phosphatidyl-1D-myo-inositol 4-phosphate.
{ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:20388919,
ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678}.
-!- SUBUNIT: Associates with the BLOC-1 and the AP-3 complexes; the
BLOC-1 complex is required for optimal binding of PI4K2A to the
AP-3 complex. Interacts with BLOC1S5 and DTNBP1 (PubMed:21998198).
Interacts with FOS; this interaction may enhance
phosphatidylinositol phosphorylation activity (By similarity).
Interacts with ITCH (PubMed:23146885).
{ECO:0000250|UniProtKB:Q2TBE6, ECO:0000269|PubMed:21998198,
ECO:0000269|PubMed:23146885}.
-!- INTERACTION:
Q96J02:ITCH; NbExp=5; IntAct=EBI-3239392, EBI-1564678;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:16443754,
ECO:0000269|PubMed:22535966}; Lipid-anchor
{ECO:0000269|PubMed:22535966}. Membrane raft
{ECO:0000269|PubMed:11279162}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q2TBE6}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250|UniProtKB:Q2TBE6}. Cell
junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q2TBE6}.
Mitochondrion {ECO:0000250|UniProtKB:Q2TBE6}. Endosome
{ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:23146885}.
Cytoplasmic vesicle {ECO:0000269|PubMed:16443754}. Membrane
{ECO:0000269|PubMed:24675427}; Lipid-anchor
{ECO:0000269|PubMed:24675427}. Cell membrane
{ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754}.
Note=Localized in neuronal cell body. Transported from neuronal
cell body to neuron projections in a BLOC-1- and AP-3-complexes-
dependent manner. Enriched in neurite tips and neuron projections
in a BLOC-1- and AP-3-complexes-dependent manner (By similarity).
Found in subdomains of the plasma membrane termed non-caveolar
membrane rafts. {ECO:0000250|UniProtKB:Q2TBE6,
ECO:0000250|UniProtKB:Q99M64}.
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression is
observed in kidney, brain, heart, skeletal muscle, and placenta
and lowest expression is observed in colon, thymus, and small
intestine. {ECO:0000269|PubMed:11279162}.
-!- PTM: Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif.
Palmitoylation is cholesterol-dependent, and required for TGN
localization. {ECO:0000269|PubMed:22535966}.
-!- PTM: Ubiquitinated by ITCH; this does not lead to proteasomal
degradation. {ECO:0000269|PubMed:23146885}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
subfamily. {ECO:0000305}.
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EMBL; AJ303098; CAC38065.1; -; mRNA.
EMBL; BT007330; AAP35994.1; -; mRNA.
EMBL; AL355315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49906.1; -; Genomic_DNA.
EMBL; CH471066; EAW49907.1; -; Genomic_DNA.
EMBL; BC003167; AAH03167.1; -; mRNA.
EMBL; AL353952; CAB89254.1; -; mRNA.
CCDS; CCDS7469.1; -.
PIR; T48687; T48687.
RefSeq; NP_060895.1; NM_018425.3.
UniGene; Hs.25300; -.
PDB; 4HND; X-ray; 3.20 A; A/B=78-453.
PDB; 4HNE; X-ray; 2.95 A; A/B=78-453.
PDB; 4PLA; X-ray; 2.77 A; A=180-468.
PDB; 4YC4; X-ray; 2.58 A; A=180-468.
PDB; 5EUT; X-ray; 2.80 A; A=179-468.
PDB; 5I0N; X-ray; 2.28 A; A=180-468.
PDBsum; 4HND; -.
PDBsum; 4HNE; -.
PDBsum; 4PLA; -.
PDBsum; 4YC4; -.
PDBsum; 5EUT; -.
PDBsum; 5I0N; -.
ProteinModelPortal; Q9BTU6; -.
SMR; Q9BTU6; -.
BioGrid; 120639; 23.
CORUM; Q9BTU6; -.
IntAct; Q9BTU6; 7.
STRING; 9606.ENSP00000359665; -.
BindingDB; Q9BTU6; -.
ChEMBL; CHEMBL2251; -.
GuidetoPHARMACOLOGY; 2498; -.
iPTMnet; Q9BTU6; -.
PhosphoSitePlus; Q9BTU6; -.
SwissPalm; Q9BTU6; -.
BioMuta; PI4K2A; -.
DMDM; 74752344; -.
EPD; Q9BTU6; -.
MaxQB; Q9BTU6; -.
PaxDb; Q9BTU6; -.
PeptideAtlas; Q9BTU6; -.
PRIDE; Q9BTU6; -.
DNASU; 55361; -.
Ensembl; ENST00000370631; ENSP00000359665; ENSG00000155252.
GeneID; 55361; -.
KEGG; hsa:55361; -.
UCSC; uc001kog.2; human.
CTD; 55361; -.
DisGeNET; 55361; -.
EuPathDB; HostDB:ENSG00000155252.13; -.
GeneCards; PI4K2A; -.
HGNC; HGNC:30031; PI4K2A.
HPA; CAB030649; -.
HPA; HPA076857; -.
MIM; 609763; gene.
neXtProt; NX_Q9BTU6; -.
OpenTargets; ENSG00000155252; -.
PharmGKB; PA162399304; -.
eggNOG; KOG2381; Eukaryota.
eggNOG; ENOG410XP06; LUCA.
GeneTree; ENSGT00390000010434; -.
HOGENOM; HOG000294076; -.
HOVERGEN; HBG059542; -.
InParanoid; Q9BTU6; -.
KO; K13711; -.
OMA; GVRDSDW; -.
OrthoDB; EOG091G09F3; -.
PhylomeDB; Q9BTU6; -.
TreeFam; TF314740; -.
BioCyc; MetaCyc:HS00573-MONOMER; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
SIGNOR; Q9BTU6; -.
ChiTaRS; PI4K2A; human.
GeneWiki; PI4K2A; -.
GenomeRNAi; 55361; -.
PRO; PR:Q9BTU6; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000155252; -.
CleanEx; HS_PI4K2A; -.
Genevisible; Q9BTU6; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0035838; C:growing cell tip; ISS:UniProtKB.
GO; GO:0044231; C:host cell presynaptic membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
GO; GO:0035651; F:AP-3 adaptor complex binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
GO; GO:0007032; P:endosome organization; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IDA:UniProtKB.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
Pfam; PF00454; PI3_PI4_kinase; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasmic vesicle; Endosome;
Golgi apparatus; Kinase; Lipoprotein; Membrane; Mitochondrion;
Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
Synapse; Synaptosome; Transferase; Ubl conjugation.
CHAIN 1 479 Phosphatidylinositol 4-kinase type 2-
alpha.
/FTId=PRO_0000285158.
DOMAIN 133 438 PI3K/PI4K.
NP_BIND 131 137 ATP. {ECO:0000269|PubMed:24675427,
ECO:0000269|PubMed:25168678}.
NP_BIND 261 264 ATP. {ECO:0000269|PubMed:24675427,
ECO:0000269|PubMed:25168678}.
REGION 157 159 Important for substrate binding.
{ECO:0000305|PubMed:24675427}.
REGION 165 178 Important for interaction with membranes.
{ECO:0000305|PubMed:24675427,
ECO:0000305|PubMed:25168678}.
REGION 268 276 Important for interaction with membranes.
{ECO:0000305|PubMed:24675427}.
REGION 359 368 Important for interaction with membranes.
{ECO:0000305|PubMed:24675427}.
COMPBIAS 39 42 Poly-Ala.
COMPBIAS 65 97 Ala-rich.
BINDING 152 152 ATP. {ECO:0000269|PubMed:24675427,
ECO:0000269|PubMed:25168678}.
BINDING 346 346 ATP. {ECO:0000269|PubMed:24675427,
ECO:0000269|PubMed:25168678}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000250|UniProtKB:Q99M64}.
LIPID 174 174 S-palmitoyl cysteine.
{ECO:0000305|PubMed:22535966,
ECO:0000305|PubMed:24675427}.
LIPID 175 175 S-palmitoyl cysteine.
{ECO:0000305|PubMed:22535966,
ECO:0000305|PubMed:24675427}.
LIPID 177 177 S-palmitoyl cysteine.
{ECO:0000305|PubMed:22535966,
ECO:0000305|PubMed:24675427}.
LIPID 178 178 S-palmitoyl cysteine.
{ECO:0000305|PubMed:22535966,
ECO:0000305|PubMed:24675427}.
MUTAGEN 129 129 R->E: Reduces enzyme activity, probably
due to impaired membrane-association;
when associated with E-275 and E-276.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 152 152 K->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:24675427,
ECO:0000269|PubMed:25168678}.
MUTAGEN 157 159 EPY->APA: Abolishes enzyme activity.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 163 163 N->A: Reduces enzyme activity.
{ECO:0000269|PubMed:25168678}.
MUTAGEN 165 172 KWTKWLQK->AAAAAAAA: Abolishes enzyme
activity. {ECO:0000269|PubMed:25168678}.
MUTAGEN 165 165 K->A: Abolishes enzyme activity; when
associated with A-168 and A-172.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 166 166 W->A: Reduces enzyme activity.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 168 168 K->A: Abolishes enzyme activity; when
associated with A-165 and A-172.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 172 172 K->A: Abolishes enzyme activity; when
associated with A-165 and A-168.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 174 178 CCPCC->FFPFF: No effect on membrane-
association.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 174 178 CCPCC->SSPSS: Abolishes palmitoylation
and impairs membrane-association.
{ECO:0000269|PubMed:22535966,
ECO:0000269|PubMed:24675427}.
MUTAGEN 184 184 L->A: Abolishes enzyme activity; when
associated with A-349.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 263 263 F->A: Abolishes enzyme activity; when
associated with A-345.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 269 269 D->A: Reduces enzyme activity by half.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 275 275 R->A: Reduces enzyme activity.
{ECO:0000269|PubMed:25168678}.
MUTAGEN 275 275 R->E: Reduces enzyme activity, probably
due to impaired membrane-association;
when associated with E-129 and E-276.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 276 276 R->E: Reduces enzyme activity, probably
due to impaired membrane-association;
when associated with E-129 and E-275.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 308 308 D->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:25168678}.
MUTAGEN 345 345 I->A: Abolishes enzyme activity; when
associated with A-263.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 349 349 L->A: Abolishes enzyme activity; when
associated with A-184.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 359 359 W->A: Strongly reduced enzyme activity,
probably due to impaired membrane-
association. Abolishes enzyme activity;
when associated with A-365 and A-368.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 365 365 Y->A: Reduces enzyme activity, probably
due to impaired membrane-association.
Abolishes enzyme activity; when
associated with A-368 and A-359.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 368 368 W->A: Reduces enzyme activity, probably
due to impaired membrane-association.
Abolishes enzyme activity; when
associated with A-359 and A-365.
{ECO:0000269|PubMed:24675427}.
MUTAGEN 445 445 Q->A: Reduces enzyme activity.
{ECO:0000269|PubMed:25168678}.
HELIX 78 93 {ECO:0000244|PDB:4HNE}.
HELIX 95 99 {ECO:0000244|PDB:4HNE}.
HELIX 108 122 {ECO:0000244|PDB:5I0N}.
STRAND 131 136 {ECO:0000244|PDB:4YC4}.
STRAND 138 141 {ECO:0000244|PDB:5I0N}.
STRAND 147 153 {ECO:0000244|PDB:5I0N}.
HELIX 154 156 {ECO:0000244|PDB:5I0N}.
TURN 164 166 {ECO:0000244|PDB:5I0N}.
HELIX 167 171 {ECO:0000244|PDB:5I0N}.
HELIX 189 203 {ECO:0000244|PDB:5I0N}.
STRAND 211 216 {ECO:0000244|PDB:5I0N}.
HELIX 225 231 {ECO:0000244|PDB:5I0N}.
STRAND 235 237 {ECO:0000244|PDB:4HNE}.
STRAND 249 251 {ECO:0000244|PDB:4HNE}.
STRAND 256 262 {ECO:0000244|PDB:5I0N}.
STRAND 266 269 {ECO:0000244|PDB:4PLA}.
HELIX 270 279 {ECO:0000244|PDB:5I0N}.
HELIX 284 304 {ECO:0000244|PDB:5I0N}.
STRAND 313 318 {ECO:0000244|PDB:5I0N}.
STRAND 339 344 {ECO:0000244|PDB:5I0N}.
TURN 359 361 {ECO:0000244|PDB:5I0N}.
HELIX 365 368 {ECO:0000244|PDB:5I0N}.
HELIX 370 373 {ECO:0000244|PDB:5I0N}.
HELIX 378 388 {ECO:0000244|PDB:5I0N}.
HELIX 391 405 {ECO:0000244|PDB:5I0N}.
HELIX 413 435 {ECO:0000244|PDB:5I0N}.
HELIX 440 444 {ECO:0000244|PDB:5I0N}.
SEQUENCE 479 AA; 54022 MW; 9C9F4CE23F197BBD CRC64;
MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG SPGHDRERQP
LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE RNEFPEDPEF EAVVRQAELA
IERCIFPERI YQGSSGSYFV KDPQGRIIAV FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG
RDCLVLNQGY LSEAGASLVD QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK
VPKVGQRFNR IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA FPLKHPDSWR
AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED LYELFKKDPG FDRGQFHKQI
AVMRGQILNL TQALKDNKSP LHLVQMPPVI VETARSHQRS SSESYTQSFQ SRKPFFSWW


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