Reviewed, UniProtKB/Swiss-Prot Q9BTU6 (P4K2A_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol 4-kinase type 2-alpha
    EC=2.7.1.67
Alternative name(s):
    Phosphatidylinositol 4-kinase type II-alpha

Gene names

Name:

PI4K2A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Together with PI4K2B and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. The phosphorylation of phosphatidylinositol (PI) to 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). Contributes to the production of InsP3 in stimulated cells By similarity.
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.
Subcellular location	Cytoplasm. Membrane raft. Note: Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. Ref.1
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. Ref.1
Sequence similarities	Belongs to the PI3/PI4-kinase family. Type II PI4K subfamily. Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphatidylinositol biosynthetic process Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.1 Inferred from direct assay. Source: UniProtKB membrane raft Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	1-phosphatidylinositol 4-kinase activity Ref.1 Inferred from direct assay. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Phosphatidylinositol 4-kinase type 2-alpha		PRO_0000285158
Regions
	Domain	133 – 438	306	PI3K/PI4K
	Compositional bias	39 – 42	4	Poly-Ala
	Compositional bias	65 – 97	33	Ala-rich
Amino acid modifications
	Modified residue	5	1	Phosphoserine Ref.6
	Modified residue	9	1	Phosphoserine Ref.6
	Modified residue	44	1	Phosphoserine Ref.7
	Modified residue	47	1	Phosphoserine Ref.6 Ref.7 Ref.11
	Modified residue	51	1	Phosphoserine Ref.6 Ref.7 Ref.11
	Modified residue	461	1	Phosphoserine Ref.9
	Modified residue	462	1	Phosphoserine Ref.7 Ref.11 Ref.9
	Modified residue	464	1	Phosphoserine Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q9BTU6-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9C9F4CE23F197BBD	FASTA	479	54,022
	10 20 30 40 50 60 MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG SPGHDRERQP 70 80 90 100 110 120 LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE RNEFPEDPEF EAVVRQAELA 130 140 150 160 170 180 IERCIFPERI YQGSSGSYFV KDPQGRIIAV FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG 190 200 210 220 230 240 RDCLVLNQGY LSEAGASLVD QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK 250 260 270 280 290 300 VPKVGQRFNR IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL 310 320 330 340 350 360 DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA FPLKHPDSWR 370 380 390 400 410 420 AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED LYELFKKDPG FDRGQFHKQI 430 440 450 460 470 AVMRGQILNL TQALKDNKSP LHLVQMPPVI VETARSHQRS SSESYTQSFQ SRKPFFSWW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family." Minogue S., Anderson J.S., Waugh M.G., dos Santos M., Corless S., Cramer R., Hsuan J.J. J. Biol. Chem. 276:16635-16640(2001) [PubMed: 11279162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-479. Tissue: Amygdala.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND SER-51, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-51 AND SER-462, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-462, MASS SPECTROMETRY.
[10]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-51 AND SER-462, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-51; SER-462 AND SER-464, MASS SPECTROMETRY. Tissue: T-cell.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ303098 mRNA. Translation: CAC38065.1. BT007330 mRNA. Translation: AAP35994.1. AL355315 Genomic DNA. Translation: CAI15460.1. BC003167 mRNA. Translation: AAH03167.1. AL353952 mRNA. Translation: CAB89254.1.
IPI	IPI00020124.
PIR	T48687.
RefSeq	NP_060895.1.
UniGene	Hs.25300
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9BTU6.
PTM databases
PhosphoSite	Q9BTU6.
Proteomic databases
PRIDE	Q9BTU6.
Genome annotation databases
Ensembl	ENST00000370631; ENSP00000359665; ENSG00000155252; Homo sapiens. [Genome view]
GeneID	55361.
KEGG	hsa:55361.
UCSC	uc001kog.1. human.
Organism-specific databases
CTD	55361.
GeneCards	GC10P099391.
H-InvDB	HIX0009098.
HGNC	HGNC:30031. PI4K2A.
MIM	609763. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13238.
HOGENOM	HBG714361.
HOVERGEN	Q9BTU6.
InParanoid	Q9BTU6.
PhylomeDB	Q9BTU6.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000043822-MONOMER.
BRENDA	2.7.1.67. 247.
Gene expression databases
ArrayExpress	Q9BTU6.
Bgee	Q9BTU6.
CleanEx	HS_PI4K2A.
Genevestigator	Q9BTU6.
Family and domain databases
InterPro	IPR000403. PI3/4_kinase_cat. [Graphical view]
Pfam	PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
PROSITE	PS00915. PI3_4_KINASE_1. False negative. PS00916. PI3_4_KINASE_2. False negative. PS50290. PI3_4_KINASE_3. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	59731.
SOURCE	Search...

Entry information

Entry name

P4K2A_HUMAN

Accession

Primary (citable) accession number: Q9BTU6
Secondary accession number(s): Q9NSG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.