Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00200
Entry Name
UniProt Accession
Theoretical PI
8.51
Molecular Weight
54022.37
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phosphatidylinositol 4-kinase type 2-alpha
Protein Synonyms/Alias
2.7.1.67; Phosphatidylinositol 4-kinase type II-alpha;
Gene Name
PI4K2A
Gene Synonyms/Alias
Created Date
01-MAY-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
174
Canonical
TKWLQKLCCPCCFGR
[1]
S-Palmitoylation
175
Canonical
KWLQKLCCPCCFGRD
[1]
S-Palmitoylation
177
Canonical
LQKLCCPCCFGRDCL
[1]
S-Palmitoylation
178
Canonical
QKLCCPCCFGRDCLV
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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). This lipid kinase is the major phosphatidylinositol 4-phosphate (PI4P) producer in the Golgi apparatus, it generates more than 50% of this molecule which is essential for the identity of the organelle, protein sorting and membrane trafficking.
Sequence Annotation
Domain: 133 438 PI3K/PI4K.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 5 5 Phosphoserine.
Modified residue: 9 9 Phosphoserine.
Modified residue: 47 47 Phosphoserine.
Modified residue: 51 51 Phosphoserine.
Modified residue: 462 462 Phosphoserine.
Modified residue: 464 464 Phosphoserine.
Protein Length
479 AA.
Protein Sequence
(Canonical)
MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG SPGHDRERQP  60
LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE RNEFPEDPEF EAVVRQAELA  120
IERCIFPERI YQGSSGSYFV KDPQGRIIAV FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG  180
RDCLVLNQGY LSEAGASLVD QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK  240
VPKVGQRFNR IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL  300
DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA FPLKHPDSWR  360
AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED LYELFKKDPG FDRGQFHKQI  420
AVMRGQILNL TQALKDNKSP LHLVQMPPVI VETARSHQRS SSESYTQSFQ SRKPFFSWW   479
FASTA
(Canonical)
>LipidDB-9606-00200|Q9BTU6
MDETSPLVSPERAQPPDYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPGSPGHDRERQP
LLDRARGAAAQGQTQTVAAQAQALAAQAAAAAHAAQAHRERNEFPEDPEFEAVVRQAELA
IERCIFPERIYQGSSGSYFVKDPQGRIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFG
RDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEK
VPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVL
DYIIRNTDRGNDNWLIKYDCPMDSSSSRDTDWVVVKEPVIKVAAIDNGLAFPLKHPDSWR
AYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQI
AVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0030425; C:dendrite; ISS:UniProtKB
GO:0031901; C:early endosome membrane; IEA:Ensembl
GO:0005768; C:endosome; ISS:UniProtKB
GO:0070382; C:exocytic vesicle; IEA:Ensembl
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0035838; C:growing cell tip; ISS:UniProtKB
GO:0044231; C:host cell presynaptic membrane; ISS:UniProtKB
GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045121; C:membrane raft; IDA:UniProtKB
GO:0005739; C:mitochondrion; ISS:UniProtKB
GO:0043005; C:neuron projection; ISS:UniProtKB
GO:0043025; C:neuronal cell body; ISS:UniProtKB
GO:0043204; C:perikaryon; IEA:Ensembl
GO:0042734; C:presynaptic membrane; ISS:UniProtKB
GO:0043234; C:protein complex; IEA:Ensembl
GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl
GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB
GO:0035651; F:AP-3 adaptor complex binding; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0000287; F:magnesium ion binding; NAS:UniProtKB
GO:0002561; P:basophil degranulation; IEA:Ensembl
GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB
GO:0046854; P:phosphatidylinositol phosphorylation; IDA:GOC
GO:0006644; P:phospholipid metabolic process; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR000403; PI3/4_kinase_cat_dom
Pfam
Pfam; PF00454; PI3_PI4_kinase;
SMART
PROSITE
PRINTS