CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020170
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylinositol 4-kinase type 2-alpha 
Protein Synonyms/Alias
 Phosphatidylinositol 4-kinase type II-alpha 
Gene Name
 PI4K2A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
141SSGSYFVKDPQGRIIubiquitination[1, 2, 3, 4, 5, 6, 7]
165PYGHLNPKWTKWLQKubiquitination[1]
240GKRLALEKVPKVGQRubiquitination[2, 4, 5, 6, 8]
268QLFVEGYKDADYWLRubiquitination[2, 6, 9]
336DTDWVVVKEPVIKVAubiquitination[2, 4, 5, 6, 8, 9]
354NGLAFPLKHPDSWRAubiquitination[5]
373WAWLPQAKVPFSQEIubiquitination[9]
381VPFSQEIKDLILPKIubiquitination[2]
435LNLTQALKDNKSPLHubiquitination[2]
473TQSFQSRKPFFSWW*ubiquitination[6, 9]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
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). 
Sequence Annotation
 DOMAIN 133 438 PI3K/PI4K.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 462 462 Phosphoserine.
 MOD_RES 464 464 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endosome; Kinase; Membrane; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse; Synaptosome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 479 AA 
Protein Sequence
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 
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:Compara.
 GO:0005768; C:endosome; ISS:UniProtKB.
 GO:0070382; C:exocytic vesicle; IEA:Compara.
 GO:0035838; C:growing cell tip; ISS:UniProtKB.
 GO:0044231; C:host cell presynaptic membrane; ISS:UniProtKB.
 GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0043025; C:neuronal cell body; ISS:UniProtKB.
 GO:0043204; C:perikaryon; IEA:Compara.
 GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0030672; C:synaptic vesicle membrane; IEA:Compara.
 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:Compara.
 GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR000403; PI3/4_kinase_cat_dom. 
Pfam
 PF00454; PI3_PI4_kinase 
SMART
  
PROSITE
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS