P4K2A_HUMAN - dbPTM
P4K2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P4K2A_HUMAN
UniProt AC Q9BTU6
Protein Name Phosphatidylinositol 4-kinase type 2-alpha
Gene Name PI4K2A
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Lipid-anchor . Membrane raft . Cell projection, dendrite . Cell junction, synapse, presynaptic cell membrane . Cell junction, synapse, synaptosome . Mitochondrion . Endosome . Cytoplasmic vesicle . Membrane
Protein Description 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)..
Protein Sequence MDETSPLVSPERAQPPDYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPGSPGHDRERQPLLDRARGAAAQGQTQTVAAQAQALAAQAAAAAHAAQAHRERNEFPEDPEFEAVVRQAELAIERCIFPERIYQGSSGSYFVKDPQGRIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDSSSSRDTDWVVVKEPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MDETSPLV
-------CCCCCCCC		10.6925944712
4Phosphorylation----MDETSPLVSPE
----CCCCCCCCCCC		31.2329255136
5Phosphorylation---MDETSPLVSPER
---CCCCCCCCCCCC		17.7529255136
9PhosphorylationDETSPLVSPERAQPP
CCCCCCCCCCCCCCC		28.8229255136
18PhosphorylationERAQPPDYTFPSGSG
CCCCCCCCCCCCCCC		18.9628796482
19PhosphorylationRAQPPDYTFPSGSGA
CCCCCCCCCCCCCCC		36.1325884760
22PhosphorylationPPDYTFPSGSGAHFP
CCCCCCCCCCCCCCC		41.2125159151
24PhosphorylationDYTFPSGSGAHFPQV
CCCCCCCCCCCCCCC		36.8229978859
44PhosphorylationRVAAAAGSGPSPPGS
EEEHHCCCCCCCCCC		42.6929255136
47PhosphorylationAAAGSGPSPPGSPGH
HHCCCCCCCCCCCCC		47.4519664994
51PhosphorylationSGPSPPGSPGHDRER
CCCCCCCCCCCCCCC		33.2219664994
124S-palmitoylationAELAIERCIFPERIY
HHHHHHHHCCCHHEE		2.1429575903
134PhosphorylationPERIYQGSSGSYFVK
CHHEEECCCCCEEEE		18.9218785766
137PhosphorylationIYQGSSGSYFVKDPQ
EEECCCCCEEEECCC		19.8328152594
138PhosphorylationYQGSSGSYFVKDPQG
EECCCCCEEEECCCC		18.8628152594
141UbiquitinationSSGSYFVKDPQGRII
CCCCEEEECCCCCEE		54.5123000965
152UbiquitinationGRIIAVFKPKNEEPY
CCEEEEEECCCCCCC		48.7827667366
159PhosphorylationKPKNEEPYGHLNPKW
ECCCCCCCCCCCHHH		22.0625839225
165UbiquitinationPYGHLNPKWTKWLQK
CCCCCCHHHHHHHHH		67.4322817900
168UbiquitinationHLNPKWTKWLQKLCC
CCCHHHHHHHHHHHC		44.8022817900
174S-palmitoylationTKWLQKLCCPCCFGR
HHHHHHHHCHHHCCC		2.9122535966
175S-palmitoylationKWLQKLCCPCCFGRD
HHHHHHHCHHHCCCC		4.1322535966
177S-palmitoylationLQKLCCPCCFGRDCL
HHHHHCHHHCCCCEE		1.5522535966
178S-palmitoylationQKLCCPCCFGRDCLV
HHHHCHHHCCCCEEE		2.1522535966
234UbiquitinationDRVKSRGKRLALEKV
HHHHHHCCCHHHHCC		43.0323000965
240UbiquitinationGKRLALEKVPKVGQR
CCCHHHHCCCCCCHH		65.7623000965
240MethylationGKRLALEKVPKVGQR
CCCHHHHCCCCCCHH		65.76-
243UbiquitinationLALEKVPKVGQRFNR
HHHHCCCCCCHHCCC		63.0823000965
243MethylationLALEKVPKVGQRFNR
HHHHCCCCCCHHCCC		63.08-
268UbiquitinationQLFVEGYKDADYWLR
EEEEECCCCHHHHHH		58.2421906983
302PhosphorylationERLVVLDYIIRNTDR
HHHHHHHHHHHCCCC		8.29-
324PhosphorylationKYDCPMDSSSSRDTD
EEECCCCCCCCCCCC		26.3526471730
325PhosphorylationYDCPMDSSSSRDTDW
EECCCCCCCCCCCCE		28.2426471730
326PhosphorylationDCPMDSSSSRDTDWV
ECCCCCCCCCCCCEE		33.0926471730
327PhosphorylationCPMDSSSSRDTDWVV
CCCCCCCCCCCCEEE		35.8026471730
336UbiquitinationDTDWVVVKEPVIKVA
CCCEEEECCCEEEEE		44.6923000965
341UbiquitinationVVKEPVIKVAAIDNG
EECCCEEEEEEEECC		26.5123000965
354UbiquitinationNGLAFPLKHPDSWRA
CCEEECCCCCCCCCC		54.0221963094
354AcetylationNGLAFPLKHPDSWRA
CCEEECCCCCCCCCC		54.0221466224
373UbiquitinationWAWLPQAKVPFSQEI
EEECCCCCCCCCHHH		45.2321987572
381UbiquitinationVPFSQEIKDLILPKI
CCCCHHHHHHHHHCC		45.8122817900
387UbiquitinationIKDLILPKISDPNFV
HHHHHHHCCCCCCHH		51.9329967540
402PhosphorylationKDLEEDLYELFKKDP
HCHHHHHHHHHHHCC		23.9425147952
406UbiquitinationEDLYELFKKDPGFDR
HHHHHHHHHCCCCCH		69.7429967540
407UbiquitinationDLYELFKKDPGFDRG
HHHHHHHHCCCCCHH		62.9229967540
418UbiquitinationFDRGQFHKQIAVMRG
CCHHHHHHHHHHHHH		44.6929967540
431PhosphorylationRGQILNLTQALKDNK
HHHHHHHHHHHHHCC		15.6620068231
435UbiquitinationLNLTQALKDNKSPLH
HHHHHHHHHCCCCCC		63.3721906983
438UbiquitinationTQALKDNKSPLHLVQ
HHHHHHCCCCCCCEE		64.6822817900
456PhosphorylationVIVETARSHQRSSSE
EEEECCHHCCCCCCH		22.8523312004
460PhosphorylationTARSHQRSSSESYTQ
CCHHCCCCCCHHHHH		31.4822167270
461PhosphorylationARSHQRSSSESYTQS
CHHCCCCCCHHHHHH		40.0722167270
462PhosphorylationRSHQRSSSESYTQSF
HHCCCCCCHHHHHHH		31.6319664994
464PhosphorylationHQRSSSESYTQSFQS
CCCCCCHHHHHHHHH		35.1122167270
465PhosphorylationQRSSSESYTQSFQSR
CCCCCHHHHHHHHHC		12.5423927012
466PhosphorylationRSSSESYTQSFQSRK
CCCCHHHHHHHHHCC		27.3222167270
468PhosphorylationSSESYTQSFQSRKPF
CCHHHHHHHHHCCCC		19.9023927012
471PhosphorylationSYTQSFQSRKPFFSW
HHHHHHHHCCCCCCC		40.0223927012
473UbiquitinationTQSFQSRKPFFSWW-
HHHHHHCCCCCCCC-		51.9621963094
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:23146885
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P4K2A_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of P4K2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
21330372
RD23A_HUMANRAD23Aphysical
21163940
CLCB_HUMANCLTBphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P4K2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-51; SER-462 ANDSER-464, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-51 ANDSER-462, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-462, ANDMASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47; SER-51 ANDSER-462, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 ANDSER-51, AND MASS SPECTROMETRY.

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