PCY1A_HUMAN - dbPTM
PCY1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCY1A_HUMAN
UniProt AC P49585
Protein Name Choline-phosphate cytidylyltransferase A
Gene Name PCYT1A
Organism Homo sapiens (Human).
Sequence Length 367
Subcellular Localization Cytoplasm, cytosol. Membrane
Peripheral membrane protein. It can interconvert between an inactive cytosolic form and an active membrane-bound form..
Protein Description Controls phosphatidylcholine synthesis..
Protein Sequence MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYDISEDEED
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-------MDAQCSAK
-------CCCHHHHH		9.7022814378
6Phosphorylation--MDAQCSAKVNARK
--CCCHHHHHHHHHH		21.0328985074
8SumoylationMDAQCSAKVNARKRR
CCCHHHHHHHHHHHH		21.52-
8SumoylationMDAQCSAKVNARKRR
CCCHHHHHHHHHHHH		21.5219608861
8UbiquitinationMDAQCSAKVNARKRR
CCCHHHHHHHHHHHH		21.5219608861
8AcetylationMDAQCSAKVNARKRR
CCCHHHHHHHHHHHH		21.5219608861
33AcetylationEEDGVPSKVQRCAVG
CCCCCCCHHHHEECC		36.0025953088
33MalonylationEEDGVPSKVQRCAVG
CCCCCCCHHHHEECC		36.0033225896
33UbiquitinationEEDGVPSKVQRCAVG
CCCCCCCHHHHEECC		36.0021906983
57AcetylationEIEVDFSKPYVRVTM
EEEEECCCCEEEEEH		40.1226051181
57UbiquitinationEIEVDFSKPYVRVTM
EEEEECCCCEEEEEH		40.1221906983
64SulfoxidationKPYVRVTMEEASRGT
CCEEEEEHHHHHCCC		3.9230846556
106PhosphorylationAKNLFPNTYLIVGVC
HHHCCCCEEEEEEEE		21.6829083192
107PhosphorylationKNLFPNTYLIVGVCS
HHCCCCEEEEEEEEC		10.8929083192
114PhosphorylationYLIVGVCSDELTHNF
EEEEEEECHHHCCCC		31.5429083192
141PhosphorylationDAVQHCRYVDEVVRN
CHHHHHHHHHHHHHH		20.0423403867
173PhosphorylationVAHDDIPYSSAGSDD
EECCCCCCCCCCCHH		18.6527251275
174PhosphorylationAHDDIPYSSAGSDDV
ECCCCCCCCCCCHHH		14.3527251275
175PhosphorylationHDDIPYSSAGSDDVY
CCCCCCCCCCCHHHH		30.7027251275
182PhosphorylationSAGSDDVYKHIKEAG
CCCCHHHHHHHHHHC		12.12-
183UbiquitinationAGSDDVYKHIKEAGM
CCCHHHHHHHHHHCC		38.4121906983
186UbiquitinationDDVYKHIKEAGMFAP
HHHHHHHHHHCCCCC		41.032190698
190SulfoxidationKHIKEAGMFAPTQRT
HHHHHHCCCCCCCCC		3.1430846556
197PhosphorylationMFAPTQRTEGISTSD
CCCCCCCCCCCCHHH		28.84-
201PhosphorylationTQRTEGISTSDIITR
CCCCCCCCHHHHHHH		32.4925693802
202PhosphorylationQRTEGISTSDIITRI
CCCCCCCHHHHHHHH		28.6225693802
203PhosphorylationRTEGISTSDIITRIV
CCCCCCHHHHHHHHH		21.7425693802
207PhosphorylationISTSDIITRIVRDYD
CCHHHHHHHHHHCCH		18.0625693802
216PhosphorylationIVRDYDVYARRNLQR
HHHCCHHHHHCCCCC		7.47-
228UbiquitinationLQRGYTAKELNVSFI
CCCCCCCCCCCCEEC		55.74-
228AcetylationLQRGYTAKELNVSFI
CCCCCCCCCCCCEEC		55.7420167786
233PhosphorylationTAKELNVSFINEKKY
CCCCCCCEECCHHHH		21.2429255136
238UbiquitinationNVSFINEKKYHLQER
CCEECCHHHHHHHHH		54.89-
2382-HydroxyisobutyrylationNVSFINEKKYHLQER
CCEECCHHHHHHHHH		54.89-
2392-HydroxyisobutyrylationVSFINEKKYHLQERV
CEECCHHHHHHHHHH		31.55-
261UbiquitinationKDVEEKSKEFVQKVE
HHHHHHHHHHHHHHH		67.26-
266SumoylationKSKEFVQKVEEKSID
HHHHHHHHHHHHHHH		46.44-
266SumoylationKSKEFVQKVEEKSID
HHHHHHHHHHHHHHH		46.44-
270UbiquitinationFVQKVEEKSIDLIQK
HHHHHHHHHHHHHHH		38.92-
271PhosphorylationVQKVEEKSIDLIQKW
HHHHHHHHHHHHHHH		25.3127251275
277UbiquitinationKSIDLIQKWEEKSRE
HHHHHHHHHHHHHHH		49.97-
282PhosphorylationIQKWEEKSREFIGSF
HHHHHHHHHHHHHHH		40.0822210691
315PhosphorylationGRMLQAISPKQSPSS
CCEEEECCCCCCCCC		29.1222167270
319PhosphorylationQAISPKQSPSSSPTR
EECCCCCCCCCCCCC		32.6422167270
321PhosphorylationISPKQSPSSSPTRER
CCCCCCCCCCCCCCC		49.0122167270
322PhosphorylationSPKQSPSSSPTRERS
CCCCCCCCCCCCCCC		43.6622167270
323PhosphorylationPKQSPSSSPTRERSP
CCCCCCCCCCCCCCC		34.3322167270
325PhosphorylationQSPSSSPTRERSPSP
CCCCCCCCCCCCCCC		47.3022167270
329PhosphorylationSSPTRERSPSPSFRW
CCCCCCCCCCCCCCC		25.6129255136
331PhosphorylationPTRERSPSPSFRWPF
CCCCCCCCCCCCCCC		34.1329255136
333PhosphorylationRERSPSPSFRWPFSG
CCCCCCCCCCCCCCC		31.6129255136
339PhosphorylationPSFRWPFSGKTSPPC
CCCCCCCCCCCCCCC		34.9920201521
342PhosphorylationRWPFSGKTSPPCSPA
CCCCCCCCCCCCCHH		50.4122167270
343PhosphorylationWPFSGKTSPPCSPAN
CCCCCCCCCCCCHHH		30.2622167270
347PhosphorylationGKTSPPCSPANLSRH
CCCCCCCCHHHHHHH		32.5920201521
352PhosphorylationPCSPANLSRHKAAAY
CCCHHHHHHHCHHCC		31.9523927012
359PhosphorylationSRHKAAAYDISEDEE
HHHCHHCCCCCCCCC		14.7523927012
362PhosphorylationKAAAYDISEDEED--
CHHCCCCCCCCCC--		35.7823927012
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 ligaseFBXL2Q9UKC9
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCY1A_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 PCY1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDIA6_HUMANPDIA6physical
22863883
S10AD_HUMANS100A13physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608940Spondylometaphyseal dysplasia with cone-rod dystrophy (SMDCRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00122Choline
DB00709Lamivudine
Regulatory Network of PCY1A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-8, AND MASSSPECTROMETRY.
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-315; SER-319; SER-343;SER-347 AND SER-362, 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-315; SER-319; SER-321;THR-325; SER-343; SER-347 AND SER-362, AND MASS 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-315; SER-339; THR-342;SER-343; SER-347; SER-352 AND SER-362, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-319, ANDMASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.
"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-315; SER-329; SER-331AND SER-362, AND MASS SPECTROMETRY.

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