PCY1A_MOUSE - dbPTM
PCY1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCY1A_MOUSE
UniProt AC P49586
Protein Name Choline-phosphate cytidylyltransferase A
Gene Name Pcyt1a
Organism Mus musculus (Mouse).
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 MDAQSSAKVNSRKRRKEAPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCRAVTCDISEDEED
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-------MDAQSSAK
-------CCHHHHHH		9.70-
6Phosphorylation--MDAQSSAKVNSRK
--CCHHHHHHHHHHH		21.7422345495
8AcetylationMDAQSSAKVNSRKRR
CCHHHHHHHHHHHHH		43.85-
11PhosphorylationQSSAKVNSRKRRKEA
HHHHHHHHHHHHCCC		42.0118779572
33UbiquitinationEEDGIPSKVQRCAVG
CCCCCCHHHHHHHCC		36.7127667366
57AcetylationEIEVDFSKPYVRVTM
EEEEECCCCEEEEEH		40.1223236377
201PhosphorylationTQRTEGISTSDIITR
CCCCCCCCHHHHHHH		32.4930635358
202PhosphorylationQRTEGISTSDIITRI
CCCCCCCHHHHHHHH		28.6230635358
203PhosphorylationRTEGISTSDIITRIV
CCCCCCHHHHHHHHH		21.7430635358
207PhosphorylationISTSDIITRIVRDYD
CCHHHHHHHHHHCCH		18.0630635358
228UbiquitinationLQRGYTAKELNVSFI
CCCCCCCCCCCCEEC		55.7422790023
233PhosphorylationTAKELNVSFINEKKY
CCCCCCCEECCHHHH		21.2421082442
240PhosphorylationSFINEKKYHLQERVD
EECCHHHHHHHHHHH		20.8718779572
281UbiquitinationLIQKWEEKSREFIGS
HHHHHHHHHHHHHHH		43.2122790023
310OxidationLKEGKGRMLQAISPK
HHHCCCCEEEECCCC		4.4217242355
315PhosphorylationGRMLQAISPKQSPSS
CCEEEECCCCCCCCC		29.1227087446
319PhosphorylationQAISPKQSPSSSPTH
EECCCCCCCCCCCCC		32.6427087446
321PhosphorylationISPKQSPSSSPTHER
CCCCCCCCCCCCCCC		49.0127087446
322PhosphorylationSPKQSPSSSPTHERS
CCCCCCCCCCCCCCC		43.6627087446
323PhosphorylationPKQSPSSSPTHERSP
CCCCCCCCCCCCCCC		37.8527087446
325PhosphorylationQSPSSSPTHERSPSP
CCCCCCCCCCCCCCC		38.0127087446
329PhosphorylationSSPTHERSPSPSFRW
CCCCCCCCCCCCCCC		27.0927742792
331PhosphorylationPTHERSPSPSFRWPF
CCCCCCCCCCCCCCC		34.1325521595
333PhosphorylationHERSPSPSFRWPFSG
CCCCCCCCCCCCCCC		31.6123684622
339PhosphorylationPSFRWPFSGKTSPSS
CCCCCCCCCCCCCCC		34.9921082442
341UbiquitinationFRWPFSGKTSPSSSP
CCCCCCCCCCCCCCC		44.6322790023
341AcetylationFRWPFSGKTSPSSSP
CCCCCCCCCCCCCCC		44.6323806337
342PhosphorylationRWPFSGKTSPSSSPA
CCCCCCCCCCCCCCC		49.7725521595
343PhosphorylationWPFSGKTSPSSSPAS
CCCCCCCCCCCCCCH		26.6926824392
345PhosphorylationFSGKTSPSSSPASLS
CCCCCCCCCCCCHHH		43.1227087446
346PhosphorylationSGKTSPSSSPASLSR
CCCCCCCCCCCHHHC		43.6627087446
347PhosphorylationGKTSPSSSPASLSRC
CCCCCCCCCCHHHCC		28.9027087446
350PhosphorylationSPSSSPASLSRCRAV
CCCCCCCHHHCCEEE		30.2027087446
352PhosphorylationSSSPASLSRCRAVTC
CCCCCHHHCCEEEEC		27.1727742792
358PhosphorylationLSRCRAVTCDISEDE
HHCCEEEECCCCCCC		11.9527742792
362PhosphorylationRAVTCDISEDEED--
EEEECCCCCCCCC--		26.2427087446
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

Oops, there are no upstream regulatory protein records of PCY1A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCY1A_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMA1_MOUSEKpna2physical
19332566
MK01_MOUSEMapk1physical
19332566
IMA1_HUMANKPNA2physical
19332566
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCY1A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319 ANDSER-347, AND MASS SPECTROMETRY.

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