PCY1B_HUMAN - dbPTM
PCY1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCY1B_HUMAN
UniProt AC Q9Y5K3
Protein Name Choline-phosphate cytidylyltransferase B
Gene Name PCYT1B
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization Endoplasmic reticulum.
Protein Description Controls phosphatidylcholine synthesis..
Protein Sequence MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK
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
6Phosphorylation--MPVVTTDAESETG
--CCEEECCCCCCCC		22.9225693802
10PhosphorylationVVTTDAESETGIPKS
EEECCCCCCCCCCHH		42.0225693802
12PhosphorylationTTDAESETGIPKSLS
ECCCCCCCCCCHHHC		50.0925693802
33 (in isoform 4)Phosphorylation-17.0619690332
33 (in isoform 3)Phosphorylation-17.0619690332
51PhosphorylationPAPFADETNCQCQAP
CCCCCCCCCCCCCCC		41.67-
71PhosphorylationIAQARLGTPADRPVR
HHHHHHCCCCCCCEE		21.64-
87UbiquitinationYADGIFDLFHSGHAR
ECCCHHHHHHHHHHH		2.6422817900
90UbiquitinationGIFDLFHSGHARALM
CHHHHHHHHHHHHHH		25.5822817900
132UbiquitinationTVMNEAERYEALRHC
EECCHHHHHHHHHHC		41.4627667366
165UbiquitinationLEKHKIDFVAHDDIP
HHHCCCCEEECCCCC		6.2722817900
165 (in isoform 3)Ubiquitination-6.2721906983
168UbiquitinationHKIDFVAHDDIPYSS
CCCCEEECCCCCCCC		28.1622817900
173PhosphorylationVAHDDIPYSSAGSDD
EECCCCCCCCCCCHH		18.6527251275
174PhosphorylationAHDDIPYSSAGSDDV
ECCCCCCCCCCCHHH		14.3527251275
175PhosphorylationHDDIPYSSAGSDDVY
CCCCCCCCCCCHHHH		30.7027251275
182PhosphorylationSAGSDDVYKHIKEAG
CCCCHHHHHHHHHHC		12.12-
183UbiquitinationAGSDDVYKHIKEAGM
CCCHHHHHHHHHHCC		38.4122817900
183 (in isoform 1)Ubiquitination-38.4121906983
183 (in isoform 2)Ubiquitination-38.4121906983
186UbiquitinationDDVYKHIKEAGMFVP
HHHHHHHHHHCCCCC		41.0322817900
197PhosphorylationMFVPTQRTEGISTSD
CCCCCCCCCCCCHHH		28.84-
201PhosphorylationTQRTEGISTSDIITR
CCCCCCCCHHHHHHH		32.4925693802
202PhosphorylationQRTEGISTSDIITRI
CCCCCCCHHHHHHHH		28.6225693802
203PhosphorylationRTEGISTSDIITRIV
CCCCCCHHHHHHHHH		21.7425693802
207PhosphorylationISTSDIITRIVRDYD
CCHHHHHHHHHHCCH		18.0625693802
210UbiquitinationSDIITRIVRDYDVYA
HHHHHHHHHCCHHHH		3.2527667366
210 (in isoform 3)Ubiquitination-3.25-
216PhosphorylationIVRDYDVYARRNLQR
HHHCCHHHHHCCCCC		7.47-
228UbiquitinationLQRGYTAKELNVSFI
CCCCCCEEECCCCHH		55.7427667366
228AcetylationLQRGYTAKELNVSFI
CCCCCCEEECCCCHH		55.7428641319
233PhosphorylationTAKELNVSFINEKRY
CEEECCCCHHHHHHH		21.2423401153
254UbiquitinationDKMKEKVKNVEERSK
HHHHHHHHCHHHHHH		67.36-
271PhosphorylationVNRVEEKSHDLIQKW
HHHHHHHCHHHHHHH		26.0521964256
297PhosphorylationLELFGPDGAWKQMFQ
HHHHCCCHHHHHHHH		36.1532645325
307PhosphorylationKQMFQERSSRMLQAL
HHHHHHHHHHHHHHH		22.8822210691
308PhosphorylationQMFQERSSRMLQALS
HHHHHHHHHHHHHHC		28.1222210691
315PhosphorylationSRMLQALSPKQSPVS
HHHHHHHCCCCCCCC		32.8219664994
315 (in isoform 2)Phosphorylation-32.8225849741
317PhosphorylationMLQALSPKQSPVSSP
HHHHHCCCCCCCCCC		61.0932142685
319PhosphorylationQALSPKQSPVSSPTR
HHHCCCCCCCCCCCC		33.1415345747
321PhosphorylationLSPKQSPVSSPTRSR
HCCCCCCCCCCCCCC		12.2432142685
322PhosphorylationSPKQSPVSSPTRSRS
CCCCCCCCCCCCCCC		33.7020068231
323PhosphorylationPKQSPVSSPTRSRSP
CCCCCCCCCCCCCCC		30.4420068231
325PhosphorylationQSPVSSPTRSRSPSR
CCCCCCCCCCCCCCC		43.1315345747
327PhosphorylationPVSSPTRSRSPSRSP
CCCCCCCCCCCCCCC		39.3223401153
329PhosphorylationSSPTRSRSPSRSPSP
CCCCCCCCCCCCCCC		28.5921406692
331PhosphorylationPTRSRSPSRSPSPTF
CCCCCCCCCCCCCCE		46.7923401153
333PhosphorylationRSRSPSRSPSPTFSW
CCCCCCCCCCCCEEE		33.7821406692
335PhosphorylationRSPSRSPSPTFSWLP
CCCCCCCCCCEEEEE		37.5128348404
337PhosphorylationPSRSPSPTFSWLPLK
CCCCCCCCEEEEECC		34.3425307156
339PhosphorylationRSPSPTFSWLPLKTS
CCCCCCEEEEECCCC		30.1321406692
345PhosphorylationFSWLPLKTSPPSSPK
EEEEECCCCCCCCCC		54.9028060719
346PhosphorylationSWLPLKTSPPSSPKA
EEEECCCCCCCCCCC		32.9728060719
349PhosphorylationPLKTSPPSSPKAASA
ECCCCCCCCCCCCHH		63.7628060719
350PhosphorylationLKTSPPSSPKAASAS
CCCCCCCCCCCCHHH		35.8728060719
355PhosphorylationPSSPKAASASISSMS
CCCCCCCHHHHHCCC		27.6621406692
357PhosphorylationSPKAASASISSMSEG
CCCCCHHHHHCCCCC		22.1021406692
359PhosphorylationKAASASISSMSEGDE
CCCHHHHHCCCCCCC		19.9329978859
360PhosphorylationAASASISSMSEGDED
CCHHHHHCCCCCCCC		25.3430576142
362PhosphorylationSASISSMSEGDEDEK
HHHHHCCCCCCCCCC		40.1323401153
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
260SPhosphorylationKinaseRPS6KA1Q15418
GPS
260SPhosphorylationKinaseRPS6KA3P51812
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCY1B_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 PCY1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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
DB00122Choline
Regulatory Network of PCY1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-233 AND SER-315, ANDMASS 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.

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