PCY1_YEAST - dbPTM
PCY1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCY1_YEAST
UniProt AC P13259
Protein Name Choline-phosphate cytidylyltransferase
Gene Name PCT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 424
Subcellular Localization Membrane. Most of its activity is membrane-associated.
Protein Description
Protein Sequence MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNELKKQNQRQRKQNFLDDPFTRKLIREASPATEFANEFTGENSTAKSPDDNGNLFSQEDDEDTNSNNTNTNSDSDSNTNSTPPSEDDDDNDRLTLENLTQKKKQSAN
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
5Phosphorylation---MANPTTGKSSIR
---CCCCCCCHHHHH		48.2430377154
6Phosphorylation--MANPTTGKSSIRA
--CCCCCCCHHHHHH		43.8230377154
9PhosphorylationANPTTGKSSIRAKLS
CCCCCCHHHHHHHCC		32.1321440633
10PhosphorylationNPTTGKSSIRAKLSN
CCCCCHHHHHHHCCC		21.4119823750
14AcetylationGKSSIRAKLSNSSLS
CHHHHHHHCCCHHHH		42.4722865919
16PhosphorylationSSIRAKLSNSSLSNL
HHHHHHCCCHHHHHH		33.6822369663
18PhosphorylationIRAKLSNSSLSNLFK
HHHHCCCHHHHHHHH		29.3122369663
19PhosphorylationRAKLSNSSLSNLFKK
HHHCCCHHHHHHHHH		39.8122369663
21PhosphorylationKLSNSSLSNLFKKNK
HCCCHHHHHHHHHCC		33.1722369663
59PhosphorylationENKDTQLTPRKRRRL
CCCCCCCCHHHHHHH		15.9519823750
67PhosphorylationPRKRRRLTKEFEEKE
HHHHHHHHHHHHHHH		27.0730377154
78PhosphorylationEEKEARYTNELPKEL
HHHHHHHHCCCCHHH		19.3621440633
192PhosphorylationLLEHKIDYVAHDDIP
HHHCCCCEEECCCCC		11.7423749301
209PhosphorylationSADSDDIYKPIKEMG
CCCCCCCHHHHHHHH		20.0823749301
210AcetylationADSDDIYKPIKEMGK
CCCCCCHHHHHHHHH		40.3724489116
217AcetylationKPIKEMGKFLTTQRT
HHHHHHHHHHHHHCC		35.5724489116
220PhosphorylationKEMGKFLTTQRTNGV
HHHHHHHHHHCCCCC		24.8228889911
221PhosphorylationEMGKFLTTQRTNGVS
HHHHHHHHHCCCCCC		20.4328889911
228PhosphorylationTQRTNGVSTSDIITK
HHCCCCCCHHHHHHH		24.4827214570
229PhosphorylationQRTNGVSTSDIITKI
HCCCCCCHHHHHHHH		28.1921440633
230PhosphorylationRTNGVSTSDIITKII
CCCCCCHHHHHHHHH		21.2121440633
235UbiquitinationSTSDIITKIIRDYDK
CHHHHHHHHHHHHHH		26.2319722269
242AcetylationKIIRDYDKYLMRNFA
HHHHHHHHHHHHHHH		33.7724489116
314AcetylationLGKKLYSKLIGNELK
HCHHHHHHHHHHHHH		30.4822865919
346PhosphorylationRKLIREASPATEFAN
HHHHHHHCHHHHHHH		15.4322369663
349PhosphorylationIREASPATEFANEFT
HHHHCHHHHHHHHHC		34.7122369663
356PhosphorylationTEFANEFTGENSTAK
HHHHHHHCCCCCCCC		37.0922890988
360PhosphorylationNEFTGENSTAKSPDD
HHHCCCCCCCCCCCC		25.9922890988
361PhosphorylationEFTGENSTAKSPDDN
HHCCCCCCCCCCCCC		50.0822890988
401PhosphorylationNTNSTPPSEDDDDND
CCCCCCCCCCCCCCC		55.66-
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
401SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCY1_YEAST !!
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 PCY1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMA1_YEASTSRP1physical
16554755
PLMT_YEASTOPI3genetic
16269340
RIC1_YEASTRIC1genetic
16269340
RGP1_YEASTRGP1genetic
16269340
PSD2_YEASTPSD2genetic
16269340
CHO2_YEASTCHO2genetic
16269340
LHS1_YEASTLHS1genetic
16269340
DGK1_YEASTDGK1genetic
16269340
ATF2_YEASTATF2genetic
16269340
MTC4_YEASTMTC4genetic
16269340
PGA3_YEASTPGA3genetic
16269340
HAC1_YEASTHAC1genetic
16269340
KRE9_YEASTKRE9physical
18467557
IMA1_YEASTSRP1physical
19141610
CHO2_YEASTCHO2genetic
17284612
GLO3_YEASTGLO3genetic
19325107
MGA2_YEASTMGA2genetic
19325107
YHN8_YEASTYHR078Wgenetic
19325107
RER1_YEASTRER1genetic
19325107
XPT1_YEASTXPT1genetic
21623372
QCR2_YEASTQCR2genetic
21623372
PHO84_YEASTPHO84genetic
21623372
ADH3_YEASTADH3genetic
21623372
TPS2_YEASTTPS2genetic
21623372
PAD1_YEASTPAD1genetic
22204397
GPT1_YEASTSCT1genetic
22323296
PLB1_YEASTPLB1genetic
23501167
ICE2_YEASTICE2genetic
23891562
DGK1_YEASTDGK1genetic
23891562
CND2_YEASTBRN1genetic
27708008
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
COPB2_YEASTSEC27genetic
27708008
BOS1_YEASTBOS1genetic
27708008
SEC65_YEASTSEC65genetic
27708008
GPI12_YEASTGPI12genetic
27708008
RIB2_YEASTRIB2genetic
27708008
RRS1_YEASTRRS1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
DIM1_YEASTDIM1genetic
27708008
SNT1_YEASTSNT1genetic
27708008
ABP1_YEASTABP1genetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
GPR1_YEASTGPR1genetic
27708008
LCMT1_YEASTPPM1genetic
27708008
SPS2_YEASTSPS2genetic
27708008
SAP1_YEASTSAP1genetic
27708008
FAR7_YEASTFAR7genetic
27708008
KEX1_YEASTKEX1genetic
27708008
YG1O_YEASTYGR035Cgenetic
27708008
RL11B_YEASTRPL11Bgenetic
27708008
RIR3_YEASTRNR3genetic
27708008
ICE2_YEASTICE2genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
DAN1_YEASTDAN1genetic
27708008
TRM2_YEASTTRM2genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
SYM1_YEASTSYM1genetic
27708008
OCA2_YEASTOCA2genetic
27708008
FAR11_YEASTFAR11genetic
27708008
ATX2_YEASTATX2genetic
27708008
KTR1_YEASTKTR1genetic
27708008
FABD_YEASTMCT1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
INO2_YEASTINO2genetic
29674565
LPP1_YEASTLPP1genetic
29674565
RSP5_YEASTRSP5genetic
29674565
CDC11_YEASTCDC11genetic
29674565
SSL1_YEASTSSL1genetic
29674565
TAD3_YEASTTAD3genetic
29674565
KAR3_YEASTKAR3genetic
29674565
ICE2_YEASTICE2genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCY1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-18; SER-19;THR-59 AND SER-346, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-18; SER-19 ANDTHR-59, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND MASSSPECTROMETRY.

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