CYPH_YEAST - dbPTM
CYPH_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYPH_YEAST
UniProt AC P14832
Protein Name Peptidyl-prolyl cis-trans isomerase
Gene Name CPR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 162
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion intermembrane space .
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function..
Protein Sequence MSQVYFDVEADGQPIGRVVFKLYNDIVPKTAENFRALCTGEKGFGYAGSPFHRVIPDFMLQGGDFTAGNGTGGKSIYGGKFPDENFKKHHDRPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVVDGYDIVKKVESLGSPSGATKARIVVAKSGEL
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
2Acetylation------MSQVYFDVE
------CCEEEEEEE		28.492687115
2Phosphorylation------MSQVYFDVE
------CCEEEEEEE		28.4924909858
5Phosphorylation---MSQVYFDVEADG
---CCEEEEEEEECC		6.0924909858
21UbiquitinationPIGRVVFKLYNDIVP
EEHHHHHHHHCCCCH		38.1523749301
21SuccinylationPIGRVVFKLYNDIVP
EEHHHHHHHHCCCCH		38.1523954790
21AcetylationPIGRVVFKLYNDIVP
EEHHHHHHHHCCCCH		38.1524489116
23PhosphorylationGRVVFKLYNDIVPKT
HHHHHHHHCCCCHHH		16.0428889911
29UbiquitinationLYNDIVPKTAENFRA
HHCCCCHHHHHHHHH		49.8523749301
29AcetylationLYNDIVPKTAENFRA
HHCCCCHHHHHHHHH		49.8524489116
29SuccinylationLYNDIVPKTAENFRA
HHCCCCHHHHHHHHH		49.8523954790
39PhosphorylationENFRALCTGEKGFGY
HHHHHHHCCCCCCCC		49.5821082442
42UbiquitinationRALCTGEKGFGYAGS
HHHHCCCCCCCCCCC		61.9723749301
42AcetylationRALCTGEKGFGYAGS
HHHHCCCCCCCCCCC		61.9724489116
46PhosphorylationTGEKGFGYAGSPFHR
CCCCCCCCCCCCCCC		12.9121440633
49PhosphorylationKGFGYAGSPFHRVIP
CCCCCCCCCCCCCCC		19.0721440633
66PhosphorylationMLQGGDFTAGNGTGG
EEECCCCCCCCCCCC		38.0921440633
71PhosphorylationDFTAGNGTGGKSIYG
CCCCCCCCCCCCCCC		46.9228889911
74AcetylationAGNGTGGKSIYGGKF
CCCCCCCCCCCCCCC		34.7224489116
74UbiquitinationAGNGTGGKSIYGGKF
CCCCCCCCCCCCCCC		34.7223749301
75PhosphorylationGNGTGGKSIYGGKFP
CCCCCCCCCCCCCCC		25.0721440633
80UbiquitinationGKSIYGGKFPDENFK
CCCCCCCCCCCCCHH		49.7323749301
80AcetylationGKSIYGGKFPDENFK
CCCCCCCCCCCCCHH		49.7324489116
80SuccinylationGKSIYGGKFPDENFK
CCCCCCCCCCCCCHH		49.7323954790
87UbiquitinationKFPDENFKKHHDRPG
CCCCCCHHHHCCCCC		63.8823749301
87AcetylationKFPDENFKKHHDRPG
CCCCCCHHHHCCCCC		63.8824489116
87SuccinylationKFPDENFKKHHDRPG
CCCCCCHHHHCCCCC		63.8823954790
88UbiquitinationFPDENFKKHHDRPGL
CCCCCHHHHCCCCCC		41.8722817900
117GlutathionylationFFITTVPCPWLDGKH
EEEEEECCCCCCCCC		3.0822833525
123UbiquitinationPCPWLDGKHVVFGEV
CCCCCCCCCEEEEEE		32.6622106047
138AcetylationVDGYDIVKKVESLGS
ECCHHHHHHHHHCCC		51.9724489116
138UbiquitinationVDGYDIVKKVESLGS
ECCHHHHHHHHHCCC		51.9722817900
138SuccinylationVDGYDIVKKVESLGS
ECCHHHHHHHHHCCC		51.9723954790
139UbiquitinationDGYDIVKKVESLGSP
CCHHHHHHHHHCCCC		40.1023749301
139AcetylationDGYDIVKKVESLGSP
CCHHHHHHHHHCCCC		40.1022865919
142PhosphorylationDIVKKVESLGSPSGA
HHHHHHHHCCCCCCC		40.8122369663
145PhosphorylationKKVESLGSPSGATKA
HHHHHCCCCCCCCEE		22.6125521595
147PhosphorylationVESLGSPSGATKARI
HHHCCCCCCCCEEEE		42.6422369663
150PhosphorylationLGSPSGATKARIVVA
CCCCCCCCEEEEEEE		28.8522890988
151UbiquitinationGSPSGATKARIVVAK
CCCCCCCEEEEEEEE		34.8223749301
151AcetylationGSPSGATKARIVVAK
CCCCCCCEEEEEEEE		34.8222865919
151SuccinylationGSPSGATKARIVVAK
CCCCCCCEEEEEEEE		34.8223954790
158UbiquitinationKARIVVAKSGEL---
EEEEEEEECCCC---		47.5923749301
159PhosphorylationARIVVAKSGEL----
EEEEEEECCCC----		27.9721440633
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 CYPH_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYPH_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 CYPH_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_YEASTRVB2physical
11805826
SIF2_YEASTSIF2physical
11805826
SNF2_YEASTSNF2physical
11805826
SNT1_YEASTSNT1physical
11805826
HOS4_YEASTHOS4physical
11805826
SAP30_YEASTSAP30physical
10899127
RPD3_YEASTRPD3physical
10899127
SET3_YEASTSET3physical
15643056
HOS2_YEASTHOS2physical
15643056
SNT1_YEASTSNT1physical
15643056
SIF2_YEASTSIF2physical
15643056
ZPR1_YEASTZPR1genetic
12242280
IME1_YEASTIME1genetic
15643056
IME2_YEASTIME2genetic
15643056
SNT1_YEASTSNT1genetic
15643056
SIF2_YEASTSIF2genetic
15643056
HOS4_YEASTHOS4genetic
15643056
SET3_YEASTSET3genetic
15643056
HOS2_YEASTHOS2genetic
15643056
CALM_YEASTCMD1physical
16554755
HOS4_YEASTHOS4physical
16429126
SIF2_YEASTSIF2physical
16429126
SNF2_YEASTSNF2physical
16429126
SNT1_YEASTSNT1physical
16429126
DPB4_YEASTDPB4genetic
17314980
SRS2_YEASTSRS2genetic
21459050
CYPH_YEASTCPR1physical
22940862
SDS3_YEASTSDS3genetic
27708008
ATC3_YEASTDRS2genetic
27708008
HAP3_YEASTHAP3genetic
27708008
SHE1_YEASTSHE1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
CYK3_YEASTCYK3genetic
27708008
BCS1_YEASTBCS1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
MNT2_YEASTMNT2genetic
27708008
PFD3_YEASTPAC10genetic
27708008
NPR3_YEASTNPR3genetic
27708008
HTD2_YEASTHTD2genetic
27708008
PTH_YEASTPTH1genetic
27708008
HPM1_YEASTHPM1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
RPE_YEASTRPE1genetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
YJ24_YEASTKCH1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
ILM1_YEASTILM1genetic
27708008
VPS13_YEASTVPS13genetic
27708008
ENV10_YEASTENV10genetic
27708008
POC1_YEASTPBA1genetic
27708008
GBLP_YEASTASC1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
HDA1_YEASTHDA1genetic
27708008
EFM6_YEASTYNL024Cgenetic
27708008
FKBP_YEASTFPR1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
TLG2_YEASTTLG2genetic
27708008
HPF1_YEASTHPF1genetic
27708008
BUD21_YEASTBUD21genetic
27708008
DIA2_YEASTDIA2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
KIN4_YEASTKIN4genetic
27708008
VPH1_YEASTVPH1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
COX10_YEASTCOX10genetic
27708008
BRR1_YEASTBRR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYPH_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Purification and properties of multiple molecular forms of yeastpeptidyl prolyl cis-trans isomerase.";
Hasumi H., Nishikawa T.;
Biochim. Biophys. Acta 1161:161-167(1993).
Cited for: CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
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 THR-71; SER-142 AND SER-145,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-145, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASSSPECTROMETRY.
"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-145, AND MASSSPECTROMETRY.

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