CYPD_YEAST - dbPTM
CYPD_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYPD_YEAST
UniProt AC P35176
Protein Name Peptidyl-prolyl cis-trans isomerase D
Gene Name CPR5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 225
Subcellular Localization Endoplasmic reticulum lumen.
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides..
Protein Sequence MKLQFFSFITLFACLFTTAIFAKEDTAEDPEITHKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTISRDPKMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKSIFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIVESGELETVPLDNKDAAKLQEEIKAEASEAAHDEL
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
45AcetylationFDINHGDKQIGRIVM
EECCCCCHHHHHHEE
48.7024489116
67PhosphorylationPQTVENFYQLTISRD
HHHHHHHHHEEECCC
17.7528132839
76AcetylationLTISRDPKMGYLNSI
EEECCCCCCCCHHHH
49.6124489116
107AcetylationHRSGIGGKSIFGNTF
CCCCCCCCCCCCCCC
34.8524489116
115AcetylationSIFGNTFKDENFDVK
CCCCCCCCCCCCCCC
63.1924489116
139N-linked_GlycosylationANRGKNTNGSQFFIT
CCCCCCCCCCCEEEE
58.47-
218PhosphorylationEEIKAEASEAAHDEL
HHHHHHHHHHHHHCC
21.1917563356

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 CYPD_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYPD_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 CYPD_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YCT1_YEASTYCT1genetic
16269340
RTN1_YEASTRTN1genetic
16269340
PFD2_YEASTGIM4genetic
16269340
GET3_YEASTGET3physical
18719252
VATA_YEASTVMA1physical
22940862
VATB_YEASTVMA2physical
22940862
MOB2_YEASTMOB2genetic
27708008
MCM10_YEASTMCM10genetic
27708008
SC61A_YEASTSEC61genetic
27708008
YBF9_YEASTYBL059Wgenetic
27708008
SWC5_YEASTSWC5genetic
27708008
STE50_YEASTSTE50genetic
27708008
ACA2_YEASTCST6genetic
27708008
ELM1_YEASTELM1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
TSA1_YEASTTSA1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
PMA2_YEASTPMA2genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
ISU1_YEASTISU1genetic
27708008
SGTA_HUMANSGTAphysical
27107014
BAG6_HUMANBAG6physical
27107014
CSEN_HUMANKCNIP3physical
27107014
SGTB_HUMANSGTBphysical
27107014
UBQL1_HUMANUBQLN1physical
27107014
ASNA_HUMANASNA1physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYPD_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-218, AND MASSSPECTROMETRY.

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