CYPC_YEAST - dbPTM
CYPC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYPC_YEAST
UniProt AC P25719
Protein Name Peptidyl-prolyl cis-trans isomerase C, mitochondrial
Gene Name CPR3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 182
Subcellular Localization Mitochondrion matrix .
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This isozyme is required for growth on lactate at high temperature..
Protein Sequence MFKRSIIQQSRLFSNSASRLGKKVFFDPAVNGTKIGRIEFELYDNVVPKTAENFRALCTGEKGWGYKGVPFHRIIPDFMIQGGDTDLTNGFGGKSIYGSKFADENFVKKHDKAGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVTKGMDIVKAIESYGTASGKPRAEIVIEEAGEL
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
14PhosphorylationIQQSRLFSNSASRLG
HHHHHCCCCCHHHHC		34.1722369663
16PhosphorylationQSRLFSNSASRLGKK
HHHCCCCCHHHHCCE		26.8222369663
18PhosphorylationRLFSNSASRLGKKVF
HCCCCCHHHHCCEEE		28.0522369663
34AcetylationDPAVNGTKIGRIEFE
ECCCCCCEEEEEEEE		44.5622865919
49AcetylationLYDNVVPKTAENFRA
ECCCCCCCCHHHHHH		49.0824489116
62AcetylationRALCTGEKGWGYKGV
HHHHCCCCCCCCCCC		62.4024489116
67AcetylationGEKGWGYKGVPFHRI
CCCCCCCCCCCHHHC		49.8724489116
94AcetylationLTNGFGGKSIYGSKF
CCCCCCCCCCCCCCC		33.7824489116
95PhosphorylationTNGFGGKSIYGSKFA
CCCCCCCCCCCCCCC		25.0727017623
99PhosphorylationGGKSIYGSKFADENF
CCCCCCCCCCCCHHH		13.9723749301
100UbiquitinationGKSIYGSKFADENFV
CCCCCCCCCCCHHHH		39.9624961812
100AcetylationGKSIYGSKFADENFV
CCCCCCCCCCCHHHH		39.9624489116
108SuccinylationFADENFVKKHDKAGL
CCCHHHHCCCCCCCC		40.0123954790
108AcetylationFADENFVKKHDKAGL
CCCHHHHCCCCCCCC		40.0124489116
117PhosphorylationHDKAGLLSMANAGPN
CCCCCCHHHHCCCCC		22.3817330950
125PhosphorylationMANAGPNTNGSQFFI
HHCCCCCCCCCCEEE		44.0527738172
133PhosphorylationNGSQFFITTVPCPWL
CCCCEEEEEECCCCC		19.3127738172
152AcetylationVVFGEVTKGMDIVKA
EEEEEECCCHHHHHH		58.3724489116
158AcetylationTKGMDIVKAIESYGT
CCCHHHHHHHHHHCC		43.9424489116
162PhosphorylationDIVKAIESYGTASGK
HHHHHHHHHCCCCCC		23.8122369663
163PhosphorylationIVKAIESYGTASGKP
HHHHHHHHCCCCCCC		13.0022369663
165PhosphorylationKAIESYGTASGKPRA
HHHHHHCCCCCCCCE		14.9322369663
167PhosphorylationIESYGTASGKPRAEI
HHHHCCCCCCCCEEE		47.3822369663
169AcetylationSYGTASGKPRAEIVI
HHCCCCCCCCEEEEE		28.9225381059
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 CYPC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYPC_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 CYPC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STE50_YEASTSTE50genetic
20093466
RV167_YEASTRVS167genetic
20093466
BST1_YEASTBST1genetic
20093466
ATG1_YEASTATG1genetic
20093466
FMC1_YEASTFMC1genetic
20093466
MGR3_YEASTMGR3genetic
20093466
RU2A_YEASTLEA1genetic
20093466
CYPC_YEASTCPR3physical
22940862
ATG1_YEASTATG1genetic
22282571
MOB1_YEASTMOB1genetic
27708008
STE50_YEASTSTE50genetic
27708008
RV161_YEASTRVS161genetic
27708008
ATG1_YEASTATG1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
RIM11_YEASTRIM11genetic
27708008
RU2A_YEASTLEA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYPC_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-99, AND MASSSPECTROMETRY.

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