CMS1_YEAST - dbPTM
CMS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMS1_YEAST
UniProt AC Q07897
Protein Name Protein CMS1
Gene Name CMS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 291
Subcellular Localization Nucleus .
Protein Description May play a role in the regulation of DNA replication and cell cycle control..
Protein Sequence MSNPDDLDDGLAYDFDAEHEVIFDAKDGSPPTKKVQKRSIEQDDDDVDDIDGKKEERNSEDDSNRPISKRQKKLQKKSKLIEKKKEESQYIVSQRKALPASSPEKIIEYLTTLIREKNPDLSVLELEELYFKRNDFLSTEKFDAERRLSNFPAFIQKFSVAPKKIVFSMSNIRVADVYRSLNGGKNCVKLFSKSKLKDDIATVERLLTDSSKKSNKNKDSLYFIATPTRMQKIIEATDLLFQGKEKLDIILDASYLDPKDNTILSFENAAVLCQVLKTFLNKKSSVKILLY
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
2Phosphorylation------MSNPDDLDD
------CCCHHHCCC
58.0028152593
29PhosphorylationIFDAKDGSPPTKKVQ
EEECCCCCCCCHHHH
37.5325752575
39PhosphorylationTKKVQKRSIEQDDDD
CHHHHCCCCCCCCCC
37.2017563356
53AcetylationDVDDIDGKKEERNSE
CCCCCCCCCHHCCCC
53.9524489116
54AcetylationVDDIDGKKEERNSED
CCCCCCCCHHCCCCC
71.0424489116
59PhosphorylationGKKEERNSEDDSNRP
CCCHHCCCCCCCCCC
48.9319823750
63PhosphorylationERNSEDDSNRPISKR
HCCCCCCCCCCCHHH
47.2419795423
68PhosphorylationDDSNRPISKRQKKLQ
CCCCCCCHHHHHHHH
25.1927214570
69AcetylationDSNRPISKRQKKLQK
CCCCCCHHHHHHHHH
60.6125381059
88PhosphorylationIEKKKEESQYIVSQR
HHHHHHHHHHHHHHH
29.4030377154
93PhosphorylationEESQYIVSQRKALPA
HHHHHHHHHHCCCCC
18.0827017623
141AcetylationNDFLSTEKFDAERRL
CCCCCCCCCCHHHHH
48.9424489116
157AcetylationNFPAFIQKFSVAPKK
CCHHHHHHHCCCCCE
34.4924489116
168PhosphorylationAPKKIVFSMSNIRVA
CCCEEEEEECCCCHH
15.4827017623
170PhosphorylationKKIVFSMSNIRVADV
CEEEEEECCCCHHHH
28.1027017623
178PhosphorylationNIRVADVYRSLNGGK
CCCHHHHHHHHCCCC
8.6027017623
195AcetylationVKLFSKSKLKDDIAT
HHHHCCCCCHHHHHH
64.3924489116
197AcetylationLFSKSKLKDDIATVE
HHCCCCCHHHHHHHH
58.0324489116
216AcetylationDSSKKSNKNKDSLYF
CCCCCCCCCCCCEEE
72.9024489116
218AcetylationSKKSNKNKDSLYFIA
CCCCCCCCCCEEEEE
50.7524489116
218SuccinylationSKKSNKNKDSLYFIA
CCCCCCCCCCEEEEE
50.7523954790
232AcetylationATPTRMQKIIEATDL
ECHHHHHHHHHHHHH
35.9924489116
244AcetylationTDLLFQGKEKLDIIL
HHHHHCCHHHCCEEE
40.6724489116

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 CMS1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMS1_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 CMS1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CMS1_YEAST !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CMS1_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-59, AND MASSSPECTROMETRY.
"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-39 AND SER-59, 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-59, AND MASSSPECTROMETRY.

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