YB085_YEAST - dbPTM
YB085_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YB085_YEAST
UniProt AC O43137
Protein Name Uncharacterized protein YBR085C-A
Gene Name YBR085C-A
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 85
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MSSALYKQSTNFTHSTGSFLQSAPVELTTVSGYQEFLKKQEKKNYEIQTVLSEDKSHGYVLKDGEVIANIIGEAKDYLLDLAGQA
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
9PhosphorylationSSALYKQSTNFTHST
CCHHCCCCCCCCCCC
22.5922369663
10PhosphorylationSALYKQSTNFTHSTG
CHHCCCCCCCCCCCC
31.6822369663
13PhosphorylationYKQSTNFTHSTGSFL
CCCCCCCCCCCCCCH
19.5822369663
15PhosphorylationQSTNFTHSTGSFLQS
CCCCCCCCCCCCHHC
31.2622369663
16PhosphorylationSTNFTHSTGSFLQSA
CCCCCCCCCCCHHCC
29.2822369663
18PhosphorylationNFTHSTGSFLQSAPV
CCCCCCCCCHHCCCE
23.9122369663
22PhosphorylationSTGSFLQSAPVELTT
CCCCCHHCCCEEEEE
36.3722369663
28PhosphorylationQSAPVELTTVSGYQE
HCCCEEEEECHHHHH
16.2022369663
29PhosphorylationSAPVELTTVSGYQEF
CCCEEEEECHHHHHH
25.8722369663
31PhosphorylationPVELTTVSGYQEFLK
CEEEEECHHHHHHHH
29.6822369663
33PhosphorylationELTTVSGYQEFLKKQ
EEEECHHHHHHHHHH
9.4322369663
45PhosphorylationKKQEKKNYEIQTVLS
HHHHHCCCEEEEEEE
24.2423749301
49PhosphorylationKKNYEIQTVLSEDKS
HCCCEEEEEEECCCC
29.1323749301
52PhosphorylationYEIQTVLSEDKSHGY
CEEEEEEECCCCCCE
39.1422369663
55UbiquitinationQTVLSEDKSHGYVLK
EEEEECCCCCCEEEC
40.0624961812
56PhosphorylationTVLSEDKSHGYVLKD
EEEECCCCCCEEECC
34.1723749301

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 YB085_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YB085_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 YB085_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC20_YEASTCDC20genetic
27708008
SLI15_YEASTSLI15genetic
27708008
CDK1_YEASTCDC28genetic
27708008
MAK21_YEASTMAK21genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CCA1_YEASTCCA1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
FIP1_YEASTFIP1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
PSB5_YEASTPRE2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YB085_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-15; THR-16 AND SER-18,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 THR-10; THR-13; SER-15 ANDSER-18, AND MASS SPECTROMETRY.
"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 THR-10, AND MASSSPECTROMETRY.

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