YM87_YEAST - dbPTM
YM87_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YM87_YEAST
UniProt AC Q04835
Protein Name Uncharacterized membrane protein YMR253C
Gene Name YMR253C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 414
Subcellular Localization Membrane
Multi-pass membrane protein . Localizes to cytoplasmic punctate structures.
Protein Description
Protein Sequence MNPSVPKVMKRENNTHLLVSKEMNDTSLQLPSTTRSLSPKESNSNEDFNVDGNETTLQRISKDYLKPNIGLVLLTVSYFFNSAMVVSTKVLENDPDDIANDRQIKPLQILLVRMVITYIGTLIYMYINKSTISDVPFGKPEVRKWLVLRGCTGFFGVFGMYYSLMYLTISDAVLITFLAPSLTIFLSWVILRERFTKVEALGSLISLLGVVLIVRPSFLFGTPELTDSSSQIVESSDPKSRLIATLVGLWGVLGMSCVYIIIRYIGKRAHAIMSVSYFSLITAIVSFIGINTIPSMKFQIPHSKKQWILFGNLGVSGFIFQLLLTMGIQRERAGRGSLMTYTQLLYAVFWDVALYKHWPNIWSWIGMIIIISATLWVIRIRAANNETTAKDLTPIIDDEENSIPLTEFDLSDSK
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
4Phosphorylation----MNPSVPKVMKR
----CCCCCCCCCCC
46.1530377154
21UbiquitinationNTHLLVSKEMNDTSL
CCEEEEECCCCCCCC
54.2023749301
27PhosphorylationSKEMNDTSLQLPSTT
ECCCCCCCCCCCCCC
19.5827017623
36PhosphorylationQLPSTTRSLSPKESN
CCCCCCCCCCCCCCC
30.9823749301
38PhosphorylationPSTTRSLSPKESNSN
CCCCCCCCCCCCCCC
34.8620377248
40UbiquitinationTTRSLSPKESNSNED
CCCCCCCCCCCCCCC
71.1023749301
42PhosphorylationRSLSPKESNSNEDFN
CCCCCCCCCCCCCCC
52.2422369663
44PhosphorylationLSPKESNSNEDFNVD
CCCCCCCCCCCCCCC
51.3722369663
117PhosphorylationLLVRMVITYIGTLIY
HHHHHHHHHHHHHHH
9.5527017623
121PhosphorylationMVITYIGTLIYMYIN
HHHHHHHHHHHHHHC
10.6327017623
124PhosphorylationTYIGTLIYMYINKST
HHHHHHHHHHHCCCC
6.2327017623
393PhosphorylationETTAKDLTPIIDDEE
CCCCHHHCCCCCCCC
23.6821440633
402PhosphorylationIIDDEENSIPLTEFD
CCCCCCCCCCCCCCC
28.9427017623
411PhosphorylationPLTEFDLSDSK----
CCCCCCCCCCC----
41.5021440633
413PhosphorylationTEFDLSDSK------
CCCCCCCCC------
36.5728889911

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 YM87_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YM87_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 YM87_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GWT1_YEASTGWT1genetic
16269340
SHR3_YEASTSHR3genetic
16269340
PGA3_YEASTPGA3genetic
16269340
ENV10_YEASTENV10genetic
27708008
INO4_YEASTINO4genetic
27708008
ALG3_YEASTALG3genetic
27708008
THRC_YEASTTHR4genetic
27708008
SLX5_YEASTSLX5genetic
27708008
SLX8_YEASTSLX8genetic
27708008
FYV10_YEASTFYV10genetic
27708008
VPS53_YEASTVPS53genetic
27708008
EOS1_YEASTEOS1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
AXL1_YEASTAXL1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YM87_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-42 AND SER-44, 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-42, AND MASSSPECTROMETRY.

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