YCR3_YEAST - dbPTM
YCR3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YCR3_YEAST
UniProt AC P25351
Protein Name Uncharacterized membrane protein YCR023C
Gene Name YCR023C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 611
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MARQKLTFKEQMDGFPWVQLVVVSLVRFSEPIAFSSLFPYVYFMVRDFNIAPNDAQVSKYSGYLSSSFALCQVISAYHWGRFSEKHGRKITLTCGLIGTSVSLLILGFSRNFYQALVARSLMGLLNGNVGVIRTIIGEIATERKHQALAFSTMPLLFQFGAVVGPMIGGFLVFRDGTMNEVPLWFPHFAKRIIRSYPYALPNVVVCMFLMFGLTNATLFLEETHPAFKDRRDYGLEVGDFIKKNIFGIQPKRRPWQKRIQDDSENIHHRNENVNSIRGQDSEEDENSPLVNTTNDDDTESIQSIDPILTRRQSVGLIRTYSLHEPTDAVHANIDTAPDGCKESSIFHHVFHTKVFYPISVNFIMALHLIVYNEFLPVFLAYDLAVDPENPKKLASKFPWKISGGIGYEPEQTGTLLSTTGIFGCFVVIFIFPIVDRNFDCLTIFRTLVKLYPIMYVMVPYVVFLQNERIPSWYTVVYLYIITGIKTFCGALTSPQIMLLIHNSSPLSCRSVINGATISISASARFIGPLVWGYIMSWSQQNDVAWVSWWSLSLFCMVALYQSYKIAPIDDNENELHGQGSEDAYNSQSQSSDLRMAHRSSLSSLSNQRCTT
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
275PhosphorylationHRNENVNSIRGQDSE
CCCCCHHHCCCCCCC		14.9123749301
298PhosphorylationNTTNDDDTESIQSID
CCCCCCCCHHHHHCC		38.3319795423
300PhosphorylationTNDDDTESIQSIDPI
CCCCCCHHHHHCCHH		28.2021440633
303PhosphorylationDDTESIQSIDPILTR
CCCHHHHHCCHHHHH		27.5621440633
309PhosphorylationQSIDPILTRRQSVGL
HHCCHHHHHCCCCCE		25.2419795423
313PhosphorylationPILTRRQSVGLIRTY
HHHHHCCCCCEEEEE		19.1517330950
319PhosphorylationQSVGLIRTYSLHEPT
CCCCEEEEEECCCCC		15.5228889911
320PhosphorylationSVGLIRTYSLHEPTD
CCCEEEEEECCCCCC		10.2117330950
321PhosphorylationVGLIRTYSLHEPTDA
CCEEEEEECCCCCCC		23.7228152593
326PhosphorylationTYSLHEPTDAVHANI
EEECCCCCCCCCCCC		33.3419779198
599PhosphorylationDLRMAHRSSLSSLSN
HHHHHHHHHHHHHHC		26.2622369663
600PhosphorylationLRMAHRSSLSSLSNQ
HHHHHHHHHHHHHCC		32.0222369663
602PhosphorylationMAHRSSLSSLSNQRC
HHHHHHHHHHHCCCC		31.0522369663
603PhosphorylationAHRSSLSSLSNQRCT
HHHHHHHHHHCCCCC		40.9022369663
605PhosphorylationRSSLSSLSNQRCTT-
HHHHHHHHCCCCCC-		32.6322369663
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 YCR3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YCR3_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 YCR3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSE4_YEASTNSE4genetic
27708008
RPN5_YEASTRPN5genetic
27708008
GLE1_YEASTGLE1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
SMT3_YEASTSMT3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
NDC80_YEASTNDC80genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
BET3_YEASTBET3genetic
27708008
BOS1_YEASTBOS1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
BET5_YEASTBET5genetic
27708008
MCM1_YEASTMCM1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
MED4_YEASTMED4genetic
27708008
APC5_YEASTAPC5genetic
27708008
GPN2_YEASTGPN2genetic
27708008
BUR1_YEASTSGV1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YCR3_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-275; SER-599 ANDSER-603, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASSSPECTROMETRY.
"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 SER-603, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-603, ANDMASS SPECTROMETRY.

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