YL257_YEAST - dbPTM
YL257_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YL257_YEAST
UniProt AC Q06146
Protein Name Uncharacterized protein YLR257W
Gene Name YLR257W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 321
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MVDARGSTPCLIGDSIRNVNDGNSLDFQYTNQFNEESEASRLLTPQTSSNHALSKMQKDDDIRDRSYTSVAELNREGALLTDEVDLENVDASKVRSNRDDLEAEEKRKKLLLLKKKQRNKSINSESFSSPSLRASKSNSLITSTDPVEDHISKYSSSGTPENITGEADDEDEDIIRNSYGQMIKNNSNRPHLAKGESYQSAEQEIDHTAPEKSEKRQERSGRSFDRQKSSAEFLRSLSRSISRGPTKNKTVSPSKGEDSRMYSTSNYSISLVDLENGPKIIPETLEEEQEDAEKEGVLMEDEGNEEYTKDLEEAANKAQPQ
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
2Acetylation------MVDARGSTP
------CCCCCCCCC		8.7315665377
7Phosphorylation-MVDARGSTPCLIGD
-CCCCCCCCCEEECC		24.5122369663
8PhosphorylationMVDARGSTPCLIGDS
CCCCCCCCCEEECCC		22.3522369663
15PhosphorylationTPCLIGDSIRNVNDG
CCEEECCCEECCCCC		20.4522890988
24PhosphorylationRNVNDGNSLDFQYTN
ECCCCCCCCCCEECC		34.5427017623
44PhosphorylationSEASRLLTPQTSSNH
HHHHHHCCCCCCHHH		20.2422369663
47PhosphorylationSRLLTPQTSSNHALS
HHHCCCCCCHHHHHH		35.0122369663
48PhosphorylationRLLTPQTSSNHALSK
HHCCCCCCHHHHHHH		24.7222369663
49PhosphorylationLLTPQTSSNHALSKM
HCCCCCCHHHHHHHH		35.7022369663
54PhosphorylationTSSNHALSKMQKDDD
CCHHHHHHHHCCCCC		27.1922369663
55AcetylationSSNHALSKMQKDDDI
CHHHHHHHHCCCCCC		46.3224489116
66PhosphorylationDDDIRDRSYTSVAEL
CCCCHHCCCCCHHHH		36.7322369663
67PhosphorylationDDIRDRSYTSVAELN
CCCHHCCCCCHHHHH		12.1522369663
68PhosphorylationDIRDRSYTSVAELNR
CCHHCCCCCHHHHHH		20.2622369663
69PhosphorylationIRDRSYTSVAELNRE
CHHCCCCCHHHHHHC		15.8822369663
81PhosphorylationNREGALLTDEVDLEN
HHCCCCCCCEECHHC		30.8522369663
92PhosphorylationDLENVDASKVRSNRD
CHHCCCHHHHHCCHH		27.5022369663
93AcetylationLENVDASKVRSNRDD
HHCCCHHHHHCCHHH		43.3124489116
96PhosphorylationVDASKVRSNRDDLEA
CCHHHHHCCHHHHHH		38.9224961812
106AcetylationDDLEAEEKRKKLLLL
HHHHHHHHHHHHHHH		62.1124489116
120AcetylationLKKKQRNKSINSESF
HHHHHHCCCCCCCCC		55.7024489116
121PhosphorylationKKKQRNKSINSESFS
HHHHHCCCCCCCCCC		30.4722369663
124PhosphorylationQRNKSINSESFSSPS
HHCCCCCCCCCCCHH		32.7122369663
126PhosphorylationNKSINSESFSSPSLR
CCCCCCCCCCCHHHH		30.1922369663
128PhosphorylationSINSESFSSPSLRAS
CCCCCCCCCHHHHHH		51.0922369663
129PhosphorylationINSESFSSPSLRASK
CCCCCCCCHHHHHHC		19.2522369663
131PhosphorylationSESFSSPSLRASKSN
CCCCCCHHHHHHCCC		32.2222369663
135PhosphorylationSSPSLRASKSNSLIT
CCHHHHHHCCCCCCC		30.1322369663
137PhosphorylationPSLRASKSNSLITST
HHHHHHCCCCCCCCC		29.2022369663
139PhosphorylationLRASKSNSLITSTDP
HHHHCCCCCCCCCCC		28.3922369663
142PhosphorylationSKSNSLITSTDPVED
HCCCCCCCCCCCHHH		30.7622890988
143PhosphorylationKSNSLITSTDPVEDH
CCCCCCCCCCCHHHH		24.6622890988
144PhosphorylationSNSLITSTDPVEDHI
CCCCCCCCCCHHHHH		35.3522890988
152PhosphorylationDPVEDHISKYSSSGT
CCHHHHHHHCCCCCC		23.3222890988
153AcetylationPVEDHISKYSSSGTP
CHHHHHHHCCCCCCC		48.8524489116
154PhosphorylationVEDHISKYSSSGTPE
HHHHHHHCCCCCCCC		13.6420377248
155PhosphorylationEDHISKYSSSGTPEN
HHHHHHCCCCCCCCC		23.0522369663
156PhosphorylationDHISKYSSSGTPENI
HHHHHCCCCCCCCCC		29.6922369663
157PhosphorylationHISKYSSSGTPENIT
HHHHCCCCCCCCCCC		40.5222369663
159PhosphorylationSKYSSSGTPENITGE
HHCCCCCCCCCCCCC		29.4022369663
164PhosphorylationSGTPENITGEADDED
CCCCCCCCCCCCCCC		40.3222369663
178PhosphorylationDEDIIRNSYGQMIKN
CCHHHHHHHHHHHHC		22.3122369663
184AcetylationNSYGQMIKNNSNRPH
HHHHHHHHCCCCCCC		44.7425381059
187PhosphorylationGQMIKNNSNRPHLAK
HHHHHCCCCCCCCCC		43.5421440633
194UbiquitinationSNRPHLAKGESYQSA
CCCCCCCCCCCHHHH		70.3522817900
197PhosphorylationPHLAKGESYQSAEQE
CCCCCCCCHHHHHHH		36.8222369663
198PhosphorylationHLAKGESYQSAEQEI
CCCCCCCHHHHHHHC		11.3722369663
200PhosphorylationAKGESYQSAEQEIDH
CCCCCHHHHHHHCCC		26.0722369663
208PhosphorylationAEQEIDHTAPEKSEK
HHHHCCCCCCHHHHH		39.9122890988
212AcetylationIDHTAPEKSEKRQER
CCCCCCHHHHHHHHH		63.9624489116
213PhosphorylationDHTAPEKSEKRQERS
CCCCCHHHHHHHHHH		46.8426447709
215AcetylationTAPEKSEKRQERSGR
CCCHHHHHHHHHHCC		67.4824489116
220PhosphorylationSEKRQERSGRSFDRQ
HHHHHHHHCCCCHHH		37.4917287358
223PhosphorylationRQERSGRSFDRQKSS
HHHHHCCCCHHHHHH		34.7217287358
229PhosphorylationRSFDRQKSSAEFLRS
CCCHHHHHHHHHHHH		26.8324909858
230PhosphorylationSFDRQKSSAEFLRSL
CCHHHHHHHHHHHHH		38.5622369663
236PhosphorylationSSAEFLRSLSRSISR
HHHHHHHHHHHHHHC		32.6122890988
238PhosphorylationAEFLRSLSRSISRGP
HHHHHHHHHHHHCCC		25.8122369663
240PhosphorylationFLRSLSRSISRGPTK
HHHHHHHHHHCCCCC		22.8822369663
242PhosphorylationRSLSRSISRGPTKNK
HHHHHHHHCCCCCCC		32.2222369663
246PhosphorylationRSISRGPTKNKTVSP
HHHHCCCCCCCCCCC		50.5022890988
250PhosphorylationRGPTKNKTVSPSKGE
CCCCCCCCCCCCCCC		35.2925005228
252PhosphorylationPTKNKTVSPSKGEDS
CCCCCCCCCCCCCCC		28.7821082442
254PhosphorylationKNKTVSPSKGEDSRM
CCCCCCCCCCCCCCC		45.8729136822
259PhosphorylationSPSKGEDSRMYSTSN
CCCCCCCCCCEEECC		18.0419823750
262PhosphorylationKGEDSRMYSTSNYSI
CCCCCCCEEECCEEE		14.0022369663
263PhosphorylationGEDSRMYSTSNYSIS
CCCCCCEEECCEEEE		18.9322369663
264PhosphorylationEDSRMYSTSNYSISL
CCCCCEEECCEEEEE		11.9622369663
265PhosphorylationDSRMYSTSNYSISLV
CCCCEEECCEEEEEE		28.0322369663
267PhosphorylationRMYSTSNYSISLVDL
CCEEECCEEEEEEEC		13.7222369663
268PhosphorylationMYSTSNYSISLVDLE
CEEECCEEEEEEECC		15.2222369663
270PhosphorylationSTSNYSISLVDLENG
EECCEEEEEEECCCC		19.1922369663
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 YL257_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YL257_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 YL257_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YL345_YEASTYLR345Wphysical
18467557
YL345_YEASTYLR345Wphysical
18719252
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YL257_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-7; THR-8; THR-44;SER-48; SER-66; TYR-67; THR-68; SER-69; SER-121; SER-126; SER-128;SER-129; SER-135; SER-137; SER-139; TYR-154; THR-159; SER-197;SER-200; SER-238; SER-240; SER-252; SER-268 AND SER-270, 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-49; SER-66; THR-68;SER-69; SER-121; SER-137; SER-139; SER-197; SER-200; SER-230; SER-236;SER-240; SER-242 AND SER-252, AND MASS SPECTROMETRY.
"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-220; SER-223; SER-238;SER-240 AND SER-242, 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 THR-44; SER-121 AND SER-129,AND MASS SPECTROMETRY.

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