BUD22_YEAST - dbPTM
BUD22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD22_YEAST
UniProt AC Q04347
Protein Name Bud site selection protein 22
Gene Name BUD22
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 519
Subcellular Localization Nucleus .
Protein Description Involved in positioning the proximal bud pole signal..
Protein Sequence MPSESSVSIYKLDQLEYQYHYLTKSLQKFEPRYPKTAKLYNCIGKKNKKKIEKLLNSLELKTLDKELDESYSKLLNNKIHYYETHLSKCIKEQIQKISKKNSSKVKDAQKNKSPSIDIEKMLATQLSLDDLALFMTRFRLIKILHQRIKQKSKKIEGDTNNKTWLNNNDYSGYINDKTSKWNPSNIWNEVITKLPSCEKLNALIGQSKIVQNLTESFDLSICLIFGFDVSAMKAKKYGAREKTANANQTHSNIDYDTDDGNEKNAIDSKSNAIGAQTQSNKETTSDNEDLLIKEYEGMLGSSGDEGEGGGYLNPNINYNEVTDEEPSEASSDEDDSDERFSDSEENEPRRKKPKLHNLPELMAGYYSGNDTEEESDEDNKNVKGKKKKRDTAEDRTAREQMSNEPKRKNRRGQRARRKIWEKKYGSQAKHVQRELEKEMEDRKQRQIEYEARVAKREAKAASLEASRSREREDRRTETNNKKEKESASTGEEHPSWIAKRLAEEKLQKAKFEGKKIKFD
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
5Phosphorylation---MPSESSVSIYKL
---CCCCCCCEEEEH		40.1430377154
28AcetylationYLTKSLQKFEPRYPK
HHHHHHHHCCCCCCC		57.9222865919
53AcetylationKNKKKIEKLLNSLEL
CCHHHHHHHHHHHHH		62.8424489116
57PhosphorylationKIEKLLNSLELKTLD
HHHHHHHHHHHHHHC		24.1630377154
78AcetylationYSKLLNNKIHYYETH
HHHHHHCHHHHHHHH		29.7722865919
113PhosphorylationKDAQKNKSPSIDIEK
HHHHHCCCCCCCHHH		33.0229136822
115PhosphorylationAQKNKSPSIDIEKML
HHHCCCCCCCHHHHH		39.7327017623
124PhosphorylationDIEKMLATQLSLDDL
CHHHHHHHHCCHHHH		26.5327017623
237PhosphorylationSAMKAKKYGAREKTA
HHHHHHHHCCCHHCC		18.4721551504
243PhosphorylationKYGAREKTANANQTH
HHCCCHHCCCCCCCC		22.0128889911
249PhosphorylationKTANANQTHSNIDYD
HCCCCCCCCCCCCCC		27.3822890988
251PhosphorylationANANQTHSNIDYDTD
CCCCCCCCCCCCCCC		38.5822890988
255PhosphorylationQTHSNIDYDTDDGNE
CCCCCCCCCCCCCCC		19.5625521595
257PhosphorylationHSNIDYDTDDGNEKN
CCCCCCCCCCCCCCC		29.7522369663
270PhosphorylationKNAIDSKSNAIGAQT
CCHHHHHCCHHCCCC		35.1322369663
277PhosphorylationSNAIGAQTQSNKETT
CCHHCCCCCCCCCCC		33.1722369663
279PhosphorylationAIGAQTQSNKETTSD
HHCCCCCCCCCCCCC		53.9422369663
283PhosphorylationQTQSNKETTSDNEDL
CCCCCCCCCCCCHHH		32.9622890988
284PhosphorylationTQSNKETTSDNEDLL
CCCCCCCCCCCHHHH		34.8625521595
285PhosphorylationQSNKETTSDNEDLLI
CCCCCCCCCCHHHHH		45.9522369663
341PhosphorylationDDSDERFSDSEENEP
CCCCCCCCCCCCCCC		46.5829688323
343PhosphorylationSDERFSDSEENEPRR
CCCCCCCCCCCCCCC		45.6829688323
365PhosphorylationLPELMAGYYSGNDTE
CHHHHHCCCCCCCCC		5.7323749301
366PhosphorylationPELMAGYYSGNDTEE
HHHHHCCCCCCCCCC		14.8021440633
367PhosphorylationELMAGYYSGNDTEEE
HHHHCCCCCCCCCCC		23.7217330950
371PhosphorylationGYYSGNDTEEESDED
CCCCCCCCCCCCCCC		49.6617330950
375PhosphorylationGNDTEEESDEDNKNV
CCCCCCCCCCCCCCC		49.9717330950
396PhosphorylationRDTAEDRTAREQMSN
CCCHHHHHHHHHHCC		42.2523607784
402PhosphorylationRTAREQMSNEPKRKN
HHHHHHHCCCHHHHC		37.4223607784
423AcetylationRRKIWEKKYGSQAKH
HHHHHHHHHHHHHHH		43.2425381059
429AcetylationKKYGSQAKHVQRELE
HHHHHHHHHHHHHHH		36.3525381059
462PhosphorylationKREAKAASLEASRSR
HHHHHHHHHHHHHHH		31.4427214570
468PhosphorylationASLEASRSREREDRR
HHHHHHHHHHHHHHH		35.6823749301
488PhosphorylationKKEKESASTGEEHPS
HHHHHHHCCCCCCHH		46.3428889911
489PhosphorylationKEKESASTGEEHPSW
HHHHHHCCCCCCHHH		48.6121440633
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 BUD22_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD22_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 BUD22_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBRL_YEASTNOP1physical
16554755
YRA1_YEASTYRA1physical
16554755
SNU13_YEASTSNU13physical
16554755
EFG1P_YEASTEFG1physical
16554755
SSB1_YEASTSSB1physical
19536198
SRS2_YEASTSRS2genetic
21459050
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD22_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 TYR-255; THR-257 ANDSER-285, 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-257 AND SER-285, ANDMASS 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-257; SER-367; THR-371AND SER-375, 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 THR-257, AND MASSSPECTROMETRY.

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