BUD2_YEAST - dbPTM
BUD2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD2_YEAST
UniProt AC P33314
Protein Name Inhibitory regulator protein BUD2/CLA2
Gene Name BUD2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1104
Subcellular Localization
Protein Description Stimulates the GTPase activity of BUD1/RSR1. Participates in the regulation of bud-site selection..
Protein Sequence MSSNNEPAQSRTSYFKLNEFLSNVKHYKNTFKGEIQWCNNLSLNDWKTHYLQITSTGALTHSIDELTADSTNIQPIIKHLQQCRIEIIKDKHSSFKDINANCNFIIQVNTSGKDNKVYLRVKSWSDFKKLLTCLIWWSSMKTNGIFNKFQVSRPLEFKSKKMAKPESLLVYKLNVFGPIVKNIVLPPATNILESPDIINNDDNSVGWFSAMGVLKSNGMLDLLLQSDGSLIYSLNISQLLRSEIRILDSSVLQSENSLFLGELPLLRSQLGLEKFRIENIASAATNSSDISQEIIVEFPLRIDLEDCFIALQSFARSEYLSITGSDKSNDMKISNSFKISILEANFQSINLNDKNNTPWSIFTDITAWGHTWARTSMVSNSSNPFWREEFQFNELLRLTNSYLEIKQLFHDLNNKKRLRLIGKIKITQEIINDTRYNKETRLPIMDVDNKNFQIGTICIKISSNLNFILPSTNFVKLEKLLMNANLSMVSNLIYKSSSSMENDNKLTQTSIIFLDIFQSLSRIEEWFHVLIDKELAKIDGTVSRINQKNLDSKHVFNSLFRGNSILTKSIEQYFFRVGNEYLSKALSAILKEIIESNKSCELDPARVKEKDEVKKRKIIADNYKRLYSWVTKIWKRLYATSNDLPIEIRNVLKIFRQKLEIICIDDTLQIILNGISGLLFLRFFCPVILNPKLFKYVSQNLNETARRNLTLISKVLLNLSTLTQFANKEPWLMKMNNFIDKRHNDLLDYIDKMTQKKLDFNSKILNLSSTISRPKLAIEQTMLDDLPQIPYLLDKNLRETEFVNLIVNFSQEDMTKMEKYNHMDNGGKGELIEEEGLLSGSSLNLSVDKKDLDSPIEVKPEIGELEFEKITENNTEIFGDDLMNLLKSDDVGSRSRDLDNGANSGIKFNSIIPKAEEEKHAMKELEQESCLLYNRINHIRKRLSGYECASSTLFEDKKYSISLSHKIFYEEIKEGKEIVLKLLNKPTNENSSARLQKFFTKGVSSKSNNTVGDSYCKFLTIDVSDENPKSSNKTSVHGTSSENGAKDDYLTLPNSQGKGNLGNRFSPTKLSRIMRKPPNADVPKEQNSRKLTRWFKKKKETGGS
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------MSSNNEPAQ
------CCCCCCCCC		53.7522814378
497PhosphorylationSNLIYKSSSSMENDN
HHHHHHCCCCCCCCC		23.4527017623
498PhosphorylationNLIYKSSSSMENDNK
HHHHHCCCCCCCCCC		40.5727017623
587PhosphorylationEYLSKALSAILKEII
HHHHHHHHHHHHHHH		20.3723607784
839PhosphorylationIEEEGLLSGSSLNLS
EEECCCCCCCEEEEE		41.4922369663
841PhosphorylationEEGLLSGSSLNLSVD
ECCCCCCCEEEEECC		28.4222369663
842PhosphorylationEGLLSGSSLNLSVDK
CCCCCCCEEEEECCH		25.4622369663
846PhosphorylationSGSSLNLSVDKKDLD
CCCEEEEECCHHHCC		27.4822369663
854PhosphorylationVDKKDLDSPIEVKPE
CCHHHCCCCCEECCC		34.7722369663
888PhosphorylationDLMNLLKSDDVGSRS
HHHHHHCCCCCCCCC		38.7319823750
893PhosphorylationLKSDDVGSRSRDLDN
HCCCCCCCCCCCCCC		27.2521551504
895PhosphorylationSDDVGSRSRDLDNGA
CCCCCCCCCCCCCCC		31.6619823750
904PhosphorylationDLDNGANSGIKFNSI
CCCCCCCCCCCHHHC		41.1623749301
959PhosphorylationTLFEDKKYSISLSHK
CCCCCCCEEEEEEHH		19.5828889911
964PhosphorylationKKYSISLSHKIFYEE
CCEEEEEEHHHHHHH		18.8828889911
991PhosphorylationNKPTNENSSARLQKF
CCCCCCCHHHHHHHH		21.1323749301
992PhosphorylationKPTNENSSARLQKFF
CCCCCCHHHHHHHHH		29.0521440633
1055PhosphorylationDYLTLPNSQGKGNLG
CEEECCCCCCCCCCC		38.0727214570
1066PhosphorylationGNLGNRFSPTKLSRI
CCCCCCCCHHHHHHH		28.5521440633
1068PhosphorylationLGNRFSPTKLSRIMR
CCCCCCHHHHHHHHC		43.3419823750
1071PhosphorylationRFSPTKLSRIMRKPP
CCCHHHHHHHHCCCC		22.7128889911
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 BUD2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD2_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 BUD2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSR1_YEASTRSR1physical
8371782
CG12_YEASTCLN2physical
11489916
SWI6_YEASTSWI6physical
16554755
BUD6_YEASTBUD6genetic
22558355
ARF3_YEASTARF3physical
23783029
RSR1_YEASTRSR1genetic
23783029
BUD5_YEASTBUD5genetic
23783029
RSR1_YEASTRSR1physical
23783029
SWC4_YEASTSWC4genetic
27708008
SMD1_YEASTSMD1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
FIP1_YEASTFIP1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TYSY_YEASTCDC21genetic
27708008
SWI4_YEASTSWI4genetic
27708008
BEM2_YEASTBEM2genetic
27708008
WDR6_YEASTRTT10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD2_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-854, 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-854, AND MASSSPECTROMETRY.
"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-854, AND MASSSPECTROMETRY.

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