RDS2_YEAST - dbPTM
RDS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RDS2_YEAST
UniProt AC P19541
Protein Name Regulator of drug sensitivity 2
Gene Name RDS2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 446
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Transcription factor which regulates the expression of genes for gluconeogenesis, the TCA cycle, and glucose metabolism. Involved in the cell wall remodeling process and drug resistance..
Protein Sequence MSANSGVKRASKAFKTCLFCKRSHVVCDKQRPCSRCVKRDIAHLCREDDIAVPNEMPSQHESSPNDNNIQGKYANKAHTGIPSDYQNEPVNKSGSTYGEELSPKLDSSLVNDTTSLLLPQQPVFVSENVGSEFSSLNEFLSMLENPLLTQTSLSSSSASNVHLENGSQTTQSPLEYQNDNRRDEIGVARQENRSPTIMSGSSNSISKGDKQDQEKEESRILANANENSAPTPKEQFFLTAADPSTEMTPEHRLKLVINAKLEAGLLKPYNYAKGYARLQDYMDKYMNQSSKQRILKPLSTIRPAFRTIARSLKDVDLVLVEESFERMLLSYDRVFTSMSMPACLCRRTGEIYRANKEFASLVDCTVDDLRDGKLAIYELMTEESAVNFWEKYGSIAFDKGQKAVLTSCSLRTKDGIRKRPCCFSFTIRRDRYNIPICIVGNFIPLS
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
63PhosphorylationMPSQHESSPNDNNIQ
CCCCCCCCCCCCCCC		25.4128889911
102PhosphorylationSTYGEELSPKLDSSL
CCCCCCCCHHCCHHH		24.2222369663
194PhosphorylationVARQENRSPTIMSGS
HHCCCCCCCCCCCCC		37.6722369663
196PhosphorylationRQENRSPTIMSGSSN
CCCCCCCCCCCCCCC		30.4722369663
199PhosphorylationNRSPTIMSGSSNSIS
CCCCCCCCCCCCCCC		31.5022369663
201PhosphorylationSPTIMSGSSNSISKG
CCCCCCCCCCCCCCC		21.0222369663
202PhosphorylationPTIMSGSSNSISKGD
CCCCCCCCCCCCCCC		37.8122369663
204PhosphorylationIMSGSSNSISKGDKQ
CCCCCCCCCCCCCHH		30.1322369663
206PhosphorylationSGSSNSISKGDKQDQ
CCCCCCCCCCCHHHH		30.3322369663
228PhosphorylationLANANENSAPTPKEQ
HHHCCCCCCCCCHHH		29.4622369663
231PhosphorylationANENSAPTPKEQFFL
CCCCCCCCCHHHCEE		46.8622369663
248PhosphorylationADPSTEMTPEHRLKL
CCCCCCCCHHHHHHH		21.2023749301
331PhosphorylationFERMLLSYDRVFTSM
HHHHHHCCCCHHCCC		14.0328889911
381PhosphorylationLAIYELMTEESAVNF
EEEEECCCHHHHHHH		49.5827017623
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 RDS2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RDS2_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 RDS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBX1_YEASTSHP1physical
16554755
SNF1_YEASTSNF1physical
17875938
ENV11_YEASTENV11genetic
20959818
UBP6_YEASTUBP6genetic
20959818
SODC_YEASTSOD1genetic
20959818
DOA1_YEASTDOA1genetic
20959818
CAT8_YEASTCAT8genetic
22687600
TOR1_YEASTTOR1genetic
25887987
KEL1_YEASTKEL1genetic
25887987
TYSY_YEASTCDC21genetic
27708008
MAK16_YEASTMAK16genetic
27708008
APC11_YEASTAPC11genetic
27708008
FAL1_YEASTFAL1genetic
27708008
TAF12_YEASTTAF12genetic
27708008
RRP41_YEASTSKI6genetic
27708008
CWC16_YEASTYJU2genetic
27708008
NOP56_YEASTNOP56genetic
27708008
TAD3_YEASTTAD3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RDS2_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-102 AND THR-231, ANDMASS SPECTROMETRY.

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