RSF2_YEAST - dbPTM
RSF2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSF2_YEAST
UniProt AC P46974
Protein Name Respiration factor 2
Gene Name RSF2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1380
Subcellular Localization Nucleus .
Protein Description Transcription factor that regulates expression of both nuclear and mitochondrial genes, and more specifically those required for glycerol-based growth and respiration..
Protein Sequence MEPFAFGRGAPALCILTAAARINLDNFVPCCWALFRLSFFFPLDPAYIRNENKETRTSWISIEFFFFVKHCLSQHTFFSKTLAPKRNFRAKKLKDIGDTRIDRADKDFLLVPEPSMFVNGNQSNFAKPAGQGILPIPKKSRIIKTDKPRPFLCPTCTRGFVRQEHLKRHQHSHTREKPYLCIFCGRCFARRDLVLRHQQKLHAALVGTGDPRRMTPAPNSTSSFASKRRHSVAADDPTDLHIIKIAGNKETILPTPKNLAGKTSEELKEAVVALAKSNNVELPVSAPVMNDKREKTPPSKAGSLGFREFKFSTKGVPVHSASSDAVIDRANTPSSMHKTKRHASFSASSAMTYMSSSNSPHHSITNFELVEDAPHQVGFSTPQMTAKQLMESVSELDLPPLTLDEPPQAIKFNLNLFNNDPSGQQQQQQQQQQNSTSSTIVNSNNGSTVATPGVYLLSSGPSLTDLLTMNSAHAGAGGYMSSHHSPFDLGCFSHDKPTVSEFNLPSSFPNTIPSNSTTASNSYSNLANQTYRQMSNEQPLMSLSPKNPPTTVSDSSSTINFNPGTNNLLEPSMEPNDKDSNIDPAAIDDKWLSEFINNSDPKSTFKINFNHFNDIGFIYSPPSSRSSIPNKSPPNHSATSLNHEKASLSPRLNLSLNGSTDLPSTPQNQLKEPSYSDPISHSSHKRRRDSVMMDYDLSNFFSSRQLDISKVLNGTEQNNSHVNDDVLTLSFPGETDSNATQKQLPVLTPSDLLSPFSVPSVSQVLFTNELRSMMLADNNIDSGAFPTTSQLNDYVTYYKEEFHPFFSFIHLPSIIPNMDSYPLLLSISMVGALYGFHSTHAKVLANAASTQIRKSLKVSEKNPETTELWVIQTLVLLTFYCIFNKNTAVIKGMHGQLTTIIRLLKASRLNLPLESLCQPPIESDHIMEYENSPHMFSKIREQYNAPNQMNKNYQYFVLAQSRIRTCHAVLLISNLFSSLVGADCCFHSVDLKCGVPCYKEELYQCRNSDEWSDLLCQYKITLDSKFSLIELSNGNEAYENCLRFLSTGDSFFYGNARVSLSTCLSLLISIHEKILIERNNARISNNNTNSNNIELDDIEWKMTSRQRIDTMLKYWENLYLKNGGILTPTENSMSTINANPAMRLIIPVYLFAKMRRCLDLAHVIEKIWLKDWSNMNKALEEVCYDMGSLREATEYALNMVDAWTSFFTYIKQGKRRIFNTPVFATTCMFTAVLVISEYMKCVEDWARGYNANNPNSALLDFSDRVLWLKAERILRRLQMNLIPKECDVLKSYTDFLRWQDKDALDLSALNEEQAQRAMDPNTDINETIQLIVAASLSSKCLYLGVQILGDAPIWPIILSFAHGLQSRAIYSVTKKRNTRI
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
208PhosphorylationLHAALVGTGDPRRMT
HHHHHHCCCCCCCCC		30.8224961812
215PhosphorylationTGDPRRMTPAPNSTS
CCCCCCCCCCCCCCC		17.9419823750
220PhosphorylationRMTPAPNSTSSFASK
CCCCCCCCCCCHHHH		28.7119823750
221PhosphorylationMTPAPNSTSSFASKR
CCCCCCCCCCHHHHH		34.7224961812
222PhosphorylationTPAPNSTSSFASKRR
CCCCCCCCCHHHHHC		24.2324961812
223PhosphorylationPAPNSTSSFASKRRH
CCCCCCCCHHHHHCC		25.5619823750
226PhosphorylationNSTSSFASKRRHSVA
CCCCCHHHHHCCCCC		25.3724961812
227AcetylationSTSSFASKRRHSVAA
CCCCHHHHHCCCCCC		50.4525381059
231PhosphorylationFASKRRHSVAADDPT
HHHHHCCCCCCCCCC		16.1919795423
238PhosphorylationSVAADDPTDLHIIKI
CCCCCCCCCEEEEEE		59.1819823750
262AcetylationTPKNLAGKTSEELKE
CCCCCCCCCHHHHHH		43.1822865919
285PhosphorylationNNVELPVSAPVMNDK
CCCCCCCCCCCCCCC		25.5621440633
296PhosphorylationMNDKREKTPPSKAGS
CCCCCCCCCCCCCCC		35.3625752575
299PhosphorylationKREKTPPSKAGSLGF
CCCCCCCCCCCCCCC		36.0224961812
303PhosphorylationTPPSKAGSLGFREFK
CCCCCCCCCCCEEEE		30.1322369663
320PhosphorylationTKGVPVHSASSDAVI
CCCCCCCCCCCCHHH		30.0422369663
322PhosphorylationGVPVHSASSDAVIDR
CCCCCCCCCCHHHHC		31.5922369663
323PhosphorylationVPVHSASSDAVIDRA
CCCCCCCCCHHHHCC		29.3422369663
332PhosphorylationAVIDRANTPSSMHKT
HHHHCCCCCCHHCCC		24.4622369663
334PhosphorylationIDRANTPSSMHKTKR
HHCCCCCCHHCCCCC		37.9521440633
335PhosphorylationDRANTPSSMHKTKRH
HCCCCCCHHCCCCCC		26.5522369663
380PhosphorylationAPHQVGFSTPQMTAK
CCCCCCCCCCHHCHH		33.0028889911
381PhosphorylationPHQVGFSTPQMTAKQ
CCCCCCCCCHHCHHH		18.4528889911
392PhosphorylationTAKQLMESVSELDLP
CHHHHHHHHHHCCCC		19.5821551504
394PhosphorylationKQLMESVSELDLPPL
HHHHHHHHHCCCCCC		41.5427017623
535PhosphorylationNQTYRQMSNEQPLMS
HHHHHHHCCCCCCCC		28.9522369663
542PhosphorylationSNEQPLMSLSPKNPP
CCCCCCCCCCCCCCC		33.1222369663
544PhosphorylationEQPLMSLSPKNPPTT
CCCCCCCCCCCCCCC		26.9022369663
580PhosphorylationMEPNDKDSNIDPAAI
CCCCCCCCCCCHHHC		41.2321551504
632PhosphorylationRSSIPNKSPPNHSAT
CCCCCCCCCCCCCCC		52.8317287358
637PhosphorylationNKSPPNHSATSLNHE
CCCCCCCCCCCCCCC		39.6221551504
639PhosphorylationSPPNHSATSLNHEKA
CCCCCCCCCCCCCHH		36.4421551504
640PhosphorylationPPNHSATSLNHEKAS
CCCCCCCCCCCCHHC		27.2221551504
647PhosphorylationSLNHEKASLSPRLNL
CCCCCHHCCCCCCCE		40.2121440633
649PhosphorylationNHEKASLSPRLNLSL
CCCHHCCCCCCCEEE		12.8920377248
655PhosphorylationLSPRLNLSLNGSTDL
CCCCCCEEECCCCCC		20.7921126336
659PhosphorylationLNLSLNGSTDLPSTP
CCEEECCCCCCCCCC		20.0621126336
660PhosphorylationNLSLNGSTDLPSTPQ
CEEECCCCCCCCCCH		42.8425521595
664PhosphorylationNGSTDLPSTPQNQLK
CCCCCCCCCCHHHCC		61.0821440633
665PhosphorylationGSTDLPSTPQNQLKE
CCCCCCCCCHHHCCC		27.2721440633
674PhosphorylationQNQLKEPSYSDPISH
HHHCCCCCCCCCCCC		38.0619823750
675PhosphorylationNQLKEPSYSDPISHS
HHCCCCCCCCCCCCC		28.0119823750
676PhosphorylationQLKEPSYSDPISHSS
HCCCCCCCCCCCCCC		41.0521440633
680PhosphorylationPSYSDPISHSSHKRR
CCCCCCCCCCCCHHH		23.7821440633
682PhosphorylationYSDPISHSSHKRRRD
CCCCCCCCCCHHHHH		27.6121440633
683PhosphorylationSDPISHSSHKRRRDS
CCCCCCCCCHHHHHC		27.8321440633
690PhosphorylationSHKRRRDSVMMDYDL
CCHHHHHCCCCCCCH		15.3124961812
695PhosphorylationRDSVMMDYDLSNFFS
HHCCCCCCCHHHHCC		10.8219779198
698PhosphorylationVMMDYDLSNFFSSRQ
CCCCCCHHHHCCCCC		28.7919779198
772PhosphorylationLFTNELRSMMLADNN
HCCHHHHHHHCCCCC		22.5919779198
798PhosphorylationLNDYVTYYKEEFHPF
HHHHHHHHHHHCCCC		11.5319779198
929PhosphorylationESDHIMEYENSPHMF
CCCCCCCCCCCHHHH		11.7521440633
932PhosphorylationHIMEYENSPHMFSKI
CCCCCCCCHHHHHHH		12.3021440633
1134PhosphorylationTPTENSMSTINANPA
CCCCCCCCCCCCCHH		26.4227017623
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 RSF2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSF2_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 RSF2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOT6_YEASTDOT6genetic
20959818
IME1_YEASTIME1genetic
20959818
TDA9_YEASTTDA9genetic
20959818
SGF73_YEASTSGF73genetic
20959818
PHO23_YEASTPHO23genetic
20959818
BUB1_YEASTBUB1genetic
21127252
BCK1_YEASTBCK1genetic
21127252
RPN5_YEASTRPN5genetic
27708008
CDC1_YEASTCDC1genetic
27708008
RMRP_YEASTSNM1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
PRI2_YEASTPRI2genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ORC1_YEASTORC1genetic
27708008
RSC9_YEASTRSC9genetic
27708008
PROF_YEASTPFY1genetic
27708008
ARP7_YEASTARP7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSF2_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-320; SER-322; SER-380;THR-381; SER-542 AND SER-544, 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 SER-322, AND MASSSPECTROMETRY.
"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-632, AND MASSSPECTROMETRY.

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