RS4A_YEAST - dbPTM
RS4A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS4A_YEAST
UniProt AC P0CX35
Protein Name 40S ribosomal protein S4-A {ECO:0000303|PubMed:9559554}
Gene Name RPS4A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 261
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel..
Protein Sequence MARGPKKHLKRLAAPHHWLLDKLSGCYAPRPSAGPHKLRESLPLIVFLRNRLKYALNGREVKAILMQRHVKVDGKVRTDTTYPAGFMDVITLDATNENFRLVYDVKGRFAVHRITDEEASYKLGKVKKVQLGKKGVPYVVTHDGRTIRYPDPNIKVNDTVKIDLASGKITDFIKFDAGKLVYVTGGRNLGRIGTIVHKERHDGGFDLVHIKDSLDNTFVTRLNNVFVIGEQGKPYISLPKGKGIKLSIAEERDRRRAQQGL
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
22UbiquitinationPHHWLLDKLSGCYAP
CHHHHHHHHCCCCCC		44.51-
22AcetylationPHHWLLDKLSGCYAP
CHHHHHHHHCCCCCC		44.5124489116
32PhosphorylationGCYAPRPSAGPHKLR
CCCCCCCCCCCCCHH		47.3317330950
37AcetylationRPSAGPHKLRESLPL
CCCCCCCCHHHHCCE		52.9924489116
37UbiquitinationRPSAGPHKLRESLPL
CCCCCCCCHHHHCCE		52.99-
41PhosphorylationGPHKLRESLPLIVFL
CCCCHHHHCCEEHHH		28.9321440633
53UbiquitinationVFLRNRLKYALNGRE
HHHHHHHHHHHCCHH		25.82-
53AcetylationVFLRNRLKYALNGRE
HHHHHHHHHHHCCHH		25.8224489116
62UbiquitinationALNGREVKAILMQRH
HHCCHHHHHEEEECE		25.5922106047
62AcetylationALNGREVKAILMQRH
HHCCHHHHHEEEECE		25.5924489116
62SuccinylationALNGREVKAILMQRH
HHCCHHHHHEEEECE		25.5923954790
71SuccinylationILMQRHVKVDGKVRT
EEEECEEEECCEECC		28.6023954790
82PhosphorylationKVRTDTTYPAGFMDV
EECCCCCCCCCEEEE		7.9927017623
95PhosphorylationDVITLDATNENFRLV
EEEEEECCCCCEEEE		42.6127017623
106SuccinylationFRLVYDVKGRFAVHR
EEEEEEECCCEEEEE		41.2823954790
106UbiquitinationFRLVYDVKGRFAVHR
EEEEEEECCCEEEEE		41.28-
106AcetylationFRLVYDVKGRFAVHR
EEEEEEECCCEEEEE		41.2824489116
115PhosphorylationRFAVHRITDEEASYK
CEEEEECCCHHHHHH		37.0017287358
120PhosphorylationRITDEEASYKLGKVK
ECCCHHHHHHCCCEE		26.5317287358
122SuccinylationTDEEASYKLGKVKKV
CCHHHHHHCCCEEEE		48.5523954790
122UbiquitinationTDEEASYKLGKVKKV
CCHHHHHHCCCEEEE		48.55-
122AcetylationTDEEASYKLGKVKKV
CCHHHHHHCCCEEEE		48.5524489116
134UbiquitinationKKVQLGKKGVPYVVT
EEEECCCCCCCEEEE		64.4422106047
155UbiquitinationRYPDPNIKVNDTVKI
ECCCCCCCCCCEEEE		41.44-
155AcetylationRYPDPNIKVNDTVKI
ECCCCCCCCCCEEEE		41.4424489116
161AcetylationIKVNDTVKIDLASGK
CCCCCEEEEECCCCC		32.3724489116
161UbiquitinationIKVNDTVKIDLASGK
CCCCCEEEEECCCCC		32.3722106047
161SuccinylationIKVNDTVKIDLASGK
CCCCCEEEEECCCCC		32.3723954790
166PhosphorylationTVKIDLASGKITDFI
EEEEECCCCCCCEEE		48.1719779198
168SuccinylationKIDLASGKITDFIKF
EEECCCCCCCEEEEE		39.6823954790
168UbiquitinationKIDLASGKITDFIKF
EEECCCCCCCEEEEE		39.6822106047
168AcetylationKIDLASGKITDFIKF
EEECCCCCCCEEEEE		39.6824489116
170PhosphorylationDLASGKITDFIKFDA
ECCCCCCCEEEEECC		28.4821440633
174UbiquitinationGKITDFIKFDAGKLV
CCCCEEEEECCCCEE		36.8722106047
174AcetylationGKITDFIKFDAGKLV
CCCCEEEEECCCCEE		36.8724489116
174SuccinylationGKITDFIKFDAGKLV
CCCCEEEEECCCCEE		36.8723954790
179UbiquitinationFIKFDAGKLVYVTGG
EEEECCCCEEEEECC		36.1822106047
179AcetylationFIKFDAGKLVYVTGG
EEEECCCCEEEEECC		36.1824489116
179SuccinylationFIKFDAGKLVYVTGG
EEEECCCCEEEEECC		36.1823954790
184PhosphorylationAGKLVYVTGGRNLGR
CCCEEEEECCCCCEE		19.0724961812
194PhosphorylationRNLGRIGTIVHKERH
CCCEEEEEEEEECCC		19.9122369663
198SuccinylationRIGTIVHKERHDGGF
EEEEEEEECCCCCCE		45.6223954790
198UbiquitinationRIGTIVHKERHDGGF
EEEEEEEECCCCCCE		45.62-
198AcetylationRIGTIVHKERHDGGF
EEEEEEEECCCCCCE		45.6224489116
211AcetylationGFDLVHIKDSLDNTF
CEEEEEEECCCCCCE		26.7924489116
211UbiquitinationGFDLVHIKDSLDNTF
CEEEEEEECCCCCCE		26.7922106047
213PhosphorylationDLVHIKDSLDNTFVT
EEEEEECCCCCCEEE		32.4023749301
233SuccinylationFVIGEQGKPYISLPK
EEECCCCCEEEECCC		34.0523954790
233UbiquitinationFVIGEQGKPYISLPK
EEECCCCCEEEECCC		34.0522106047
233AcetylationFVIGEQGKPYISLPK
EEECCCCCEEEECCC		34.0524489116
235PhosphorylationIGEQGKPYISLPKGK
ECCCCCEEEECCCCC		13.4621440633
237PhosphorylationEQGKPYISLPKGKGI
CCCCEEEECCCCCCC		32.5421440633
240SuccinylationKPYISLPKGKGIKLS
CEEEECCCCCCCCCE		77.7823954790
240AcetylationKPYISLPKGKGIKLS
CEEEECCCCCCCCCE		77.7824489116
240UbiquitinationKPYISLPKGKGIKLS
CEEEECCCCCCCCCE		77.78-
245UbiquitinationLPKGKGIKLSIAEER
CCCCCCCCCEEEHHH		44.87-
245AcetylationLPKGKGIKLSIAEER
CCCCCCCCCEEEHHH		44.8724489116
247PhosphorylationKGKGIKLSIAEERDR
CCCCCCCEEEHHHHH		18.1022369663
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 RS4A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS4A_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 RS4A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS8_YEASTRPT6physical
20494970
SRO9_YEASTSRO9physical
20494970
COG3_YEASTCOG3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
BRL1_YEASTBRL1genetic
27708008
KRE9_YEASTKRE9genetic
27708008
CDC24_YEASTCDC24genetic
27708008
CDC27_YEASTCDC27genetic
27708008
APC11_YEASTAPC11genetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPN5_YEASTRPN5genetic
27708008
CDC1_YEASTCDC1genetic
27708008
ACT_YEASTACT1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRP43_YEASTPRP43genetic
27708008
RU1C_YEASTYHC1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
PSB5_YEASTPRE2genetic
27708008
ELP1_YEASTIKI3genetic
27708008
MSC1_YEASTMSC1genetic
27708008
MAC1_YEASTMAC1genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
YP078_YEASTYPR078Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS4A_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-247, 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 THR-115; SER-120 ANDSER-247, 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 SER-32, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168, AND MASSSPECTROMETRY.

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