RS3A2_YEAST - dbPTM
RS3A2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS3A2_YEAST
UniProt AC P23248
Protein Name 40S ribosomal protein S1-B {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:9559554}
Gene Name RPS1B {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 255
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 MAVGKNKRLSRGKKGLKKKVVDPFTRKEWFDIKAPSTFENRNVGKTLVNKSTGLKNASDALKGRVVEVCLADLQGSEDHSFRKVKLRVDEVQGKNLLTNFHGMDFTTDKLRSMVRKWQTLIEANVTVKTSDDYVLRIFAIAFTRKQANQVKRHSYAQSSHIRAIRKVISEILTREVQNSTLAQLTSKLIPEVINKEIENATKDIFPLQNIHVRKVKLLKQPKFDVGALMALHGEGSGEEKGKKVSGFKDEVLETV
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------MAVGKNKRL
------CCCCCCCCC		20.83-
7Acetylation-MAVGKNKRLSRGKK
-CCCCCCCCCCCCCC		59.1925381059
13UbiquitinationNKRLSRGKKGLKKKV
CCCCCCCCCCCCCCC		42.4222817900
14UbiquitinationKRLSRGKKGLKKKVV
CCCCCCCCCCCCCCC		72.7622817900
17UbiquitinationSRGKKGLKKKVVDPF
CCCCCCCCCCCCCCC		60.2522817900
18UbiquitinationRGKKGLKKKVVDPFT
CCCCCCCCCCCCCCC		56.7122817900
19UbiquitinationGKKGLKKKVVDPFTR
CCCCCCCCCCCCCCC		46.0023749301
19AcetylationGKKGLKKKVVDPFTR
CCCCCCCCCCCCCCC		46.0022865919
25PhosphorylationKKVVDPFTRKEWFDI
CCCCCCCCCHHHCCC		46.3421440633
27UbiquitinationVVDPFTRKEWFDIKA
CCCCCCCHHHCCCCC		57.1323749301
272-HydroxyisobutyrylationVVDPFTRKEWFDIKA
CCCCCCCHHHCCCCC		57.13-
27AcetylationVVDPFTRKEWFDIKA
CCCCCCCHHHCCCCC		57.1324489116
33SuccinylationRKEWFDIKAPSTFEN
CHHHCCCCCCCCCCC		56.9723954790
33UbiquitinationRKEWFDIKAPSTFEN
CHHHCCCCCCCCCCC		56.9723749301
33AcetylationRKEWFDIKAPSTFEN
CHHHCCCCCCCCCCC		56.9724489116
36PhosphorylationWFDIKAPSTFENRNV
HCCCCCCCCCCCCCC		51.0620377248
37PhosphorylationFDIKAPSTFENRNVG
CCCCCCCCCCCCCCC		33.6325521595
45AcetylationFENRNVGKTLVNKST
CCCCCCCHHEEECCC		34.1122865919
45UbiquitinationFENRNVGKTLVNKST
CCCCCCCHHEEECCC		34.1123749301
45SuccinylationFENRNVGKTLVNKST
CCCCCCCHHEEECCC		34.1123954790
46PhosphorylationENRNVGKTLVNKSTG
CCCCCCHHEEECCCC		29.9723749301
50AcetylationVGKTLVNKSTGLKNA
CCHHEEECCCCCCCH		41.7524489116
50UbiquitinationVGKTLVNKSTGLKNA
CCHHEEECCCCCCCH		41.7523749301
502-HydroxyisobutyrylationVGKTLVNKSTGLKNA
CCHHEEECCCCCCCH		41.75-
51PhosphorylationGKTLVNKSTGLKNAS
CHHEEECCCCCCCHH		23.6221440633
52PhosphorylationKTLVNKSTGLKNASD
HHEEECCCCCCCHHH		48.4121440633
55AcetylationVNKSTGLKNASDALK
EECCCCCCCHHHHHC		52.3822865919
552-HydroxyisobutyrylationVNKSTGLKNASDALK
EECCCCCCCHHHHHC		52.38-
55UbiquitinationVNKSTGLKNASDALK
EECCCCCCCHHHHHC		52.3823749301
58PhosphorylationSTGLKNASDALKGRV
CCCCCCHHHHHCCCE		32.5823749301
622-HydroxyisobutyrylationKNASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.52-
62AcetylationKNASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5222865919
62SuccinylationKNASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5223954790
62UbiquitinationKNASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5223749301
76PhosphorylationCLADLQGSEDHSFRK
EHHHHCCCCCCCEEE		27.2217287358
80PhosphorylationLQGSEDHSFRKVKLR
HCCCCCCCEEEEEEE		38.7817330950
83UbiquitinationSEDHSFRKVKLRVDE
CCCCCEEEEEEEEEE		41.5317644757
85UbiquitinationDHSFRKVKLRVDEVQ
CCCEEEEEEEEEECC		33.3417644757
94AcetylationRVDEVQGKNLLTNFH
EEEECCCCCCHHCCC		27.6024489116
94UbiquitinationRVDEVQGKNLLTNFH
EEEECCCCCCHHCCC		27.6023749301
109AcetylationGMDFTTDKLRSMVRK
CCCCCHHHHHHHHHH		43.6524489116
109UbiquitinationGMDFTTDKLRSMVRK
CCCCCHHHHHHHHHH		43.6523749301
112PhosphorylationFTTDKLRSMVRKWQT
CCHHHHHHHHHHHHH		31.8717287358
116UbiquitinationKLRSMVRKWQTLIEA
HHHHHHHHHHHHHHC		32.0417644757
128UbiquitinationIEANVTVKTSDDYVL
HHCCCEEECCCHHHH		32.7117644757
143PhosphorylationRIFAIAFTRKQANQV
HHHHHEECHHHHHHH		28.1217287358
145UbiquitinationFAIAFTRKQANQVKR
HHHEECHHHHHHHHC		51.1817644757
151UbiquitinationRKQANQVKRHSYAQS
HHHHHHHHCHHHHHH		34.3315699485
1512-HydroxyisobutyrylationRKQANQVKRHSYAQS
HHHHHHHHCHHHHHH		34.33-
154PhosphorylationANQVKRHSYAQSSHI
HHHHHCHHHHHHHHH		26.6217287358
158PhosphorylationKRHSYAQSSHIRAIR
HCHHHHHHHHHHHHH		18.7321440633
159PhosphorylationRHSYAQSSHIRAIRK
CHHHHHHHHHHHHHH		15.7417287358
166UbiquitinationSHIRAIRKVISEILT
HHHHHHHHHHHHHHH		37.4917644757
169PhosphorylationRAIRKVISEILTREV
HHHHHHHHHHHHHHH		22.9029136822
173PhosphorylationKVISEILTREVQNST
HHHHHHHHHHHHCCH		30.3721440633
179PhosphorylationLTREVQNSTLAQLTS
HHHHHHCCHHHHHHH		14.0128889911
186PhosphorylationSTLAQLTSKLIPEVI
CHHHHHHHHHHHHHH		33.7728889911
187SuccinylationTLAQLTSKLIPEVIN
HHHHHHHHHHHHHHH		45.2423954790
187AcetylationTLAQLTSKLIPEVIN
HHHHHHHHHHHHHHH		45.2424489116
187UbiquitinationTLAQLTSKLIPEVIN
HHHHHHHHHHHHHHH		45.2417644757
195AcetylationLIPEVINKEIENATK
HHHHHHHHHHHHHCC		49.2824489116
195SuccinylationLIPEVINKEIENATK
HHHHHHHHHHHHHCC		49.2823954790
195UbiquitinationLIPEVINKEIENATK
HHHHHHHHHHHHHCC		49.2824961812
202AcetylationKEIENATKDIFPLQN
HHHHHHCCCCCCCCC		46.5524489116
202SuccinylationKEIENATKDIFPLQN
HHHHHHCCCCCCCCC		46.5523954790
202UbiquitinationKEIENATKDIFPLQN
HHHHHHCCCCCCCCC		46.5523749301
214UbiquitinationLQNIHVRKVKLLKQP
CCCCEEEEEEECCCC		42.5017644757
216UbiquitinationNIHVRKVKLLKQPKF
CCEEEEEEECCCCCC		51.6517644757
2192-HydroxyisobutyrylationVRKVKLLKQPKFDVG
EEEEEECCCCCCCHH		75.01-
222AcetylationVKLLKQPKFDVGALM
EEECCCCCCCHHHHH		52.2624489116
222UbiquitinationVKLLKQPKFDVGALM
EEECCCCCCCHHHHH		52.2617644757
236PhosphorylationMALHGEGSGEEKGKK
HHHCCCCCCCCCCCC		38.4322369663
240AcetylationGEGSGEEKGKKVSGF
CCCCCCCCCCCCCCC		72.2624489116
240UbiquitinationGEGSGEEKGKKVSGF
CCCCCCCCCCCCCCC		72.2623749301
242UbiquitinationGSGEEKGKKVSGFKD
CCCCCCCCCCCCCCH		62.1622817900
242AcetylationGSGEEKGKKVSGFKD
CCCCCCCCCCCCCCH		62.1624489116
243UbiquitinationSGEEKGKKVSGFKDE
CCCCCCCCCCCCCHH		50.7523749301
245PhosphorylationEEKGKKVSGFKDEVL
CCCCCCCCCCCHHHH		47.6022369663
248AcetylationGKKVSGFKDEVLETV
CCCCCCCCHHHHHCC		57.4124489116
248UbiquitinationGKKVSGFKDEVLETV
CCCCCCCCHHHHHCC		57.4123749301
248SuccinylationGKKVSGFKDEVLETV
CCCCCCCCHHHHHCC		57.4123954790
254PhosphorylationFKDEVLETV------
CCHHHHHCC------		27.6222369663
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 RS3A2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS3A2_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 RS3A2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUD31_YEASTBUD31genetic
20093466
HMO1_YEASTHMO1genetic
20093466
MNN10_YEASTMNN10genetic
20093466
RKM4_YEASTRKM4genetic
20093466
SHE9_YEASTSHE9genetic
20093466
BEM2_YEASTBEM2genetic
20093466
SIC1_YEASTSIC1genetic
20093466
FKS1_YEASTFKS1genetic
20093466
RS3A1_YEASTRPS1Agenetic
20093466
SWS2_YEASTSWS2genetic
20093466
SUN4_YEASTSUN4genetic
20093466
DOM34_YEASTDOM34genetic
20093466
HSP7F_YEASTSSE1genetic
20093466
SUR1_YEASTSUR1genetic
20093466
SYT1_YEASTSYT1genetic
20093466
SRS2_YEASTSRS2genetic
21459050
BUD31_YEASTBUD31genetic
27708008
MBA1_YEASTMBA1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
UBP6_YEASTUBP6genetic
27708008
STB5_YEASTSTB5genetic
27708008
AIM18_YEASTAIM18genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
NGL2_YEASTNGL2genetic
27708008
DOM34_YEASTDOM34genetic
27708008
CY1_YEASTCYT1genetic
27708008
MNE1_YEASTMNE1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
SYT1_YEASTSYT1genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS3A2_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-245 AND THR-254, ANDMASS 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-245, 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-80; SER-154 AND SER-159,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-245 AND THR-254, ANDMASS SPECTROMETRY.
"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-76, AND MASSSPECTROMETRY.

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