RS3A1_YEAST - dbPTM
RS3A1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS3A1_YEAST
UniProt AC P33442
Protein Name 40S ribosomal protein S1-A {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:9559554}
Gene Name RPS1A {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 MAVGKNKRLSKGKKGQKKRVVDPFTRKEWFDIKAPSTFENRNVGKTLVNKSTGLKSASDALKGRVVEVCLADLQGSEDHSFRKIKLRVDEVQGKNLLTNFHGMDFTTDKLRSMVRKWQTLIEANVTVKTSDDYVLRIFAIAFTRKQANQVKRHSYAQSSHIRAIRKVISEILTKEVQGSTLAQLTSKLIPEVINKEIENATKDIFPLQNIHVRKVKLLKQPKFDVGALMALHGEGSGEEKGKKVTGFKDEVLETV
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		20.8310601260
7Acetylation-MAVGKNKRLSKGKK
-CCCCCCCCCCCCCC		59.1925381059
18UbiquitinationKGKKGQKKRVVDPFT
CCCCCCCCCCCCCCC		42.4017644757
25PhosphorylationKRVVDPFTRKEWFDI
CCCCCCCCCHHHCCC		46.3421440633
27UbiquitinationVVDPFTRKEWFDIKA
CCCCCCCHHHCCCCC		57.1323749301
33UbiquitinationRKEWFDIKAPSTFEN
CHHHCCCCCCCCCCC		56.9723749301
36PhosphorylationWFDIKAPSTFENRNV
HCCCCCCCCCCCCCC		51.0620377248
37PhosphorylationFDIKAPSTFENRNVG
CCCCCCCCCCCCCCC		33.6325521595
45UbiquitinationFENRNVGKTLVNKST
CCCCCCCCCEEECCC		34.1123749301
46PhosphorylationENRNVGKTLVNKSTG
CCCCCCCCEEECCCC		29.9723749301
50UbiquitinationVGKTLVNKSTGLKSA
CCCCEEECCCCCCCH		41.7523749301
51PhosphorylationGKTLVNKSTGLKSAS
CCCEEECCCCCCCHH		23.6221440633
52PhosphorylationKTLVNKSTGLKSASD
CCEEECCCCCCCHHH		48.4121440633
55AcetylationVNKSTGLKSASDALK
EECCCCCCCHHHHHC		45.3722865919
55UbiquitinationVNKSTGLKSASDALK
EECCCCCCCHHHHHC		45.3723749301
56PhosphorylationNKSTGLKSASDALKG
ECCCCCCCHHHHHCC		37.7417330950
58PhosphorylationSTGLKSASDALKGRV
CCCCCCHHHHHCCCE		30.4323749301
62UbiquitinationKSASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5223749301
62SuccinylationKSASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5223954790
62AcetylationKSASDALKGRVVEVC
CCHHHHHCCCEEEEE		46.5224489116
76PhosphorylationCLADLQGSEDHSFRK
EHHHHCCCCCCCCEE		27.2217330950
80PhosphorylationLQGSEDHSFRKIKLR
HCCCCCCCCEEEEEE		38.7817330950
83UbiquitinationSEDHSFRKIKLRVDE
CCCCCCEEEEEEEEE		42.0317644757
85UbiquitinationDHSFRKIKLRVDEVQ
CCCCEEEEEEEEECC		33.0217644757
94UbiquitinationRVDEVQGKNLLTNFH
EEEECCCCCCHHCCC		27.6023749301
109UbiquitinationGMDFTTDKLRSMVRK
CCCCCHHHHHHHHHH		43.6523749301
112PhosphorylationFTTDKLRSMVRKWQT
CCHHHHHHHHHHHHH		31.8717287358
116UbiquitinationKLRSMVRKWQTLIEA
HHHHHHHHHHHHHHC		32.0417644757
128UbiquitinationIEANVTVKTSDDYVL
HHCCCEEECCCHHHH		32.7117644757
143PhosphorylationRIFAIAFTRKQANQV
HHHEHEECHHHHHHH		28.1217287358
145UbiquitinationFAIAFTRKQANQVKR
HEHEECHHHHHHHHC		51.1817644757
151UbiquitinationRKQANQVKRHSYAQS
HHHHHHHHCHHHHHH		34.3315699485
154PhosphorylationANQVKRHSYAQSSHI
HHHHHCHHHHHHHHH		26.6217287358
158PhosphorylationKRHSYAQSSHIRAIR
HCHHHHHHHHHHHHH		18.7321440633
159PhosphorylationRHSYAQSSHIRAIRK
CHHHHHHHHHHHHHH		15.7417287358
166UbiquitinationSHIRAIRKVISEILT
HHHHHHHHHHHHHHH		37.4917644757
169PhosphorylationRAIRKVISEILTKEV
HHHHHHHHHHHHHHC		22.9029136822
174UbiquitinationVISEILTKEVQGSTL
HHHHHHHHHCCCCHH		53.0623749301
174SuccinylationVISEILTKEVQGSTL
HHHHHHHHHCCCCHH		53.0623954790
174AcetylationVISEILTKEVQGSTL
HHHHHHHHHCCCCHH		53.0624489116
186PhosphorylationSTLAQLTSKLIPEVI
CHHHHHHHHHHHHHH		33.7719779198
187UbiquitinationTLAQLTSKLIPEVIN
HHHHHHHHHHHHHHH		45.2424961812
195UbiquitinationLIPEVINKEIENATK
HHHHHHHHHHHHHCC		49.2824961812
202UbiquitinationKEIENATKDIFPLQN
HHHHHHCCCCCCCCC		46.5523749301
214UbiquitinationLQNIHVRKVKLLKQP
CCCCEEEEEEECCCC		42.5017644757
216UbiquitinationNIHVRKVKLLKQPKF
CCEEEEEEECCCCCC		51.6517644757
222UbiquitinationVKLLKQPKFDVGALM
EEECCCCCCCHHHHH		52.2617644757
236PhosphorylationMALHGEGSGEEKGKK
HHHCCCCCCCCCCCE		38.4322369663
240UbiquitinationGEGSGEEKGKKVTGF
CCCCCCCCCCEECCC		72.2623749301
242UbiquitinationGSGEEKGKKVTGFKD
CCCCCCCCEECCCCH		55.9522817900
243UbiquitinationSGEEKGKKVTGFKDE
CCCCCCCEECCCCHH		54.4124961812
245PhosphorylationEEKGKKVTGFKDEVL
CCCCCEECCCCHHHH		45.8622369663
248SuccinylationGKKVTGFKDEVLETV
CCEECCCCHHHHHCC		55.0823954790
248AcetylationGKKVTGFKDEVLETV
CCEECCCCHHHHHCC		55.0824489116
248UbiquitinationGKKVTGFKDEVLETV
CCEECCCCHHHHHCC		55.0823749301
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 RS3A1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS3A1_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 RS3A1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS3A2_YEASTRPS1Bgenetic
22377630
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
RRP8_YEASTRRP8genetic
27708008
RS23A_YEASTRPS23Agenetic
27708008
RS23B_YEASTRPS23Agenetic
27708008
MET5_YEASTMET5genetic
27708008
PSB6_YEASTPRE7genetic
27708008
CDC27_YEASTCDC27genetic
27708008
MCM7_YEASTMCM7genetic
27708008
APC11_YEASTAPC11genetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPN5_YEASTRPN5genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
PSB3_YEASTPUP3genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC12_YEASTCDC12genetic
27708008
CTF8_YEASTCTF8genetic
27708008
MET30_YEASTMET30genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
IPL1_YEASTIPL1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
HUR1_YEASTHUR1genetic
27708008
GCN1_YEASTGCN1genetic
27708008
CSK21_YEASTCKA1genetic
27708008
SWE1_YEASTSWE1genetic
27708008
FEN1_YEASTRAD27genetic
27708008
LST4_YEASTLST4genetic
27708008
DCOR_YEASTSPE1genetic
27708008
PEX1_YEASTPEX1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SDHB_YEASTSDH2genetic
27708008
SIC1_YEASTSIC1genetic
27708008
RS3A2_YEASTRPS1Bgenetic
27708008
RAD14_YEASTRAD14genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
RAD1_YEASTRAD1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
SRO7_YEASTSRO7genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS3A1_YEAST

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND PARTIAL ACETYLATION AT ALA-2 BYNATA.
Phosphorylation
ReferencePubMed
"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-76; SER-112 AND THR-143,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-236 AND THR-245, 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 THR-254, AND MASSSPECTROMETRY.
"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 THR-254, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory