RS20_YEAST - dbPTM
RS20_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS20_YEAST
UniProt AC P38701
Protein Name 40S ribosomal protein S20 {ECO:0000303|PubMed:9559554}
Gene Name RPS20 {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 121
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 MSDFQKEKVEEQEQQQQQIIKIRITLTSTKVKQLENVSSNIVKNAEQHNLVKKGPVRLPTKVLKISTRKTPNGEGSKTWETYEMRIHKRYIDLEAPVQIVKRITQITIEPGVDVEVVVASN
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
2Phosphorylation------MSDFQKEKV
------CCHHHHHHH		47.3215665377
2Acetylation------MSDFQKEKV
------CCHHHHHHH		47.3210601260
6Acetylation--MSDFQKEKVEEQE
--CCHHHHHHHHHHH		60.5424489116
6Ubiquitination--MSDFQKEKVEEQE
--CCHHHHHHHHHHH		60.5422817900
8UbiquitinationMSDFQKEKVEEQEQQ
CCHHHHHHHHHHHHH		63.0823749301
8SuccinylationMSDFQKEKVEEQEQQ
CCHHHHHHHHHHHHH		63.0823954790
8AcetylationMSDFQKEKVEEQEQQ
CCHHHHHHHHHHHHH		63.0824489116
212-HydroxyisobutyrylationQQQQQIIKIRITLTS
HHHHHHHEEEEEECC		27.79-
21UbiquitinationQQQQQIIKIRITLTS
HHHHHHHEEEEEECC		27.7923749301
21AcetylationQQQQQIIKIRITLTS
HHHHHHHEEEEEECC		27.7924489116
27PhosphorylationIKIRITLTSTKVKQL
HEEEEEECCCCHHHH		26.2130377154
28PhosphorylationKIRITLTSTKVKQLE
EEEEEECCCCHHHHH		29.3721440633
302-HydroxyisobutyrylationRITLTSTKVKQLENV
EEEECCCCHHHHHCC		47.40-
30UbiquitinationRITLTSTKVKQLENV
EEEECCCCHHHHHCC		47.4023749301
32UbiquitinationTLTSTKVKQLENVSS
EECCCCHHHHHCCCH		51.2023749301
38PhosphorylationVKQLENVSSNIVKNA
HHHHHCCCHHHHHCH		29.2921440633
39PhosphorylationKQLENVSSNIVKNAE
HHHHCCCHHHHHCHH		26.7128152593
43UbiquitinationNVSSNIVKNAEQHNL
CCCHHHHHCHHHCCC		46.7923749301
43AcetylationNVSSNIVKNAEQHNL
CCCHHHHHCHHHCCC		46.7924489116
43SuccinylationNVSSNIVKNAEQHNL
CCCHHHHHCHHHCCC		46.7923954790
52UbiquitinationAEQHNLVKKGPVRLP
HHHCCCCCCCCCCCC		56.0023749301
52SuccinylationAEQHNLVKKGPVRLP
HHHCCCCCCCCCCCC		56.0023954790
52AcetylationAEQHNLVKKGPVRLP
HHHCCCCCCCCCCCC		56.0024489116
53UbiquitinationEQHNLVKKGPVRLPT
HHCCCCCCCCCCCCC		62.0522817900
60PhosphorylationKGPVRLPTKVLKIST
CCCCCCCCEEEEEEE		38.0727214570
61UbiquitinationGPVRLPTKVLKISTR
CCCCCCCEEEEEEEC		43.5617644757
64UbiquitinationRLPTKVLKISTRKTP
CCCCEEEEEEECCCC		37.2822817900
642-HydroxyisobutyrylationRLPTKVLKISTRKTP
CCCCEEEEEEECCCC		37.28-
69AcetylationVLKISTRKTPNGEGS
EEEEEECCCCCCCCC		69.3124489116
69UbiquitinationVLKISTRKTPNGEGS
EEEEEECCCCCCCCC		69.3122817900
77SuccinylationTPNGEGSKTWETYEM
CCCCCCCCCCEEEEE		69.3923954790
77AcetylationTPNGEGSKTWETYEM
CCCCCCCCCCEEEEE		69.3924489116
77UbiquitinationTPNGEGSKTWETYEM
CCCCCCCCCCEEEEE		69.3924961812
88UbiquitinationTYEMRIHKRYIDLEA
EEEEEEEHHCCCCCC		44.5217644757
90PhosphorylationEMRIHKRYIDLEAPV
EEEEEHHCCCCCCCH		12.0021440633
1012-HydroxyisobutyrylationEAPVQIVKRITQITI
CCCHHHHHHHHEEEE		39.45-
101UbiquitinationEAPVQIVKRITQITI
CCCHHHHHHHHEEEE		39.4523749301
101AcetylationEAPVQIVKRITQITI
CCCHHHHHHHHEEEE		39.4524489116
101SuccinylationEAPVQIVKRITQITI
CCCHHHHHHHHEEEE		39.4523954790
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 RS20_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS20_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 RS20_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4B_YEASTTIF3physical
23236192
NEP1_YEASTEMG1genetic
27708008
RPC6_YEASTRPC34genetic
27708008
DED1_YEASTDED1genetic
27708008
CDC27_YEASTCDC27genetic
27708008
RPAB1_YEASTRPB5genetic
27708008
TAF5_YEASTTAF5genetic
27708008
ARPC1_YEASTARC40genetic
27708008
SCC1_YEASTMCD1genetic
27708008
APC11_YEASTAPC11genetic
27708008
DPOD_YEASTPOL3genetic
27708008
NSE4_YEASTNSE4genetic
27708008
TAF12_YEASTTAF12genetic
27708008
TRS23_YEASTTRS23genetic
27708008
ACT_YEASTACT1genetic
27708008
COPD_YEASTRET2genetic
27708008
PRS8_YEASTRPT6genetic
27708008
PRP18_YEASTPRP18genetic
27708008
DAM1_YEASTDAM1genetic
27708008
YIP1_YEASTYIP1genetic
27708008
HACD_YEASTPHS1genetic
27708008
CDC16_YEASTCDC16genetic
27708008
NTR2_YEASTNTR2genetic
27708008
RU1C_YEASTYHC1genetic
27708008
POB3_YEASTPOB3genetic
27708008
SEC65_YEASTSEC65genetic
27708008
UTP15_YEASTUTP15genetic
27708008
PRP2_YEASTPRP2genetic
27708008
APC5_YEASTAPC5genetic
27708008
SEC62_YEASTSEC62genetic
27708008
HRR25_YEASTHRR25genetic
27708008
NSL1_YEASTNSL1genetic
27708008
PRP4_YEASTPRP4genetic
27708008
RV161_YEASTRVS161genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PEX19_YEASTPEX19genetic
27708008
VAM6_YEASTVAM6genetic
27708008
MAF1_YEASTMAF1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
UBP6_YEASTUBP6genetic
27708008
HBS1_YEASTHBS1genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
MGR3_YEASTMGR3genetic
27708008
GBLP_YEASTASC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
EOS1_YEASTEOS1genetic
27708008
2A5D_YEASTRTS1genetic
27708008
YME1_YEASTYME1genetic
27708008
BRR1_YEASTBRR1genetic
27708008
LTV1_YEASTLTV1physical
26831757
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS20_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.
"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 ACETYLATION AT SER-2 BY NATA.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8, AND MASS SPECTROMETRY.
"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: PROTEIN SEQUENCE OF 7-21, MASS SPECTROMETRY, AND UBIQUITINATION [LARGESCALE ANALYSIS] AT LYS-8.

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