RS6A_YEAST - dbPTM
RS6A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS6A_YEAST
UniProt AC P0CX37
Protein Name 40S ribosomal protein S6-A {ECO:0000303|PubMed:9559554}
Gene Name RPS6A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 236
Subcellular Localization Cytoplasm . Nucleus, nucleolus .
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. [PubMed: 22096102 eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly]
Protein Sequence MKLNISYPVNGSQKTFEIDDEHRIRVFFDKRIGQEVDGEAVGDEFKGYVFKISGGNDKQGFPMKQGVLLPTRIKLLLTKNVSCYRPRRDGERKRKSVRGAIVGPDLAVLALVIVKKGEQELEGLTDTTVPKRLGPKRANNIRKFFGLSKEDDVRDFVIRREVTKGEKTYTKAPKIQRLVTPQRLQRKRHQRALKVRNAQAQREAAAEYAQLLAKRLSERKAEKAEIRKRRASSLKA
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
2Succinylation------MKLNISYPV
------CCCEEEEEC		50.6823954790
2Ubiquitination------MKLNISYPV
------CCCEEEEEC		50.68-
6Phosphorylation--MKLNISYPVNGSQ
--CCCEEEEECCCCE		23.4722369663
7Phosphorylation-MKLNISYPVNGSQK
-CCCEEEEECCCCEE		13.8522369663
12PhosphorylationISYPVNGSQKTFEID
EEEECCCCEEEEEEC		24.2522369663
14AcetylationYPVNGSQKTFEIDDE
EECCCCEEEEEECCH		57.8024489116
14UbiquitinationYPVNGSQKTFEIDDE
EECCCCEEEEEECCH		57.80-
46UbiquitinationEAVGDEFKGYVFKIS
EECCCCCCEEEEEEE		47.48-
46SuccinylationEAVGDEFKGYVFKIS
EECCCCCCEEEEEEE		47.4823954790
46AcetylationEAVGDEFKGYVFKIS
EECCCCCCEEEEEEE		47.4824489116
51AcetylationEFKGYVFKISGGNDK
CCCEEEEEEECCCCC		26.3924489116
51SuccinylationEFKGYVFKISGGNDK
CCCEEEEEEECCCCC		26.3923954790
53PhosphorylationKGYVFKISGGNDKQG
CEEEEEEECCCCCCC		41.0421551504
58AcetylationKISGGNDKQGFPMKQ
EEECCCCCCCCCCCC		57.2124489116
58UbiquitinationKISGGNDKQGFPMKQ
EEECCCCCCCCCCCC		57.21-
64UbiquitinationDKQGFPMKQGVLLPT
CCCCCCCCCCEECCC		44.10-
74AcetylationVLLPTRIKLLLTKNV
EECCCHHHEEECCCC		29.7724489116
79AcetylationRIKLLLTKNVSCYRP
HHHEEECCCCCCCCC		56.1524489116
79UbiquitinationRIKLLLTKNVSCYRP
HHHEEECCCCCCCCC		56.15-
82PhosphorylationLLLTKNVSCYRPRRD
EEECCCCCCCCCCCC		18.1528889911
116AcetylationLALVIVKKGEQELEG
HEEEEEECCHHHHCC		57.7024489116
116UbiquitinationLALVIVKKGEQELEG
HEEEEEECCHHHHCC		57.7022106047
125PhosphorylationEQELEGLTDTTVPKR
HHHHCCCCCCCCCHH		42.0021440633
127PhosphorylationELEGLTDTTVPKRLG
HHCCCCCCCCCHHHC		25.1824961812
128PhosphorylationLEGLTDTTVPKRLGP
HCCCCCCCCCHHHCH		37.3121440633
131AcetylationLTDTTVPKRLGPKRA
CCCCCCCHHHCHHHH		56.7924489116
131SuccinylationLTDTTVPKRLGPKRA
CCCCCCCHHHCHHHH		56.7923954790
131UbiquitinationLTDTTVPKRLGPKRA
CCCCCCCHHHCHHHH		56.7922106047
143UbiquitinationKRANNIRKFFGLSKE
HHHHHHHHHHCCCCC		41.05-
143AcetylationKRANNIRKFFGLSKE
HHHHHHHHHHCCCCC		41.0524489116
148PhosphorylationIRKFFGLSKEDDVRD
HHHHHCCCCCCCCHH		34.0927214570
149SuccinylationRKFFGLSKEDDVRDF
HHHHCCCCCCCCHHH		70.9223954790
149AcetylationRKFFGLSKEDDVRDF
HHHHCCCCCCCCHHH		70.9224489116
149UbiquitinationRKFFGLSKEDDVRDF
HHHHCCCCCCCCHHH		70.9222106047
163PhosphorylationFVIRREVTKGEKTYT
HHHEEEECCCCCCCC		28.6920377248
164AcetylationVIRREVTKGEKTYTK
HHEEEECCCCCCCCC		70.9625381059
164SuccinylationVIRREVTKGEKTYTK
HHEEEECCCCCCCCC		70.9623954790
167AcetylationREVTKGEKTYTKAPK
EEECCCCCCCCCCCH		56.3424489116
171UbiquitinationKGEKTYTKAPKIQRL
CCCCCCCCCCHHHHH		52.88-
171AcetylationKGEKTYTKAPKIQRL
CCCCCCCCCCHHHHH		52.8824489116
180PhosphorylationPKIQRLVTPQRLQRK
CHHHHHCCHHHHHHH		20.4917287358
214UbiquitinationEYAQLLAKRLSERKA
HHHHHHHHHHHHHHH		54.5722106047
214AcetylationEYAQLLAKRLSERKA
HHHHHHHHHHHHHHH		54.5724489116
214SuccinylationEYAQLLAKRLSERKA
HHHHHHHHHHHHHHH		54.5723954790
223AcetylationLSERKAEKAEIRKRR
HHHHHHHHHHHHHHH		57.0624489116
232PhosphorylationEIRKRRASSLKA---
HHHHHHHHHCCC---		34.1019823750
233PhosphorylationIRKRRASSLKA----
HHHHHHHHCCC----		32.6719823750
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 RS6A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS6A_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 RS6A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
YAJ9_YEASTYAR029Wgenetic
20093466
ADT3_YEASTAAC3genetic
20093466
NHP6B_YEASTNHP6Bgenetic
20093466
NHP10_YEASTNHP10genetic
20093466
HMO1_YEASTHMO1genetic
20093466
LSM6_YEASTLSM6genetic
20093466
CP56_YEASTDIT2genetic
20093466
PAC11_YEASTPAC11genetic
20093466
UBP6_YEASTUBP6genetic
20093466
PDR1_YEASTPDR1genetic
20093466
THP2_YEASTTHP2genetic
20093466
STB5_YEASTSTB5genetic
20093466
COPE_YEASTSEC28genetic
20093466
DENR_YEASTTMA22genetic
20093466
YJ24_YEASTKCH1genetic
20093466
HOC1_YEASTHOC1genetic
20093466
IME1_YEASTIME1genetic
20093466
SDHA_YEASTSDH1genetic
20093466
HBS1_YEASTHBS1genetic
20093466
SIC1_YEASTSIC1genetic
20093466
DPH5_YEASTDPH5genetic
20093466
MSS1_YEASTMSS1genetic
20093466
RHO2_YEASTRHO2genetic
20093466
SWS2_YEASTSWS2genetic
20093466
DOM34_YEASTDOM34genetic
20093466
ENV9_YEASTENV9genetic
20093466
COX10_YEASTCOX10genetic
20093466
SUR1_YEASTSUR1genetic
20093466
KPC1_YEASTPKC1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
RSC8_YEASTRSC8genetic
27708008
ESP1_YEASTESP1genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
CWC16_YEASTYJU2genetic
27708008
RPF2_YEASTRPF2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
CDC27_YEASTCDC27genetic
27708008
SNU23_YEASTSNU23genetic
27708008
CDC53_YEASTCDC53genetic
27708008
SNU56_YEASTSNU56genetic
27708008
SMT3_YEASTSMT3genetic
27708008
PSB3_YEASTPUP3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRP21_YEASTPRP21genetic
27708008
ESS1_YEASTESS1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
CDC91_YEASTGAB1genetic
27708008
ERO1_YEASTERO1genetic
27708008
UTP15_YEASTUTP15genetic
27708008
SGT1_YEASTSGT1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
ADT3_YEASTAAC3genetic
27708008
IMG2_YEASTIMG2genetic
27708008
NHP10_YEASTNHP10genetic
27708008
LSM6_YEASTLSM6genetic
27708008
PT122_YEASTPET122genetic
27708008
IES1_YEASTIES1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
RTG2_YEASTRTG2genetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
DENR_YEASTTMA22genetic
27708008
YJ24_YEASTKCH1genetic
27708008
IME1_YEASTIME1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
COX7_YEASTCOX7genetic
27708008
DOM34_YEASTDOM34genetic
27708008
SWS2_YEASTSWS2genetic
27708008
MNE1_YEASTMNE1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS6A_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-232 AND SER-233, 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-232 AND SER-233, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-233, ANDMASS SPECTROMETRY.
"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-163 AND THR-180, ANDMASS SPECTROMETRY.

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