RS8B_YEAST - dbPTM
RS8B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS8B_YEAST
UniProt AC P0CX40
Protein Name 40S ribosomal protein S8-B {ECO:0000303|PubMed:9559554}
Gene Name RPS8B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 200
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 MGISRDSRHKRSATGAKRAQFRKKRKFELGRQPANTKIGAKRIHSVRTRGGNKKYRALRIETGNFSWASEGISKKTRIAGVVYHPSNNELVRTNTLTKAAIVQIDATPFRQWFEAHYGQTLGKKKNVKEEETVAKSKNAERKWAARAASAKIESSVESQFSAGRLYACISSRPGQSGRCDGYILEGEELAFYLRRLTAKK
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
4Phosphorylation----MGISRDSRHKR
----CCCCCCCHHHH		25.0619823750
7Phosphorylation-MGISRDSRHKRSAT
-CCCCCCCHHHHHCH		34.8619823750
23UbiquitinationAKRAQFRKKRKFELG
HHHHHHHHHHHCCCC		59.2122817900
24UbiquitinationKRAQFRKKRKFELGR
HHHHHHHHHHCCCCC		57.4722817900
26UbiquitinationAQFRKKRKFELGRQP
HHHHHHHHCCCCCCC		52.6622817900
37UbiquitinationGRQPANTKIGAKRIH
CCCCCCCCCCCEEEE		38.6623749301
41UbiquitinationANTKIGAKRIHSVRT
CCCCCCCEEEEEEEE		46.8222817900
62PhosphorylationYRALRIETGNFSWAS
EEEEEEEECCCCCCC		34.7517287358
66PhosphorylationRIETGNFSWASEGIS
EEEECCCCCCCCCCC		26.2317287358
69PhosphorylationTGNFSWASEGISKKT
ECCCCCCCCCCCCCC		30.0517287358
73PhosphorylationSWASEGISKKTRIAG
CCCCCCCCCCCEEEE		38.6717287358
74UbiquitinationWASEGISKKTRIAGV
CCCCCCCCCCEEEEE		57.1323749301
75UbiquitinationASEGISKKTRIAGVV
CCCCCCCCCEEEEEE		35.9222817900
76PhosphorylationSEGISKKTRIAGVVY
CCCCCCCCEEEEEEE		30.9220377248
83PhosphorylationTRIAGVVYHPSNNEL
CEEEEEEECCCCCCE		12.9528889911
86PhosphorylationAGVVYHPSNNELVRT
EEEEECCCCCCEEEC		38.6921440633
93PhosphorylationSNNELVRTNTLTKAA
CCCCEEECCCCCEEE		25.6921440633
95PhosphorylationNELVRTNTLTKAAIV
CCEEECCCCCEEEEE		34.8820377248
98UbiquitinationVRTNTLTKAAIVQID
EECCCCCEEEEEEEE		38.6423749301
107PhosphorylationAIVQIDATPFRQWFE
EEEEEECCCHHHHHH		21.1521440633
120PhosphorylationFEAHYGQTLGKKKNV
HHHHHHCCCCCCCCC		32.8721440633
123UbiquitinationHYGQTLGKKKNVKEE
HHHCCCCCCCCCCHH		64.7822817900
124UbiquitinationYGQTLGKKKNVKEEE
HHCCCCCCCCCCHHH		48.0222817900
125UbiquitinationGQTLGKKKNVKEEET
HCCCCCCCCCCHHHH		71.1522817900
128UbiquitinationLGKKKNVKEEETVAK
CCCCCCCCHHHHHHH		69.6523749301
132PhosphorylationKNVKEEETVAKSKNA
CCCCHHHHHHHHHHH		29.1023749301
135UbiquitinationKEEETVAKSKNAERK
CHHHHHHHHHHHHHH		58.5922106047
149PhosphorylationKWAARAASAKIESSV
HHHHHHHHHHHHHHH		29.1622369663
151UbiquitinationAARAASAKIESSVES
HHHHHHHHHHHHHHH		44.5023749301
154PhosphorylationAASAKIESSVESQFS
HHHHHHHHHHHHHHC		43.0622369663
155PhosphorylationASAKIESSVESQFSA
HHHHHHHHHHHHHCC		19.6722369663
158PhosphorylationKIESSVESQFSAGRL
HHHHHHHHHHCCCCE		34.0822369663
161PhosphorylationSSVESQFSAGRLYAC
HHHHHHHCCCCEEEE		23.3722369663
170PhosphorylationGRLYACISSRPGQSG
CCEEEEEECCCCCCC		21.8521440633
171PhosphorylationRLYACISSRPGQSGR
CEEEEEECCCCCCCC		23.6821440633
176PhosphorylationISSRPGQSGRCDGYI
EECCCCCCCCCCEEE		33.8328889911
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 RS8B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS8B_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 RS8B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRP41_YEASTSKI6genetic
19061648
URB1_YEASTURB1genetic
19061648
CCA1_YEASTCCA1genetic
19061648
PHO89_YEASTPHO89genetic
27708008
BLM10_YEASTBLM10genetic
27708008
SWI6_YEASTSWI6genetic
27708008
CSM3_YEASTCSM3genetic
27708008
STB2_YEASTSTB2genetic
27708008
TPP1_YEASTTPP1genetic
27708008
SGF29_YEASTSGF29genetic
27708008
BIK1_YEASTBIK1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
POG1_YEASTPOG1genetic
27708008
SWE1_YEASTSWE1genetic
27708008
MUD2_YEASTMUD2genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
PNPH_YEASTPNP1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
VAM3_YEASTVAM3genetic
27708008
SUR1_YEASTSUR1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS8B_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 THR-107; SER-154; SER-155AND SER-158, AND MASS 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-62; SER-66; SER-69 ANDSER-73, AND MASS SPECTROMETRY.

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