RS9B_YEAST - dbPTM
RS9B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS9B_YEAST
UniProt AC P05755
Protein Name 40S ribosomal protein S9-B {ECO:0000303|PubMed:9559554}
Gene Name RPS9B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 195
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 uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly]
Protein Sequence MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAAEEAEDEE
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
8PhosphorylationMPRAPRTYSKTYSTP
CCCCCCCCCCCCCCC		14.9528889911
9PhosphorylationPRAPRTYSKTYSTPK
CCCCCCCCCCCCCCC		20.2217330950
10UbiquitinationRAPRTYSKTYSTPKR
CCCCCCCCCCCCCCC		40.8623749301
13PhosphorylationRTYSKTYSTPKRPYE
CCCCCCCCCCCCCCC		43.3928889911
14PhosphorylationTYSKTYSTPKRPYES
CCCCCCCCCCCCCCH		23.5524961812
16UbiquitinationSKTYSTPKRPYESSR
CCCCCCCCCCCCHHC		67.1222106047
21PhosphorylationTPKRPYESSRLDAEL
CCCCCCCHHCHHHHH		18.2124961812
22PhosphorylationPKRPYESSRLDAELK
CCCCCCHHCHHHHHH		25.5617287358
29UbiquitinationSRLDAELKLAGEFGL
HCHHHHHHHHHHHCC		28.0023749301
392-HydroxyisobutyrylationGEFGLKNKREIYRIS
HHHCCCCHHHHHHHH		50.23-
46PhosphorylationKREIYRISFQLSKIR
HHHHHHHHHHHHHHH		9.6528889911
50PhosphorylationYRISFQLSKIRRAAR
HHHHHHHHHHHHHHH		18.4330377154
65UbiquitinationDLLTRDEKDPKRLFE
HHHHCCCCCHHHHHH		81.3422817900
682-HydroxyisobutyrylationTRDEKDPKRLFEGNA
HCCCCCHHHHHHHHH		72.38-
68UbiquitinationTRDEKDPKRLFEGNA
HCCCCCHHHHHHHHH		72.3822817900
87PhosphorylationLVRVGVLSEDKKKLD
HHHHCCCCCCHHHHH		41.1517287358
902-HydroxyisobutyrylationVGVLSEDKKKLDYVL
HCCCCCCHHHHHHEE		47.99-
92UbiquitinationVLSEDKKKLDYVLAL
CCCCCHHHHHHEEEE		52.9423749301
922-HydroxyisobutyrylationVLSEDKKKLDYVLAL
CCCCCHHHHHHEEEE		52.94-
1002-HydroxyisobutyrylationLDYVLALKVEDFLER
HHHEEEEEHHHHHHH		37.66-
111PhosphorylationFLERRLQTQVYKLGL
HHHHHHHHHHHHHCH		25.2922369663
115UbiquitinationRLQTQVYKLGLAKSV
HHHHHHHHHCHHHCH		36.9024961812
1152-HydroxyisobutyrylationRLQTQVYKLGLAKSV
HHHHHHHHHCHHHCH		36.90-
120UbiquitinationVYKLGLAKSVHHARV
HHHHCHHHCHHHHHH		59.0423749301
1202-HydroxyisobutyrylationVYKLGLAKSVHHARV
HHHHCHHHCHHHHHH		59.04-
130PhosphorylationHHARVLITQRHIAVG
HHHHHHHHHHHHHHC		18.5217287358
138UbiquitinationQRHIAVGKQIVNIPS
HHHHHHCCEEEECCC		30.1923749301
145PhosphorylationKQIVNIPSFMVRLDS
CEEEECCCEEEECCC		23.3722369663
152PhosphorylationSFMVRLDSEKHIDFA
CEEEECCCCCCCCCC		53.8122369663
154UbiquitinationMVRLDSEKHIDFAPT
EEECCCCCCCCCCCC		50.2223749301
161PhosphorylationKHIDFAPTSPFGGAR
CCCCCCCCCCCCCCC		45.6722369663
162PhosphorylationHIDFAPTSPFGGARP
CCCCCCCCCCCCCCC		19.7122369663
180UbiquitinationARRNAARKAEASGEA
HHHHHHHHHHHHHHH		45.9423749301
184PhosphorylationAARKAEASGEAAEEA
HHHHHHHHHHHHHHH		28.7722369663
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 RS9B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS9B_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 RS9B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
HAL5_YEASTHAL5genetic
20206679
SRS2_YEASTSRS2genetic
21459050
RPF1_YEASTRPF1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
COPA_YEASTCOP1genetic
27708008
GPI8_YEASTGPI8genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SN114_YEASTSNU114genetic
27708008
RU1C_YEASTYHC1genetic
27708008
ERO1_YEASTERO1genetic
27708008
UTP15_YEASTUTP15genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
VPS24_YEASTVPS24genetic
27708008
BAS1_YEASTBAS1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
TLG2_YEASTTLG2genetic
27708008
VPS68_YEASTVPS68genetic
27708008
RAS1_YEASTRAS1genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
RS9A_YEASTRPS9Agenetic
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 RS9B_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-9; SER-145; THR-161;SER-162 AND SER-184, AND MASS 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-162, 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-87 AND THR-130, AND MASSSPECTROMETRY.
"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-9 AND SER-184, AND MASSSPECTROMETRY.
"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-184, AND MASSSPECTROMETRY.

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