RS9A_YEAST - dbPTM
RS9A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS9A_YEAST
UniProt AC O13516
Protein Name 40S ribosomal protein S9-A {ECO:0000303|PubMed:9559554}
Gene Name RPS9A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 197
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 MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE
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
10AcetylationRAPRTYSKTYSTPKR
CCCCCCCCCCCCCCC		40.8624489116
10UbiquitinationRAPRTYSKTYSTPKR
CCCCCCCCCCCCCCC		40.8623749301
13PhosphorylationRTYSKTYSTPKRPYE
CCCCCCCCCCCCCCC		43.3928889911
14PhosphorylationTYSKTYSTPKRPYES
CCCCCCCCCCCCCCH		23.5524961812
16AcetylationSKTYSTPKRPYESSR
CCCCCCCCCCCCHHC		67.1224489116
16UbiquitinationSKTYSTPKRPYESSR
CCCCCCCCCCCCHHC		67.1222106047
21PhosphorylationTPKRPYESSRLDAEL
CCCCCCCHHCHHHHH		18.2124961812
22PhosphorylationPKRPYESSRLDAELK
CCCCCCHHCHHHHHH		25.5617287358
29UbiquitinationSRLDAELKLAGEFGL
HCHHHHHHHHHHHCC		28.0023749301
37AcetylationLAGEFGLKNKKEIYR
HHHHHCCCCHHHHHH		68.0822865919
37SuccinylationLAGEFGLKNKKEIYR
HHHHHCCCCHHHHHH		68.0823954790
46PhosphorylationKKEIYRISFQLSKIR
HHHHHHHHHHHHHHH		9.6528889911
50PhosphorylationYRISFQLSKIRRAAR
HHHHHHHHHHHHHHH		18.4330377154
51AcetylationRISFQLSKIRRAARD
HHHHHHHHHHHHHHH		49.1524489116
65UbiquitinationDLLTRDEKDPKRLFE
HHHHCCCCCHHHHHH		81.3422817900
65AcetylationDLLTRDEKDPKRLFE
HHHHCCCCCHHHHHH		81.3424489116
68UbiquitinationTRDEKDPKRLFEGNA
HCCCCCHHHHHHHHH		72.3822817900
87PhosphorylationLVRVGVLSEDKKKLD
HHHHCCCCCCHHHHH		41.1517287358
90AcetylationVGVLSEDKKKLDYVL
HCCCCCCHHHHHHEE		47.9924489116
90SuccinylationVGVLSEDKKKLDYVL
HCCCCCCHHHHHHEE		47.9923954790
91AcetylationGVLSEDKKKLDYVLA
CCCCCCHHHHHHEEE		71.5324489116
92AcetylationVLSEDKKKLDYVLAL
CCCCCHHHHHHEEEE		52.9424489116
92SuccinylationVLSEDKKKLDYVLAL
CCCCCHHHHHHEEEE		52.9423954790
92UbiquitinationVLSEDKKKLDYVLAL
CCCCCHHHHHHEEEE		52.9423749301
111PhosphorylationFLERRLQTQVYKLGL
HHHHHHHHHHHHHCH		25.2922369663
115AcetylationRLQTQVYKLGLAKSV
HHHHHHHHHCHHHCH		36.9024489116
115SuccinylationRLQTQVYKLGLAKSV
HHHHHHHHHCHHHCH		36.9023954790
115UbiquitinationRLQTQVYKLGLAKSV
HHHHHHHHHCHHHCH		36.9024961812
120UbiquitinationVYKLGLAKSVHHARV
HHHHCHHHCHHHHHH		59.0423749301
120AcetylationVYKLGLAKSVHHARV
HHHHCHHHCHHHHHH		59.0422865919
130PhosphorylationHHARVLITQRHIAVG
HHHHHHHHHHHHHHC		18.5217287358
138UbiquitinationQRHIAVGKQIVNIPS
HHHHHHCCEEEECCC		30.1923749301
138AcetylationQRHIAVGKQIVNIPS
HHHHHHCCEEEECCC		30.1924489116
145PhosphorylationKQIVNIPSFMVRLDS
CEEEECCCEEEECCC		23.3722369663
152PhosphorylationSFMVRLDSEKHIDFA
CEEEECCCCCCCCCC		53.8122369663
154UbiquitinationMVRLDSEKHIDFAPT
EEECCCCCCCCCCCC		50.2223749301
154AcetylationMVRLDSEKHIDFAPT
EEECCCCCCCCCCCC		50.2224489116
161PhosphorylationKHIDFAPTSPFGGAR
CCCCCCCCCCCCCCC		45.6722369663
162PhosphorylationHIDFAPTSPFGGARP
CCCCCCCCCCCCCCC		19.7122369663
180UbiquitinationARRNAARKAEASGEA
HHHHHHHHHHHHHHH		45.9423749301
184PhosphorylationAARKAEASGEAADEA
HHHHHHHHHHHHHHH		28.7721082442
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 RS9A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS9A_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 RS9A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
RS9B_YEASTRPS9Bphysical
16554755
RQC2_YEASTTAE2genetic
20691087
RTC6_YEASTRTC6genetic
20691087
RS9B_YEASTRPS9Bgenetic
22377630
MOB2_YEASTMOB2genetic
27708008
HIR1_YEASTHIR1genetic
27708008
ATG9_YEASTATG9genetic
27708008
DLD1_YEASTDLD1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
UAP1_YEASTQRI1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
RSP5_YEASTRSP5genetic
27708008
CDC4_YEASTCDC4genetic
27708008
CDC20_YEASTCDC20genetic
27708008
DNA2_YEASTDNA2genetic
27708008
STS1_YEASTSTS1genetic
27708008
RPC9_YEASTRPC17genetic
27708008
PRP21_YEASTPRP21genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
SN114_YEASTSNU114genetic
27708008
ORC1_YEASTORC1genetic
27708008
TAP42_YEASTTAP42genetic
27708008
APC5_YEASTAPC5genetic
27708008
PMT2_YEASTPMT2genetic
27708008
SEO1_YEASTSEO1genetic
27708008
NUP60_YEASTNUP60genetic
27708008
TOD6_YEASTTOD6genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
ICS2_YEASTICS2genetic
27708008
AIM4_YEASTAIM4genetic
27708008
FAT2_YEASTPCS60genetic
27708008
PDP2_YEASTPTC6genetic
27708008
LHP1_YEASTLHP1genetic
27708008
GIS1_YEASTGIS1genetic
27708008
ENT5_YEASTENT5genetic
27708008
LCMT1_YEASTPPM1genetic
27708008
SDC1_YEASTSDC1genetic
27708008
FIT1_YEASTFIT1genetic
27708008
YEQ9_YEASTYER079Wgenetic
27708008
SPR6_YEASTSPR6genetic
27708008
BCK2_YEASTBCK2genetic
27708008
IES1_YEASTIES1genetic
27708008
AGP3_YEASTAGP3genetic
27708008
MED5_YEASTNUT1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
VEL1_YEASTVEL1genetic
27708008
ECL1_YEASTECL1genetic
27708008
SNG1_YEASTSNG1genetic
27708008
TRX2_YEASTTRX2genetic
27708008
AP18B_YEASTYAP1802genetic
27708008
SAY1_YEASTSAY1genetic
27708008
BGL2_YEASTBGL2genetic
27708008
YG5X_YEASTYGR283Cgenetic
27708008
SA185_YEASTSAP185genetic
27708008
ASF1_YEASTASF1genetic
27708008
RPE_YEASTRPE1genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
KAPC_YEASTTPK3genetic
27708008
GEX2_YEASTGEX2genetic
27708008
BRE2_YEASTBRE2genetic
27708008
IDHC_YEASTIDP2genetic
27708008
YL177_YEASTYLR177Wgenetic
27708008
VTA1_YEASTVTA1genetic
27708008
UBC12_YEASTUBC12genetic
27708008
CDC73_YEASTCDC73genetic
27708008
PSP2_YEASTPSP2genetic
27708008
ITT1_YEASTITT1genetic
27708008
NU188_YEASTNUP188genetic
27708008
SOK2_YEASTSOK2genetic
27708008
PGM2_YEASTPGM2genetic
27708008
DYN3_YEASTDYN3genetic
27708008
YM16A_YEASTYMR316C-Agenetic
27708008
ADH6_YEASTADH6genetic
27708008
HDA1_YEASTHDA1genetic
27708008
NST1_YEASTNST1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
HMS1_YEASTHMS1genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
ALG8_YEASTALG8genetic
27708008
MOD5_YEASTMOD5genetic
27708008
VTS1_YEASTVTS1genetic
27708008
SUE1_YEASTSUE1genetic
27708008
HDA3_YEASTHDA3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS9A_YEAST

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Related Literatures of Post-Translational Modification
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-22, AND MASSSPECTROMETRY.

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