RS23A_YEAST - dbPTM
RS23A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS23A_YEAST
UniProt AC P0CX29
Protein Name 40S ribosomal protein S23-A {ECO:0000303|PubMed:9559554}
Gene Name RPS23A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 145
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 MGKGKPRGLNSARKLRVHRRNNRWAENNYKKRLLGTAFKSSPFGGSSHAKGIVLEKLGIESKQPNSAIRKCVRVQLIKNGKKVTAFVPNDGCLNFVDENDEVLLAGFGRKGKAKGDIPGVRFKVVKVSGVSLLALWKEKKEKPRS
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
30SuccinylationRWAENNYKKRLLGTA
CHHHHHHHHHHHHHH		33.2823954790
30AcetylationRWAENNYKKRLLGTA
CHHHHHHHHHHHHHH		33.2825381059
30UbiquitinationRWAENNYKKRLLGTA
CHHHHHHHHHHHHHH		33.28-
39AcetylationRLLGTAFKSSPFGGS
HHHHHHHHCCCCCCC		47.7824489116
39UbiquitinationRLLGTAFKSSPFGGS
HHHHHHHHCCCCCCC		47.78-
40PhosphorylationLLGTAFKSSPFGGSS
HHHHHHHCCCCCCCH		36.4729136822
41PhosphorylationLGTAFKSSPFGGSSH
HHHHHHCCCCCCCHH		25.4919823750
46PhosphorylationKSSPFGGSSHAKGIV
HCCCCCCCHHHCEEE		21.2329136822
47PhosphorylationSSPFGGSSHAKGIVL
CCCCCCCHHHCEEEE		30.6429136822
50SuccinylationFGGSSHAKGIVLEKL
CCCCHHHCEEEEHHH		43.6923954790
50AcetylationFGGSSHAKGIVLEKL
CCCCHHHCEEEEHHH		43.6924489116
50UbiquitinationFGGSSHAKGIVLEKL
CCCCHHHCEEEEHHH		43.69-
56UbiquitinationAKGIVLEKLGIESKQ
HCEEEEHHHCCCCCC		48.1022106047
56AcetylationAKGIVLEKLGIESKQ
HCEEEEHHHCCCCCC		48.1024489116
62UbiquitinationEKLGIESKQPNSAIR
HHHCCCCCCCCHHHH		57.91-
64HydroxylationLGIESKQPNSAIRKC
HCCCCCCCCHHHHHH		40.2424550462
78AcetylationCVRVQLIKNGKKVTA
HHEEEEEECCCEEEE		69.1422865919
114UbiquitinationFGRKGKAKGDIPGVR
CCCCCCCCCCCCCCC		61.68-
126UbiquitinationGVRFKVVKVSGVSLL
CCCEEEEEECCCCHH		33.40-
128PhosphorylationRFKVVKVSGVSLLAL
CEEEEEECCCCHHHH		27.9722369663
131PhosphorylationVVKVSGVSLLALWKE
EEEECCCCHHHHHHH		22.6122369663
137UbiquitinationVSLLALWKEKKEKPR
CCHHHHHHHHHCCCC		61.58-
137AcetylationVSLLALWKEKKEKPR
CCHHHHHHHHHCCCC		61.5824489116
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 RS23A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
64PHydroxylation

24550462
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 RS23A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAP3_YEASTHAP3genetic
20093466
BEM1_YEASTBEM1genetic
20093466
ERV15_YEASTERV15genetic
20093466
PYC2_YEASTPYC2genetic
20093466
ELO2_YEASTELO2genetic
20093466
GCN20_YEASTGCN20genetic
20093466
DSD1_YEASTDSD1genetic
20093466
ITC1_YEASTITC1genetic
20093466
KA122_YEASTKAP122genetic
20093466
PHO81_YEASTPHO81genetic
20093466
YHS7_YEASTYHR127Wgenetic
20093466
GPP1_YEASTGPP1genetic
20093466
PRY1_YEASTPRY1genetic
20093466
DENR_YEASTTMA22genetic
20093466
HBS1_YEASTHBS1genetic
20093466
SRL3_YEASTSRL3genetic
20093466
RL40A_YEASTRPL40Bgenetic
20093466
RL40B_YEASTRPL40Bgenetic
20093466
DPH5_YEASTDPH5genetic
20093466
YL287_YEASTYLR287Cgenetic
20093466
DOM34_YEASTDOM34genetic
20093466
MDHC_YEASTMDH2genetic
20093466
DPP3_YEASTYOL057Wgenetic
20093466
ETT1_YEASTETT1genetic
20093466
VPS17_YEASTVPS17genetic
20093466
MDL2_YEASTMDL2genetic
20093466
SUR1_YEASTSUR1genetic
20093466
RTC6_YEASTRTC6genetic
20691087
SLU7_YEASTSLU7genetic
27708008
SWC4_YEASTSWC4genetic
27708008
MYO2_YEASTMYO2genetic
27708008
RS14A_YEASTRPS14Agenetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
LSM2_YEASTLSM2genetic
27708008
PSB6_YEASTPRE7genetic
27708008
CDC10_YEASTCDC10genetic
27708008
NOT1_YEASTCDC39genetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPN5_YEASTRPN5genetic
27708008
DNLI1_YEASTCDC9genetic
27708008
DAD1_YEASTDAD1genetic
27708008
PDC2_YEASTPDC2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CAB5_YEASTCAB5genetic
27708008
GPI8_YEASTGPI8genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSA1_YEASTSCL1genetic
27708008
STT3_YEASTSTT3genetic
27708008
GPI10_YEASTGPI10genetic
27708008
SMC3_YEASTSMC3genetic
27708008
PRS7_YEASTRPT1genetic
27708008
COFI_YEASTCOF1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
ERO1_YEASTERO1genetic
27708008
SGT1_YEASTSGT1genetic
27708008
MED4_YEASTMED4genetic
27708008
GRPE_YEASTMGE1genetic
27708008
SYLC_YEASTCDC60genetic
27708008
ELO2_YEASTELO2genetic
27708008
PP2A2_YEASTPPH22genetic
27708008
YD241_YEASTYDL241Wgenetic
27708008
MAF1_YEASTMAF1genetic
27708008
TRM1_YEASTTRM1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
KA122_YEASTKAP122genetic
27708008
ITC1_YEASTITC1genetic
27708008
DSD1_YEASTDSD1genetic
27708008
YHS7_YEASTYHR127Wgenetic
27708008
DENR_YEASTTMA22genetic
27708008
KKQ8_YEASTKKQ8genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
MDHC_YEASTMDH2genetic
27708008
BUB3_YEASTBUB3genetic
27708008
ETT1_YEASTETT1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
PTPA2_YEASTRRD2genetic
27708008
MDL2_YEASTMDL2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS23A_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-128, AND MASSSPECTROMETRY.

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