RSSA1_YEAST - dbPTM
RSSA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSSA1_YEAST
UniProt AC P32905
Protein Name 40S ribosomal protein S0-A {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554}
Gene Name RPS0A {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 252
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. [PubMed: 22096102 uS2 is required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits]
Protein Sequence MSLPATFDLTPEDAQLLLAANTHLGARNVQVHQEPYVFNARPDGVHVINVGKTWEKLVLAARIIAAIPNPEDVVAISSRTFGQRAVLKFAAHTGATPIAGRFTPGSFTNYITRSFKEPRLVIVTDPRSDAQAIKEASYVNIPVIALTDLDSPSEFVDVAIPCNNRGKHSIGLIWYLLAREVLRLRGALVDRTQPWSIMPDLYFYRDPEEVEQQVAEEATTEEAGEEEAKEEVTEEQAEATEWAEENADNVEW
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
2Acetylation------MSLPATFDL
------CCCCCEECC		42.9610601260
2Phosphorylation------MSLPATFDL
------CCCCCEECC		42.9622369663
6Phosphorylation--MSLPATFDLTPED
--CCCCCEECCCHHH		18.7522369663
10PhosphorylationLPATFDLTPEDAQLL
CCCEECCCHHHHHHH		26.8622369663
22PhosphorylationQLLLAANTHLGARNV
HHHHHHCCCCCCCCE		17.4730377154
36PhosphorylationVQVHQEPYVFNARPD
EEEECCCEEEECCCC		19.5428889911
52AcetylationVHVINVGKTWEKLVL
EEEEECCCCHHHHHH		46.3024489116
52UbiquitinationVHVINVGKTWEKLVL
EEEEECCCCHHHHHH		46.3023749301
562-HydroxyisobutyrylationNVGKTWEKLVLAARI
ECCCCHHHHHHHHHH		35.14-
56AcetylationNVGKTWEKLVLAARI
ECCCCHHHHHHHHHH		35.1424489116
56UbiquitinationNVGKTWEKLVLAARI
ECCCCHHHHHHHHHH		35.1422817900
882-HydroxyisobutyrylationFGQRAVLKFAAHTGA
CCHHHHHHHHHHCCC		26.76-
88AcetylationFGQRAVLKFAAHTGA
CCHHHHHHHHHHCCC		26.7624489116
88UbiquitinationFGQRAVLKFAAHTGA
CCHHHHHHHHHHCCC		26.7623749301
93PhosphorylationVLKFAAHTGATPIAG
HHHHHHHCCCCCCCC		24.6421082442
96PhosphorylationFAAHTGATPIAGRFT
HHHHCCCCCCCCCCC		19.3027214570
103PhosphorylationTPIAGRFTPGSFTNY
CCCCCCCCCCCHHHH		25.9425752575
106PhosphorylationAGRFTPGSFTNYITR
CCCCCCCCHHHHHHC		30.0528152593
108PhosphorylationRFTPGSFTNYITRSF
CCCCCCHHHHHHCCC		28.8922369663
110PhosphorylationTPGSFTNYITRSFKE
CCCCHHHHHHCCCCC		10.7022369663
112PhosphorylationGSFTNYITRSFKEPR
CCHHHHHHCCCCCCC		15.2022369663
1162-HydroxyisobutyrylationNYITRSFKEPRLVIV
HHHHCCCCCCCEEEE		68.97-
128PhosphorylationVIVTDPRSDAQAIKE
EEEECCCCHHHHHHH		42.5628889911
138PhosphorylationQAIKEASYVNIPVIA
HHHHHHHCCCCCEEE		12.4521440633
167UbiquitinationIPCNNRGKHSIGLIW
EECCCCCCCHHHHHH		30.8323749301
219PhosphorylationQQVAEEATTEEAGEE
HHHHHHHCHHHHCHH		37.7128132839
220PhosphorylationQVAEEATTEEAGEEE
HHHHHHCHHHHCHHH		38.5928132839
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 RSSA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSSA1_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 RSSA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOM1_YEASTTOM1genetic
11238398
RAS2_YEASTRAS2genetic
9055077
STE11_YEASTSTE11genetic
9055077
STE12_YEASTSTE12genetic
9055077
RSSA2_YEASTRPS0Bgenetic
8626693
ARO1_YEASTARO1physical
16429126
HSP60_YEASTHSP60physical
16429126
PFKA1_YEASTPFK1physical
16429126
TBA1_YEASTTUB1physical
16429126
RL24A_YEASTRPL24Aphysical
16429126
RS17B_YEASTRPS17Bphysical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
RS9B_YEASTRPS9Bphysical
16429126
RL4A_YEASTRPL4Aphysical
16429126
RTC6_YEASTRTC6genetic
20691087
RSSA2_YEASTRPS0Bgenetic
22377630
EIF3A_YEASTRPG1physical
22792338
GBLP_YEASTASC1physical
22792338
RS22A_YEASTRPS22Aphysical
22792338
RS22B_YEASTRPS22Bphysical
22792338
RSSA2_YEASTRPS0Bgenetic
22792338
EIF3C_YEASTNIP1physical
22792338
IF2G_YEASTGCD11physical
22792338
IF5_YEASTTIF5physical
22792338
RQC2_YEASTTAE2genetic
23178123
KPC1_YEASTPKC1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
PSB7_YEASTPRE4genetic
27708008
SWC4_YEASTSWC4genetic
27708008
PAN1_YEASTPAN1genetic
27708008
ARP4_YEASTARP4genetic
27708008
KRE9_YEASTKRE9genetic
27708008
ARP3_YEASTARP3genetic
27708008
SMC4_YEASTSMC4genetic
27708008
NOP56_YEASTNOP56genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ARPC2_YEASTARC35genetic
27708008
IPL1_YEASTIPL1genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
MMM1_YEASTMMM1genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
PSB6_YEASTPRE7genetic
27708008
CDC27_YEASTCDC27genetic
27708008
FBRL_YEASTNOP1genetic
27708008
RPN6_YEASTRPN6genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SLY1_YEASTSLY1genetic
27708008
SPC19_YEASTSPC19genetic
27708008
TFB1_YEASTTFB1genetic
27708008
GPI8_YEASTGPI8genetic
27708008
UTP5_YEASTUTP5genetic
27708008
CDC4_YEASTCDC4genetic
27708008
MOB2_YEASTMOB2genetic
27708008
RPN11_YEASTRPN11genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PSA1_YEASTSCL1genetic
27708008
STT3_YEASTSTT3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
BET1_YEASTBET1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
ESS1_YEASTESS1genetic
27708008
COFI_YEASTCOF1genetic
27708008
GAA1_YEASTGAA1genetic
27708008
ERG27_YEASTERG27genetic
27708008
RU1C_YEASTYHC1genetic
27708008
IMB1_YEASTKAP95genetic
27708008
PRP2_YEASTPRP2genetic
27708008
PSB5_YEASTPRE2genetic
27708008
CSG2_YEASTCSG2genetic
27708008
ECM8_YEASTECM8genetic
27708008
FTH1_YEASTFTH1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
SEM1_YEASTSEM1genetic
27708008
GCN20_YEASTGCN20genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
DBP3_YEASTDBP3genetic
27708008
IST3_YEASTIST3genetic
27708008
RM49_YEASTMRP49genetic
27708008
EI2BA_YEASTGCN3genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
SIC1_YEASTSIC1genetic
27708008
SPH1_YEASTSPH1genetic
27708008
USA1_YEASTUSA1genetic
27708008
PHO84_YEASTPHO84genetic
27708008
GBLP_YEASTASC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
TRM10_YEASTTRM10genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSSA1_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-103 AND THR-112, 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 THR-112, AND MASSSPECTROMETRY.

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