RSSA2_YEAST - dbPTM
RSSA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSSA2_YEAST
UniProt AC P46654
Protein Name 40S ribosomal protein S0-B {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554}
Gene Name RPS0B {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 MSLPATFDLTPEDAQLLLAANTHLGARNVQVHQEPYVFNARPDGVHVINVGKTWEKLVLAARIIAAIPNPEDVVAISSRTYGQRAVLKFAAHTGATPIAGRFTPGSFTNYITRSFKEPRLVIVTDPRLDAQAIKEASYVNIPVIALTDLDSPSEFVDVAIPCNNRGKHSIGLIWYLLAREVLRLRGALVDRTQPWSIMPDLYFYRNPEEVEQVAEEAAAAEEGEEEEVKEEVTEGQAEATEWAEENADNVEW
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
2Phosphorylation------MSLPATFDL
------CCCCCEECC		42.9622369663
2Acetylation------MSLPATFDL
------CCCCCEECC		42.9610601260
6Phosphorylation--MSLPATFDLTPED
--CCCCCEECCCHHH		18.7522369663
10PhosphorylationLPATFDLTPEDAQLL
CCCEECCCHHHHHHH		26.8622369663
22PhosphorylationQLLLAANTHLGARNV
HHHHHHCCCCCCCCE		17.4730377154
36PhosphorylationVQVHQEPYVFNARPD
EEEECCCEEEECCCC		19.5428889911
52UbiquitinationVHVINVGKTWEKLVL
EEEEECCCCHHHHHH		46.3023749301
56UbiquitinationNVGKTWEKLVLAARI
ECCCCHHHHHHHHHH		35.1422817900
88UbiquitinationYGQRAVLKFAAHTGA
HHHHHHHHHHHHCCC		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
138PhosphorylationQAIKEASYVNIPVIA
HHHHHHHCCCCCEEE		12.4521440633
167UbiquitinationIPCNNRGKHSIGLIW
EECCCCCCCHHHHHH		30.8323749301
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 RSSA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSSA2_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 RSSA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLNA_YEASTGLN1physical
16554755
ATS1_YEASTATS1genetic
20093466
ATG8_YEASTATG8genetic
20093466
BAP2_YEASTBAP2genetic
20093466
IPT1_YEASTIPT1genetic
20093466
NUM1_YEASTNUM1genetic
20093466
HMO1_YEASTHMO1genetic
20093466
CEM1_YEASTCEM1genetic
20093466
UBP6_YEASTUBP6genetic
20093466
XRN1_YEASTXRN1genetic
20093466
ASK10_YEASTASK10genetic
20093466
RSSA1_YEASTRPS0Agenetic
20093466
YOR1_YEASTYOR1genetic
20093466
OSH3_YEASTOSH3genetic
20093466
COPE_YEASTSEC28genetic
20093466
MTC1_YEASTMTC1genetic
20093466
DPH4_YEASTJJJ3genetic
20093466
NFU1_YEASTNFU1genetic
20093466
HBS1_YEASTHBS1genetic
20093466
SYM1_YEASTSYM1genetic
20093466
HMDH1_YEASTHMG1genetic
20093466
YNB0_YEASTYNL010Wgenetic
20093466
DOM34_YEASTDOM34genetic
20093466
CYP8_YEASTCPR8genetic
20093466
WHI5_YEASTWHI5genetic
20093466
LCB4_YEASTLCB4genetic
20093466
SPO19_YEASTSPO19genetic
20093466
SUR1_YEASTSUR1genetic
20093466
SRS2_YEASTSRS2genetic
21459050
CMR1_YEASTCMR1genetic
22842922
RS16A_YEASTRPS16Bgenetic
27708008
RS16B_YEASTRPS16Bgenetic
27708008
ASK10_YEASTASK10genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
NUM1_YEASTNUM1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
MRM2_YEASTMRM2genetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
YOR1_YEASTYOR1genetic
27708008
ASF1_YEASTASF1genetic
27708008
MTC1_YEASTMTC1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
SUR1_YEASTSUR1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSSA2_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.
Phosphorylation
ReferencePubMed
"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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