RS30B_YEAST - dbPTM
RS30B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS30B_YEAST
UniProt AC P0CX34
Protein Name 40S ribosomal protein S30-B {ECO:0000303|PubMed:9559554}
Gene Name RPS30B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 63
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 MAKVHGSLARAGKVKSQTPKVEKTEKPKKPKGRAYKRLLYTRRFVNVTLVNGKRRMNPGPSVQ
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
3Ubiquitination-----MAKVHGSLAR
-----CCCCHHHHHH		33.2017644757
7Phosphorylation-MAKVHGSLARAGKV
-CCCCHHHHHHCCCC		12.1819795423
15UbiquitinationLARAGKVKSQTPKVE
HHHCCCCCCCCCCCC		40.0917644757
16PhosphorylationARAGKVKSQTPKVEK
HHCCCCCCCCCCCCC		42.1217287358
18PhosphorylationAGKVKSQTPKVEKTE
CCCCCCCCCCCCCCC		31.9730377154
20UbiquitinationKVKSQTPKVEKTEKP
CCCCCCCCCCCCCCC		67.4317644757
23UbiquitinationSQTPKVEKTEKPKKP
CCCCCCCCCCCCCCC		66.0417644757
26UbiquitinationPKVEKTEKPKKPKGR
CCCCCCCCCCCCCCH		68.3317644757
28UbiquitinationVEKTEKPKKPKGRAY
CCCCCCCCCCCCHHH		86.6317644757
29UbiquitinationEKTEKPKKPKGRAYK
CCCCCCCCCCCHHHH		61.5617644757
41PhosphorylationAYKRLLYTRRFVNVT
HHHHHHHEEEEEEEE		18.4817287358
48PhosphorylationTRRFVNVTLVNGKRR
EEEEEEEEEECCEEC		21.5622369663
53UbiquitinationNVTLVNGKRRMNPGP
EEEEECCEECCCCCC		31.4623749301
61PhosphorylationRRMNPGPSVQ-----
ECCCCCCCCC-----		38.7822369663
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 RS30B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS30B_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 RS30B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H3_YEASTHHT1genetic
20093466
MBA1_YEASTMBA1genetic
20093466
SWR1_YEASTSWR1genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
XRN1_YEASTXRN1genetic
20093466
RSSA1_YEASTRPS0Agenetic
20093466
UBA4_YEASTUBA4genetic
20093466
COX23_YEASTCOX23genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
DENR_YEASTTMA22genetic
20093466
OSM1_YEASTOSM1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
CBT1_YEASTCBT1genetic
20093466
RM49_YEASTMRP49genetic
20093466
COXM1_YEASTCMC1genetic
20093466
HBS1_YEASTHBS1genetic
20093466
COX12_YEASTCOX12genetic
20093466
CDC73_YEASTCDC73genetic
20093466
GBLP_YEASTASC1genetic
20093466
FKBP_YEASTFPR1genetic
20093466
OCA2_YEASTOCA2genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
DOM34_YEASTDOM34genetic
20093466
ARE2_YEASTARE2genetic
20093466
CY1_YEASTCYT1genetic
20093466
SKI7_YEASTSKI7genetic
20093466
FYV12_YEASTFYV12genetic
20093466
LIPA_YEASTLIP5genetic
20093466
THTR_YEASTTUM1genetic
20093466
YO289_YEASTYOR289Wgenetic
20093466
MDL2_YEASTMDL2genetic
20093466
ALG5_YEASTALG5genetic
20093466
RU2A_YEASTLEA1genetic
20093466
SUR1_YEASTSUR1genetic
20093466
ESP1_YEASTESP1genetic
27708008
MDM34_YEASTMDM34genetic
27708008
QCR9_YEASTQCR9genetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
SDS3_YEASTSDS3genetic
27708008
SIN3_YEASTSIN3genetic
27708008
DBF4_YEASTDBF4genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SCC2_YEASTSCC2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
CDC20_YEASTCDC20genetic
27708008
YHS2_YEASTCIA2genetic
27708008
SMC3_YEASTSMC3genetic
27708008
COFI_YEASTCOF1genetic
27708008
ERG27_YEASTERG27genetic
27708008
SPC24_YEASTSPC24genetic
27708008
NOG2_YEASTNOG2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
IPL1_YEASTIPL1genetic
27708008
MBA1_YEASTMBA1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
RM01_YEASTMRPL1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
YGY5_YEASTYGL235Wgenetic
27708008
MTO1_YEASTMTO1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
COX23_YEASTCOX23genetic
27708008
DENR_YEASTTMA22genetic
27708008
COXM1_YEASTCMC1genetic
27708008
RM49_YEASTMRP49genetic
27708008
SAC1_YEASTSAC1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
BPT1_YEASTBPT1genetic
27708008
COX12_YEASTCOX12genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
GBLP_YEASTASC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
FKBP_YEASTFPR1genetic
27708008
CY1_YEASTCYT1genetic
27708008
FYV12_YEASTFYV12genetic
27708008
YO289_YEASTYOR289Wgenetic
27708008
MNE1_YEASTMNE1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
SUR1_YEASTSUR1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
ALG5_YEASTALG5genetic
27708008
MDL2_YEASTMDL2genetic
27708008
MSS18_YEASTMSS18genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS30B_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-7, 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-16; THR-41 AND THR-48,AND MASS SPECTROMETRY.

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