RS28A_YEAST - dbPTM
RS28A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS28A_YEAST
UniProt AC Q3E7X9
Protein Name 40S ribosomal protein S28-A {ECO:0000303|PubMed:9559554}
Gene Name RPS28A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 67
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 MDNKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR
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
1Acetylation-------MDNKTPVT
-------CCCCCCCH		13.3010601260
4Acetylation----MDNKTPVTLAK
----CCCCCCCHHHH		50.3624489116
5Phosphorylation---MDNKTPVTLAKV
---CCCCCCCHHHHH		29.2822369663
8PhosphorylationMDNKTPVTLAKVIKV
CCCCCCCHHHHHHHH		23.3822369663
11UbiquitinationKTPVTLAKVIKVLGR
CCCCHHHHHHHHHCC		47.8322817900
14UbiquitinationVTLAKVIKVLGRTGS
CHHHHHHHHHCCCCC		34.1023749301
19PhosphorylationVIKVLGRTGSRGGVT
HHHHHCCCCCCCCEE		37.4022369663
21PhosphorylationKVLGRTGSRGGVTQV
HHHCCCCCCCCEEEE		27.4322369663
26PhosphorylationTGSRGGVTQVRVEFL
CCCCCCEEEEEEEEE		25.3122369663
36PhosphorylationRVEFLEDTSRTIVRN
EEEEECCCCCHHHHC		15.6722369663
37PhosphorylationVEFLEDTSRTIVRNV
EEEECCCCCHHHHCC		39.4822369663
39PhosphorylationFLEDTSRTIVRNVKG
EECCCCCHHHHCCCC		24.4822369663
59PhosphorylationDILVLMESEREARRL
CEEEEECHHHHHHHC		28.1727017623
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 RS28A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS28A_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 RS28A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EDC3_YEASTEDC3physical
11283351
DCP1_YEASTDCP1physical
11283351
EDC3_YEASTEDC3genetic
18408161
DCP1_YEASTDCP1physical
18719252
RS28B_YEASTRPS28Bgenetic
22377630
PAT1_YEASTPAT1physical
24830408
YAJ9_YEASTYAR029Wgenetic
27708008
PAT1_YEASTPAT1genetic
27708008
PDP2_YEASTPTC6genetic
27708008
GPR1_YEASTGPR1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
SEM1_YEASTSEM1genetic
27708008
GPP1_YEASTGPP1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
TM184_YEASTYKR051Wgenetic
27708008
HBS1_YEASTHBS1genetic
27708008
RS28B_YEASTRPS28Bgenetic
27708008
DOM34_YEASTDOM34genetic
27708008
PUB1_YEASTPUB1genetic
27708008
NAA30_YEASTMAK3genetic
27708008
MED1_YEASTMED1genetic
27708008
VPS4_YEASTVPS4genetic
27708008
DCP1A_HUMANDCP1Aphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS28A_YEAST

loading...

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: ACETYLATION AT MET-1 BY NATB.
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-21 AND THR-26, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory