RLA2_YEAST - dbPTM
RLA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA2_YEAST
UniProt AC P05319
Protein Name 60S acidic ribosomal protein P2-alpha {ECO:0000303|PubMed:9559554}
Gene Name RPP2A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 106
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 MKYLAAYLLLNAAGNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAAEESDDDMGFGLFD
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
2Ubiquitination------MKYLAAYLL
------CHHHHHHHH		49.3123749301
16PhosphorylationLLNAAGNTPDATKIK
HHHHHCCCCCHHHHH		22.9427214570
20PhosphorylationAGNTPDATKIKAILE
HCCCCCHHHHHHHHH		40.4524961812
21AcetylationGNTPDATKIKAILES
CCCCCHHHHHHHHHH		43.8824489116
21UbiquitinationGNTPDATKIKAILES
CCCCCHHHHHHHHHH		43.8822817900
23UbiquitinationTPDATKIKAILESVG
CCCHHHHHHHHHHCC		30.8122817900
28PhosphorylationKIKAILESVGIEIED
HHHHHHHHCCCEECC		23.389398162
37UbiquitinationGIEIEDEKVSSVLSA
CCEECCHHHHHHHHH		60.7923749301
39PhosphorylationEIEDEKVSSVLSALE
EECCHHHHHHHHHHC		26.2922369663
40PhosphorylationIEDEKVSSVLSALEG
ECCHHHHHHHHHHCC		30.0222369663
43PhosphorylationEKVSSVLSALEGKSV
HHHHHHHHHHCCCCH		28.7522369663
48UbiquitinationVLSALEGKSVDELIT
HHHHHCCCCHHHHHH		37.6224961812
48AcetylationVLSALEGKSVDELIT
HHHHHCCCCHHHHHH		37.6224489116
48SuccinylationVLSALEGKSVDELIT
HHHHHCCCCHHHHHH		37.6223954790
49PhosphorylationLSALEGKSVDELITE
HHHHCCCCHHHHHHC		45.7322369663
55PhosphorylationKSVDELITEGNEKLA
CCHHHHHHCCCHHEE		50.9222369663
71PhosphorylationVPAAGPASAGGAAAA
CCCCCCCCHHHHHHH		30.4922369663
79PhosphorylationAGGAAAASGDAAAEE
HHHHHHHHCCHHHHH		32.2625521595
96PhosphorylationEEEAAEESDDDMGFG
HHHHHHHCCCCCCCC		37.5325521595
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 RLA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA2_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 RLA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP26_YEASTHSP26physical
19536198
MDM10_YEASTMDM10genetic
20093466
NUM1_YEASTNUM1genetic
20093466
RV167_YEASTRVS167genetic
20093466
UBP6_YEASTUBP6genetic
20093466
SGF73_YEASTSGF73genetic
20093466
SLX9_YEASTSLX9genetic
20093466
QCR9_YEASTQCR9genetic
20093466
OTU2_YEASTOTU2genetic
20093466
CHS7_YEASTCHS7genetic
20093466
COPE_YEASTSEC28genetic
20093466
ALN_YEASTDAL1genetic
20093466
LDB18_YEASTLDB18genetic
20093466
BRE2_YEASTBRE2genetic
20093466
SIC1_YEASTSIC1genetic
20093466
SWI6_YEASTSWI6genetic
20093466
GBLP_YEASTASC1genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
YVC1_YEASTYVC1genetic
20093466
RLA2_YEASTRPP2Aphysical
17040491
RLA4_YEASTRPP2Bphysical
17040491
RLA4_YEASTRPP2Bphysical
14617190
RLA1_YEASTRPP1Aphysical
14617190
RLA3_YEASTRPP1Bphysical
14617190
RLA0_YEASTRPP0physical
14617190
RLA0_YEASTRPP0genetic
22275522
RLA4_YEASTRPP2Bgenetic
22377630
SGF73_YEASTSGF73genetic
27708008
EXO84_YEASTEXO84genetic
27708008
CDC4_YEASTCDC4genetic
27708008
PRS8_YEASTRPT6genetic
27708008
DAM1_YEASTDAM1genetic
27708008
SEC65_YEASTSEC65genetic
27708008
PSB5_YEASTPRE2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
REI1_YEASTREI1genetic
27708008
RV161_YEASTRVS161genetic
27708008
NUM1_YEASTNUM1genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
RV167_YEASTRVS167genetic
27708008
UBP6_YEASTUBP6genetic
27708008
AAKG_YEASTSNF4genetic
27708008
SLH1_YEASTSLH1genetic
27708008
OTU2_YEASTOTU2genetic
27708008
ALN_YEASTDAL1genetic
27708008
MRT4_YEASTMRT4genetic
27708008
LDB18_YEASTLDB18genetic
27708008
SIC1_YEASTSIC1genetic
27708008
UBX2_YEASTUBX2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLA2_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 THR-16; SER-39; SER-49;SER-79 AND SER-96, AND MASS SPECTROMETRY.
"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-96, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.

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