RLA4_YEAST - dbPTM
RLA4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA4_YEAST
UniProt AC P02400
Protein Name 60S acidic ribosomal protein P2-beta {ECO:0000303|PubMed:9559554}
Gene Name RPP2B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 110
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 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD
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
3Phosphorylation-----MKYLAAYLLL
-----CHHHHHHHHH		10.5622369663
7Phosphorylation-MKYLAAYLLLVQGG
-CHHHHHHHHHHCCC		7.7122369663
19PhosphorylationQGGNAAPSAADIKAV
CCCCCCCCHHHHHHH		31.2222369663
29PhosphorylationDIKAVVESVGAEVDE
HHHHHHHHHCCCCCH		17.7817287358
44PhosphorylationARINELLSSLEGKGS
HHHHHHHHHHCCCCC		45.5622369663
45PhosphorylationRINELLSSLEGKGSL
HHHHHHHHHCCCCCH		30.3422369663
49UbiquitinationLLSSLEGKGSLEEII
HHHHHCCCCCHHHHH		35.6323749301
49SuccinylationLLSSLEGKGSLEEII
HHHHHCCCCCHHHHH		35.6323954790
51PhosphorylationSSLEGKGSLEEIIAE
HHHCCCCCHHHHHHH		35.7728132839
61UbiquitinationEIIAEGQKKFATVPT
HHHHHHHHHEEECCC		61.7923749301
61SuccinylationEIIAEGQKKFATVPT
HHHHHHHHHEEECCC		61.7923954790
61AcetylationEIIAEGQKKFATVPT
HHHHHHHHHEEECCC		61.7924489116
62UbiquitinationIIAEGQKKFATVPTG
HHHHHHHHEEECCCC		32.1324961812
622-HydroxyisobutyrylationIIAEGQKKFATVPTG
HHHHHHHHEEECCCC		32.13-
65PhosphorylationEGQKKFATVPTGGAS
HHHHHEEECCCCCHH		30.1022369663
68PhosphorylationKKFATVPTGGASSAA
HHEEECCCCCHHHHH		43.8624909858
72PhosphorylationTVPTGGASSAAAGAA
ECCCCCHHHHHHHHH		24.6320377248
73PhosphorylationVPTGGASSAAAGAAG
CCCCCHHHHHHHHHH		22.7622369663
92UbiquitinationGDAAEEEKEEEAKEE
CCHHHHHHHHHHHHH		73.9522106047
92AcetylationGDAAEEEKEEEAKEE
CCHHHHHHHHHHHHH		73.9524489116
100PhosphorylationEEEAKEESDDDMGFG
HHHHHHHCCCCCCCC		47.6422369663
104OxidationKEESDDDMGFGLFD-
HHHCCCCCCCCCCC-		6.5315665377
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 RLA4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA4_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 RLA4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN4_YEASTGCN4genetic
18423200
SLA1_YEASTSLA1genetic
20093466
CST26_YEASTCST26genetic
20093466
UBC4_YEASTUBC4genetic
20093466
UBS1_YEASTUBS1genetic
20093466
DER1_YEASTDER1genetic
20093466
UBP1_YEASTUBP1genetic
20093466
NUP59_YEASTASM4genetic
20093466
NUM1_YEASTNUM1genetic
20093466
BOI2_YEASTBOI2genetic
20093466
UBP6_YEASTUBP6genetic
20093466
RT31_YEASTYMR31genetic
20093466
XRN1_YEASTXRN1genetic
20093466
SCS3_YEASTSCS3genetic
20093466
YG35_YEASTYGR125Wgenetic
20093466
SLH1_YEASTSLH1genetic
20093466
YHH7_YEASTYSC83genetic
20093466
SLT2_YEASTSLT2genetic
20093466
STB5_YEASTSTB5genetic
20093466
ELO1_YEASTELO1genetic
20093466
MHP1_YEASTMHP1genetic
20093466
DPH4_YEASTJJJ3genetic
20093466
DHOM_YEASTHOM6genetic
20093466
MNN4_YEASTMNN4genetic
20093466
IRS4_YEASTIRS4genetic
20093466
DYHC_YEASTDYN1genetic
20093466
TGL4_YEASTTGL4genetic
20093466
LDB18_YEASTLDB18genetic
20093466
ERG3_YEASTERG3genetic
20093466
SIC1_YEASTSIC1genetic
20093466
SRL2_YEASTSRL2genetic
20093466
POC1_YEASTPBA1genetic
20093466
ERFB_YEASTERF2genetic
20093466
SRR1L_YEASTBER1genetic
20093466
BUL2_YEASTBUL2genetic
20093466
BUB2_YEASTBUB2genetic
20093466
GBLP_YEASTASC1genetic
20093466
ATC8_YEASTDNF3genetic
20093466
RIT1_YEASTRIT1genetic
20093466
DYN3_YEASTDYN3genetic
20093466
HDA1_YEASTHDA1genetic
20093466
PUB1_YEASTPUB1genetic
20093466
IRA2_YEASTIRA2genetic
20093466
RLA2_YEASTRPP2Agenetic
20093466
SFL1_YEASTSFL1genetic
20093466
YO214_YEASTSPR2genetic
20093466
ENV9_YEASTENV9genetic
20093466
LIS1_YEASTPAC1genetic
20093466
PUT4_YEASTPUT4genetic
20093466
KAR9_YEASTKAR9genetic
20093466
SPO19_YEASTSPO19genetic
20093466
SUR1_YEASTSUR1genetic
20093466
SKI3_YEASTSKI3genetic
20093466
RLA2_YEASTRPP2Aphysical
20225338
RLA4_YEASTRPP2Bphysical
17040491
SRS2_YEASTSRS2genetic
21459050
RLA0_YEASTRPP0physical
14617190
RLA1_YEASTRPP1Aphysical
14617190
RLA3_YEASTRPP1Bphysical
14617190
SIR2_YEASTSIR2genetic
21902802
RLA0_YEASTRPP0genetic
22275522
CMR1_YEASTCMR1genetic
22842922
SWC3_YEASTSWC3genetic
27708008
ATC3_YEASTDRS2genetic
27708008
H4_YEASTHHF1genetic
27708008
UBC4_YEASTUBC4genetic
27708008
PAT1_YEASTPAT1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
NUM1_YEASTNUM1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
XRN1_YEASTXRN1genetic
27708008
SLH1_YEASTSLH1genetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
DHOM_YEASTHOM6genetic
27708008
ERG3_YEASTERG3genetic
27708008
SIC1_YEASTSIC1genetic
27708008
SRL2_YEASTSRL2genetic
27708008
POC1_YEASTPBA1genetic
27708008
SRR1L_YEASTBER1genetic
27708008
GBLP_YEASTASC1genetic
27708008
RLA2_YEASTRPP2Agenetic
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 RLA4_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-100, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, 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-29, 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-100, AND MASSSPECTROMETRY.
"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 SER-100, AND MASSSPECTROMETRY.

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