RL24A_YEAST - dbPTM
RL24A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL24A_YEAST
UniProt AC P04449
Protein Name 60S ribosomal protein L24-A {ECO:0000303|PubMed:9559554}
Gene Name RPL24A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 155
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 MKVEIDSFSGAKIYPGRGTLFVRGDSKIFRFQNSKSASLFKQRKNPRRIAWTVLFRKHHKKGITEEVAKKRSRKTVKAQRPITGASLDLIKERRSLKPEVRKANREEKLKANKEKKKAEKAARKAEKAKSAGTQSSKFSKQQAKGAFQKVAATSR
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------MKVEIDSFS
------CCEEEECCC		48.8823749301
7Phosphorylation-MKVEIDSFSGAKIY
-CCEEEECCCCCEEE		27.2922369663
9PhosphorylationKVEIDSFSGAKIYPG
CEEEECCCCCEEECC		41.6220377248
122-HydroxyisobutyrylationIDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.42-
12SuccinylationIDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4223954790
12AcetylationIDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4224489116
12UbiquitinationIDSFSGAKIYPGRGT
EECCCCCEEECCCCE		46.4223749301
19PhosphorylationKIYPGRGTLFVRGDS
EEECCCCEEEEECCC		18.7021440633
26PhosphorylationTLFVRGDSKIFRFQN
EEEEECCCEEEEEEC		30.4022369663
27SuccinylationLFVRGDSKIFRFQNS
EEEECCCEEEEEECC		51.0823954790
272-HydroxyisobutyrylationLFVRGDSKIFRFQNS
EEEECCCEEEEEECC		51.08-
27UbiquitinationLFVRGDSKIFRFQNS
EEEECCCEEEEEECC		51.0823749301
27AcetylationLFVRGDSKIFRFQNS
EEEECCCEEEEEECC		51.0824489116
34PhosphorylationKIFRFQNSKSASLFK
EEEEEECCCCHHHHH		19.7321551504
352-HydroxyisobutyrylationIFRFQNSKSASLFKQ
EEEEECCCCHHHHHH		58.55-
35SuccinylationIFRFQNSKSASLFKQ
EEEEECCCCHHHHHH		58.5523954790
35AcetylationIFRFQNSKSASLFKQ
EEEEECCCCHHHHHH		58.5524489116
35UbiquitinationIFRFQNSKSASLFKQ
EEEEECCCCHHHHHH		58.5523749301
38PhosphorylationFQNSKSASLFKQRKN
EECCCCHHHHHHCCC		41.2421440633
41AcetylationSKSASLFKQRKNPRR
CCCHHHHHHCCCHHH		55.2624489116
41UbiquitinationSKSASLFKQRKNPRR
CCCHHHHHHCCCHHH		55.2623749301
44UbiquitinationASLFKQRKNPRRIAW
HHHHHHCCCHHHHHH		69.6622817900
52PhosphorylationNPRRIAWTVLFRKHH
CHHHHHHHHHHHHHH		9.7922369663
57UbiquitinationAWTVLFRKHHKKGIT
HHHHHHHHHHHCCCC		42.6022817900
60UbiquitinationVLFRKHHKKGITEEV
HHHHHHHHCCCCHHH		53.0322817900
61UbiquitinationLFRKHHKKGITEEVA
HHHHHHHCCCCHHHH		51.7123749301
64PhosphorylationKHHKKGITEEVAKKR
HHHHCCCCHHHHHHH		34.4623749301
69SuccinylationGITEEVAKKRSRKTV
CCCHHHHHHHCCCCC		54.6223954790
69UbiquitinationGITEEVAKKRSRKTV
CCCHHHHHHHCCCCC		54.6217644757
70UbiquitinationITEEVAKKRSRKTVK
CCHHHHHHHCCCCCH		45.9617644757
74UbiquitinationVAKKRSRKTVKAQRP
HHHHHCCCCCHHCCC		59.9422817900
77UbiquitinationKRSRKTVKAQRPITG
HHCCCCCHHCCCCCC		43.9923749301
77AcetylationKRSRKTVKAQRPITG
HHCCCCCHHCCCCCC		43.9924489116
83PhosphorylationVKAQRPITGASLDLI
CHHCCCCCCHHHHHH		29.4022369663
86PhosphorylationQRPITGASLDLIKER
CCCCCCHHHHHHHHH		24.6222369663
91AcetylationGASLDLIKERRSLKP
CHHHHHHHHHHCCCH		53.0924489116
912-HydroxyisobutyrylationGASLDLIKERRSLKP
CHHHHHHHHHHCCCH		53.09-
91UbiquitinationGASLDLIKERRSLKP
CHHHHHHHHHHCCCH		53.0923749301
91SuccinylationGASLDLIKERRSLKP
CHHHHHHHHHHCCCH		53.0923954790
95PhosphorylationDLIKERRSLKPEVRK
HHHHHHHCCCHHHHH		47.1419823750
97UbiquitinationIKERRSLKPEVRKAN
HHHHHCCCHHHHHHH		40.1423749301
97AcetylationIKERRSLKPEVRKAN
HHHHHCCCHHHHHHH		40.1424489116
102UbiquitinationSLKPEVRKANREEKL
CCCHHHHHHHHHHHH		56.0117644757
120UbiquitinationKEKKKAEKAARKAEK
HHHHHHHHHHHHHHH		52.8122817900
124UbiquitinationKAEKAARKAEKAKSA
HHHHHHHHHHHHHHC		57.0522817900
127UbiquitinationKAARKAEKAKSAGTQ
HHHHHHHHHHHCCCC		67.0122817900
129UbiquitinationARKAEKAKSAGTQSS
HHHHHHHHHCCCCCH		52.4822817900
135PhosphorylationAKSAGTQSSKFSKQQ
HHHCCCCCHHHCHHH		35.0223749301
136PhosphorylationKSAGTQSSKFSKQQA
HHCCCCCHHHCHHHH		28.0921440633
137UbiquitinationSAGTQSSKFSKQQAK
HCCCCCHHHCHHHHH		59.9323749301
1372-HydroxyisobutyrylationSAGTQSSKFSKQQAK
HCCCCCHHHCHHHHH		59.93-
137AcetylationSAGTQSSKFSKQQAK
HCCCCCHHHCHHHHH		59.9324489116
140UbiquitinationTQSSKFSKQQAKGAF
CCCHHHCHHHHHHHH		49.9522817900
140AcetylationTQSSKFSKQQAKGAF
CCCHHHCHHHHHHHH		49.9525381059
1442-HydroxyisobutyrylationKFSKQQAKGAFQKVA
HHCHHHHHHHHHHHH		46.57-
144UbiquitinationKFSKQQAKGAFQKVA
HHCHHHHHHHHHHHH		46.5723749301
144SuccinylationKFSKQQAKGAFQKVA
HHCHHHHHHHHHHHH		46.5723954790
149AcetylationQAKGAFQKVAATSR-
HHHHHHHHHHHCCC-		27.6424489116
1492-HydroxyisobutyrylationQAKGAFQKVAATSR-
HHHHHHHHHHHCCC-		27.64-
149UbiquitinationQAKGAFQKVAATSR-
HHHHHHHHHHHCCC-		27.6423749301
153PhosphorylationAFQKVAATSR-----
HHHHHHHCCC-----		18.4624909858
154PhosphorylationFQKVAATSR------
HHHHHHCCC------		31.1324909858
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 RL24A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL24A_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 RL24A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL3_YEASTRPL3physical
18559667
RLA0_YEASTRPP0physical
18559667
RS8A_YEASTRPS8Aphysical
18559667
RS8B_YEASTRPS8Aphysical
18559667
MAK11_YEASTMAK11physical
18658244
PESC_YEASTNOP7physical
18658244
NOG1_YEASTNOG1physical
18658244
NOG2_YEASTNOG2physical
18658244
ARX1_YEASTARX1physical
18658244
RL5_YEASTRPL5physical
19797079
SRS2_YEASTSRS2genetic
21459050
RL24B_YEASTRPL24Bgenetic
22377630
RLA0_YEASTRPP0physical
27775710
MEX67_YEASTMEX67physical
27775710
PVH1_YEASTYVH1physical
27775710
MRT4_YEASTMRT4physical
27775710
IF6_YEASTTIF6physical
27775710
NMD3_YEASTNMD3physical
27775710
RL10_YEASTRPL10physical
27775710
TCPZ_YEASTCCT6genetic
27708008
DAL81_YEASTDAL81genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ENV10_YEASTENV10genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
UBC3_YEASTCDC34genetic
27708008
MAK21_YEASTMAK21genetic
27708008
SYF1_YEASTSYF1genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
PP12_YEASTGLC7genetic
27708008
ACT_YEASTACT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
KRE9_YEASTKRE9genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SDO1_YEASTSDO1genetic
27708008
ERG27_YEASTERG27genetic
27708008
NOP56_YEASTNOP56genetic
27708008
GSP1_YEASTGSP1genetic
27708008
CDC25_YEASTCDC25genetic
27708008
RLA0_YEASTRPP0genetic
27708008
AFG2_YEASTAFG2genetic
27708008
POB3_YEASTPOB3genetic
27708008
LIP1_YEASTLIP1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
DED1_YEASTDED1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
ATC3_YEASTDRS2genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
CSG2_YEASTCSG2genetic
27708008
DPH7_YEASTRRT2genetic
27708008
SGF29_YEASTSGF29genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VMS1_YEASTVMS1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
WDR59_YEASTMTC5genetic
27708008
SHE9_YEASTSHE9genetic
27708008
FCY2_YEASTFCY2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
MSH4_YEASTMSH4genetic
27708008
SLH1_YEASTSLH1genetic
27708008
YIA6_YEASTYIA6genetic
27708008
FMC1_YEASTFMC1genetic
27708008
YIT6_YEASTYIR016Wgenetic
27708008
MND2_YEASTMND2genetic
27708008
MGA2_YEASTMGA2genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
OPT1_YEASTOPT1genetic
27708008
IME1_YEASTIME1genetic
27708008
SFC1_YEASTSFC1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
ERG3_YEASTERG3genetic
27708008
SIC1_YEASTSIC1genetic
27708008
SWI6_YEASTSWI6genetic
27708008
FKS1_YEASTFKS1genetic
27708008
REH1_YEASTREH1genetic
27708008
GBLP_YEASTASC1genetic
27708008
MLH1_YEASTMLH1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
YNF0_YEASTYNL050Cgenetic
27708008
SKI7_YEASTSKI7genetic
27708008
SPS4_YEASTSPS4genetic
27708008
PPQ1_YEASTPPQ1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL24A_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-9; THR-83 AND SER-86,AND MASS SPECTROMETRY.
"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-86, 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-26; SER-86 AND SER-95,AND MASS SPECTROMETRY.
"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-86, 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-86, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.

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