RL4A_YEAST - dbPTM
RL4A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL4A_YEAST
UniProt AC P10664
Protein Name 60S ribosomal protein L4-A {ECO:0000303|PubMed:9559554}
Gene Name RPL4A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 362
Subcellular Localization Cytoplasm . Nucleus .
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. [PubMed: 22096102 uL4 participates in the regulation of the accumulation of its own mRNA]
Protein Sequence MSRPQVTVHSLTGEATANALPLPAVFSAPIRPDIVHTVFTSVNKNKRQAYAVSEKAGHQTSAESWGTGRAVARIPRVGGGGTGRSGQGAFGNMCRGGRMFAPTKTWRKWNVKVNHNEKRYATASAIAATAVASLVLARGHRVEKIPEIPLVVSTDLESIQKTKEAVAALKAVGAHSDLLKVLKSKKLRAGKGKYRNRRWTQRRGPLVVYAEDNGIVKALRNVPGVETANVASLNLLQLAPGAHLGRFVIWTEAAFTKLDQVWGSETVASSKVGYTLPSHIISTSDVTRIINSSEIQSAIRPAGQATQKRTHVLKKNPLKNKQVLLRLNPYAKVFAAEKLGSKKAEKTGTKPAAVFTETLKHD
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
2Phosphorylation------MSRPQVTVH
------CCCCCEEEE		53.3021126336
2Acetylation------MSRPQVTVH
------CCCCCEEEE		53.301544921
10PhosphorylationRPQVTVHSLTGEATA
CCCEEEEECCCCCCC		24.2424961812
12PhosphorylationQVTVHSLTGEATANA
CEEEEECCCCCCCCC		35.6724961812
16PhosphorylationHSLTGEATANALPLP
EECCCCCCCCCCCCC		19.0124961812
53PhosphorylationKRQAYAVSEKAGHQT
CHHEEEEECCCCCCC		25.8023749301
55UbiquitinationQAYAVSEKAGHQTSA
HEEEEECCCCCCCCH		52.7623749301
55AcetylationQAYAVSEKAGHQTSA
HEEEEECCCCCCCCH		52.7624489116
60PhosphorylationSEKAGHQTSAESWGT
ECCCCCCCCHHHHCC		24.9922369663
61PhosphorylationEKAGHQTSAESWGTG
CCCCCCCCHHHHCCC		24.3822369663
64PhosphorylationGHQTSAESWGTGRAV
CCCCCHHHHCCCCCE		30.4423749301
67PhosphorylationTSAESWGTGRAVARI
CCHHHHCCCCCEEEC		19.7528889911
85PhosphorylationGGGGTGRSGQGAFGN
CCCCCCCCCCCCCCC		36.4922369663
104AcetylationGRMFAPTKTWRKWNV
CCCCCCCCEEECCEE		45.0624489116
104UbiquitinationGRMFAPTKTWRKWNV
CCCCCCCCEEECCEE		45.0623749301
104MethylationGRMFAPTKTWRKWNV
CCCCCCCCEEECCEE		45.0620137074
108UbiquitinationAPTKTWRKWNVKVNH
CCCCEEECCEEECCC		34.3822817900
112AcetylationTWRKWNVKVNHNEKR
EEECCEEECCCCCHH		33.8222865919
112UbiquitinationTWRKWNVKVNHNEKR
EEECCEEECCCCCHH		33.8222817900
118UbiquitinationVKVNHNEKRYATASA
EECCCCCHHHHHHHH		56.9017644757
120PhosphorylationVNHNEKRYATASAIA
CCCCCHHHHHHHHHH		21.2622369663
122PhosphorylationHNEKRYATASAIAAT
CCCHHHHHHHHHHHH		16.5322369663
124PhosphorylationEKRYATASAIAATAV
CHHHHHHHHHHHHHH		18.8222369663
129PhosphorylationTASAIAATAVASLVL
HHHHHHHHHHHHHHH		16.7922369663
133PhosphorylationIAATAVASLVLARGH
HHHHHHHHHHHHCCC		16.6522369663
144AcetylationARGHRVEKIPEIPLV
HCCCCCCCCCCCCEE		61.7824489116
144UbiquitinationARGHRVEKIPEIPLV
HCCCCCCCCCCCCEE		61.7823749301
153PhosphorylationPEIPLVVSTDLESIQ
CCCCEEEECCHHHHH		14.5524961812
154PhosphorylationEIPLVVSTDLESIQK
CCCEEEECCHHHHHH		32.7524961812
158PhosphorylationVVSTDLESIQKTKEA
EEECCHHHHHHHHHH		37.3021440633
1612-HydroxyisobutyrylationTDLESIQKTKEAVAA
CCHHHHHHHHHHHHH		60.95-
161AcetylationTDLESIQKTKEAVAA
CCHHHHHHHHHHHHH		60.9524489116
161UbiquitinationTDLESIQKTKEAVAA
CCHHHHHHHHHHHHH		60.9517644757
1632-HydroxyisobutyrylationLESIQKTKEAVAALK
HHHHHHHHHHHHHHH		51.19-
163UbiquitinationLESIQKTKEAVAALK
HHHHHHHHHHHHHHH		51.1923749301
170SuccinylationKEAVAALKAVGAHSD
HHHHHHHHHHHCCHH		35.9823954790
170UbiquitinationKEAVAALKAVGAHSD
HHHHHHHHHHHCCHH		35.9823749301
1702-HydroxyisobutyrylationKEAVAALKAVGAHSD
HHHHHHHHHHHCCHH		35.98-
170AcetylationKEAVAALKAVGAHSD
HHHHHHHHHHHCCHH		35.9824489116
176PhosphorylationLKAVGAHSDLLKVLK
HHHHHCCHHHHHHHH		29.4422369663
180AcetylationGAHSDLLKVLKSKKL
HCCHHHHHHHHHCCC		53.4724489116
1802-HydroxyisobutyrylationGAHSDLLKVLKSKKL
HCCHHHHHHHHHCCC		53.47-
180UbiquitinationGAHSDLLKVLKSKKL
HCCHHHHHHHHHCCC		53.4717644757
200PhosphorylationKYRNRRWTQRRGPLV
CCCCCCCHHCCCCEE		15.4717287358
217AcetylationAEDNGIVKALRNVPG
ECCCCHHHHHHCCCC		39.5224489116
217UbiquitinationAEDNGIVKALRNVPG
ECCCCHHHHHHCCCC		39.5223749301
257UbiquitinationWTEAAFTKLDQVWGS
EEHHHCCCHHHHHCC		43.5423749301
264PhosphorylationKLDQVWGSETVASSK
CHHHHHCCCCCCCCC		17.8730377154
269PhosphorylationWGSETVASSKVGYTL
HCCCCCCCCCCCCCC		26.7619779198
270PhosphorylationGSETVASSKVGYTLP
CCCCCCCCCCCCCCC		22.9421440633
271AcetylationSETVASSKVGYTLPS
CCCCCCCCCCCCCCC		36.8624489116
271UbiquitinationSETVASSKVGYTLPS
CCCCCCCCCCCCCCC		36.8623749301
274PhosphorylationVASSKVGYTLPSHII
CCCCCCCCCCCCCEE		14.2126447709
275PhosphorylationASSKVGYTLPSHIIS
CCCCCCCCCCCCEEE		26.6821440633
278PhosphorylationKVGYTLPSHIISTSD
CCCCCCCCCEEEHHH		30.3622369663
282PhosphorylationTLPSHIISTSDVTRI
CCCCCEEEHHHCEEE		22.6622369663
283PhosphorylationLPSHIISTSDVTRII
CCCCEEEHHHCEEEC		20.6622369663
284PhosphorylationPSHIISTSDVTRIIN
CCCEEEHHHCEEECC		24.2422369663
287PhosphorylationIISTSDVTRIINSSE
EEEHHHCEEECCHHH		22.5722369663
292PhosphorylationDVTRIINSSEIQSAI
HCEEECCHHHHHHHH		20.9522369663
293PhosphorylationVTRIINSSEIQSAIR
CEEECCHHHHHHHHC		33.9422369663
297PhosphorylationINSSEIQSAIRPAGQ
CCHHHHHHHHCCCCH		31.1822369663
306PhosphorylationIRPAGQATQKRTHVL
HCCCCHHHHHCCCCC		27.0822369663
308AcetylationPAGQATQKRTHVLKK
CCCHHHHHCCCCCCC		55.7124489116
3082-HydroxyisobutyrylationPAGQATQKRTHVLKK
CCCHHHHHCCCCCCC		55.71-
308UbiquitinationPAGQATQKRTHVLKK
CCCHHHHHCCCCCCC		55.7123749301
314AcetylationQKRTHVLKKNPLKNK
HHCCCCCCCCCCCCC		49.7925381059
321SuccinylationKKNPLKNKQVLLRLN
CCCCCCCCEEEEHHC		39.9523954790
321UbiquitinationKKNPLKNKQVLLRLN
CCCCCCCCEEEEHHC		39.9523749301
321AcetylationKKNPLKNKQVLLRLN
CCCCCCCCEEEEHHC		39.9524489116
332AcetylationLRLNPYAKVFAAEKL
EHHCHHHHHHHHHHH		31.8524489116
332UbiquitinationLRLNPYAKVFAAEKL
EHHCHHHHHHHHHHH		31.8523749301
3322-HydroxyisobutyrylationLRLNPYAKVFAAEKL
EHHCHHHHHHHHHHH		31.85-
332SuccinylationLRLNPYAKVFAAEKL
EHHCHHHHHHHHHHH		31.8523954790
338AcetylationAKVFAAEKLGSKKAE
HHHHHHHHHCCHHHH		54.1224489116
3382-HydroxyisobutyrylationAKVFAAEKLGSKKAE
HHHHHHHHHCCHHHH		54.12-
338UbiquitinationAKVFAAEKLGSKKAE
HHHHHHHHHCCHHHH		54.1223749301
341PhosphorylationFAAEKLGSKKAEKTG
HHHHHHCCHHHHHHC		41.2321440633
342UbiquitinationAAEKLGSKKAEKTGT
HHHHHCCHHHHHHCC		54.9622817900
343AcetylationAEKLGSKKAEKTGTK
HHHHCCHHHHHHCCC		64.5723572591
343UbiquitinationAEKLGSKKAEKTGTK
HHHHCCHHHHHHCCC		64.5722817900
346UbiquitinationLGSKKAEKTGTKPAA
HCCHHHHHHCCCCCE		58.0517644757
347PhosphorylationGSKKAEKTGTKPAAV
CCHHHHHHCCCCCEE		41.4021440633
349PhosphorylationKKAEKTGTKPAAVFT
HHHHHHCCCCCEEEE		38.8021440633
350AcetylationKAEKTGTKPAAVFTE
HHHHHCCCCCEEEEC		33.7224489116
350SuccinylationKAEKTGTKPAAVFTE
HHHHHCCCCCEEEEC		33.7223954790
350UbiquitinationKAEKTGTKPAAVFTE
HHHHHCCCCCEEEEC		33.7217644757
360SuccinylationAVFTETLKHD-----
EEEECCCCCC-----		53.8223954790
360UbiquitinationAVFTETLKHD-----
EEEECCCCCC-----		53.8217644757
360AcetylationAVFTETLKHD-----
EEEECCCCCC-----		53.8224489116
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 RL4A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL4A_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 RL4A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSM1_YEASTLSM1genetic
20876302
PAT1_YEASTPAT1genetic
20876302
XRN1_YEASTXRN1genetic
20876302
RL4B_YEASTRPL4Bgenetic
22377630
DAP2_YEASTDAP2physical
24072706
CGR1_YEASTCGR1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
RAD10_YEASTRAD10genetic
27708008
REI1_YEASTREI1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
SOK1_YEASTSOK1genetic
27708008
WDR59_YEASTMTC5genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
LSM6_YEASTLSM6genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
PSP1_YEASTPSP1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
XRN1_YEASTXRN1genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
MTC1_YEASTMTC1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
SWE1_YEASTSWE1genetic
27708008
RAD26_YEASTRAD26genetic
27708008
SPA2_YEASTSPA2genetic
27708008
PSP2_YEASTPSP2genetic
27708008
ESC1_YEASTESC1genetic
27708008
YNE6_YEASTYNL046Wgenetic
27708008
RNH2A_YEASTRNH201genetic
27708008
TOP1_YEASTTOP1genetic
27708008
VAM3_YEASTVAM3genetic
27708008
RGS2_YEASTRGS2genetic
27708008
YO304_YEASTBIL1genetic
27708008
MTHR1_YEASTMET12genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
MDM36_YEASTMDM36genetic
27708008
AXL1_YEASTAXL1genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL4A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"NH2-terminal acetylation of ribosomal proteins of Saccharomycescerevisiae.";
Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
J. Biol. Chem. 267:5442-5445(1992).
Cited for: PROTEIN SEQUENCE OF 2-21, AND ACETYLATION AT SER-2 BY NATA.
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-60; SER-176; SER-278;SER-282; THR-283; SER-284; THR-287; SER-293 AND SER-297, 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-282; SER-284 ANDSER-293, 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 THR-200, AND MASSSPECTROMETRY.

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