RL21A_YEAST - dbPTM
RL21A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL21A_YEAST
UniProt AC Q02753
Protein Name 60S ribosomal protein L21-A {ECO:0000303|PubMed:9559554}
Gene Name RPL21A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 160
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 MGKSHGYRSRTRYMFQRDFRKHGAVHLSTYLKVYKVGDIVDIKANGSIQKGMPHKFYQGKTGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAKAQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI
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
11PhosphorylationSHGYRSRTRYMFQRD
CCCHHHHCCHHHHHC		27.6521440633
21UbiquitinationMFQRDFRKHGAVHLS
HHHHCHHHCCCEEEE		46.5122817900
28PhosphorylationKHGAVHLSTYLKVYK
HCCCEEEEEEEEEEE		10.5022369663
29PhosphorylationHGAVHLSTYLKVYKV
CCCEEEEEEEEEEEE		38.9523749301
30PhosphorylationGAVHLSTYLKVYKVG
CCEEEEEEEEEEEEC		10.9322369663
32UbiquitinationVHLSTYLKVYKVGDI
EEEEEEEEEEEECCE		32.8623749301
35SuccinylationSTYLKVYKVGDIVDI
EEEEEEEEECCEEEE		42.6123954790
35UbiquitinationSTYLKVYKVGDIVDI
EEEEEEEEECCEEEE		42.6123749301
352-HydroxyisobutyrylationSTYLKVYKVGDIVDI
EEEEEEEEECCEEEE		42.61-
35AcetylationSTYLKVYKVGDIVDI
EEEEEEEEECCEEEE		42.6124489116
43AcetylationVGDIVDIKANGSIQK
ECCEEEEECCCCCCC		31.1924489116
43SuccinylationVGDIVDIKANGSIQK
ECCEEEEECCCCCCC		31.1923954790
43UbiquitinationVGDIVDIKANGSIQK
ECCEEEEECCCCCCC		31.1923749301
50UbiquitinationKANGSIQKGMPHKFY
ECCCCCCCCCCCCEE		56.3522817900
55AcetylationIQKGMPHKFYQGKTG
CCCCCCCCEECCCCE		39.6424489116
55UbiquitinationIQKGMPHKFYQGKTG
CCCCCCCCEECCCCE		39.6423749301
60SuccinylationPHKFYQGKTGVVYNV
CCCEECCCCEEEEEE		26.9523954790
60UbiquitinationPHKFYQGKTGVVYNV
CCCEECCCCEEEEEE		26.9523749301
60AcetylationPHKFYQGKTGVVYNV
CCCEECCCCEEEEEE		26.9524489116
602-HydroxyisobutyrylationPHKFYQGKTGVVYNV
CCCEECCCCEEEEEE		26.95-
61PhosphorylationHKFYQGKTGVVYNVT
CCEECCCCEEEEEEC		41.8721440633
68PhosphorylationTGVVYNVTKSSVGVI
CEEEEEECHHHHHHH		22.9022369663
69UbiquitinationGVVYNVTKSSVGVII
EEEEEECHHHHHHHH		36.1323749301
70PhosphorylationVVYNVTKSSVGVIIN
EEEEECHHHHHHHHE		22.3822369663
71PhosphorylationVYNVTKSSVGVIINK
EEEECHHHHHHHHEE		25.1719823750
78UbiquitinationSVGVIINKMVGNRYL
HHHHHHEEHHCHHHH		25.2623749301
78AcetylationSVGVIINKMVGNRYL
HHHHHHEEHHCHHHH		25.2624489116
87UbiquitinationVGNRYLEKRLNLRVE
HCHHHHHHHHCCCHH		60.6415699485
872-HydroxyisobutyrylationVGNRYLEKRLNLRVE
HCHHHHHHHHCCCHH		60.64-
97UbiquitinationNLRVEHIKHSKCRQE
CCCHHHHCCCHHHHH		43.6722817900
97AcetylationNLRVEHIKHSKCRQE
CCCHHHHCCCHHHHH		43.6725381059
972-HydroxyisobutyrylationNLRVEHIKHSKCRQE
CCCHHHHCCCHHHHH		43.67-
100UbiquitinationVEHIKHSKCRQEFLE
HHHHCCCHHHHHHHH		32.9122817900
110UbiquitinationQEFLERVKANAAKRA
HHHHHHHHHHHHHHH		41.9922817900
1102-HydroxyisobutyrylationQEFLERVKANAAKRA
HHHHHHHHHHHHHHH		41.99-
115UbiquitinationRVKANAAKRAEAKAQ
HHHHHHHHHHHHHHH		50.1322817900
120UbiquitinationAAKRAEAKAQGVAVQ
HHHHHHHHHHCEEEE		32.5223749301
1202-HydroxyisobutyrylationAAKRAEAKAQGVAVQ
HHHHHHHHHHCEEEE		32.52-
129AcetylationQGVAVQLKRQPAQPR
HCEEEEEECCCCCCC		31.7124489116
129SuccinylationQGVAVQLKRQPAQPR
HCEEEEEECCCCCCC		31.7123954790
1292-HydroxyisobutyrylationQGVAVQLKRQPAQPR
HCEEEEEECCCCCCC		31.71-
129UbiquitinationQGVAVQLKRQPAQPR
HCEEEEEECCCCCCC		31.7123749301
138PhosphorylationQPAQPRESRIVSTEG
CCCCCCCCCEEECCC		28.6923749301
142PhosphorylationPRESRIVSTEGNVPQ
CCCCCEEECCCCCCC		20.5422890988
143PhosphorylationRESRIVSTEGNVPQT
CCCCEEECCCCCCCC		36.7022890988
150PhosphorylationTEGNVPQTLAPVPYE
CCCCCCCCCCCCCCC		20.8622890988
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 RL21A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL21A_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 RL21A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN4_YEASTGCN4genetic
18423200
RL21B_YEASTRPL21Bgenetic
22377630
GEM1_YEASTGEM1genetic
27708008
BUD14_YEASTBUD14genetic
27708008
YD012_YEASTYDL012Cgenetic
27708008
RPN4_YEASTRPN4genetic
27708008
GPR1_YEASTGPR1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
SOK1_YEASTSOK1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
PAC11_YEASTPAC11genetic
27708008
GCN20_YEASTGCN20genetic
27708008
COG7_YEASTCOG7genetic
27708008
AROC_YEASTARO2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
GCN1_YEASTGCN1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
ARP1_YEASTARP1genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
SYS1_YEASTSYS1genetic
27708008
RAV1_YEASTRAV1genetic
27708008
CBF1_YEASTCBF1genetic
27708008
ERG3_YEASTERG3genetic
27708008
RAD10_YEASTRAD10genetic
27708008
YNE6_YEASTYNL046Wgenetic
27708008
RNH2A_YEASTRNH201genetic
27708008
FKBP_YEASTFPR1genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
VAM3_YEASTVAM3genetic
27708008
COQ7_YEASTCAT5genetic
27708008
DGK1_YEASTDGK1genetic
27708008
COX10_YEASTCOX10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL21A_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-71; SER-142 AND THR-143,AND MASS SPECTROMETRY.

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