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Protein

60S ribosomal protein L21-A

Gene

RPL21A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Miscellaneous

There are 2 genes for eL21 in yeast.Curated

GO - Molecular functioni

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-29133-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L21-A1 Publication
Alternative name(s):
Large ribosomal subunit protein eL21-A1 Publication
Gene namesi
Name:RPL21A1 Publication
Synonyms:URP1
Ordered Locus Names:YBR191W
ORF Names:YBR1401
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR191W.
SGDiS000000395. RPL21A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001496822 – 16060S ribosomal protein L21-AAdd BLAST159

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ02753.
PRIDEiQ02753.

PTM databases

iPTMnetiQ02753.

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi32888. 69 interactors.
IntActiQ02753. 7 interactors.
MINTiMINT-1324156.
STRINGi4932.YBR191W.

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 10Combined sources4
Turni12 – 14Combined sources3
Helixi28 – 31Combined sources4
Beta strandi39 – 42Combined sources4
Helixi55 – 57Combined sources3
Beta strandi61 – 67Combined sources7
Beta strandi69 – 80Combined sources12
Beta strandi83 – 92Combined sources10
Helixi93 – 95Combined sources3
Beta strandi96 – 98Combined sources3
Helixi100 – 102Combined sources3
Helixi103 – 120Combined sources18
Turni121 – 123Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-Q4-100[»]
3J6Xelectron microscopy6.10611-160[»]
3J6Yelectron microscopy6.10611-160[»]
3J77electron microscopy6.20711-160[»]
3J78electron microscopy6.30711-160[»]
3JCTelectron microscopy3.08T1-160[»]
4U3MX-ray3.00N1/n12-160[»]
4U3NX-ray3.20N1/n12-160[»]
4U3UX-ray2.90N1/n12-160[»]
4U4NX-ray3.10N1/n12-160[»]
4U4OX-ray3.60N1/n12-160[»]
4U4QX-ray3.00N1/n12-160[»]
4U4RX-ray2.80N1/n12-160[»]
4U4UX-ray3.00N1/n12-160[»]
4U4YX-ray3.20N1/n12-160[»]
4U4ZX-ray3.10N1/n12-160[»]
4U50X-ray3.20N1/n12-160[»]
4U51X-ray3.20N1/n12-160[»]
4U52X-ray3.00N1/n12-160[»]
4U53X-ray3.30N1/n12-160[»]
4U55X-ray3.20N1/n12-160[»]
4U56X-ray3.45N1/n12-160[»]
4U6FX-ray3.10N1/n12-160[»]
4V4Belectron microscopy11.70BQ1-100[»]
4V6Ielectron microscopy8.80BU1-160[»]
4V7Felectron microscopy8.70T1-160[»]
4V7RX-ray4.00BT/DT1-160[»]
4V88X-ray3.00BT/DT1-160[»]
4V8Telectron microscopy8.10T1-160[»]
4V8Yelectron microscopy4.30BT2-160[»]
4V8Zelectron microscopy6.60BT2-160[»]
4V91electron microscopy3.70T1-160[»]
5APNelectron microscopy3.91T1-160[»]
5APOelectron microscopy3.41T1-160[»]
5DATX-ray3.15N1/n12-160[»]
5DC3X-ray3.25N1/n12-160[»]
5DGEX-ray3.45N1/n12-160[»]
5DGFX-ray3.30N1/n12-160[»]
5DGVX-ray3.10N1/n12-160[»]
5FCIX-ray3.40N1/n12-160[»]
5FCJX-ray3.10N1/n12-160[»]
5FL8electron microscopy9.50T1-160[»]
5GAKelectron microscopy3.88V1-160[»]
5H4Pelectron microscopy3.07T1-160[»]
5I4LX-ray3.10N1/n12-160[»]
5JCSelectron microscopy9.50T1-160[»]
5JUOelectron microscopy4.00Y1-160[»]
5JUPelectron microscopy3.50Y1-160[»]
5JUSelectron microscopy4.20Y1-160[»]
5JUTelectron microscopy4.00Y1-160[»]
5JUUelectron microscopy4.00Y1-160[»]
5LYBX-ray3.25N1/n12-160[»]
5M1Jelectron microscopy3.30T52-160[»]
5MC6electron microscopy3.80BJ1-160[»]
5T62electron microscopy3.30g1-160[»]
5T6Relectron microscopy4.50g1-160[»]
5TGAX-ray3.30N1/n12-160[»]
5TGMX-ray3.50N1/n12-160[»]
ProteinModelPortaliQ02753.
SMRiQ02753.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02753.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000001293.
HOGENOMiHOG000194513.
InParanoidiQ02753.
KOiK02889.
OMAiHVKHSKS.
OrthoDBiEOG092C537Y.

Family and domain databases

Gene3Di2.30.30.70. 1 hit.
InterProiView protein in InterPro
IPR001147. Ribosomal_L21e.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
PANTHERiPTHR20981. PTHR20981. 1 hit.
PfamiView protein in Pfam
PF01157. Ribosomal_L21e. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiView protein in PROSITE
PS01171. RIBOSOMAL_L21E. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSHGYRSR TRYMFQRDFR KHGAVHLSTY LKVYKVGDIV DIKANGSIQK
60 70 80 90 100
GMPHKFYQGK TGVVYNVTKS SVGVIINKMV GNRYLEKRLN LRVEHIKHSK
110 120 130 140 150
CRQEFLERVK ANAAKRAEAK AQGVAVQLKR QPAQPRESRI VSTEGNVPQT
160
LAPVPYETFI
Length:160
Mass (Da):18,242
Last modified:July 1, 1993 - v1
Checksum:i45286521C8473A72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86408 Genomic DNA. Translation: AAA35202.1.
Z36059 Genomic DNA. Translation: CAA85153.1.
Z21487 Genomic DNA. Translation: CAA79677.1.
U02073 Genomic DNA. Translation: AAB60284.1.
BK006936 Genomic DNA. Translation: DAA07305.1.
PIRiS28921.
RefSeqiNP_009750.1. NM_001178539.1.

Genome annotation databases

EnsemblFungiiYBR191W; YBR191W; YBR191W.
GeneIDi852489.
KEGGisce:YBR191W.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiRL21A_YEAST
AccessioniPrimary (citable) accession number: Q02753
Secondary accession number(s): D6VQI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 5, 2017
This is version 149 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names