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Protein

60S ribosomal protein L22-A

Gene

RPL22A

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

Present with 60400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL22 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32215-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 L22-A1 Publication
Alternative name(s):
L1c
Large ribosomal subunit protein eL22-A1 Publication
RP4
YL31
Gene namesi
Name:RPL22A1 Publication
Ordered Locus Names:YLR061W
ORF Names:L2168
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR061W.
SGDiS000004051. RPL22A.

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 methionineiRemoved2 Publications
ChainiPRO_00002155142 – 12160S ribosomal protein L22-AAdd BLAST120

Proteomic databases

MaxQBiP05749.
PRIDEiP05749.
TopDownProteomicsiP05749.

PTM databases

iPTMnetiP05749.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). 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

BioGridi31336. 378 interactors.
IntActiP05749. 5 interactors.
MINTiMINT-4494605.

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 18Combined sources6
Helixi20 – 23Combined sources4
Turni24 – 26Combined sources3
Helixi30 – 38Combined sources9
Beta strandi42 – 45Combined sources4
Beta strandi46 – 48Combined sources3
Turni49 – 53Combined sources5
Beta strandi54 – 58Combined sources5
Beta strandi60 – 70Combined sources11
Helixi73 – 86Combined sources14
Turni90 – 92Combined sources3
Beta strandi94 – 99Combined sources6
Beta strandi102 – 106Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10621-121[»]
3J6Yelectron microscopy6.10621-121[»]
3J77electron microscopy6.20721-121[»]
3J78electron microscopy6.30721-121[»]
3JCTelectron microscopy3.08U1-121[»]
4U3MX-ray3.00N2/n22-121[»]
4U3NX-ray3.20N2/n22-121[»]
4U3UX-ray2.90N2/n22-121[»]
4U4NX-ray3.10N2/n22-121[»]
4U4OX-ray3.60N2/n22-121[»]
4U4QX-ray3.00N2/n22-121[»]
4U4RX-ray2.80N2/n22-121[»]
4U4UX-ray3.00N2/n22-121[»]
4U4YX-ray3.20N2/n22-121[»]
4U4ZX-ray3.10N2/n22-121[»]
4U50X-ray3.20N2/n22-121[»]
4U51X-ray3.20N2/n22-121[»]
4U52X-ray3.00N2/n22-121[»]
4U53X-ray3.30N2/n22-121[»]
4U55X-ray3.20N2/n22-121[»]
4U56X-ray3.45N2/n22-121[»]
4U6FX-ray3.10N2/n22-121[»]
4V6Ielectron microscopy8.80BW1-121[»]
4V7Felectron microscopy8.70V1-121[»]
4V88X-ray3.00BU/DU1-121[»]
4V8Telectron microscopy8.10U1-121[»]
4V8Yelectron microscopy4.30BU2-121[»]
4V8Zelectron microscopy6.60BU2-121[»]
4V91electron microscopy3.70U1-121[»]
5APNelectron microscopy3.91U1-121[»]
5APOelectron microscopy3.41U1-121[»]
5DATX-ray3.15N2/n22-121[»]
5DC3X-ray3.25N2/n22-121[»]
5DGEX-ray3.45N2/n22-121[»]
5DGFX-ray3.30N2/n22-121[»]
5DGVX-ray3.10N2/n22-121[»]
5FCIX-ray3.40N2/n22-121[»]
5FCJX-ray3.10N2/n22-121[»]
5FL8electron microscopy9.50U1-121[»]
5GAKelectron microscopy3.88W1-121[»]
5H4Pelectron microscopy3.07U1-121[»]
5I4LX-ray3.10N2/n29-108[»]
5JCSelectron microscopy9.50U1-121[»]
5JUOelectron microscopy4.00Z1-121[»]
5JUPelectron microscopy3.50Z1-121[»]
5JUSelectron microscopy4.20Z1-121[»]
5JUTelectron microscopy4.00Z1-121[»]
5JUUelectron microscopy4.00Z1-121[»]
5LYBX-ray3.25N2/n29-108[»]
5M1Jelectron microscopy3.30U59-108[»]
5MC6electron microscopy3.80BL1-121[»]
5T62electron microscopy3.30h1-121[»]
5T6Relectron microscopy4.50h1-121[»]
5TGAX-ray3.30N2/n29-108[»]
5TGMX-ray3.50N2/n29-108[»]
ProteinModelPortaliP05749.
SMRiP05749.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000003719.
HOGENOMiHOG000198396.
InParanoidiP05749.
KOiK02891.
OrthoDBiEOG092C5FK9.

Family and domain databases

InterProiView protein in InterPro
IPR002671. Ribosomal_L22e.
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiView protein in Pfam
PF01776. Ribosomal_L22e. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPNTSRKQK IAKTFTVDVS SPTENGVFDP ASYAKYLIDH IKVEGAVGNL
60 70 80 90 100
GNAVTVTEDG TVVTVVSTAK FSGKYLKYLT KKYLKKNQLR DWIRFVSTKT
110 120
NEYRLAFYQV TPEEDEEEDE E
Length:121
Mass (Da):13,693
Last modified:January 23, 2007 - v3
Checksum:iAFF542E484A52069
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49N → D AA sequence (PubMed:6814480).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94607 Genomic DNA. Translation: CAA64308.1.
Z73233 Genomic DNA. Translation: CAA97592.1.
BK006945 Genomic DNA. Translation: DAA09379.1.
PIRiS61635.
RefSeqiNP_013162.1. NM_001181948.1.

Genome annotation databases

EnsemblFungiiYLR061W; YLR061W; YLR061W.
GeneIDi850750.
KEGGisce:YLR061W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94607 Genomic DNA. Translation: CAA64308.1.
Z73233 Genomic DNA. Translation: CAA97592.1.
BK006945 Genomic DNA. Translation: DAA09379.1.
PIRiS61635.
RefSeqiNP_013162.1. NM_001181948.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10621-121[»]
3J6Yelectron microscopy6.10621-121[»]
3J77electron microscopy6.20721-121[»]
3J78electron microscopy6.30721-121[»]
3JCTelectron microscopy3.08U1-121[»]
4U3MX-ray3.00N2/n22-121[»]
4U3NX-ray3.20N2/n22-121[»]
4U3UX-ray2.90N2/n22-121[»]
4U4NX-ray3.10N2/n22-121[»]
4U4OX-ray3.60N2/n22-121[»]
4U4QX-ray3.00N2/n22-121[»]
4U4RX-ray2.80N2/n22-121[»]
4U4UX-ray3.00N2/n22-121[»]
4U4YX-ray3.20N2/n22-121[»]
4U4ZX-ray3.10N2/n22-121[»]
4U50X-ray3.20N2/n22-121[»]
4U51X-ray3.20N2/n22-121[»]
4U52X-ray3.00N2/n22-121[»]
4U53X-ray3.30N2/n22-121[»]
4U55X-ray3.20N2/n22-121[»]
4U56X-ray3.45N2/n22-121[»]
4U6FX-ray3.10N2/n22-121[»]
4V6Ielectron microscopy8.80BW1-121[»]
4V7Felectron microscopy8.70V1-121[»]
4V88X-ray3.00BU/DU1-121[»]
4V8Telectron microscopy8.10U1-121[»]
4V8Yelectron microscopy4.30BU2-121[»]
4V8Zelectron microscopy6.60BU2-121[»]
4V91electron microscopy3.70U1-121[»]
5APNelectron microscopy3.91U1-121[»]
5APOelectron microscopy3.41U1-121[»]
5DATX-ray3.15N2/n22-121[»]
5DC3X-ray3.25N2/n22-121[»]
5DGEX-ray3.45N2/n22-121[»]
5DGFX-ray3.30N2/n22-121[»]
5DGVX-ray3.10N2/n22-121[»]
5FCIX-ray3.40N2/n22-121[»]
5FCJX-ray3.10N2/n22-121[»]
5FL8electron microscopy9.50U1-121[»]
5GAKelectron microscopy3.88W1-121[»]
5H4Pelectron microscopy3.07U1-121[»]
5I4LX-ray3.10N2/n29-108[»]
5JCSelectron microscopy9.50U1-121[»]
5JUOelectron microscopy4.00Z1-121[»]
5JUPelectron microscopy3.50Z1-121[»]
5JUSelectron microscopy4.20Z1-121[»]
5JUTelectron microscopy4.00Z1-121[»]
5JUUelectron microscopy4.00Z1-121[»]
5LYBX-ray3.25N2/n29-108[»]
5M1Jelectron microscopy3.30U59-108[»]
5MC6electron microscopy3.80BL1-121[»]
5T62electron microscopy3.30h1-121[»]
5T6Relectron microscopy4.50h1-121[»]
5TGAX-ray3.30N2/n29-108[»]
5TGMX-ray3.50N2/n29-108[»]
ProteinModelPortaliP05749.
SMRiP05749.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31336. 378 interactors.
IntActiP05749. 5 interactors.
MINTiMINT-4494605.

PTM databases

iPTMnetiP05749.

Proteomic databases

MaxQBiP05749.
PRIDEiP05749.
TopDownProteomicsiP05749.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR061W; YLR061W; YLR061W.
GeneIDi850750.
KEGGisce:YLR061W.

Organism-specific databases

EuPathDBiFungiDB:YLR061W.
SGDiS000004051. RPL22A.

Phylogenomic databases

GeneTreeiENSGT00390000003719.
HOGENOMiHOG000198396.
InParanoidiP05749.
KOiK02891.
OrthoDBiEOG092C5FK9.

Enzyme and pathway databases

BioCyciYEAST:G3O-32215-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).

Miscellaneous databases

PROiPR:P05749.

Family and domain databases

InterProiView protein in InterPro
IPR002671. Ribosomal_L22e.
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiView protein in Pfam
PF01776. Ribosomal_L22e. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL22A_YEAST
AccessioniPrimary (citable) accession number: P05749
Secondary accession number(s): D6VY63
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 141 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.