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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: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, 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-A
Alternative name(s):
L1c
RP4
YL31
Gene namesi
Name:RPL22A
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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 12112060S ribosomal protein L22-APRO_0000215514Add
BLAST

Proteomic databases

MaxQBiP05749.
TopDownProteomicsiP05749.

PTM databases

iPTMnetiP05749.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi31336. 95 interactions.
IntActiP05749. 5 interactions.
MINTiMINT-4494605.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Helixi20 – 234Combined sources
Turni24 – 263Combined sources
Helixi30 – 389Combined sources
Beta strandi42 – 454Combined sources
Beta strandi46 – 483Combined sources
Turni49 – 535Combined sources
Beta strandi54 – 585Combined sources
Beta strandi60 – 7011Combined sources
Helixi73 – 8614Combined sources
Turni90 – 923Combined sources
Beta strandi94 – 996Combined sources
Beta strandi102 – 1065Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5DC3X-ray3.25N2/n22-121[»]
5FCIX-ray3.40N2/n22-121[»]
5FCJX-ray3.10N2/n22-121[»]
5FL8electron microscopy9.50U1-121[»]
5GAKelectron microscopy3.88W1-121[»]
5I4LX-ray3.10N2/n29-108[»]
ProteinModelPortaliP05749.
SMRiP05749. Positions 9-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22e family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003719.
HOGENOMiHOG000198396.
InParanoidiP05749.
KOiK02891.
OrthoDBiEOG092C5FK9.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491N → D AA sequence (PubMed:6814480).Curated

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
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[»]
5DC3X-ray3.25N2/n22-121[»]
5FCIX-ray3.40N2/n22-121[»]
5FCJX-ray3.10N2/n22-121[»]
5FL8electron microscopy9.50U1-121[»]
5GAKelectron microscopy3.88W1-121[»]
5I4LX-ray3.10N2/n29-108[»]
ProteinModelPortaliP05749.
SMRiP05749. Positions 9-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31336. 95 interactions.
IntActiP05749. 5 interactions.
MINTiMINT-4494605.

PTM databases

iPTMnetiP05749.

Proteomic databases

MaxQBiP05749.
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

PROiP05749.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL22A_YEAST
AccessioniPrimary (citable) accession number: P05749
Secondary accession number(s): D6VY63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 60400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for L22 in yeast.

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.