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Protein

40S ribosomal protein S22-A

Gene

RPS22A

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 40400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for uS8 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-31622-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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:
40S ribosomal protein S22-A1 Publication
Alternative name(s):
RP50
S24
Small ribosomal subunit protein uS8-A1 Publication
YP58
YS22
Gene namesi
Name:RPS22A1 Publication
Synonyms:RPS24, RPS24A
Ordered Locus Names:YJL190C
ORF Names:J0355
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL190C.
SGDiS000003726. RPS22A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001266232 – 13040S ribosomal protein S22-AAdd BLAST129

Proteomic databases

MaxQBiP0C0W1.
PRIDEiP0C0W1.
TopDownProteomicsiP0C0W1.

PTM databases

iPTMnetiP0C0W1.

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

BioGridi33573. 103 interactors.
DIPiDIP-5473N.
IntActiP0C0W1. 38 interactors.
MINTiMINT-479211.

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 19Combined sources14
Beta strandi23 – 29Combined sources7
Helixi32 – 43Combined sources12
Beta strandi50 – 53Combined sources4
Beta strandi56 – 58Combined sources3
Beta strandi60 – 64Combined sources5
Beta strandi70 – 74Combined sources5
Helixi85 – 93Combined sources9
Beta strandi94 – 96Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi101 – 106Combined sources6
Beta strandi109 – 112Combined sources4
Helixi113 – 119Combined sources7
Beta strandi123 – 130Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-H4-130[»]
3J6Xelectron microscopy6.10221-130[»]
3J6Yelectron microscopy6.10221-130[»]
3J77electron microscopy6.20221-130[»]
3J78electron microscopy6.30221-130[»]
3V88X-ray3.00W1-130[»]
4U3MX-ray3.00D2/d22-130[»]
4U3NX-ray3.20D2/d22-130[»]
4U3UX-ray2.90D2/d22-130[»]
4U4NX-ray3.10D2/d22-130[»]
4U4OX-ray3.60D2/d22-130[»]
4U4QX-ray3.00D2/d22-130[»]
4U4RX-ray2.80D2/d22-130[»]
4U4UX-ray3.00D2/d22-130[»]
4U4YX-ray3.20D2/d22-130[»]
4U4ZX-ray3.10D2/d22-130[»]
4U50X-ray3.20D2/d22-130[»]
4U51X-ray3.20D2/d22-130[»]
4U52X-ray3.00D2/d22-130[»]
4U53X-ray3.30D2/d22-130[»]
4U55X-ray3.20D2/d22-130[»]
4U56X-ray3.45D2/d22-130[»]
4U6FX-ray3.10D2/d22-130[»]
4V4Belectron microscopy11.70AH2-130[»]
4V6Ielectron microscopy8.80AH1-130[»]
4V7RX-ray4.00AO/CO1-130[»]
4V88X-ray3.00AW/CW1-130[»]
4V8Yelectron microscopy4.30AW1-130[»]
4V8Zelectron microscopy6.60AW1-130[»]
4V92electron microscopy3.70W2-130[»]
5DATX-ray3.15D22-130[»]
d22-130[»]
5DC3X-ray3.25D2/d22-130[»]
5DGEX-ray3.45D2/d22-130[»]
5DGFX-ray3.30D2/d22-130[»]
5DGVX-ray3.10D2/d22-130[»]
5FCIX-ray3.40D2/d22-130[»]
5FCJX-ray3.10D2/d22-130[»]
5I4LX-ray3.10D2/d22-130[»]
5JPQelectron microscopy7.30z1-130[»]
5JUOelectron microscopy4.00TB1-130[»]
5JUPelectron microscopy3.50TB1-130[»]
5JUSelectron microscopy4.20TB1-130[»]
5JUTelectron microscopy4.00TB1-130[»]
5JUUelectron microscopy4.00TB1-130[»]
5LYBX-ray3.25D2/d22-130[»]
5M1Jelectron microscopy3.30W22-130[»]
5MC6electron microscopy3.80b1-130[»]
5TGAX-ray3.30D2/d22-130[»]
5TGMX-ray3.50D2/d22-130[»]
5TZSelectron microscopy5.10E1-130[»]
5WYJelectron microscopy8.70SX1-130[»]
5WYKelectron microscopy4.50SX1-130[»]
ProteinModelPortaliP0C0W1.
SMRiP0C0W1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0W1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000003021.
HOGENOMiHOG000204097.
InParanoidiP0C0W1.
KOiK02957.
OMAiSHITNSE.
OrthoDBiEOG092C5DJJ.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A. 1 hit.
InterProiView protein in InterPro
IPR000630. Ribosomal_S8.
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiView protein in Pfam
PF00410. Ribosomal_S8. 1 hit.
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiView protein in PROSITE
PS00053. RIBOSOMAL_S8. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0C0W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRSSVLADA LNAINNAEKT GKRQVLIRPS SKVIIKFLQV MQKHGYIGEF
60 70 80 90 100
EYIDDHRSGK IVVQLNGRLN KCGVISPRFN VKIGDIEKWT ANLLPARQFG
110 120 130
YVILTTSAGI MDHEEARRKH VSGKILGFVY
Length:130
Mass (Da):14,626
Last modified:January 23, 2007 - v2
Checksum:iED34BEF6A5442CC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01962 Genomic DNA. Translation: CAA25998.1.
X77688 Genomic DNA. Translation: CAA54770.1.
Z49465 Genomic DNA. Translation: CAA89485.1.
BK006943 Genomic DNA. Translation: DAA08617.1.
PIRiA23082. R4BY24.
RefSeqiNP_012345.1. NM_001181623.1.

Genome annotation databases

EnsemblFungiiYJL190C; YJL190C; YJL190C.
GeneIDi853249.
KEGGisce:YJL190C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01962 Genomic DNA. Translation: CAA25998.1.
X77688 Genomic DNA. Translation: CAA54770.1.
Z49465 Genomic DNA. Translation: CAA89485.1.
BK006943 Genomic DNA. Translation: DAA08617.1.
PIRiA23082. R4BY24.
RefSeqiNP_012345.1. NM_001181623.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-H4-130[»]
3J6Xelectron microscopy6.10221-130[»]
3J6Yelectron microscopy6.10221-130[»]
3J77electron microscopy6.20221-130[»]
3J78electron microscopy6.30221-130[»]
3V88X-ray3.00W1-130[»]
4U3MX-ray3.00D2/d22-130[»]
4U3NX-ray3.20D2/d22-130[»]
4U3UX-ray2.90D2/d22-130[»]
4U4NX-ray3.10D2/d22-130[»]
4U4OX-ray3.60D2/d22-130[»]
4U4QX-ray3.00D2/d22-130[»]
4U4RX-ray2.80D2/d22-130[»]
4U4UX-ray3.00D2/d22-130[»]
4U4YX-ray3.20D2/d22-130[»]
4U4ZX-ray3.10D2/d22-130[»]
4U50X-ray3.20D2/d22-130[»]
4U51X-ray3.20D2/d22-130[»]
4U52X-ray3.00D2/d22-130[»]
4U53X-ray3.30D2/d22-130[»]
4U55X-ray3.20D2/d22-130[»]
4U56X-ray3.45D2/d22-130[»]
4U6FX-ray3.10D2/d22-130[»]
4V4Belectron microscopy11.70AH2-130[»]
4V6Ielectron microscopy8.80AH1-130[»]
4V7RX-ray4.00AO/CO1-130[»]
4V88X-ray3.00AW/CW1-130[»]
4V8Yelectron microscopy4.30AW1-130[»]
4V8Zelectron microscopy6.60AW1-130[»]
4V92electron microscopy3.70W2-130[»]
5DATX-ray3.15D22-130[»]
d22-130[»]
5DC3X-ray3.25D2/d22-130[»]
5DGEX-ray3.45D2/d22-130[»]
5DGFX-ray3.30D2/d22-130[»]
5DGVX-ray3.10D2/d22-130[»]
5FCIX-ray3.40D2/d22-130[»]
5FCJX-ray3.10D2/d22-130[»]
5I4LX-ray3.10D2/d22-130[»]
5JPQelectron microscopy7.30z1-130[»]
5JUOelectron microscopy4.00TB1-130[»]
5JUPelectron microscopy3.50TB1-130[»]
5JUSelectron microscopy4.20TB1-130[»]
5JUTelectron microscopy4.00TB1-130[»]
5JUUelectron microscopy4.00TB1-130[»]
5LYBX-ray3.25D2/d22-130[»]
5M1Jelectron microscopy3.30W22-130[»]
5MC6electron microscopy3.80b1-130[»]
5TGAX-ray3.30D2/d22-130[»]
5TGMX-ray3.50D2/d22-130[»]
5TZSelectron microscopy5.10E1-130[»]
5WYJelectron microscopy8.70SX1-130[»]
5WYKelectron microscopy4.50SX1-130[»]
ProteinModelPortaliP0C0W1.
SMRiP0C0W1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33573. 103 interactors.
DIPiDIP-5473N.
IntActiP0C0W1. 38 interactors.
MINTiMINT-479211.

PTM databases

iPTMnetiP0C0W1.

Proteomic databases

MaxQBiP0C0W1.
PRIDEiP0C0W1.
TopDownProteomicsiP0C0W1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL190C; YJL190C; YJL190C.
GeneIDi853249.
KEGGisce:YJL190C.

Organism-specific databases

EuPathDBiFungiDB:YJL190C.
SGDiS000003726. RPS22A.

Phylogenomic databases

GeneTreeiENSGT00390000003021.
HOGENOMiHOG000204097.
InParanoidiP0C0W1.
KOiK02957.
OMAiSHITNSE.
OrthoDBiEOG092C5DJJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31622-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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

EvolutionaryTraceiP0C0W1.
PROiPR:P0C0W1.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A. 1 hit.
InterProiView protein in InterPro
IPR000630. Ribosomal_S8.
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiView protein in Pfam
PF00410. Ribosomal_S8. 1 hit.
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiView protein in PROSITE
PS00053. RIBOSOMAL_S8. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRS22A_YEAST
AccessioniPrimary (citable) accession number: P0C0W1
Secondary accession number(s): D6VW01, P04648
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 101 of the entry and version 2 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.