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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

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-31622-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S22-A
Alternative name(s):
RP50
S24
YP58
YS22
Gene namesi
Name:RPS22A
Synonyms:RPS24, RPS24A
Ordered Locus Names:YJL190C
ORF Names:J0355
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL190C.
SGDiS000003726. RPS22A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 13012940S ribosomal protein S22-APRO_0000126623Add
BLAST

Proteomic databases

PeptideAtlasiP0C0W1.

Interactioni

Subunit structurei

Component of the small 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

BioGridi33573. 134 interactions.
DIPiDIP-5473N.
IntActiP0C0W1. 36 interactions.
MINTiMINT-479211.
STRINGi4932.YJL190C.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1914Combined sources
Beta strandi23 – 297Combined sources
Helixi32 – 4312Combined sources
Beta strandi50 – 534Combined sources
Beta strandi56 – 583Combined sources
Beta strandi60 – 645Combined sources
Beta strandi70 – 745Combined sources
Helixi85 – 939Combined sources
Beta strandi94 – 963Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi109 – 1124Combined sources
Helixi113 – 1197Combined sources
Beta strandi123 – 1308Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0C0W1.
SMRiP0C0W1. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0W1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003021.
HOGENOMiHOG000204097.
InParanoidiP0C0W1.
KOiK02957.
OMAiIGEFEEI.
OrthoDBiEOG7RJQ47.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

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
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[»]
ProteinModelPortaliP0C0W1.
SMRiP0C0W1. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33573. 134 interactions.
DIPiDIP-5473N.
IntActiP0C0W1. 36 interactions.
MINTiMINT-479211.
STRINGi4932.YJL190C.

Proteomic databases

PeptideAtlasiP0C0W1.

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.
OMAiIGEFEEI.
OrthoDBiEOG7RJQ47.

Enzyme and pathway databases

BioCyciYEAST:G3O-31622-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Miscellaneous databases

EvolutionaryTraceiP0C0W1.
NextBioi973490.
PROiP0C0W1.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genes for yeast ribosomal proteins S24 and L46 are adjacent and divergently transcribed."
    Leer R.J., van Raamsdonk-Duin M.M.C., Kraakman P., Mager W.H., Planta R.J.
    Nucleic Acids Res. 13:701-709(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes."
    Purnelle B., Coster F., Goffeau A.
    Yeast 10:1235-1249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Isolation of seventeen proteins and amino-terminal amino acid sequences of eight proteins from cytoplasmic ribosomes of yeast."
    Otaka E., Higo K., Osawa S.
    Biochemistry 21:4545-4550(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-44.
  6. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  7. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
    Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
    J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 4-130, ELECTRON MICROSCOPY.
  10. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRS22A_YEAST
AccessioniPrimary (citable) accession number: P0C0W1
Secondary accession number(s): D6VW01, P04648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 40400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S22 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

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 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.