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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: -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

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP0C0W1
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, 104 interactors
DIPiDIP-5473N
IntActiP0C0W1, 38 interactors
MINTiP0C0W1
STRINGi4932.YJL190C

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[»]
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[»]
5LL6electron microscopy3.90b1-130[»]
5LYBX-ray3.25D2/d22-130[»]
5M1Jelectron microscopy3.30W22-130[»]
5MC6electron microscopy3.80b1-130[»]
5MEIX-ray3.50X/d22-130[»]
5NDGX-ray3.70D2/d22-130[»]
5NDVX-ray3.30D2/d22-130[»]
5NDWX-ray3.70D2/d22-130[»]
5OBMX-ray3.40D2/d22-130[»]
5ON6X-ray3.10X/d22-130[»]
5TBWX-ray3.00X/d22-130[»]
5TGAX-ray3.30D2/d22-130[»]
5TGMX-ray3.50D2/d22-130[»]
5TZSelectron microscopy5.10E1-130[»]
5WLCelectron microscopy3.80LE1-130[»]
5WYJelectron microscopy8.70SX1-130[»]
5WYKelectron microscopy4.50SX1-130[»]
6EMLelectron microscopy3.60b1-130[»]
6FAIelectron microscopy3.40W1-130[»]
ProteinModelPortaliP0C0W1
SMRiP0C0W1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0W1

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000003021
HOGENOMiHOG000204097
InParanoidiP0C0W1
KOiK02957
OMAiYGIMDHE
OrthoDBiEOG092C5DJJ

Family and domain databases

HAMAPiMF_01302_A Ribosomal_S8_A, 1 hit
InterProiView protein in InterPro
IPR000630 Ribosomal_S8
IPR035987 Ribosomal_S8_sf
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

Similar proteinsi

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: April 25, 2018
This is version 110 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
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Main funding by: National Institutes of Health