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Protein

40S ribosomal protein S24-A

Gene

RPS24A

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

  • nucleotide binding Source: InterPro
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30245-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 S24-A
Alternative name(s):
RP50
Gene namesi
Name:RPS24A
Synonyms:RPS24EA
Ordered Locus Names:YER074W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

SGDiS000000876. RPS24A.

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 methionineiRemovedCombined sources2 Publications
Chaini2 – 13513440S ribosomal protein S24-APRO_0000137636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources2 Publications
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineCombined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA. Also partially acetylated by NatC.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP0CX31.
TopDownProteomicsiP0CX31.

PTM databases

iPTMnetiP0CX31.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX31. differential.

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

BioGridi34923. 76 interactions.
36817. 127 interactions.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi16 – 183Combined sources
Beta strandi20 – 289Combined sources
Beta strandi30 – 323Combined sources
Helixi37 – 459Combined sources
Turni46 – 494Combined sources
Helixi52 – 543Combined sources
Beta strandi55 – 628Combined sources
Beta strandi66 – 7712Combined sources
Helixi79 – 857Combined sources
Helixi88 – 947Combined sources
Beta strandi95 – 973Combined sources
Helixi105 – 11511Combined sources
Beta strandi120 – 1223Combined sources
Helixi123 – 13210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-D1-135[»]
3J6Xelectron microscopy6.10241-135[»]
3J6Yelectron microscopy6.10241-135[»]
3J77electron microscopy6.20241-135[»]
3J78electron microscopy6.30241-135[»]
3V88X-ray3.00Y1-135[»]
4U3MX-ray3.00D4/d42-135[»]
4U3NX-ray3.20D4/d42-135[»]
4U3UX-ray2.90D4/d42-135[»]
4U4NX-ray3.10D4/d42-135[»]
4U4OX-ray3.60D4/d42-135[»]
4U4QX-ray3.00D4/d42-135[»]
4U4RX-ray2.80D4/d42-135[»]
4U4UX-ray3.00D4/d42-135[»]
4U4YX-ray3.20D4/d42-135[»]
4U4ZX-ray3.10D4/d42-135[»]
4U50X-ray3.20D4/d42-135[»]
4U51X-ray3.20D4/d42-135[»]
4U52X-ray3.00D4/d42-135[»]
4U53X-ray3.30D4/d42-135[»]
4U55X-ray3.20D4/d42-135[»]
4U56X-ray3.45D4/d42-135[»]
4U6FX-ray3.10D4/d42-135[»]
4V6Ielectron microscopy8.80AU1-135[»]
4V88X-ray3.00AY/CY1-135[»]
4V8Yelectron microscopy4.30AY1-135[»]
4V8Zelectron microscopy6.60AY1-135[»]
4V92electron microscopy3.70Y2-135[»]
ProteinModelPortaliP0CX31.
SMRiP0CX31. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S24e family.Curated

Phylogenomic databases

HOGENOMiHOG000186306.
InParanoidiP0CX31.
KOiK02974.
OrthoDBiEOG7ZD27J.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_00545. Ribosomal_S24e.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001976. Ribosomal_S24e.
IPR018098. Ribosomal_S24e_CS.
[Graphical view]
PANTHERiPTHR10496. PTHR10496. 1 hit.
PfamiPF01282. Ribosomal_S24e. 1 hit.
[Graphical view]
ProDomiPD006052. Ribosomal_S24e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00529. RIBOSOMAL_S24E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAVTIRTR KVISNPLLAR KQFVVDVLHP NRANVSKDEL REKLAEVYKA
60 70 80 90 100
EKDAVSVFGF RTQFGGGKSV GFGLVYNSVA EAKKFEPTYR LVRYGLAEKV
110 120 130
EKASRQQRKQ KKNRDKKIFG TGKRLAKKVA RRNAD
Length:135
Mass (Da):15,329
Last modified:June 28, 2011 - v1
Checksum:i81B82D361207442A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161P → D AA sequence (PubMed:1544921).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18814 Genomic DNA. Translation: AAB64613.1.
BK006939 Genomic DNA. Translation: DAA07733.1.
PIRiS48410.
RefSeqiNP_010997.3. NM_001178965.3.
NP_012195.1. NM_001179419.1.

Genome annotation databases

EnsemblFungiiYER074W; YER074W; YER074W.
YIL069C; YIL069C; YIL069C.
GeneIDi854741.
856805.
KEGGisce:YER074W.
sce:YIL069C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18814 Genomic DNA. Translation: AAB64613.1.
BK006939 Genomic DNA. Translation: DAA07733.1.
PIRiS48410.
RefSeqiNP_010997.3. NM_001178965.3.
NP_012195.1. NM_001179419.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-D1-135[»]
3J6Xelectron microscopy6.10241-135[»]
3J6Yelectron microscopy6.10241-135[»]
3J77electron microscopy6.20241-135[»]
3J78electron microscopy6.30241-135[»]
3V88X-ray3.00Y1-135[»]
4U3MX-ray3.00D4/d42-135[»]
4U3NX-ray3.20D4/d42-135[»]
4U3UX-ray2.90D4/d42-135[»]
4U4NX-ray3.10D4/d42-135[»]
4U4OX-ray3.60D4/d42-135[»]
4U4QX-ray3.00D4/d42-135[»]
4U4RX-ray2.80D4/d42-135[»]
4U4UX-ray3.00D4/d42-135[»]
4U4YX-ray3.20D4/d42-135[»]
4U4ZX-ray3.10D4/d42-135[»]
4U50X-ray3.20D4/d42-135[»]
4U51X-ray3.20D4/d42-135[»]
4U52X-ray3.00D4/d42-135[»]
4U53X-ray3.30D4/d42-135[»]
4U55X-ray3.20D4/d42-135[»]
4U56X-ray3.45D4/d42-135[»]
4U6FX-ray3.10D4/d42-135[»]
4V6Ielectron microscopy8.80AU1-135[»]
4V88X-ray3.00AY/CY1-135[»]
4V8Yelectron microscopy4.30AY1-135[»]
4V8Zelectron microscopy6.60AY1-135[»]
4V92electron microscopy3.70Y2-135[»]
ProteinModelPortaliP0CX31.
SMRiP0CX31. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34923. 76 interactions.
36817. 127 interactions.

PTM databases

iPTMnetiP0CX31.

Proteomic databases

MaxQBiP0CX31.
TopDownProteomicsiP0CX31.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER074W; YER074W; YER074W.
YIL069C; YIL069C; YIL069C.
GeneIDi854741.
856805.
KEGGisce:YER074W.
sce:YIL069C.

Organism-specific databases

SGDiS000000876. RPS24A.

Phylogenomic databases

HOGENOMiHOG000186306.
InParanoidiP0CX31.
KOiK02974.
OrthoDBiEOG7ZD27J.

Enzyme and pathway databases

BioCyciYEAST:G3O-30245-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

NextBioi977455.
PROiP0CX31.

Gene expression databases

ExpressionAtlasiP0CX31. differential.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_00545. Ribosomal_S24e.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001976. Ribosomal_S24e.
IPR018098. Ribosomal_S24e_CS.
[Graphical view]
PANTHERiPTHR10496. PTHR10496. 1 hit.
PfamiPF01282. Ribosomal_S24e. 1 hit.
[Graphical view]
ProDomiPD006052. Ribosomal_S24e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00529. RIBOSOMAL_S24E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
    Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
    J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, ACETYLATION AT SER-2 BY NATA.
  4. "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.
  5. "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, ACETYLATION AT SER-2 BY NATA.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS24A_YEAST
AccessioniPrimary (citable) accession number: P0CX31
Secondary accession number(s): D3DLX9, P26782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 13, 2016
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for S24 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.