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Protein

40S ribosomal protein S29-A

Gene

RPS29A

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

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211ZincSequence Analysis
Metal bindingi24 – 241ZincSequence Analysis
Metal bindingi39 – 391ZincSequence Analysis
Metal bindingi42 – 421ZincSequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32454-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 S29-A
Alternative name(s):
S36
YS29
Gene namesi
Name:RPS29A
Synonyms:RPS36A, YS29A
Ordered Locus Names:YLR388W
ORF Names:L8084.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR388W.
SGDiS000004380. RPS29A.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. 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 – 565540S ribosomal protein S29-APRO_0000131032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41057.
PeptideAtlasiP41057.
PRIDEiP41057.

Expressioni

Gene expression databases

GenevestigatoriP41057.

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

BioGridi31647. 49 interactions.
DIPiDIP-4643N.
IntActiP41057. 4 interactions.
MINTiMINT-475802.

Structurei

Secondary structure

1
56
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi13 – 153Combined sources
Helixi16 – 183Combined sources
Turni22 – 243Combined sources
Beta strandi28 – 314Combined sources
Helixi33 – 353Combined sources
Helixi40 – 5011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10291-56[»]
3J6Yelectron microscopy6.10291-56[»]
3J77electron microscopy6.20291-56[»]
3J78electron microscopy6.30291-56[»]
3V88X-ray3.00d1-56[»]
4U3MX-ray3.00D9/d92-56[»]
4U3NX-ray3.20D9/d92-56[»]
4U3UX-ray2.90D9/d92-56[»]
4U4NX-ray3.10D9/d92-56[»]
4U4OX-ray3.60D9/d92-56[»]
4U4QX-ray3.00D9/d92-56[»]
4U4RX-ray2.80D9/d92-56[»]
4U4UX-ray3.00D9/d92-56[»]
4U4YX-ray3.20D9/d92-56[»]
4U4ZX-ray3.10D9/d92-56[»]
4U50X-ray3.20D9/d92-56[»]
4U51X-ray3.20D9/d92-56[»]
4U52X-ray3.00D9/d92-56[»]
4U53X-ray3.30D9/d92-56[»]
4U55X-ray3.20D9/d92-56[»]
4U56X-ray3.45D9/d92-56[»]
4U6FX-ray3.10D9/d92-56[»]
4V6Ielectron microscopy8.80AN1-56[»]
4V7RX-ray4.00AS/CS1-56[»]
4V88X-ray3.00Ad/Cd1-56[»]
4V8Yelectron microscopy4.30A31-56[»]
4V8Zelectron microscopy6.60A31-56[»]
ProteinModelPortaliP41057.
SMRiP41057. Positions 4-56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S14P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005814.
HOGENOMiHOG000231300.
InParanoidiP41057.
KOiK02980.
OMAiCFREKAA.
OrthoDBiEOG7SV17Z.

Family and domain databases

InterProiIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P41057-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHENVWFSH PRRYGKGSRQ CRVCSSHTGL IRKYGLNICR QCFREKANDI

GFNKFR
Length:56
Mass (Da):6,661
Last modified:January 23, 2007 - v3
Checksum:iF1A6900EE27748C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71W → G AA sequence (PubMed:18782943).Curated
Sequence conflicti14 – 141Y → F in ABM97475 (PubMed:17244705).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14676 Genomic DNA. Translation: BAA03507.1.
U19729 Genomic DNA. Translation: AAB82350.1.
EF123131 mRNA. Translation: ABM97475.1.
BK006945 Genomic DNA. Translation: DAA09689.1.
PIRiS48503.
RefSeqiNP_013492.3. NM_001182277.3.

Genome annotation databases

EnsemblFungiiYLR388W; YLR388W; YLR388W.
GeneIDi851104.
KEGGisce:YLR388W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14676 Genomic DNA. Translation: BAA03507.1.
U19729 Genomic DNA. Translation: AAB82350.1.
EF123131 mRNA. Translation: ABM97475.1.
BK006945 Genomic DNA. Translation: DAA09689.1.
PIRiS48503.
RefSeqiNP_013492.3. NM_001182277.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10291-56[»]
3J6Yelectron microscopy6.10291-56[»]
3J77electron microscopy6.20291-56[»]
3J78electron microscopy6.30291-56[»]
3V88X-ray3.00d1-56[»]
4U3MX-ray3.00D9/d92-56[»]
4U3NX-ray3.20D9/d92-56[»]
4U3UX-ray2.90D9/d92-56[»]
4U4NX-ray3.10D9/d92-56[»]
4U4OX-ray3.60D9/d92-56[»]
4U4QX-ray3.00D9/d92-56[»]
4U4RX-ray2.80D9/d92-56[»]
4U4UX-ray3.00D9/d92-56[»]
4U4YX-ray3.20D9/d92-56[»]
4U4ZX-ray3.10D9/d92-56[»]
4U50X-ray3.20D9/d92-56[»]
4U51X-ray3.20D9/d92-56[»]
4U52X-ray3.00D9/d92-56[»]
4U53X-ray3.30D9/d92-56[»]
4U55X-ray3.20D9/d92-56[»]
4U56X-ray3.45D9/d92-56[»]
4U6FX-ray3.10D9/d92-56[»]
4V6Ielectron microscopy8.80AN1-56[»]
4V7RX-ray4.00AS/CS1-56[»]
4V88X-ray3.00Ad/Cd1-56[»]
4V8Yelectron microscopy4.30A31-56[»]
4V8Zelectron microscopy6.60A31-56[»]
ProteinModelPortaliP41057.
SMRiP41057. Positions 4-56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31647. 49 interactions.
DIPiDIP-4643N.
IntActiP41057. 4 interactions.
MINTiMINT-475802.

Proteomic databases

MaxQBiP41057.
PeptideAtlasiP41057.
PRIDEiP41057.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR388W; YLR388W; YLR388W.
GeneIDi851104.
KEGGisce:YLR388W.

Organism-specific databases

EuPathDBiFungiDB:YLR388W.
SGDiS000004380. RPS29A.

Phylogenomic databases

GeneTreeiENSGT00390000005814.
HOGENOMiHOG000231300.
InParanoidiP41057.
KOiK02980.
OMAiCFREKAA.
OrthoDBiEOG7SV17Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-32454-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

NextBioi967800.
PROiP41057.

Gene expression databases

GenevestigatoriP41057.

Family and domain databases

InterProiIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S.cerevisiae YS29A gene for ribosomal protein YS29."
    Suzuki K., Otaka E.
    Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing."
    Juneau K., Palm C., Miranda M., Davis R.W.
    Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-20.
    Strain: ATCC 201390 / BY4743.
  5. "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes."
    Otaka E., Higo K., Itoh T.
    Mol. Gen. Genet. 195:544-546(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE.
  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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS29A_YEAST
AccessioniPrimary (citable) accession number: P41057
Secondary accession number(s): A2TBM8, D6VZ23, P05761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 120 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 6490 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S29 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

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.