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Protein

40S ribosomal protein S14-A

Gene

RPS14A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.1 Publication

GO - Molecular functioni

  • mRNA binding Source: SGD
  • 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
  • ribosomal small subunit assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-29345-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 S14-A
Alternative name(s):
RP59A
Gene namesi
Name:RPS14A
Synonyms:CRY1, RPL59
Ordered Locus Names:YCR031C
ORF Names:YCR31C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR031C.
SGDiS000000627. RPS14A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
  • nucleolus Source: UniProtKB-SubCell
  • small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 13713640S ribosomal protein S14-APRO_0000123359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP06367.

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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.2 Publications

Protein-protein interaction databases

BioGridi31014. 141 interactions.
IntActiP06367. 22 interactions.
MINTiMINT-4083975.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Beta strandi19 – 224Combined sources
Beta strandi25 – 284Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 395Combined sources
Turni44 – 463Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 7418Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Helixi96 – 983Combined sources
Helixi99 – 1068Combined sources
Turni107 – 1093Combined sources
Beta strandi111 – 1177Combined sources
Turni131 – 1333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-K9-133[»]
3J6Xelectron microscopy6.10141-137[»]
3J6Yelectron microscopy6.10141-137[»]
3J77electron microscopy6.20141-137[»]
3J78electron microscopy6.30141-137[»]
3V88X-ray3.00O1-137[»]
4U3MX-ray3.00C4/c42-137[»]
4U3NX-ray3.20C4/c42-137[»]
4U3UX-ray2.90C4/c42-137[»]
4U4NX-ray3.10C4/c42-137[»]
4U4OX-ray3.60C4/c42-137[»]
4U4QX-ray3.00C4/c42-137[»]
4U4RX-ray2.80C4/c42-137[»]
4U4UX-ray3.00C4/c42-137[»]
4U4YX-ray3.20C4/c42-137[»]
4U4ZX-ray3.10C4/c42-137[»]
4U50X-ray3.20C4/c42-137[»]
4U51X-ray3.20C4/c42-137[»]
4U52X-ray3.00C4/c42-137[»]
4U53X-ray3.30C4/c42-137[»]
4U55X-ray3.20C4/c42-137[»]
4U56X-ray3.45C4/c42-137[»]
4U6FX-ray3.10C4/c42-137[»]
4V4Belectron microscopy11.70AK2-137[»]
4V6Ielectron microscopy8.80AK1-137[»]
4V7RX-ray4.00AH/CH1-137[»]
4V88X-ray3.00AO/CO1-137[»]
4V8Yelectron microscopy4.30AO1-137[»]
4V8Zelectron microscopy6.60AO1-137[»]
4V92electron microscopy3.70O11-137[»]
ProteinModelPortaliP06367.
SMRiP06367. Positions 11-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06367.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S11P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000000703.
HOGENOMiHOG000111598.
InParanoidiP06367.
KOiK02955.
OMAiMYGGMKV.
OrthoDBiEOG7WHHPF.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNVVQARDN SQVFGVARIY ASFNDTFVHV TDLSGKETIA RVTGGMKVKA
60 70 80 90 100
DRDESSPYAA MLAAQDVAAK CKEVGITAVH VKIRATGGTR TKTPGPGGQA
110 120 130
ALRALARSGL RIGRIEDVTP VPSDSTRKKG GRRGRRL
Length:137
Mass (Da):14,537
Last modified:January 23, 2007 - v5
Checksum:i65A9212E10340A95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721K → R in AAA34530 (PubMed:3037334).Curated
Sequence conflicti123 – 1231S → C in AAA34530 (PubMed:3037334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16126 Genomic DNA. Translation: AAA34530.1.
X59720 Genomic DNA. Translation: CAC42981.1.
BK006937 Genomic DNA. Translation: DAA07510.1.
PIRiA02726. R5BY59.
RefSeqiNP_009960.2. NM_001178745.1.

Genome annotation databases

EnsemblFungiiYCR031C; YCR031C; YCR031C.
GeneIDi850397.
KEGGisce:YCR031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16126 Genomic DNA. Translation: AAA34530.1.
X59720 Genomic DNA. Translation: CAC42981.1.
BK006937 Genomic DNA. Translation: DAA07510.1.
PIRiA02726. R5BY59.
RefSeqiNP_009960.2. NM_001178745.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-K9-133[»]
3J6Xelectron microscopy6.10141-137[»]
3J6Yelectron microscopy6.10141-137[»]
3J77electron microscopy6.20141-137[»]
3J78electron microscopy6.30141-137[»]
3V88X-ray3.00O1-137[»]
4U3MX-ray3.00C4/c42-137[»]
4U3NX-ray3.20C4/c42-137[»]
4U3UX-ray2.90C4/c42-137[»]
4U4NX-ray3.10C4/c42-137[»]
4U4OX-ray3.60C4/c42-137[»]
4U4QX-ray3.00C4/c42-137[»]
4U4RX-ray2.80C4/c42-137[»]
4U4UX-ray3.00C4/c42-137[»]
4U4YX-ray3.20C4/c42-137[»]
4U4ZX-ray3.10C4/c42-137[»]
4U50X-ray3.20C4/c42-137[»]
4U51X-ray3.20C4/c42-137[»]
4U52X-ray3.00C4/c42-137[»]
4U53X-ray3.30C4/c42-137[»]
4U55X-ray3.20C4/c42-137[»]
4U56X-ray3.45C4/c42-137[»]
4U6FX-ray3.10C4/c42-137[»]
4V4Belectron microscopy11.70AK2-137[»]
4V6Ielectron microscopy8.80AK1-137[»]
4V7RX-ray4.00AH/CH1-137[»]
4V88X-ray3.00AO/CO1-137[»]
4V8Yelectron microscopy4.30AO1-137[»]
4V8Zelectron microscopy6.60AO1-137[»]
4V92electron microscopy3.70O11-137[»]
ProteinModelPortaliP06367.
SMRiP06367. Positions 11-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31014. 141 interactions.
IntActiP06367. 22 interactions.
MINTiMINT-4083975.

Proteomic databases

MaxQBiP06367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR031C; YCR031C; YCR031C.
GeneIDi850397.
KEGGisce:YCR031C.

Organism-specific databases

EuPathDBiFungiDB:YCR031C.
SGDiS000000627. RPS14A.

Phylogenomic databases

GeneTreeiENSGT00390000000703.
HOGENOMiHOG000111598.
InParanoidiP06367.
KOiK02955.
OMAiMYGGMKV.
OrthoDBiEOG7WHHPF.

Enzyme and pathway databases

BioCyciYEAST:G3O-29345-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

EvolutionaryTraceiP06367.
NextBioi965926.
PROiP06367.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene."
    Larkin J.C., Thompson J.R., Woolford J.L. Jr.
    Mol. Cell. Biol. 7:1764-1775(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 72 AND 123.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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: ACETYLATION AT SER-2 BY NATA.
  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, ACETYLATION AT SER-2 BY NATA.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "The small-subunit processome is a ribosome assembly intermediate."
    Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J.
    Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME, SUBCELLULAR LOCATION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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 9-133, ELECTRON MICROSCOPY.
  12. "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 nameiRS14A_YEAST
AccessioniPrimary (citable) accession number: P06367
Secondary accession number(s): D6VR41, Q96VG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 151 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 29600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S14 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.