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P06367 (RS14A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S14-A
Alternative name(s):
RP59A
Gene names
Name:RPS14A
Synonyms:CRY1, RPL59
Ordered Locus Names:YCR031C
ORF Names:YCR31C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Ref.9

Subunit structure

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. Ref.6 Ref.9

Subcellular location

Cytoplasm By similarity. Nucleusnucleolus Ref.9.

Post-translational modification

N-terminally acetylated by acetyltransferase NatA. Ref.5 Ref.7

Miscellaneous

Present with 29600 molecules/cell in log phase SD medium.

There are 2 genes for S14 in yeast.

Sequence similarities

Belongs to the ribosomal protein S11P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 13713640S ribosomal protein S14-A HAMAP-Rule MF_01310
PRO_0000123359

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.7 Ref.10

Experimental info

Sequence conflict721K → R in AAA34530. Ref.1
Sequence conflict1231S → C in AAA34530. Ref.1

Secondary structure

......................... 137
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06367 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 65A9212E10340A95

FASTA13714,537
        10         20         30         40         50         60 
MSNVVQARDN SQVFGVARIY ASFNDTFVHV TDLSGKETIA RVTGGMKVKA DRDESSPYAA 

        70         80         90        100        110        120 
MLAAQDVAAK CKEVGITAVH VKIRATGGTR TKTPGPGGQA ALRALARSGL RIGRIEDVTP 

       130 
VPSDSTRKKG GRRGRRL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16126 Genomic DNA. Translation: AAA34530.1.
X59720 Genomic DNA. Translation: CAC42981.1.
BK006937 Genomic DNA. Translation: DAA07510.1.
PIRR5BY59. A02726.
RefSeqNP_009960.2. NM_001178745.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-K9-133[»]
1S1Helectron microscopy11.70K2-137[»]
3IZBelectron microscopy-K1-137[»]
3O2ZX-ray4.00H1-137[»]
3O30X-ray4.00H1-137[»]
3U5CX-ray3.00O1-137[»]
3U5GX-ray3.00O1-137[»]
4BYLelectron microscopy4.30O1-137[»]
4BYTelectron microscopy6.60O1-137[»]
ProteinModelPortalP06367.
SMRP06367. Positions 10-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31014. 138 interactions.
IntActP06367. 22 interactions.
MINTMINT-4083975.
STRING4932.YCR031C.

Proteomic databases

MaxQBP06367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR031C; YCR031C; YCR031C.
GeneID850397.
KEGGsce:YCR031C.

Organism-specific databases

SGDS000000627. RPS14A.

Phylogenomic databases

GeneTreeENSGT00390000000703.
HOGENOMHOG000111598.
KOK02955.
OMANDRDEAS.
OrthoDBEOG7WHHPF.

Enzyme and pathway databases

BioCycYEAST:G3O-29345-MONOMER.

Gene expression databases

GenevestigatorP06367.

Family and domain databases

Gene3D3.30.420.80. 1 hit.
HAMAPMF_01310. Ribosomal_S11.
InterProIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERPTHR11759. PTHR11759. 1 hit.
PfamPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06367.
NextBio965926.

Entry information

Entry nameRS14A_YEAST
AccessionPrimary (citable) accession number: P06367
Secondary accession number(s): D6VR41, Q96VG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 139 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references