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P26783

- RS5_YEAST

UniProt

P26783 - RS5_YEAST

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Protein

40S ribosomal protein S5

Gene
RPS5, RPS2, YJR123W, J2045
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. RNA binding Source: InterPro
  3. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. regulation of translational fidelity Source: SGD
  3. rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S5
Alternative name(s):
RP14
S2
YS8
Gene namesi
Name:RPS5
Synonyms:RPS2
Ordered Locus Names:YJR123W
ORF Names:J2045
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

SGDiS000003884. RPS5.

Subcellular locationi

Cytoplasm By similarity

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 – 22522440S ribosomal protein S5PRO_0000124540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei27 – 271Phosphothreonine1 Publication

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26783.
PaxDbiP26783.
PeptideAtlasiP26783.
PRIDEiP26783.

2D gel databases

UCD-2DPAGEP26783.

Expressioni

Gene expression databases

GenevestigatoriP26783.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BUL1P485243EBI-16150,EBI-3881

Protein-protein interaction databases

BioGridi33879. 157 interactions.
DIPiDIP-5092N.
IntActiP26783. 66 interactions.
MINTiMINT-480795.
STRINGi4932.YJR123W.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 388
Beta strandi43 – 453
Turni56 – 583
Beta strandi69 – 713
Beta strandi78 – 803
Helixi83 – 864
Helixi89 – 979
Helixi101 – 1033
Helixi107 – 12317
Helixi129 – 13810
Beta strandi143 – 1475
Beta strandi151 – 1544
Beta strandi158 – 1614
Helixi164 – 18320
Beta strandi186 – 1883
Helixi190 – 20213
Beta strandi206 – 2083
Helixi209 – 22315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-G76-225[»]
1S1Helectron microscopy11.70G76-225[»]
1VW9electron microscopy6.10G1-225[»]
1VWVelectron microscopy6.10G1-225[»]
2NOQelectron microscopy7.30F76-225[»]
3IZBelectron microscopy-F1-225[»]
3O2ZX-ray4.00D1-225[»]
3O30X-ray4.00D1-225[»]
3U5CX-ray3.00F1-225[»]
3U5GX-ray3.00F1-225[»]
4BYLelectron microscopy4.30F1-225[»]
4BYTelectron microscopy6.60F1-225[»]
4CUYelectron microscopy3.70F20-225[»]
ProteinModelPortaliP26783.
SMRiP26783. Positions 20-225.

Miscellaneous databases

EvolutionaryTraceiP26783.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0049.
GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
KOiK02989.
OMAiKEHHISH.
OrthoDBiEOG7MD52N.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. S7_S5_E_A. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26783-1 [UniParc]FASTAAdd to Basket

« Hide

MSDTEAPVEV QEDFEVVEEF TPVVLATPIP EEVQQAQTEI KLFNKWSFEE    50
VEVKDASLVD YVQVRQPIFV AHTAGRYANK RFRKAQCPII ERLTNSLMMN 100
GRNNGKKLKA VRIIKHTLDI INVLTDQNPI QVVVDAITNT GPREDTTRVG 150
GGGAARRQAV DVSPLRRVNQ AIALLTIGAR EAAFRNIKTI AETLAEELIN 200
AAKGSSTSYA IKKKDELERV AKSNR 225
Length:225
Mass (Da):25,039
Last modified:January 23, 2007 - v3
Checksum:iCD3F743B56CB1127
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89368 Genomic DNA. Translation: CAA61550.1.
Z49623 Genomic DNA. Translation: CAA89654.1.
AY692868 Genomic DNA. Translation: AAT92887.1.
BK006943 Genomic DNA. Translation: DAA08908.1.
PIRiS55720.
RefSeqiNP_012657.1. NM_001181781.1.

Genome annotation databases

EnsemblFungiiYJR123W; YJR123W; YJR123W.
GeneIDi853587.
KEGGisce:YJR123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89368 Genomic DNA. Translation: CAA61550.1 .
Z49623 Genomic DNA. Translation: CAA89654.1 .
AY692868 Genomic DNA. Translation: AAT92887.1 .
BK006943 Genomic DNA. Translation: DAA08908.1 .
PIRi S55720.
RefSeqi NP_012657.1. NM_001181781.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K5X model - G 76-225 [» ]
1S1H electron microscopy 11.70 G 76-225 [» ]
1VW9 electron microscopy 6.10 G 1-225 [» ]
1VWV electron microscopy 6.10 G 1-225 [» ]
2NOQ electron microscopy 7.30 F 76-225 [» ]
3IZB electron microscopy - F 1-225 [» ]
3O2Z X-ray 4.00 D 1-225 [» ]
3O30 X-ray 4.00 D 1-225 [» ]
3U5C X-ray 3.00 F 1-225 [» ]
3U5G X-ray 3.00 F 1-225 [» ]
4BYL electron microscopy 4.30 F 1-225 [» ]
4BYT electron microscopy 6.60 F 1-225 [» ]
4CUY electron microscopy 3.70 F 20-225 [» ]
ProteinModelPortali P26783.
SMRi P26783. Positions 20-225.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33879. 157 interactions.
DIPi DIP-5092N.
IntActi P26783. 66 interactions.
MINTi MINT-480795.
STRINGi 4932.YJR123W.

2D gel databases

UCD-2DPAGE P26783.

Proteomic databases

MaxQBi P26783.
PaxDbi P26783.
PeptideAtlasi P26783.
PRIDEi P26783.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR123W ; YJR123W ; YJR123W .
GeneIDi 853587.
KEGGi sce:YJR123W.

Organism-specific databases

SGDi S000003884. RPS5.

Phylogenomic databases

eggNOGi COG0049.
GeneTreei ENSGT00390000010806.
HOGENOMi HOG000039066.
KOi K02989.
OMAi KEHHISH.
OrthoDBi EOG7MD52N.

Enzyme and pathway databases

BioCyci YEAST:G3O-31744-MONOMER.
Reactomei REACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.

Miscellaneous databases

EvolutionaryTracei P26783.
NextBioi 974388.
PROi P26783.

Gene expression databases

Genevestigatori P26783.

Family and domain databases

Gene3Di 1.10.455.10. 1 hit.
InterProi IPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view ]
PANTHERi PTHR11205. PTHR11205. 1 hit.
Pfami PF00177. Ribosomal_S7. 1 hit.
[Graphical view ]
SUPFAMi SSF47973. SSF47973. 1 hit.
TIGRFAMsi TIGR01028. S7_S5_E_A. 1 hit.
PROSITEi PS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae."
    Ignatovich O., Cooper M., Kulesza H.M., Beggs J.D.
    Nucleic Acids Res. 23:4616-4619(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: PROTEIN SEQUENCE OF 2-21, 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. "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 THR-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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].
  10. "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 76-225, ELECTRON MICROSCOPY.
  11. "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 OF 76-225, ELECTRON MICROSCOPY.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 76-225.

Entry informationi

Entry nameiRS5_YEAST
AccessioniPrimary (citable) accession number: P26783
Secondary accession number(s): D6VWU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 130 of the entry and version 3 of the sequence. [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

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

External Data

Dasty 3

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