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Protein

40S ribosomal protein S2

Gene

RPS2

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

Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.1 Publication

GO - Molecular functioni

  1. small ribosomal subunit rRNA binding Source: SGD
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. positive regulation of translational fidelity Source: SGD
  2. rRNA export from nucleus Source: SGD
  3. rRNA processing Source: UniProtKB-KW
  4. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30620-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.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S2
Alternative name(s):
Omnipotent suppressor protein SUP44
RP12
S4
YS5
Gene namesi
Name:RPS2
Synonyms:RPS4, SUP38, SUP44
Ordered Locus Names:YGL123W
ORF Names:G2893
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003091. RPS2.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: SGD
  2. nucleolus Source: UniProtKB-SubCell
  3. 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 – 25425340S ribosomal protein S2PRO_0000131684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei11 – 111Asymmetric dimethylarginine; by HMT1; alternate2 Publications
Modified residuei11 – 111Omega-N-methylarginine; by HMT1; alternate2 Publications

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP25443.
PaxDbiP25443.
PeptideAtlasiP25443.

Expressioni

Gene expression databases

GenevestigatoriP25443.

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

BioGridi33128. 61 interactions.
IntActiP25443. 11 interactions.
MINTiMINT-4808257.
STRINGi4932.YGL123W.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 467Combined sources
Helixi53 – 586Combined sources
Helixi66 – 716Combined sources
Beta strandi80 – 856Combined sources
Beta strandi88 – 903Combined sources
Beta strandi93 – 953Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi107 – 12014Combined sources
Helixi121 – 13414Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi165 – 1717Combined sources
Beta strandi178 – 1803Combined sources
Helixi182 – 1909Combined sources
Beta strandi195 – 2028Combined sources
Helixi207 – 21913Combined sources
Helixi220 – 2234Combined sources
Helixi227 – 2293Combined sources
Helixi239 – 2424Combined sources
Helixi244 – 2474Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-E75-223[»]
3J6Xelectron microscopy6.10D1-254[»]
3J6Yelectron microscopy6.10D1-254[»]
3J77electron microscopy6.20C1-254[»]
3J78electron microscopy6.30C1-254[»]
3V88X-ray3.00C1-254[»]
4U3MX-ray3.00D/g2-254[»]
4U3NX-ray3.20D/g2-254[»]
4U3UX-ray2.90D/g2-254[»]
4U4NX-ray3.10D/g2-254[»]
4U4OX-ray3.60D/g2-254[»]
4U4QX-ray3.00D/g2-254[»]
4U4RX-ray2.80D/g2-254[»]
4U4UX-ray3.00D/g2-254[»]
4U4YX-ray3.20D/g2-254[»]
4U4ZX-ray3.10D/g2-254[»]
4U50X-ray3.20D/g2-254[»]
4U51X-ray3.20D/g2-254[»]
4U52X-ray3.00D/g2-254[»]
4U53X-ray3.30D/g2-254[»]
4U55X-ray3.20D/g2-254[»]
4U56X-ray3.45D/g2-254[»]
4U6FX-ray3.10D/g2-254[»]
4V4Belectron microscopy11.70E75-223[»]
4V6Ielectron microscopy-E1-254[»]
4V7RX-ray4.00B1-254[»]
4V88X-ray3.00C1-254[»]
4V8Yelectron microscopy4.30C1-254[»]
4V8Zelectron microscopy6.60C1-254[»]
4V92electron microscopy3.70C34-249[»]
ProteinModelPortaliP25443.
SMRiP25443. Positions 34-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 13964S5 DRBMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S5P family.Curated
Contains 1 S5 DRBM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0098.
GeneTreeiENSGT00390000001433.
HOGENOMiHOG000072596.
InParanoidiP25443.
KOiK02981.
OMAiSPYSEFK.
OrthoDBiEOG7C8GV0.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. rpsE_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25443-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAPEAQQQK RGGFGGRNRG RPNRRGPRNT EEKGWVPVTK LGRLVKAGKI
60 70 80 90 100
TTIEEIFLHS LPVKEFQIID TLLPGLQDEV MNIKPVQKQT RAGQRTRFKA
110 120 130 140 150
VVVVGDSNGH VGLGIKTAKE VAGAIRAGII IAKLSVIPIR RGYWGTNLGQ
160 170 180 190 200
PHSLATKTTG KCGSVTVRLI PAPRGSGIVA SPAVKKLLQL AGVEDVYTQS
210 220 230 240 250
NGKTRTLENT LKAAFVAIGN TYGFLTPNLW AEQPLPVSPL DIYSDEASAQ

KKRF
Length:254
Mass (Da):27,450
Last modified:January 23, 2007 - v3
Checksum:i5EFDA4C7DE7BDFFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59375 Genomic DNA. Translation: AAA63576.1.
X94106 Genomic DNA. Translation: CAA63835.1.
Z72645 Genomic DNA. Translation: CAA96831.1.
AY557815 Genomic DNA. Translation: AAS56141.1.
BK006941 Genomic DNA. Translation: DAA07986.1.
PIRiA36363. R3BYS2.
RefSeqiNP_011392.1. NM_001180988.1.

Genome annotation databases

EnsemblFungiiYGL123W; YGL123W; YGL123W.
GeneIDi852754.
KEGGisce:YGL123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59375 Genomic DNA. Translation: AAA63576.1.
X94106 Genomic DNA. Translation: CAA63835.1.
Z72645 Genomic DNA. Translation: CAA96831.1.
AY557815 Genomic DNA. Translation: AAS56141.1.
BK006941 Genomic DNA. Translation: DAA07986.1.
PIRiA36363. R3BYS2.
RefSeqiNP_011392.1. NM_001180988.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-E75-223[»]
3J6Xelectron microscopy6.10D1-254[»]
3J6Yelectron microscopy6.10D1-254[»]
3J77electron microscopy6.20C1-254[»]
3J78electron microscopy6.30C1-254[»]
3V88X-ray3.00C1-254[»]
4U3MX-ray3.00D/g2-254[»]
4U3NX-ray3.20D/g2-254[»]
4U3UX-ray2.90D/g2-254[»]
4U4NX-ray3.10D/g2-254[»]
4U4OX-ray3.60D/g2-254[»]
4U4QX-ray3.00D/g2-254[»]
4U4RX-ray2.80D/g2-254[»]
4U4UX-ray3.00D/g2-254[»]
4U4YX-ray3.20D/g2-254[»]
4U4ZX-ray3.10D/g2-254[»]
4U50X-ray3.20D/g2-254[»]
4U51X-ray3.20D/g2-254[»]
4U52X-ray3.00D/g2-254[»]
4U53X-ray3.30D/g2-254[»]
4U55X-ray3.20D/g2-254[»]
4U56X-ray3.45D/g2-254[»]
4U6FX-ray3.10D/g2-254[»]
4V4Belectron microscopy11.70E75-223[»]
4V6Ielectron microscopy-E1-254[»]
4V7RX-ray4.00B1-254[»]
4V88X-ray3.00C1-254[»]
4V8Yelectron microscopy4.30C1-254[»]
4V8Zelectron microscopy6.60C1-254[»]
4V92electron microscopy3.70C34-249[»]
ProteinModelPortaliP25443.
SMRiP25443. Positions 34-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33128. 61 interactions.
IntActiP25443. 11 interactions.
MINTiMINT-4808257.
STRINGi4932.YGL123W.

Proteomic databases

MaxQBiP25443.
PaxDbiP25443.
PeptideAtlasiP25443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL123W; YGL123W; YGL123W.
GeneIDi852754.
KEGGisce:YGL123W.

Organism-specific databases

SGDiS000003091. RPS2.

Phylogenomic databases

eggNOGiCOG0098.
GeneTreeiENSGT00390000001433.
HOGENOMiHOG000072596.
InParanoidiP25443.
KOiK02981.
OMAiSPYSEFK.
OrthoDBiEOG7C8GV0.

Enzyme and pathway databases

BioCyciYEAST:G3O-30620-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.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTraceiP25443.
NextBioi972192.
PROiP25443.

Gene expression databases

GenevestigatoriP25443.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. rpsE_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein."
    All-Robyn J.A., Brown N., Otaka E., Liebman S.W.
    Mol. Cell. Biol. 10:6544-6553(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of a putative methylenetetrahydrofolate reductase by sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII."
    Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L., Cerdan E.
    Yeast 12:1047-1051(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "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 2-11, ACETYLATION AT SER-2.
  7. "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.
  8. "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.
  9. "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes."
    Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.
    EMBO J. 22:1370-1380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "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.
  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].
  12. "Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae."
    Lipson R.S., Webb K.J., Clarke S.G.
    Biochem. Biophys. Res. Commun. 391:1658-1662(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION BY HMT1.
  13. "Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation."
    Young B.D., Weiss D.I., Zurita-Lopez C.I., Webb K.J., Clarke S.G., McBride A.E.
    Biochemistry 51:5091-5104(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-11.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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].
  16. "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 75-223.
  17. "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 75-223, ELECTRON MICROSCOPY.
  18. Cited for: STRUCTURE BY ELECTRON MICROSCOPY.
  19. "Crystal structure of the eukaryotic ribosome."
    Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
    Science 330:1203-1209(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 1-254.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-254.
  21. "Molecular architecture of a eukaryotic translational initiation complex."
    Fernandez I.S., Bai X.C., Hussain T., Kelley A.C., Lorsch J.R., Ramakrishnan V., Scheres S.H.
    Science 342:1240585-1240585(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 1-254.

Entry informationi

Entry nameiRS2_YEAST
AccessioniPrimary (citable) accession number: P25443
Secondary accession number(s): D6VU25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 138 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.