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Protein

Eukaryotic peptide chain release factor subunit 1

Gene

SUP45

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

Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.By similarity1 Publication

GO - Molecular functioni

  • translation release factor activity Source: SGD
  • translation release factor activity, codon specific Source: SGD

GO - Biological processi

  • DNA-templated transcription, termination Source: SGD
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-29097-MONOMER.
ReactomeiR-SCE-72764. Eukaryotic Translation Termination.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic peptide chain release factor subunit 1
Short name:
Eukaryotic release factor 1
Short name:
eRF1
Alternative name(s):
Omnipotent suppressor protein 1
Gene namesi
Name:SUP45
Synonyms:SAL4, SUP1
Ordered Locus Names:YBR143C
ORF Names:YBR1120
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR143C.
SGDiS000000347. SUP45.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • cytosol Source: Reactome
  • translation release factor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Eukaryotic peptide chain release factor subunit 1PRO_0000143167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821N5-methylglutamine2 Publications
Modified residuei421 – 4211PhosphoserineCombined sources

Post-translational modificationi

N5-methylated on Gln-182 by MTQ2.2 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP12385.
PeptideAtlasiP12385.

PTM databases

iPTMnetiP12385.

Interactioni

Subunit structurei

Heterodimer of two subunits, one of which binds GTP. Interacts with TPA1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RLI1Q031955EBI-6533,EBI-35146

Protein-protein interaction databases

BioGridi32843. 62 interactions.
DIPiDIP-800N.
IntActiP12385. 44 interactions.
MINTiMINT-560710.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CRMelectron microscopy8.75X140-421[»]
4CRNelectron microscopy9.10X1-437[»]
ProteinModelPortaliP12385.
SMRiP12385. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic release factor 1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000009004.
HOGENOMiHOG000224681.
InParanoidiP12385.
KOiK03265.
OMAiETIRYTF.
OrthoDBiEOG7KQ2B7.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.30.960.10. 1 hit.
InterProiIPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR029064. L30e-like.
IPR004403. Peptide_chain-rel_eRF1/aRF1.
IPR024049. Release_factor_eRF1/aRF1_N.
[Graphical view]
PANTHERiPTHR10113. PTHR10113. 1 hit.
PfamiPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SMARTiSM01194. eRF1_1. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsiTIGR03676. aRF1/eRF1. 1 hit.

Sequencei

Sequence statusi: Complete.

P12385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNEVEKNIE IWKVKKLVQS LEKARGNGTS MISLVIPPKG QIPLYQKMLT
60 70 80 90 100
DEYGTASNIK SRVNRLSVLS AITSTQQKLK LYNTLPKNGL VLYCGDIITE
110 120 130 140 150
DGKEKKVTFD IEPYKPINTS LYLCDNKFHT EVLSELLQAD DKFGFIVMDG
160 170 180 190 200
QGTLFGSVSG NTRTVLHKFT VDLPKKHGRG GQSALRFARL REEKRHNYVR
210 220 230 240 250
KVAEVAVQNF ITNDKVNVKG LILAGSADFK TDLAKSELFD PRLACKVISI
260 270 280 290 300
VDVSYGGENG FNQAIELSAE ALANVKYVQE KKLLEAYFDE ISQDTGKFCY
310 320 330 340 350
GIDDTLKALD LGAVEKLIVF ENLETIRYTF KDAEDNEVIK FAEPEAKDKS
360 370 380 390 400
FAIDKATGQE MDVVSEEPLI EWLAANYKNF GATLEFITDK SSEGAQFVTG
410 420 430
FGGIGAMLRY KVNFEQLVDE SEDEYYDEDE GSDYDFI
Length:437
Mass (Da):49,006
Last modified:October 5, 2010 - v2
Checksum:i9B59133EE3B1F61E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411Q → L in CAA27719 (PubMed:3526282).Curated
Sequence conflicti41 – 411Q → L in M28042 (PubMed:3037308).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04082 Genomic DNA. Translation: CAA27719.1.
M28042 Genomic DNA. No translation available.
Z36012 Genomic DNA. Translation: CAA85101.1.
X73531 Genomic DNA. Translation: CAA51935.1.
BK006936 Genomic DNA. Translation: DAA07259.1.
PIRiS46014.
RefSeqiNP_009701.3. NM_001178491.3.

Genome annotation databases

EnsemblFungiiYBR143C; YBR143C; YBR143C.
GeneIDi852440.
KEGGisce:YBR143C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04082 Genomic DNA. Translation: CAA27719.1.
M28042 Genomic DNA. No translation available.
Z36012 Genomic DNA. Translation: CAA85101.1.
X73531 Genomic DNA. Translation: CAA51935.1.
BK006936 Genomic DNA. Translation: DAA07259.1.
PIRiS46014.
RefSeqiNP_009701.3. NM_001178491.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CRMelectron microscopy8.75X140-421[»]
4CRNelectron microscopy9.10X1-437[»]
ProteinModelPortaliP12385.
SMRiP12385. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32843. 62 interactions.
DIPiDIP-800N.
IntActiP12385. 44 interactions.
MINTiMINT-560710.

PTM databases

iPTMnetiP12385.

Proteomic databases

MaxQBiP12385.
PeptideAtlasiP12385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR143C; YBR143C; YBR143C.
GeneIDi852440.
KEGGisce:YBR143C.

Organism-specific databases

EuPathDBiFungiDB:YBR143C.
SGDiS000000347. SUP45.

Phylogenomic databases

GeneTreeiENSGT00390000009004.
HOGENOMiHOG000224681.
InParanoidiP12385.
KOiK03265.
OMAiETIRYTF.
OrthoDBiEOG7KQ2B7.

Enzyme and pathway databases

BioCyciYEAST:G3O-29097-MONOMER.
ReactomeiR-SCE-72764. Eukaryotic Translation Termination.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP12385.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.30.960.10. 1 hit.
InterProiIPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR029064. L30e-like.
IPR004403. Peptide_chain-rel_eRF1/aRF1.
IPR024049. Release_factor_eRF1/aRF1_N.
[Graphical view]
PANTHERiPTHR10113. PTHR10113. 1 hit.
PfamiPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SMARTiSM01194. eRF1_1. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsiTIGR03676. aRF1/eRF1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast omnipotent suppressor SUP1 (SUP45): nucleotide sequence of the wildtype and a mutant gene."
    Breining P., Piepersberg W.
    Nucleic Acids Res. 14:5187-5197(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Nucleotide sequence of mutant and wild-type alelles of the SUP1 gene and comparison of transcripts of SUP1 and SUP2 genes."
    Surguchev A.P., Telkov M.V., Smirnov V.N., Breining P., Piepersberg W.
    Mol. Biol. (Mosk.) 21:347-358(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [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. "Sequence and function analysis of a 2.73 kb fragment of Saccharomyces cerevisiae chromosome II."
    Miosga T., Zimmermann F.K.
    Yeast 9:1273-1277(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-432.
    Strain: ATCC 200060 / W303.
  6. "The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae."
    Stansfield I., Jones K.M., Kushnirov V.V., Dagkesamanskaya A.R., Poznyakovski A.I., Paushkin S.V., Nierras C.R., Cox B.S., Ter-Avanesyan M.D., Tuite M.F.
    EMBO J. 14:4365-4373(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene."
    Heurgue-Hamard V., Champ S., Mora L., Merkulova-Rainon T., Kisselev L.L., Buckingham R.H.
    J. Biol. Chem. 280:2439-2445(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-182, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae."
    Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.
    Mol. Cell. Biol. 26:5237-5248(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPA1.
  11. "The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p."
    Polevoda B., Span L., Sherman F.
    J. Biol. Chem. 281:2562-2571(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-182, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].

Entry informationi

Entry nameiERF1_YEAST
AccessioniPrimary (citable) accession number: P12385
Secondary accession number(s): D6VQD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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 one 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.