Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Eukaryotic peptide chain release factor GTP-binding subunit

Gene

SUP35

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 translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei273 – 2731Interacts with GTP/GDPBy similarity
Sitei407 – 4071Interacts with GTP/GDPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi267 – 2748GTPBy similarity
Nucleotide bindingi344 – 3485GTPBy similarity
Nucleotide bindingi406 – 4094GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • translation release factor activity Source: SGD

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Prion

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29761-MONOMER.
ReactomeiR-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 GTP-binding subunit
Alternative name(s):
ERF-3
Short name:
ERF3
ERF2
G1 to S phase transition protein 1
Omnipotent suppressor protein 2
PSI no more protein 2
Polypeptide release factor 3
Translation release factor 3
Gene namesi
Name:SUP35
Synonyms:GST1, PNM2, SAL3, SUF12, SUP2
Ordered Locus Names:YDR172W
ORF Names:YD9395.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR172W.
SGDiS000002579. SUP35.

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

Amyloid, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 685684Eukaryotic peptide chain release factor GTP-binding subunitPRO_0000091482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei571 – 5711PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05453.
PeptideAtlasiP05453.

PTM databases

iPTMnetiP05453.

Interactioni

Subunit structurei

Heterodimer of two subunits, one of which binds GTP. Interacts with polyadenylate-binding protein PAB1, and TPA1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ECM32P326443EBI-6540,EBI-22223
GLE1Q123152EBI-6540,EBI-7635
ITT1Q046383EBI-6540,EBI-27858

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32225. 253 interactions.
DIPiDIP-376N.
IntActiP05453. 38 interactions.
MINTiMINT-516826.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YJOX-ray1.30A8-13[»]
1YJPX-ray1.80A7-13[»]
2OMMX-ray2.00A7-13[»]
4CRNelectron microscopy9.10P256-685[»]
ProteinModelPortaliP05453.
SMRiP05453. Positions 256-685.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 484227tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 239238Interaction with PAB1Add
BLAST
Regioni5 – 135131Prion domain (PrD)Add
BLAST
Regioni139 – 249111ChargedAdd
BLAST
Regioni267 – 2748G1PROSITE-ProRule annotation
Regioni323 – 3275G2PROSITE-ProRule annotation
Regioni344 – 3474G3PROSITE-ProRule annotation
Regioni406 – 4094G4PROSITE-ProRule annotation
Regioni448 – 4503G5PROSITE-ProRule annotation

Domaini

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00620000087924.
HOGENOMiHOG000229291.
InParanoidiP05453.
KOiK03267.
OMAiHACVEEV.
OrthoDBiEOG715QCW.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR003285. Sup35.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
PR01343. YEASTERF.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSNQGNNQ QNYQQYSQNG NQQQGNNRYQ GYQAYNAQAQ PAGGYYQNYQ
60 70 80 90 100
GYSGYQQGGY QQYNPDAGYQ QQYNPQGGYQ QYNPQGGYQQ QFNPQGGRGN
110 120 130 140 150
YKNFNYNNNL QGYQAGFQPQ SQGMSLNDFQ KQQKQAAPKP KKTLKLVSSS
160 170 180 190 200
GIKLANATKK VGTKPAESDK KEEEKSAETK EPTKEPTKVE EPVKKEEKPV
210 220 230 240 250
QTEEKTEEKS ELPKVEDLKI SESTHNTNNA NVTSADALIK EQEEEVDDEV
260 270 280 290 300
VNDMFGGKDH VSLIFMGHVD AGKSTMGGNL LYLTGSVDKR TIEKYEREAK
310 320 330 340 350
DAGRQGWYLS WVMDTNKEER NDGKTIEVGK AYFETEKRRY TILDAPGHKM
360 370 380 390 400
YVSEMIGGAS QADVGVLVIS ARKGEYETGF ERGGQTREHA LLAKTQGVNK
410 420 430 440 450
MVVVVNKMDD PTVNWSKERY DQCVSNVSNF LRAIGYNIKT DVVFMPVSGY
460 470 480 490 500
SGANLKDHVD PKECPWYTGP TLLEYLDTMN HVDRHINAPF MLPIAAKMKD
510 520 530 540 550
LGTIVEGKIE SGHIKKGQST LLMPNKTAVE IQNIYNETEN EVDMAMCGEQ
560 570 580 590 600
VKLRIKGVEE EDISPGFVLT SPKNPIKSVT KFVAQIAIVE LKSIIAAGFS
610 620 630 640 650
CVMHVHTAIE EVHIVKLLHK LEKGTNRKSK KPPAFAKKGM KVIAVLETEA
660 670 680
PVCVETYQDY PQLGRFTLRD QGTTIAIGKI VKIAE
Length:685
Mass (Da):76,551
Last modified:November 1, 1988 - v1
Checksum:i43912A6D77DFA153
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → C in CAA68760 (PubMed:2841115).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21129 Genomic DNA. Translation: AAA35133.1.
X07163 Genomic DNA. Translation: CAA30155.1.
Y00829 Genomic DNA. Translation: CAA68760.1.
Z46727 Genomic DNA. Translation: CAA86677.1.
BK006938 Genomic DNA. Translation: DAA12014.1.
PIRiS00733. EFBYS2.
RefSeqiNP_010457.3. NM_001180479.3.

Genome annotation databases

EnsemblFungiiYDR172W; YDR172W; YDR172W.
GeneIDi851752.
KEGGisce:YDR172W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21129 Genomic DNA. Translation: AAA35133.1.
X07163 Genomic DNA. Translation: CAA30155.1.
Y00829 Genomic DNA. Translation: CAA68760.1.
Z46727 Genomic DNA. Translation: CAA86677.1.
BK006938 Genomic DNA. Translation: DAA12014.1.
PIRiS00733. EFBYS2.
RefSeqiNP_010457.3. NM_001180479.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YJOX-ray1.30A8-13[»]
1YJPX-ray1.80A7-13[»]
2OMMX-ray2.00A7-13[»]
4CRNelectron microscopy9.10P256-685[»]
ProteinModelPortaliP05453.
SMRiP05453. Positions 256-685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32225. 253 interactions.
DIPiDIP-376N.
IntActiP05453. 38 interactions.
MINTiMINT-516826.

PTM databases

iPTMnetiP05453.

Proteomic databases

MaxQBiP05453.
PeptideAtlasiP05453.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR172W; YDR172W; YDR172W.
GeneIDi851752.
KEGGisce:YDR172W.

Organism-specific databases

EuPathDBiFungiDB:YDR172W.
SGDiS000002579. SUP35.

Phylogenomic databases

GeneTreeiENSGT00620000087924.
HOGENOMiHOG000229291.
InParanoidiP05453.
KOiK03267.
OMAiHACVEEV.
OrthoDBiEOG715QCW.

Enzyme and pathway databases

BioCyciYEAST:G3O-29761-MONOMER.
ReactomeiR-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

EvolutionaryTraceiP05453.
NextBioi969510.
PROiP05453.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR003285. Sup35.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
PR01343. YEASTERF.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae."
    Kushnirov V.V., Ter-Avanesyan M.D., Telckov M.V., Surguchov A.P., Smirnov V.N., Inge-Vechtomov S.G.
    Gene 66:45-54(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Localization of possible functional domains in sup2 gene product of the yeast Saccharomyces cerevisiae."
    Kushnirov V.V., Ter-Avanesyan M.D., Surguchov A.P., Smirnov V.N., Inge-Vechtomov S.G.
    FEBS Lett. 215:257-260(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "SUF12 suppressor protein of yeast. A fusion protein related to the EF-1 family of elongation factors."
    Wilson P.G., Culbertson M.R.
    J. Mol. Biol. 199:559-573(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain."
    Kukuchi Y., Shimatake H., Kikuchi A.
    EMBO J. 7:1175-1182(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "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.
  8. "Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor."
    Paushkin S.V., Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D.
    EMBO J. 15:3127-3134(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, AGGREGATION.
  9. "Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae."
    Derkatch I.L., Chernoff Y.O., Kushnirov V.V., Inge-Vechtomov S.G., Liebman S.W.
    Genetics 144:1375-1386(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION.
  10. "Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae."
    Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W.
    Genetics 147:507-519(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, PRION CURING.
  11. "Prions affect the appearance of other prions: the story of [PIN(+)]."
    Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.
    Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION.
  12. "Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation."
    Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G., Philippe M., Zhouravleva G.
    Mol. Cell. Biol. 22:3301-3315(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAB1.
  13. "Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation."
    Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S., Katada T.
    J. Biol. Chem. 278:38287-38291(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAB1.
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay."
    Kobayashi T., Funakoshi Y., Hoshino S., Katada T.
    J. Biol. Chem. 279:45693-45700(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAB1.
  16. "Protein-only transmission of three yeast prion strains."
    King C.Y., Diaz-Avalos R.
    Nature 428:319-323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION PROPAGATION, AMYLOID STRUCTURE.
  17. "Conformational variations in an infectious protein determine prion strain differences."
    Tanaka M., Chien P., Naber N., Cooke R., Weissman J.S.
    Nature 428:323-328(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION PROPAGATION, AMYLOID STRUCTURE.
  18. "A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay."
    Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A.
    Nature 432:112-118(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAB1.
  19. "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.
  20. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  21. "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].
  22. "The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system."
    Lancaster A.K., Bardill J.P., True H.L., Masel J.
    Genetics 184:393-400(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION APPEARANCE.
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Structure of the cross-beta spine of amyloid-like fibrils."
    Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., Eisenberg D.
    Nature 435:773-778(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 7-13.
  25. "Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure."
    Shewmaker F., Wickner R.B., Tycko R.
    Proc. Natl. Acad. Sci. U.S.A. 103:19754-19759(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-253.

Entry informationi

Entry nameiERF3_YEAST
AccessioniPrimary (citable) accession number: P05453
Secondary accession number(s): D6VSF4, P05420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 11, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

[PSI+] is the prion form of SUP35 (PubMed:8978027). [PSI+] is the result of a conformational change of the cellular SUP35 protein that becomes self-propagating and infectious. This conformational change generates a form of SUP35 that assembles into amyloid fibrils. [PSI+]-aggregates sequester soluble SUP35, resulting in defects in faithful translation termination by read-through of translation termination codons (PubMed:8670813). [PSI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PSI+] propagation (PubMed:9335589). It is speculated that the prion form would be at least mildly deleterious in most environments, but it might sometimes increases evolvability in certain harsh environments (PubMed:19917766).4 Publications
Present with 78900 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.