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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)DescriptionActionsGraphical viewLength
Sitei273Interacts with GTP/GDPBy similarity1
Sitei407Interacts with GTP/GDPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi267 – 274GTPBy similarity8
Nucleotide bindingi344 – 348GTPBy similarity5
Nucleotide bindingi406 – 409GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • translation release factor activity Source: SGD

GO - Biological processi

  • cytoplasmic translational termination Source: GO_Central
  • 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-429958. mRNA decay by 3' to 5' exoribonuclease.
R-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 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000914822 – 685Eukaryotic peptide chain release factor GTP-binding subunitAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei571PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05453.
PRIDEiP05453.

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
SUP45P123855EBI-6540,EBI-6533

Protein-protein interaction databases

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YJOX-ray1.30A8-13[»]
1YJPX-ray1.80A7-13[»]
2OMMX-ray2.00A7-13[»]
4CRNelectron microscopy9.10P256-685[»]
5K2Eelectron microscopy1.00A8-13[»]
5K2Felectron microscopy1.00A8-13[»]
5K2Gelectron microscopy1.10A7-13[»]
5K2Helectron microscopy1.05A7-13[»]
ProteinModelPortaliP05453.
SMRiP05453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini258 – 484tr-type GPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 239Interaction with PAB1Add BLAST238
Regioni5 – 135Prion domain (PrD)Add BLAST131
Regioni139 – 249ChargedAdd BLAST111
Regioni267 – 274G1PROSITE-ProRule annotation8
Regioni323 – 327G2PROSITE-ProRule annotation5
Regioni344 – 347G3PROSITE-ProRule annotation4
Regioni406 – 409G4PROSITE-ProRule annotation4
Regioni448 – 450G5PROSITE-ProRule annotation3

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.
OMAiWYRGEPL.
OrthoDBiEOG092C2HV8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti53S → C in CAA68760 (PubMed:2841115).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YJOX-ray1.30A8-13[»]
1YJPX-ray1.80A7-13[»]
2OMMX-ray2.00A7-13[»]
4CRNelectron microscopy9.10P256-685[»]
5K2Eelectron microscopy1.00A8-13[»]
5K2Felectron microscopy1.00A8-13[»]
5K2Gelectron microscopy1.10A7-13[»]
5K2Helectron microscopy1.05A7-13[»]
ProteinModelPortaliP05453.
SMRiP05453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP05453.

Proteomic databases

MaxQBiP05453.
PRIDEiP05453.

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.
OMAiWYRGEPL.
OrthoDBiEOG092C2HV8.

Enzyme and pathway databases

BioCyciYEAST:G3O-29761-MONOMER.
ReactomeiR-SCE-429958. mRNA decay by 3' to 5' exoribonuclease.
R-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

EvolutionaryTraceiP05453.
PROiP05453.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. 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.
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...

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: November 30, 2016
This is version 183 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.