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Entry version 215 (07 Oct 2020)
Sequence version 1 (01 Nov 1988)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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 increase evolvability in certain harsh environments (PubMed:19917766).4 Publications
Present with 78900 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei273Interacts with GTP/GDPBy similarity1
Sitei407Interacts with GTP/GDPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi267 – 274GTPBy similarity8
Nucleotide bindingi344 – 348GTPBy similarity5
Nucleotide bindingi406 – 409GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPrion
Biological processProtein biosynthesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
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)

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SUP35
Synonyms:GST1, PNM2, SAL3, SUF12, SUP2
Ordered Locus Names:YDR172W
ORF Names:YD9395.05
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDR172W

Saccharomyces Genome Database

More...
SGDi
S000002579, SUP35

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3308902

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000914822 – 685Eukaryotic peptide chain release factor GTP-binding subunitAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei571PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P05453

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P05453

PRoteomics IDEntifications database

More...
PRIDEi
P05453

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P05453

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of two subunits, one of which binds GTP.

Interacts with polyadenylate-binding protein PAB1, and TPA1.

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32225, 885 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-435, Translation release factor ERF1-ERF3 complex

Database of interacting proteins

More...
DIPi
DIP-376N

Protein interaction database and analysis system

More...
IntActi
P05453, 40 interactors

Molecular INTeraction database

More...
MINTi
P05453

STRING: functional protein association networks

More...
STRINGi
4932.YDR172W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P05453, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P05453

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P05453

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P05453

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini258 – 484tr-type GPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0459, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000169696

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007265_3_8_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05453

KEGG Orthology (KO)

More...
KOi
K03267

Identification of Orthologs from Complete Genome Data

More...
OMAi
NDETCTG

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR003285, Sup35
IPR000795, TF_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR009001, Transl_elong_EF1A/Init_IF2_C
IPR004160, Transl_elong_EFTu/EF1A_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit
PF03143, GTP_EFTU_D3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00315, ELONGATNFCT
PR01343, YEASTERF

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50447, SSF50447, 1 hit
SSF50465, SSF50465, 1 hit
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i43912A6D77DFA153
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti53S → C in CAA68760 (PubMed:2841115).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S00733, EFBYS2

NCBI Reference Sequences

More...
RefSeqi
NP_010457.3, NM_001180479.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR172W_mRNA; YDR172W; YDR172W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851752

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR172W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
BMRBiP05453
SMRiP05453
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32225, 885 interactors
ComplexPortaliCPX-435, Translation release factor ERF1-ERF3 complex
DIPiDIP-376N
IntActiP05453, 40 interactors
MINTiP05453
STRINGi4932.YDR172W

Chemistry databases

ChEMBLiCHEMBL3308902

PTM databases

iPTMnetiP05453

Proteomic databases

MaxQBiP05453
PaxDbiP05453
PRIDEiP05453

Genome annotation databases

EnsemblFungiiYDR172W_mRNA; YDR172W; YDR172W
GeneIDi851752
KEGGisce:YDR172W

Organism-specific databases

EuPathDBiFungiDB:YDR172W
SGDiS000002579, SUP35

Phylogenomic databases

eggNOGiKOG0459, Eukaryota
GeneTreeiENSGT00940000169696
HOGENOMiCLU_007265_3_8_1
InParanoidiP05453
KOiK03267
OMAiNDETCTG

Enzyme and pathway databases

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

EvolutionaryTraceiP05453

Protein Ontology

More...
PROi
PR:P05453
RNActiP05453, protein

Family and domain databases

InterProiView protein in InterPro
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR003285, Sup35
IPR000795, TF_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR009001, Transl_elong_EF1A/Init_IF2_C
IPR004160, Transl_elong_EFTu/EF1A_C
PfamiView protein in Pfam
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit
PF03143, GTP_EFTU_D3, 1 hit
PRINTSiPR00315, ELONGATNFCT
PR01343, YEASTERF
SUPFAMiSSF50447, SSF50447, 1 hit
SSF50465, SSF50465, 1 hit
SSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERF3_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05453
Secondary accession number(s): D6VSF4, P05420
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 7, 2020
This is version 215 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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