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Entry version 163 (26 Feb 2020)
Sequence version 1 (01 Oct 1993)
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Protein

ATPase family gene 2 protein

Gene

AFG2

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

ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (PubMed:12006565, PubMed:17646390, PubMed:23185031, PubMed:24371142). Plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RLP24 from the pre-ribosomal particles (PubMed:17646390, PubMed:23185031, PubMed:24371142). This step facilitates the subsequent release of other shuttling proteins such as NOG1 and allows the transition of the pre-ribosomal particles to later maturation forms that bind REI1 (PubMed:17646390, PubMed:23185031, PubMed:24371142). Essential for viability (PubMed:8109176, PubMed:24371142).5 Publications

Miscellaneous

Present with 799 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The hexamer is activated by RLP24 during pre-60S ribosomal particle maturation; RLP24 activates ATPase activity of both ATP-binding regions and increases cooperativity between AFG2 subunits (PubMed:23185031). The second ATP-binding region is inhibited by diazaborine; the inhibition requires prior ATP binding specifically to the second ATP-binding region (PubMed:24371142).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=35 µM for ATP1 Publication
  2. KM=270 µM for ATP1 Publication
  1. Vmax=1.99 µmol/h/mg enzyme1 Publication
  2. Vmax=28.7 µmol/h/mg enzyme (in presence of RLP24)1 Publication

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 bindingi286 – 293ATP 1Sequence analysis1 Publication8
Nucleotide bindingi557 – 564ATP 2Sequence analysis1 Publication8

<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 functionChaperone, Hydrolase
Biological processRibosome biogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32461-MONOMER

<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:
ATPase family gene 2 protein1 Publication (EC:3.6.4.103 Publications)
Alternative name(s):
Diazaborine resistance gene 1 protein1 Publication
<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:AFG21 PublicationImported
Synonyms:DRG11 Publication
Ordered Locus Names:YLR397C
ORF Names:L8084.16
<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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR397C

Saccharomyces Genome Database

More...
SGDi
S000004389 AFG2

<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

Keywords - Cellular componenti

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi343F → L in dgr1-sup*; moderate loss of catalytic activity. No growth defect. Restores growth and formation of 60S ribosomal subunit maturation but not catalytic activity or oligomerization; when associated with S-457. 1 Publication1
Mutagenesisi346E → Q: Reduces basal and RLP24-dependent ATPase activity. Increases interaction with RLP24. Slightly reduces RLP24 release. Does not affect composition of pre-60S ribosomal particles or growth. 2 Publications1
Mutagenesisi457L → S in afg2-18, drg1-18 or drg1-ts; temperature sensitive mutant. At the restrictive temperature of 37 degree Celsius, impaired growth. Severe loss of ATPase activity, homohexamer formation and 60S ribosomal subunit maturation. Prevents the release of shuttling proteins NOG1, RLP24 and ARX1 from cytoplasmic pre-60S particles resulting in their cytoplasmic accumulation. Loss of interaction with RLP24 and pre-60S particles. Restores growth and formation of 60S ribosomal subunit maturation but not catalytic activity or oligomerization; when associated with L-343. 3 Publications1
Mutagenesisi561 – 562CS → TG: Increases ATPase activity and reduces affinity for ATP. Mild defect in oligomerization. 1 Publication2
Mutagenesisi561C → T in drg1-11; severe loss of ATPase activity. Severe loss of oligomerization. Resistant to diazaborine-mediated growth inhibition. 1 Publication1
Mutagenesisi562S → G: Increases ATPase activity. Loss of oligomerization. 1 Publication1
Mutagenesisi569A → V in drg1-3; resistant to diazaborine-mediated growth inhibition. 1 Publication1
Mutagenesisi617E → Q: Increases basal ATPase activity. Reduces RLP24-mediated activation. Does not affect interaction with RLP24. Prevents the release of shuttling proteins RLP24, NOG1 and MEX67 from cytoplasmic pre-60S ribosomal particles. Does not affect the interaction with pre-60S ribosomal particles. 3 Publications1
Mutagenesisi725V → E in drg1-1; slight loss of ATPase activity. No effect on affinity for ATP or oligomerization. Resistant to diazaborine-mediated growth inhibition. No defect in RLP24 release from pre-60S ribosomal particles in the absence or in the presence of diazaborine. 2 Publications1
Mutagenesisi725V → L in drg1-4; resistant to diazaborine-mediated growth inhibition. 1 Publication1

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000845921 – 780ATPase family gene 2 proteinAdd BLAST780

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32794

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

More...
PaxDbi
P32794

PRoteomics IDEntifications database

More...
PRIDEi
P32794

<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

Homohexamer; ATP binding induces oligomerization (PubMed:12006565, PubMed:23185031).

Forms a ring-shaped particle of about 12 nm diameter, that displays 6-fold radial symmetry (PubMed:12006565). Associates with cytoplasmic pre-60S ribosomal particles containing ARX1, ALB1, RLP24 and NOG1 (PubMed:17646390). Binds to pre-60S ribosomal particles soon after their export from the nucleus and is released before REI1 and LSG1 are incorporated into the particles (PubMed:17646390). Hexameric form interacts with RLP24 (via C-terminal); the interaction recruits AFG2 to pre-60S ribosomal particles and promotes AFG2 ATPase activity and RLP24 release from pre-60S ribosomal particles (PubMed:23185031, PubMed:24371142).

Interacts (via N-terminus) with nucleoporin NUP116 (via N-terminus); the interaction is required for RLP24 release from pre-60S ribosomal particles (PubMed:23185031).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31656, 325 interactors

Database of interacting proteins

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DIPi
DIP-4470N

Protein interaction database and analysis system

More...
IntActi
P32794, 10 interactors

Molecular INTeraction database

More...
MINTi
P32794

STRING: functional protein association networks

More...
STRINGi
4932.YLR397C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32794 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

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

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SMRi
P32794

Database of comparative protein structure models

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ModBasei
Search...

<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

<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 first ATP-binding region binds ATP with low affinity whereas the second ATP-binding region binds ATP with high affinity (PubMed:12006565). ATP hydrolysis mediated by the second ATP binding region releases RLP24 from pre-60S ribosomal particles whereas the ATP hydrolysis mediated by the first ATP binding region is subsequently required for RLP24 dissociation from AFG2, probably by disassembling AFG2 into monomers (PubMed:23185031, PubMed:24371142).1 Publication2 Publications

<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

Belongs to the AAA ATPase family. AFG2 subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000688_12_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P32794

KEGG Orthology (KO)

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KOi
K14575

Identification of Orthologs from Complete Genome Data

More...
OMAi
DVGDMAE

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR041569 AAA_lid_3
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 2 hits
PF17862 AAA_lid_3, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00674 AAA, 2 hits

<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.

P32794-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPKSSSSGS KKKSSASSNS ADAKASKFKL PAEFITRPHP SKDHGKETCT
60 70 80 90 100
AYIHPNVLSS LEINPGSFCT VGKIGENGIL VIARAGDEEV HPVNVITLST
110 120 130 140 150
TIRSVGNLIL GDRLELKKAQ VQPPYATKVT VGSLQGYNIL ECMEEKVIQK
160 170 180 190 200
LLDDSGVIMP GMIFQNLKTK AGDESIDVVI TDASDDSLPD VSQLDLNMDD
210 220 230 240 250
MYGGLDNLFY LSPPFIFRKG STHITFSKET QANRKYNLPE PLSYAAVGGL
260 270 280 290 300
DKEIESLKSA IEIPLHQPTL FSSFGVSPPR GILLHGPPGT GKTMLLRVVA
310 320 330 340 350
NTSNAHVLTI NGPSIVSKYL GETEAALRDI FNEARKYQPS IIFIDEIDSI
360 370 380 390 400
APNRANDDSG EVESRVVATL LTLMDGMGAA GKVVVIAATN RPNSVDPALR
410 420 430 440 450
RPGRFDQEVE IGIPDVDARF DILTKQFSRM SSDRHVLDSE AIKYIASKTH
460 470 480 490 500
GYVGADLTAL CRESVMKTIQ RGLGTDANID KFSLKVTLKD VESAMVDIRP
510 520 530 540 550
SAMREIFLEM PKVYWSDIGG QEELKTKMKE MIQLPLEASE TFARLGISAP
560 570 580 590 600
KGVLLYGPPG CSKTLTAKAL ATESGINFLA VKGPEIFNKY VGESERAIRE
610 620 630 640 650
IFRKARSAAP SIIFFDEIDA LSPDRDGSST SAANHVLTSL LNEIDGVEEL
660 670 680 690 700
KGVVIVAATN RPDEIDAALL RPGRLDRHIY VGPPDVNARL EILKKCTKKF
710 720 730 740 750
NTEESGVDLH ELADRTEGYS GAEVVLLCQE AGLAAIMEDL DVAKVELRHF
760 770 780
EKAFKGIARG ITPEMLSYYE EFALRSGSSS
Length:780
Mass (Da):84,748
Last modified:October 1, 1993 - 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:i75094DFA3D401D4E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L14615 Unassigned DNA Translation: AAC37367.1
U19729 Genomic DNA Translation: AAB82355.1
AY693116 Genomic DNA Translation: AAT93135.1
BK006945 Genomic DNA Translation: DAA09698.1

Protein sequence database of the Protein Information Resource

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PIRi
S39110

NCBI Reference Sequences

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RefSeqi
NP_013501.1, NM_001182285.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR397C_mRNA; YLR397C; YLR397C

Database of genes from NCBI RefSeq genomes

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GeneIDi
851113

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR397C

<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
L14615 Unassigned DNA Translation: AAC37367.1
U19729 Genomic DNA Translation: AAB82355.1
AY693116 Genomic DNA Translation: AAT93135.1
BK006945 Genomic DNA Translation: DAA09698.1
PIRiS39110
RefSeqiNP_013501.1, NM_001182285.1

3D structure databases

SMRiP32794
ModBaseiSearch...

Protein-protein interaction databases

BioGridi31656, 325 interactors
DIPiDIP-4470N
IntActiP32794, 10 interactors
MINTiP32794
STRINGi4932.YLR397C

Proteomic databases

MaxQBiP32794
PaxDbiP32794
PRIDEiP32794

Genome annotation databases

EnsemblFungiiYLR397C_mRNA; YLR397C; YLR397C
GeneIDi851113
KEGGisce:YLR397C

Organism-specific databases

EuPathDBiFungiDB:YLR397C
SGDiS000004389 AFG2

Phylogenomic databases

HOGENOMiCLU_000688_12_3_1
InParanoidiP32794
KOiK14575
OMAiDVGDMAE

Enzyme and pathway databases

BioCyciYEAST:G3O-32461-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32794
RNActiP32794 protein

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR041569 AAA_lid_3
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00004 AAA, 2 hits
PF17862 AAA_lid_3, 2 hits
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00674 AAA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiAFG2_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: P32794
Secondary accession number(s): D6VZ32
<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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 26, 2020
This is version 163 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

Reference proteome

Documents

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