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Entry version 180 (02 Jun 2021)
Sequence version 1 (01 Feb 1995)
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Protein

Ubiquitin-like modifier-activating enzyme ATG7

Gene

ATG7

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

E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity.

22 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei507Glycyl thioester intermediate1 Publication1

<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

Biological processAutophagy, Protein transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1632852, Macroautophagy
R-SCE-6798695, Neutrophil degranulation

<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:
Ubiquitin-like modifier-activating enzyme ATG7
Alternative name(s):
ATG12-activating enzyme E1 ATG7
Autophagy-related protein 7
Cytoplasm to vacuole targeting protein 2
<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:ATG7
Synonyms:APG7, CVT2
Ordered Locus Names:YHR171W
<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 VIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000001214, ATG7

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YHR171W

<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>Mutagenesisi333G → A: Loss of interaction with ATG8 and ATG12, and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 2 Publications1
Mutagenesisi443R → A: Loss of interaction with ATG8. 1 Publication1
Mutagenesisi466S → A: Loss of interaction with ATG8; when associated with F-486 and A-490. 1 Publication1
Mutagenesisi486Y → F: Loss of interaction with ATG8; when associated with A-466 and A-490. 1 Publication1
Mutagenesisi490D → A: Loss of interaction with ATG8; when associated with A-466 and F-486. 1 Publication1
Mutagenesisi507C → A: Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 4 Publications1
Mutagenesisi507C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and ATG8 (substrate) or between ATG7 and ATG12 (substrate), a stable complex with an O-ester bond is formed. No more formation of ATG12-ATG5 conjugate. 3 Publications1
Mutagenesisi511R → A: Impaired homodimerization and ATP-binding. Homodimerization and ATP-binding are recovered when it heterodimerizes with an ATG7 molecule with a R-524 mutation. 1 Publication1
Mutagenesisi524E → R: Impaired homodimerization and ATP-binding. Homodimerization and ATP-binding are recovered when it heterodimerizes with an ATG7 molecule with a A-511 mutation. 1 Publication1
Mutagenesisi550R → A: Loss of interaction with ATG8. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002128221 – 630Ubiquitin-like modifier-activating enzyme ATG7Add BLAST630

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38862

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

More...
PaxDbi
P38862

PRoteomics IDEntifications database

More...
PRIDEi
P38862

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P38862

<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

Homodimer; homodimerization is required for ATP-binding (PubMed:11139573, PubMed:21193819, PubMed:29295865).

Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191).

Interacts also with ATG3 (PubMed:11139573, PubMed:17227760, PubMed:22056771, PubMed:23142976).

11 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
36605, 120 interactors

Database of interacting proteins

More...
DIPi
DIP-1196N

Protein interaction database and analysis system

More...
IntActi
P38862, 8 interactors

Molecular INTeraction database

More...
MINTi
P38862

STRING: functional protein association networks

More...
STRINGi
4932.YHR171W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P38862, 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

Secondary structure

1630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P38862

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

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SMRi
P38862

Database of comparative protein structure models

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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
P38862

<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

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>Regioni591 – 630HomodimerizationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi331 – 336GXGXXG motif6

<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 C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C-terminal 17 residues are required for the ATG8 lipidation.
The GxGxxG motif is important for the function, possibly through binding with ATP.

<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 ATG7 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2337, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000017509

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012998_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38862

Identification of Orthologs from Complete Genome Data

More...
OMAi
PMAGHPI

Family and domain databases

Database of protein disorder

More...
DisProti
DP02249

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.140.100, 1 hit
3.40.140.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006285, Atg7
IPR032197, Atg7_N
IPR042522, Atg7_N_1
IPR042523, Atg7_N_2
IPR000594, ThiF_NAD_FAD-bd
IPR035985, Ubiquitin-activating_enz

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16420, ATG7_N, 1 hit
PF00899, ThiF, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF69572, SSF69572, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01381, E1_like_apg7, 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.

P38862-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN
60 70 80 90 100
IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL
110 120 130 140 150
FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS
160 170 180 190 200
TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT
210 220 230 240 250
KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL
260 270 280 290 300
NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
310 320 330 340 350
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK
360 370 380 390 400
ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK
410 420 430 440 450
LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS
460 470 480 490 500
NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD
510 520 530 540 550
RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR
560 570 580 590 600
GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
610 620 630
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
Length:630
Mass (Da):71,428
Last modified:February 1, 1995 - 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:i561EEC94F0ED57F5
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
AB017925 Genomic DNA Translation: BAA33474.1
U00027 Genomic DNA Translation: AAB68016.1
BK006934 Genomic DNA Translation: DAA06864.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48910

NCBI Reference Sequences

More...
RefSeqi
NP_012041.1, NM_001179302.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR171W_mRNA; YHR171W; YHR171W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856576

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR171W

<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
AB017925 Genomic DNA Translation: BAA33474.1
U00027 Genomic DNA Translation: AAB68016.1
BK006934 Genomic DNA Translation: DAA06864.1
PIRiS48910
RefSeqiNP_012041.1, NM_001179302.1

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
2LI5NMR-B601-630[»]
3RUIX-ray1.91A293-630[»]
3RUJX-ray2.10A1-294[»]
3T7EX-ray2.25A289-630[»]
3T7FX-ray1.89A1-289[»]
3T7GX-ray2.08A/B1-289[»]
3T7HX-ray1.60A/B1-289[»]
3VH1X-ray3.00A1-595[»]
3VH2X-ray3.30A1-613[»]
3VH3X-ray2.00A295-630[»]
3VH4X-ray2.65A295-630[»]
4GSJX-ray1.70A1-289[»]
4GSKX-ray2.90A/B1-613[»]
4GSLX-ray2.70A/B1-613[»]
5YECX-ray2.15A/C295-630[»]
BMRBiP38862
SMRiP38862
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36605, 120 interactors
DIPiDIP-1196N
IntActiP38862, 8 interactors
MINTiP38862
STRINGi4932.YHR171W

Proteomic databases

MaxQBiP38862
PaxDbiP38862
PRIDEiP38862
TopDownProteomicsiP38862

Genome annotation databases

EnsemblFungiiYHR171W_mRNA; YHR171W; YHR171W
GeneIDi856576
KEGGisce:YHR171W

Organism-specific databases

SGDiS000001214, ATG7
VEuPathDBiFungiDB:YHR171W

Phylogenomic databases

eggNOGiKOG2337, Eukaryota
GeneTreeiENSGT00390000017509
HOGENOMiCLU_012998_2_1_1
InParanoidiP38862
OMAiPMAGHPI

Enzyme and pathway databases

ReactomeiR-SCE-1632852, Macroautophagy
R-SCE-6798695, Neutrophil degranulation

Miscellaneous databases

EvolutionaryTraceiP38862

Protein Ontology

More...
PROi
PR:P38862
RNActiP38862, protein

Family and domain databases

DisProtiDP02249
Gene3Di3.40.140.100, 1 hit
3.40.140.70, 1 hit
InterProiView protein in InterPro
IPR006285, Atg7
IPR032197, Atg7_N
IPR042522, Atg7_N_1
IPR042523, Atg7_N_2
IPR000594, ThiF_NAD_FAD-bd
IPR035985, Ubiquitin-activating_enz
PfamiView protein in Pfam
PF16420, ATG7_N, 1 hit
PF00899, ThiF, 1 hit
SUPFAMiSSF69572, SSF69572, 1 hit
TIGRFAMsiTIGR01381, E1_like_apg7, 1 hit

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 nameiATG7_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: P38862
Secondary accession number(s): D3DLC0
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 2, 2021
This is version 180 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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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