ATG12 Atg12p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: ATG12
Official Full Name: Atg12p
Primary source: SGD:S000000421
Locus tag: YBR217W
See related: AllianceGenome:SGD:S000000421; FungiDB:YBR217W; VEuPathDB:YBR217W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: APG12
Summary: Enables enzyme activator activity and protein tag activity. Contributes to Atg8-family ligase activity. Involved in autophagy of mitochondrion; cytoplasm to vacuole targeting by the Cvt pathway; and macroautophagy. Located in cytosol. Part of Atg12-Atg5-Atg16 complex. Orthologous to human ATG12 (autophagy related 12). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See ATG12 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (657832..658392)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Intrinsically Disordered N Terminus in Atg12 from Yeast Is Necessary for the Functional Structure of the Protein.
Title: The Intrinsically Disordered N Terminus in Atg12 from Yeast Is Necessary for the Functional Structure of the Protein.
Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.
Title: Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.
Here, the authors discover a novel mechanism for the PAS targeting of Atg12-Atg5-Atg16, which is mediated by the interaction of Atg12 with the Atg1 kinase complex that serves as a scaffold for pre-autophagosomal structure organization.
Title: Two distinct mechanisms target the autophagy-related E3 complex to the pre-autophagosomal structure.
Atg1, Atg8 and the Atg16-Atg12-Atg5 complex were present at both the VICS and the cup-shaped IM.
Title: Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae.
Atg12 functions as a binding module for Atg3, the E2 enzyme for Atg8, thus endowing Atg5 with the ability to interact with Atg3 to facilitate Atg8 lipidation.
Title: Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation.
Atg12-Atg5 induces a reorientation of the cysteine residue toward the threonine residue, which enhances the conjugase activity of Atg3
Title: Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site.
It was shown that the yeast Atg5-Atg12/Atg16 complex directly binds membranes. Membrane binding is mediated by Atg5, inhibited by Atg12 and activated by Atg16.
Title: Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16 complex during autophagosome formation.
the Atg12-Atg5 conjugate is a ubiquitin-protein ligase (E3)-like enzyme for Atg8-PE conjugation reaction, distinctively promoting protein-lipid conjugation
Title: The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy.
F154 plays a critical role in the assembly of a functional Atg12-Atg5.Atg16 complex that is requisite for autophagosome formation.
Title: Structure-function relationship of Atg12, a ubiquitin-like modifier essential for autophagy.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
contributes_to Atg8-family ligase activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to Atg8-family ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables enzyme activator activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tag activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein tag activity	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in C-terminal protein lipidation	IDA Inferred from Direct Assay more info	PubMed
involved_in autophagosome assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in autophagosome assembly	IEA Inferred from Electronic Annotation more info
involved_in autophagosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in autophagosome maturation	IBA Inferred from Biological aspect of Ancestor more info
involved_in autophagy	IEA Inferred from Electronic Annotation more info
involved_in autophagy of mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
involved_in autophagy of mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cytoplasm to vacuole targeting by the Cvt pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in glycophagy	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleophagy	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in piecemeal microautophagy of the nucleus	IBA Inferred from Biological aspect of Ancestor more info
involved_in piecemeal microautophagy of the nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein lipidation involved in autophagosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of Atg12-Atg5-Atg16 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Atg12-Atg5-Atg16 complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in autophagosome membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
is_active_in phagophore assembly site membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in phagophore assembly site membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Atg12p

NP_009776.1

Ubiquitin-like modifier involved in autophagy and the Cvt pathway; conserved; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg5p-Atg12p conjugate enhances E2 activity of Atg3p by rearranging its catalytic site, also forms a complex with Atg16p; the Atg5-Atg12/Atg16 complex binds to membranes and is essential for autophagosome formation; homolog of mammalian ULK1