SAN1 ubiquitin-protein ligase SAN1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SAN1
Official Full Name: ubiquitin-protein ligase SAN1
Primary source: SGD:S000002550
Locus tag: YDR143C
See related: AllianceGenome:SGD:S000002550; FungiDB:YDR143C; VEuPathDB:YDR143C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables ubiquitin-protein transferase activity. Involved in nuclear protein quality control by the ubiquitin-proteasome system. Located in cytoplasm and nucleus. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See SAN1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (742042..743874, complement)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites.
Title: The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites.
Study shows that San1 is involved in ubiquitylation and proteasomal degradation of the Spt16.
Title: Fine-Tuning of FACT by the Ubiquitin Proteasome System in Regulation of Transcriptional Elongation.
Cdc34 and Ubc1 are both sufficient for promoting San1 activity, San1 functions preferentially with Ubc1, including when both Ubc1 and Cdc34 are present.
Title: The San1 Ubiquitin Ligase Functions Preferentially with Ubiquitin-conjugating Enzyme Ubc1 during Protein Quality Control.
This study shows that an increasing molecular mass of substrates prevents nuclear San1-triggered proteasomal degradation but renders them susceptible to cytoplasmic Ubr1-triggered degradation.
Title: Molecular mass as a determinant for nuclear San1-dependent targeting of misfolded cytosolic proteins to proteasomal degradation.
Data indicate that the presence of key residues in San1 have been evolutionarily minimized to avoid self-destruction either in cis or in trans.
Title: Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction.
Data indicate that the Hsp70, Ssa1p, facilitates an interaction between a novel misfolded substrate and San1p.
Title: Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase.
phenotypic and biochemical studies of Ubr1 and San1 indicate that two strategies are employed for cytoplasmic QC: chaperone-assisted ubiquitination by Ubr1 and chaperone-dependent delivery to nuclear San1
Title: Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1.

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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
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin-protein transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in nuclear protein quality control by the ubiquitin-proteasome system	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to misfolded protein	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ubiquitin-dependent protein catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IMP Inferred from Mutant Phenotype more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisome	HDA more info	PubMed

General protein information

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Preferred Names: ubiquitin-protein ligase SAN1

NP_010427.3

Ubiquitin-protein ligase; role in proteasome-dependent degradation of aberrant nuclear proteins; targets substrates with regions of exposed hydrophobicity; contains intrinsically disordered regions involved in substrate recognition; prefers a window of exposed hydrophobicity that causes a particular level of protein insolubility, suggesting that San1p evolved to target highly aggregation-prone proteins; localizes to the cytoplasm, nucleus and peroxisomes

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001136.10 Reference assembly

Range

742042..743874 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180450.3 → NP_010427.3 TPA: ubiquitin-protein ligase SAN1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010427.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VSC6, P22470

UniProtKB/TrEMBL

A6ZYA3, G2WAP3, N1P4T6

Conserved Domains (2) summary

COG5243
Location:242 → 424

HRD1; HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones]

pfam13639
Location:251 → 280

zf-RING_2; Ring finger domain