SIZ1 SUMO ligase SIZ1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SIZ1
Official Full Name: SUMO ligase SIZ1
Primary source: SGD:S000002817
Locus tag: YDR409W
See related: AllianceGenome:SGD:S000002817; FungiDB:YDR409W; VEuPathDB:YDR409W
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: ULL1
Summary: Enables SUMO transferase activity and double-stranded DNA binding activity. Involved in several processes, including DNA double-strand break attachment to nuclear envelope; negative regulation of protein ubiquitination; and protein sumoylation. Located in chromatin and septin ring. Orthologous to several human genes including PIAS2 (protein inhibitor of activated STAT 2); PIAS3 (protein inhibitor of activated STAT 3); and PIAS4 (protein inhibitor of activated STAT 4). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SIZ1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (1289406..1292120)

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

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SUMOylation stabilizes sister kinetochore biorientation to allow timely anaphase.
Title: SUMOylation stabilizes sister kinetochore biorientation to allow timely anaphase.
Siz1 can be ubiquitylated in vivo and is degraded in an Slx5-dependent manner.
Title: A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.
defects in Rad6 postreplication repair pathway and Siz1/Srs2 homologous recombination suppression (HRS) pathway genes suppressed the increased gross chromosomal rearrangement rates seen in asf1 mutants
Title: The Saccharomyces cerevisiae Rad6 postreplication repair and Siz1/Srs2 homologous recombination-inhibiting pathways process DNA damage that arises in asf1 mutants.
Report structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Title: Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
NMR titration experiments showed that yeast Siz1 SAP domain uses alpha2-helix for DNA binding.
Title: Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa.
The SUMO-specific ligase Siz1 both stimulates the overall efficiency of sumoylation and selects the modification site on PCNA.
Title: Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae.
the SP-RING and PINIT of Ull1/Siz1 are core domains of the SUMO ligase, and the other domains are regulatory for protein stability and subcellular localization
Title: Yeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory domains.
data suggest that SUMO attachment negatively regulates Flp1 levels, which may partially account for the increased 2 microm copy number in the siz1Delta siz2Delta strain
Title: Misregulation of 2 microm circle copy number in a SUMO pathway mutant.

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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 SUMO ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables SUMO transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables SUMO transferase activity	IEA Inferred from Electronic Annotation more info
enables SUMO transferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables double-stranded DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA double-strand break attachment to nuclear envelope	IGI Inferred from Genetic Interaction more info	PubMed
involved_in chromosome segregation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of protein ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of protein ubiquitination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein sumoylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein sumoylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein sumoylation	IEA Inferred from Electronic Annotation more info
involved_in protein sumoylation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein sumoylation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cellular bud neck	IEA Inferred from Electronic Annotation more info
located_in chromatin	IBA Inferred from Biological aspect of Ancestor more info
located_in chromatin	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in septin ring	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: SUMO ligase SIZ1

NP_010697.3

SUMO E3 ligase; promotes attachment of small ubiquitin-related modifier sumo (Smt3p) to primarily cytoplasmic proteins; regulates Rsp5p ubiquitin ligase activity and is in turn itself regulated by Rsp5p; required for sumoylation of septins and histone H3 variant Cse4p, a prerequisite for STUbL-mediated Ub-dependent degradation; localizes to the septin ring; acts as an adapter between E2, Ubc9p and substrates; tends to compensate for survival of DNA damage in absence of Nfi1p

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

1289406..1292120

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180717.3 → NP_010697.3 TPA: SUMO ligase SIZ1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010697.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VT41, Q04195, Q06762, Q7LIJ4

UniProtKB/TrEMBL

B5VGU1, N1P5I8

Conserved Domains (3) summary

smart00513
Location:34 → 68

SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation

cd16793
Location:358 → 405

SP-RING_ScSiz_like; SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and similar proteins

pfam14324
Location:176 → 311

PINIT; PINIT domain