RAD4 Rad4p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: RAD4
Official Full Name: Rad4p
Primary source: SGD:S000000964
Locus tag: YER162C
See related: AllianceGenome:SGD:S000000964; FungiDB:YER162C; VEuPathDB:YER162C
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 single-strand break-containing DNA binding activity. Involved in DNA metabolic process; negative regulation of transcription by RNA polymerase II; and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in cytosol and nucleus. Part of nucleotide-excision repair factor 2 complex. Used to study xeroderma pigmentosum. Human ortholog(s) of this gene implicated in pancreatic cancer; serous cystadenocarcinoma; xeroderma pigmentosum; and xeroderma pigmentosum group C. Orthologous to human XPC (XPC complex subunit, DNA damage recognition and repair factor). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See RAD4 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 1

Sequence:: Chromosome: V; NC_001137.3 (500630..502894, complement)

Chromosome V - NC_001137.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair.
Title: Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair.
Lactate Induces Cisplatin Resistance in S. cerevisiae through a Rad4p-Dependent Process.
Title: Lactate Induces Cisplatin Resistance in S. cerevisiae through a Rad4p-Dependent Process.
The DNA damage-sensing NER repair factor XPC-RAD23B does not recognize bulky DNA lesions with a missing nucleotide opposite the lesion.
Title: The DNA damage-sensing NER repair factor XPC-RAD23B does not recognize bulky DNA lesions with a missing nucleotide opposite the lesion.
Tethering-facilitated DNA 'opening' and complementary roles of beta-hairpin motifs in the Rad4/XPC DNA damage sensor protein.
Title: Tethering-facilitated DNA 'opening' and complementary roles of β-hairpin motifs in the Rad4/XPC DNA damage sensor protein.
Sequence specificity, energetics and mechanism of mismatch recognition by DNA damage sensing protein Rad4/XPC has been reported.
Title: Sequence specificity, energetics and mechanism of mismatch recognition by DNA damage sensing protein Rad4/XPC.
Enhanced spontaneous DNA twisting/bending fluctuations promote mismatch recognition by the Rad4 nucleotide excision repair complex.
Title: Enhanced spontaneous DNA twisting/bending fluctuations unveiled by fluorescence lifetime distributions promote mismatch recognition by the Rad4 nucleotide excision repair complex.
Upon binding of RAD4 to the DNA, the global free energy minimum is shifted to the extrahelical state indicating the key role of RAD4-DNA interactions in catalyzing the dinucleotide base extrusion in the DNA-RAD4 complex.
Title: Molecular Mechanism, Dynamics, and Energetics of Protein-Mediated Dinucleotide Flipping in a Mismatched DNA: A Computational Study of the RAD4-DNA Complex.
Rad4-Rad23 forms non-motile complexes or conducts a one-dimensional search for DNA lesions via either random diffusion or constrained motion.
Title: Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process.
Rad4 recognizes lesions in a step-wise "twist-open" mechanism, in which preliminary twisting represents Rad4 interconverting between search and interrogation modes.
Title: Twist-open mechanism of DNA damage recognition by the Rad4/XPC nucleotide excision repair complex.
Rad4/XPC uses a kinetic gating mechanism whereby lesion selectivity arises from the kinetic competition between DNA opening and the residence time of Rad4/XPC per site.
Title: Kinetic gating mechanism of DNA damage recognition by Rad4/XPC.

Submit: New GeneRIF Correction See all GeneRIFs (19)

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
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables damaged DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables damaged DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables damaged DNA binding	IEA Inferred from Electronic Annotation more info
enables single-strand break-containing DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables single-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in DNA topological change	IDA Inferred from Direct Assay more info	PubMed
involved_in mismatch repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of transcription by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nucleotide-excision repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleotide-excision repair	IEA Inferred from Electronic Annotation more info
involved_in nucleotide-excision repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of XPC complex	IBA Inferred from Biological aspect of Ancestor more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
part_of nucleotide-excision repair factor 2 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of nucleotide-excision repair factor 2 complex	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Rad4p

NP_011089.4

Damaged-DNA binding subunit of Nuclear Excision Repair Factor 2; recognizes and binds damaged DNA with Rad23p during nucleotide excision repair (NER); also involved with Rad23p in turnover of ubiquitylated proteins; Rad4p-Rad23p heterodimer binds to promoters of DNA damage response genes to repress their transcription in the absence of DNA damage; RAD4 and RAD51 pathways confer resistance to benzo[a]pyrene dihydrodiol

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_001137.3 Reference assembly

Range

500630..502894 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179052.4 → NP_011089.4 TPA: Rad4p [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011089.4

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DM70, P14736

UniProtKB/TrEMBL

B5VHT9, N1P562

Conserved Domains (1) summary

COG5535
Location:1 → 669

RAD4; DNA repair protein RAD4 [DNA replication, recombination, and repair]