RAD18 RAD18 homolog (S. cerevisiae) [Homo sapiens] - Gene

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Summary

Official Symbol: RAD18provided by HGNC
Official Full Name: RAD18 homolog (S. cerevisiae)provided by HGNC
Primary source: HGNC:18278
See related: Ensembl:ENSG00000070950; HPRD:09242; MIM:605256; Vega:OTTHUMG00000090545
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: RNF73
Summary: The protein encoded by this gene is highly similar to S. cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions through its interaction with Rad6, which is an ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Similar to its yeast counterpart, this protein is able to interact with the human homolog of yeast Rad6 protein through a conserved ring-finger motif. Mutation of this motif results in defective replication of UV-damaged DNA and hypersensitivity to multiple mutagens. [provided by RefSeq, Jul 2008]

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Genomic context

Location :: 3p25-p24

Sequence :: Chromosome: 3; NC_000003.11 (8918880..9005159, complement)

See RAD18 in Epigenomics, MapViewer

Chromosome 3 - NC_000003.11 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

RAD18 interacts with BRCTx in a phosphorylation-dependent manner
Title: RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage.
The results demonstrate that RAD6A and RAD18 form a ternary complex, RAD6A-(RAD18)(2) and the presence of only one RAD6-binding domain in the two RAD18 subunits is sufficient for ternary complex formation and the ligase activity.
Title: Asymmetric nature of two subunits of RAD18, a RING-type ubiquitin ligase E3, in the human RAD6A-RAD18 ternary complex.
Data indicate that association of RAD18 with DSBs through ubiquitylated H2A and other ubiquitylated chromatin components allows recruitment of RAD9.
Title: Human RAD18 interacts with ubiquitylated chromatin components and facilitates RAD9 recruitment to DNA double strand breaks.
Data show that the homodimeric Rad18 RING domain can recruit two Rad6b E2 enzymes, whereas the full-length Rad18 homodimer binds only to a single Rad6b molecule.
Title: Symmetry and asymmetry of the RING-RING dimer of Rad18.
A novel pathway of Rad18-dependent DSB repair that is dissociable from known Rad18-mediated DNA repair mechanisms based on its independence from PCNA ubiquitination and requirement for E3 ligase activity.
Title: Rad18 E3 ubiquitin ligase activity mediates Fanconi anemia pathway activation and cell survival following DNA Topoisomerase 1 inhibition.
These data suggest a key role for the E3 ligase activity of RAD18 in the recruitment of FANCD2 and FANCI to chromatin and the events leading to their ubiquitylation during S phase.
Title: The E3 ubiquitin ligase RAD18 regulates ubiquitylation and chromatin loading of FANCD2 and FANCI.
E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6.
Title: E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6.
showed that the function of FA signaling pathway is at least partly mediated through coupling with hRad6/hRad18 signaling (HHR6 pathway)
Title: Convergence of Rad6/Rad18 and Fanconi anemia tumor suppressor pathways upon DNA damage.
RAD18-mediated PCNA monoubiquitination is a central hub for the mobilization of the Fanconi anemia DNA repair network pathway.
Title: RAD18-mediated ubiquitination of PCNA activates the Fanconi anemia DNA repair network.
Rad18 promotes FA core complex-dependent FANCD2 ubiquitination in a manner that is secondary to PCNA mono-ubiquitination.
Title: Rad18-mediated translesion synthesis of bulky DNA adducts is coupled to activation of the Fanconi anemia DNA repair pathway.

Submit: New GeneRIF Correction See all (31)

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Phenotypes

Review eQTL and phenotype association data in this region using PheGenI

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HIV-1 protein interactions

Protein	Gene	Interaction	Pubs
integrase	gag-pol	HIV-1 Integrase interacts with (co-immunoprecipitates) and co-localizes with hRad18 suggesting a role for hRad18 in the DNA repair events associated with the HIV-1 integration process	PubMed

Go to the HIV-1, Human Protein Interaction Database

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Products	Interactant	Other Gene	Source	Pubs	Description
Q9NS91	Q9NS91	RAD18	HPRD	PubMed
Q9NS91	P49459	UBE2A	HPRD	PubMed
Q9NS91	P63146	UBE2B	HPRD	PubMed
BioGRID:121212	BioGRID:123978	ANKRD32	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:113914	CDC7	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity
BioGRID:121212	BioGRID:108474	FANCD2	BioGRID	PubMed	Affinity Capture-Western; Co-localization
BioGRID:121212	BioGRID:120511	FANCI	BioGRID	PubMed	Co-localization
BioGRID:121212	BioGRID:128742	HIST1H2AA	BioGRID	PubMed	Affinity Capture-Western
BioGRID:121212	BioGRID:112480	HLTF	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:110763	NBN	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:111142	PCNA	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity; Reconstituted Complex
BioGRID:121212	BioGRID:111425	POLH	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Co-localization; Reconstituted Complex
BioGRID:121212	BioGRID:119532	POLK	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:131695	POLN	BioGRID	PubMed	Affinity Capture-Western
BioGRID:121212	BioGRID:121212	RAD18	BioGRID	PubMed	Co-crystal Structure; Reconstituted Complex
BioGRID:121212	BioGRID:111825	RAD51	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:129208	SHPRH	BioGRID	PubMed	Affinity Capture-Western
BioGRID:121212	BioGRID:117071	SRRM2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:121212	BioGRID:112497	SUMO2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:121212	BioGRID:234474	Shprh	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:121212	BioGRID:212040	Smc6	BioGRID	PubMed	Affinity Capture-MS
BioGRID:121212	BioGRID:113011	TP53BP1	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity; Reconstituted Complex
BioGRID:121212	BioGRID:113102	TSG101	BioGRID	PubMed	Two-hybrid
BioGRID:121212	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS; Reconstituted Complex
BioGRID:121212	BioGRID:113167	UBE2A	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:121212	BioGRID:113168	UBE2B	BioGRID	PubMed	Affinity Capture-Western; Co-crystal Structure; Co-purification; Reconstituted Complex; Two-hybrid
BioGRID:121212	BioGRID:113177	UBE2I	BioGRID	PubMed	Two-hybrid

Function	Evidence Code	Pubs
Y-form DNA binding	IDA Inferred from Direct Assay more info	PubMed
damaged DNA binding	NAS Non-traceable Author Statement more info	PubMed
ligase activity	IEA Inferred from Electronic Annotation more info
metal ion binding	IEA Inferred from Electronic Annotation more info
protein binding	IPI Inferred from Physical Interaction more info
ubiquitin protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed
zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
DNA repair	NAS Non-traceable Author Statement more info	PubMed
negative regulation of DNA recombination	IEA Inferred from Electronic Annotation more info
response to UV	IEA Inferred from Electronic Annotation more info
spermatogenesis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
XY body	IEA Inferred from Electronic Annotation more info
chromatin	IEA Inferred from Electronic Annotation more info
nucleus	NAS Non-traceable Author Statement more info	PubMed
replication fork	IDA Inferred from Direct Assay more info	PubMed

General protein information

Preferred Names: E3 ubiquitin-protein ligase RAD18

Names: E3 ubiquitin-protein ligase RAD18; hHR18; hRAD18; RING finger protein 73; RAD18, S. cerevisiae, homolog; postreplication repair protein RAD18; postreplication repair protein hRAD18p

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_020165.3 → NP_064550.3 E3 ubiquitin-protein ligase RAD18

Status: REVIEWED

Source sequence(s)

AC008151, AC034186, AK023075, DW433240

Consensus CDS

CCDS2571.1

UniProtKB/Swiss-Prot

Q9NS91

Related

ENSP00000264926, OTTHUMP00000115649, ENST00000264926, OTTHUMT00000207071

Conserved Domains (4) summary

cd00162
Location:25 – 63
Blast Score: 117

RING; RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...

smart00734
Location:201 – 223
Blast Score: 100

ZnF_Rad18; Rad18-like CCHC zinc finger

TIGR00599
Location:13 – 363
Blast Score: 298

rad18; DNA repair protein rad18

cl02640
Location:262 – 282
Blast Score: 80

SAP; SAP domain

RefSeqs of Annotated Genomes: Build 37.3

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

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000003.11 Reference GRCh37.p5 Primary Assembly

Range

8918880..9005159, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000135.1 Alternate HuRef

Range

8853076..8939344, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AC008151.1 (152060..178241)	None
genomic	AC034186.5 (87199..147282)	None
genomic	AY961989.1	AAX44049.1
genomic	CH471055.1	EAW63948.1
		EAW63949.1
mRNA	AB035274.2	BAA99284.1
mRNA	AF169796.1	AAF80856.1
mRNA	AK023075.1	BAB14392.1
mRNA	AK222771.1	BAD96491.1
mRNA	AY004333.1	AAF86618.1
mRNA	BC001302.1	AAH01302.1
mRNA	DW433240.1	None
other-genetic	DQ891197.2	ABM82123.1
other-genetic	DQ894380.2	ABM85306.1