RNF168 ring finger protein 168, E3 ubiquitin protein ligase [Homo sapiens] - Gene

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Summary

Official Symbol: RNF168provided by HGNC
Official Full Name: ring finger protein 168, E3 ubiquitin protein ligaseprovided by HGNC
Primary source: HGNC:26661
See related: Ensembl:ENSG00000163961; HPRD:08190; MIM:612688; Vega:OTTHUMG00000155582
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: FLJ35794; FLJ39749
Summary: This gene encodes an E3 ubiquitin ligase protein that contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. The protein is involved in DNA double-strand break (DSB) repair. Mutations in this gene result in Riddle syndrome. [provided by RefSeq, Sep 2011]

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Genomic context

Location :: 3q29

Sequence :: Chromosome: 3; NC_000003.11 (196195654..196230639, complement)

See RNF168 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?

Data show that depletion of RNF8, as well as of the E3 ligase RNF168, reduces telomere-induced genome instability.
Title: DNA-damage response and repair activities at uncapped telomeres depend on RNF8.
Studies indicate that Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity.
Title: The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks.
The viral protein ICP0 targets RNF8 and RNF168 for degradation, thereby preventing the deposition of repressive ubiquitin marks and counteracting this repair protein recruitment.
Title: The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0.
this study reveals that human NIPBL is a novel protein recruited to DSB sites, and the recruitment is controlled by MDC1, RNF168 and HP1gamma.
Title: Recruitment of the cohesin loading factor NIPBL to DNA double-strand breaks depends on MDC1, RNF168 and HP1γ in human cells.
The E3 Ubiquitin ligases, RNF8 and RNF168, are recruited to DNA damage foci in late mitosis, presumably to prime sites for the DNA damage response, 53BP1, recruitment in early G1.
Title: Give me a break, but not in mitosis: the mitotic DNA damage response marks DNA double-strand breaks with early signaling events.
identification of a novel ubiquitin binding domain present in RNF168, and characterized the interaction surface with ubiquitin, centered on two Leu residues
Title: UMI, a novel RNF168 ubiquitin binding domain involved in the DNA damage signaling pathway.
Data identify RNF8 and RNF168, cellular histone ubiquitin ligases responsible for anchoring repair factors at sites of damage, as new targets for ICP0-mediated degradation.
Title: A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses.
Data show that the ATM signalling mediator proteins MDC1, RNF8, RNF168 and 53BP1 are also required for heterochromatic DSB repair.
Title: 53BP1-dependent robust localized KAP-1 phosphorylation is essential for heterochromatic DNA double-strand break repair.
Ubiquitin ligase does not protect cells from Nutlin-3-mediated apoptosis, indicating that RNF168 does not regulate 53BP1 protein.
Title: The RNF8/RNF168 ubiquitin ligase cascade facilitates class switch recombination.
RNF168 is a ubiquitin ligase that functions as chromatin modifier, through histone ubiquitination; upon DNA lesions, RNF168 is recruited to DNA damage response foci where it contributes to increase the amount of ubiquitinated proteins.
Title: RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX.

Submit: New GeneRIF Correction See all (11)

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Phenotypes

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Products	Interactant	Other Gene	Source	Pubs	Description
Q8IYW5	Q13571	LAPTM5	HPRD	PubMed
Q8IYW5	Q9UJ41	RABGEF1	HPRD	PubMed
Q8IYW5	Q9Y3C5	RNF11	HPRD	PubMed
BioGRID:127922	BioGRID:109268	H2AFX	BioGRID	PubMed	Biochemical Activity
BioGRID:127922	BioGRID:114438	HERC2	BioGRID	PubMed	Affinity Capture-Western
BioGRID:127922	BioGRID:113933	HIST2H2AA3	BioGRID	PubMed	Affinity Capture-Western
BioGRID:127922	BioGRID:113934	HIST2H2AC	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity
BioGRID:127922	BioGRID:113945	HIST2H2BE	BioGRID	PubMed	Affinity Capture-Western
BioGRID:127922	BioGRID:112497	SUMO2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:127922	BioGRID:113011	TP53BP1	BioGRID	PubMed	Co-localization
BioGRID:127922	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS; Reconstituted Complex
BioGRID:127922	BioGRID:113175	UBE2G2	BioGRID	PubMed	Two-hybrid
BioGRID:127922	BioGRID:113182	UBE2N	BioGRID	PubMed	Affinity Capture-Western

Function	Evidence Code	Pubs
chromatin binding	IDA Inferred from Direct Assay more info	PubMed
histone binding	IDA Inferred from Direct Assay 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	PubMed
ubiquitin binding	IDA Inferred from Direct Assay more info	PubMed
ubiquitin-protein ligase activity	IDA Inferred from Direct Assay more info	PubMed
zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
chromatin modification	IEA Inferred from Electronic Annotation more info
double-strand break repair	IDA Inferred from Direct Assay more info	PubMed
histone H2A K63-linked ubiquitination	IDA Inferred from Direct Assay more info	PubMed
positive regulation of DNA repair	IDA Inferred from Direct Assay more info	PubMed
response to ionizing radiation	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
nucleus	IDA Inferred from Direct Assay more info	PubMed
ubiquitin ligase complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

Preferred Names: E3 ubiquitin-protein ligase RNF168

Names: E3 ubiquitin-protein ligase RNF168

NP_689830.2

EC 6.3.2.-

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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.

Genomic

NG_023425.1 RefSeqGene

Range

5001..39986

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_152617.3 → NP_689830.2 E3 ubiquitin-protein ligase RNF168

Status: REVIEWED

Source sequence(s)

AC117490, AK054732, BC033791, BC047483

Consensus CDS

CCDS3317.1

UniProtKB/Swiss-Prot

Q8IYW5

Related

ENSP00000320898, OTTHUMP00000208312, ENST00000318037, OTTHUMT00000340778

Conserved Domains (1) summary

cd00162
Location:15 – 58
Blast Score: 118

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 ...

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

196195654..196230639, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000135.1 Alternate HuRef

Range

193493420..193527598, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AC092933.21 (2012..14545)	None
genomic	AC117490.3 (26582..47955)	None
genomic	CH471191.2	EAW53649.1
		EAW53650.1
		EAW53651.1
mRNA	AK054732.1	BAB70801.1
mRNA	AK093113.1	BAC04060.1
mRNA	AK097068.1	None
mRNA	BC017442.1	None
mRNA	BC029433.1	None
mRNA	BC033791.1	AAH33791.1
mRNA	BC047483.1	None