Rnf4 ring finger protein 4 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Rnf4provided by MGI
Official Full Name: ring finger protein 4provided by MGI
Primary source: MGI:MGI:1201691
See related: Ensembl:ENSMUSG00000029110 AllianceGenome:MGI:1201691
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: SNURF; Gtrgeo8
Summary: This gene encodes a small nuclear RING finger protein that mediates ubiquitylation of polysumoylated proteins. Deficiency of the encoded protein in mice leads to embryonic lethality and global DNA hypermethylation. A similar protein in humans is required for arsenic-induced degradation of promyelocytic leukemia protein in acute promyelocytic leukemia. Alternative splicing of this gene results in multiple transcript variants. A pseudogene for this gene has been identified on chromosome 10. [provided by RefSeq, Jan 2015]
Expression: Ubiquitous expression in placenta adult (RPKM 51.2), CNS E11.5 (RPKM 42.5) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 5 B2; 5 17.87 cM

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	5	NC_000071.7 (34493594..34510789)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	5	NC_000071.6 (34336250..34353445)

Chromosome 5 - NC_000071.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

RNF4 sustains Myc-driven tumorigenesis by facilitating DNA replication.
Title: RNF4 sustains Myc-driven tumorigenesis by facilitating DNA replication.
The E3 Ubiquitin-Protein Ligase RNF4 Promotes TNF-alpha-Induced Cell Death Triggered by RIPK1.
Title: The E3 Ubiquitin-Protein Ligase RNF4 Promotes TNF-α-Induced Cell Death Triggered by RIPK1.
These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure.
Title: Manipulating PML SUMOylation via Silencing UBC9 and RNF4 Regulates Cardiac Fibrosis.
This paper identifies a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones.
Title: RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.
fork collapse in Atr-deleted cells is mediated through the combined effects the sumo targeted E3-ubiquitin ligase RNF4 and activation of the AURKA-PLK1 pathway
Title: RNF4 and PLK1 are required for replication fork collapse in ATR-deficient cells.
Rnf4 controls protein localization at DNA damage sites by integrating SUMOylation and ubiquitylation events.
Title: RNF4 is required for DNA double-strand break repair in vivo.
SUMO interacting motif is dispensable for PML SUMOylation and interaction with RNF4 but is required for efficient PML ubiquitination, recruitment of proteasome components within NBs and proteasome-dependent degradation of PML in response to AsO
Title: Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms.
Rnf4 deficiency is embryonic lethal with higher levels of methylation in genomic DNA. Mechanistic studies show that RNF4 interacts with and requires the base excision repair enzymes TDG and APE1 for active demethylation.
Title: Identification of RING finger protein 4 (RNF4) as a modulator of DNA demethylation through a functional genomics screen.
Mammalian RNF4, an active ubiquitin E3 ligase, is an orthologue of Rfp1/Rfp2. Rfp1 and Rfp2 lack E3 activity but recruit Slx8, an active RING-finger ubiquitin ligase, through a RING-RING interaction, to form a functional E3.
Title: Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins.
results suggest a role for small nuclear ring finger protein(SNURF/RNF4) in fetal germ cell development as well as in oocyte and granulosa cell maturation in an estrogen- and gonadotropin-regulated fashion
Title: Small nuclear RING finger protein expression during gonad development: regulation by gonadotropins and estrogen in the postnatal ovary.

Submit: New GeneRIF Correction See all GeneRIFs (14)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Gene trapped (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:236298

RH126561 (e-PCR)
- UniSTS:209687

RH136248 (e-PCR)
- UniSTS:210242

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA binding	ISO Inferred from Sequence Orthology more info
enables DNA binding	ISS Inferred from Sequence or Structural Similarity more info
enables SUMO polymer binding	ISO Inferred from Sequence Orthology more info
enables SUMO polymer binding	ISS Inferred from Sequence or Structural Similarity more info
enables TBP-class protein binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables nuclear androgen receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear estrogen receptor binding	ISO Inferred from Sequence Orthology more info
enables nucleosome binding	ISO Inferred from Sequence Orthology more info
enables nucleosome binding	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables transcription factor binding	IPI Inferred from Physical Interaction more info	PubMed
enables ubiquitin conjugating enzyme binding	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin protein ligase activity	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase activity	ISS Inferred from Sequence or Structural Similarity more info
enables ubiquitin-protein transferase activity	ISO Inferred from Sequence Orthology more info
enables ubiquitin-protein transferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cellular response to gamma radiation	ISO Inferred from Sequence Orthology more info
involved_in cellular response to hydroxyurea	ISO Inferred from Sequence Orthology more info
involved_in cellular response to testosterone stimulus	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein localization to chromatin	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of protein localization to chromatin	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA-templated transcription	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA-templated transcription	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of transcription by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within positive regulation of transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of transcription by RNA polymerase II	ISS Inferred from Sequence or Structural Similarity more info
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K11-linked ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein K11-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K48-linked ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein K48-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K6-linked ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein K6-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K63-linked ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein K63-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein autoubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein autoubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in regulation of kinetochore assembly	ISO Inferred from Sequence Orthology more info
involved_in regulation of kinetochore assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of spindle assembly	ISO Inferred from Sequence Orthology more info
involved_in regulation of spindle assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to arsenic-containing substance	IEA Inferred from Electronic Annotation more info
involved_in response to arsenic-containing substance	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
colocalizes_with PML body	IBA Inferred from Biological aspect of Ancestor more info
located_in PML body	IEA Inferred from Electronic Annotation more info
colocalizes_with PML body	ISO Inferred from Sequence Orthology more info
located_in PML body	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in microtubule end	IEA Inferred from Electronic Annotation more info
located_in microtubule end	ISO Inferred from Sequence Orthology more info
located_in nuclear body	ISO Inferred from Sequence Orthology more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF4

Names: E3 ubiquitin ligase RNF4; RING-type E3 ubiquitin transferase RNF4

NP_001291198.1

EC 2.3.2.27

NP_001291199.1

EC 2.3.2.27

NP_035408.1

EC 2.3.2.27

NCBI Reference Sequences (RefSeq)

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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_001304269.1 → NP_001291198.1 E3 ubiquitin-protein ligase RNF4

See identical proteins and their annotated locations for NP_001291198.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in the 5' UTR, compared to variant 1. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AC104889, AK147057, BY275961, BY505719

Consensus CDS

CCDS57336.1

UniProtKB/Swiss-Prot

O35941, Q541Z6, Q9QZS2

UniProtKB/TrEMBL

Q3TXE6

Related

ENSMUSP00000030992.6, ENSMUST00000030992.13

Conserved Domains (1) summary

pfam13639
Location:135 → 181

zf-RING_2; Ring finger domain
NM_001304270.1 → NP_001291199.1 E3 ubiquitin-protein ligase RNF4

See identical proteins and their annotated locations for NP_001291199.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) contains an alternate exon in the 5' UTR, compared to variant 1. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AC104889, AK019656, BY505719

Consensus CDS

CCDS57336.1

UniProtKB/Swiss-Prot

O35941, Q541Z6, Q9QZS2

UniProtKB/TrEMBL

Q3TXE6

Related

ENSMUSP00000138411.2, ENSMUST00000182047.2

Conserved Domains (1) summary

pfam13639
Location:135 → 181

zf-RING_2; Ring finger domain
NM_011278.5 → NP_035408.1 E3 ubiquitin-protein ligase RNF4

See identical proteins and their annotated locations for NP_035408.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AC104889

Consensus CDS

CCDS57336.1

UniProtKB/Swiss-Prot

O35941, Q541Z6, Q9QZS2

UniProtKB/TrEMBL

Q3TXE6

Related

ENSMUSP00000138555.2, ENSMUST00000182709.8

Conserved Domains (1) summary

pfam13639
Location:135 → 181

zf-RING_2; Ring finger domain