Rnf8 ring finger protein 8 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Rnf8provided by RGD
Official Full Name: ring finger protein 8provided by RGD
Primary source: RGD:1308035
See related: Ensembl:ENSRNOG00000047171 AllianceGenome:RGD:1308035
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Predicted to enable several functions, including protein homodimerization activity; ubiquitin protein ligase activity; and ubiquitin protein ligase binding activity. Predicted to be involved in several processes, including DNA metabolic process; protein ubiquitination; and regulation of nucleobase-containing compound metabolic process. Predicted to be located in chromosome, telomeric region; cytoplasm; and nucleoplasm. Predicted to be part of ubiquitin ligase complex. Predicted to be active in cytosol; nucleus; and site of double-strand break. Orthologous to human RNF8 (ring finger protein 8). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Adrenal (RPKM 65.2), Liver (RPKM 52.1) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 20p12

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	20	NC_086038.1 (7683890..7708437)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	20	NC_051355.1 (7682258..7710448)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	20	NC_005119.4 (8285380..8309858)

Chromosome 20 - NC_086038.1 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Knockdown or conditional knockout of RNF8 or UBC13 in rodent cerebellar granule neurons robustly increases the number of parallel fiber presynaptic boutons and functional parallel fiber/Purkinje cell synapses. In contrast to the role of nuclear RNF8 in proliferating cells, RNF8 operates in the cytoplasm in neurons to suppress synapse differentiation.
Title: RNF8/UBC13 ubiquitin signaling suppresses synapse formation in the mammalian brain.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH137336 (e-PCR)
- UniSTS:219424

BF387562 (e-PCR)
- UniSTS:244396

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables chromatin binding	ISO Inferred from Sequence Orthology more info
enables chromatin binding	ISS Inferred from Sequence or Structural Similarity more info
enables histone binding	IBA Inferred from Biological aspect of Ancestor more info
enables histone binding	ISO Inferred from Sequence Orthology more info
enables histone binding	ISS Inferred from Sequence or Structural Similarity more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
enables ubiquitin binding	IEA Inferred from Electronic Annotation 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 ligase binding	ISO Inferred from Sequence Orthology more info
enables ubiquitin-protein transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin-protein transferase activity	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in DNA damage response	ISO Inferred from Sequence Orthology more info
involved_in DNA damage response	ISS Inferred from Sequence or Structural Similarity more info
involved_in DNA repair-dependent chromatin remodeling	ISO Inferred from Sequence Orthology more info
involved_in DNA repair-dependent chromatin remodeling	ISS Inferred from Sequence or Structural Similarity more info
involved_in biological_process	ND No biological Data available more info
involved_in cell division	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in double-strand break repair	ISO Inferred from Sequence Orthology more info
involved_in double-strand break repair	ISS Inferred from Sequence or Structural Similarity more info
involved_in double-strand break repair via nonhomologous end joining	ISO Inferred from Sequence Orthology more info
involved_in double-strand break repair via nonhomologous end joining	ISS Inferred from Sequence or Structural Similarity more info
involved_in epigenetic regulation of gene expression	ISO Inferred from Sequence Orthology more info
involved_in epigenetic regulation of gene expression	ISS Inferred from Sequence or Structural Similarity more info
involved_in isotype switching	ISO Inferred from Sequence Orthology more info
involved_in isotype switching	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of transcription elongation by RNA polymerase II	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of transcription elongation by RNA polymerase II	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of DNA repair	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA repair	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of double-strand break repair via homologous recombination	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of double-strand break repair via homologous recombination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K48-linked ubiquitination	IBA Inferred from Biological aspect of Ancestor 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 response to ionizing radiation	ISO Inferred from Sequence Orthology more info
involved_in response to ionizing radiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in signal transduction in response to DNA damage	ISO Inferred from Sequence Orthology more info
involved_in sperm DNA condensation	ISO Inferred from Sequence Orthology more info
involved_in sperm DNA condensation	ISS Inferred from Sequence or Structural Similarity more info
involved_in ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ubiquitin-dependent protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in ubiquitin-dependent protein catabolic process	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in chromosome, telomeric region	ISO Inferred from Sequence Orthology more info
located_in chromosome, telomeric region	ISS Inferred from Sequence or Structural Similarity more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in midbody	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
is_active_in site of double-strand break	IBA Inferred from Biological aspect of Ancestor more info
located_in site of double-strand break	ISO Inferred from Sequence Orthology more info
located_in site of double-strand break	ISS Inferred from Sequence or Structural Similarity more info
part_of ubiquitin ligase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ubiquitin ligase complex	ISO Inferred from Sequence Orthology more info
part_of ubiquitin ligase complex	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF8

Names: RING-type E3 ubiquitin transferase RNF8; ring finger protein 8, E3 ubiquitin protein ligase

NP_001020898.1

EC 2.3.2.27

XP_006256288.1

EC 2.3.2.27

XP_063135299.1

EC 2.3.2.27

XP_063135300.1

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_001025727.1 → NP_001020898.1 E3 ubiquitin-protein ligase RNF8

See identical proteins and their annotated locations for NP_001020898.1

Status: VALIDATED

Source sequence(s)

BC099079

UniProtKB/Swiss-Prot

Q4KLN8

UniProtKB/TrEMBL

A0A0G2K858

Related

ENSRNOP00000059852.1, ENSRNOT00000065629.3

Conserved Domains (4) summary

COG1716
Location:38 → 109

FHA; Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]

cd00060
Location:17 → 110

FHA; Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins ...

cd00162
Location:404 → 446

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 ...

pfam11262
Location:267 → 325

Tho2; Transcription factor/nuclear export subunit protein 2

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

Reference GRCr8

Genomic

NC_086038.1 Reference GRCr8

Range

7683890..7708437

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_063279229.1 → XP_063135299.1 E3 ubiquitin-protein ligase RNF8 isoform X1
XM_063279230.1 → XP_063135300.1 E3 ubiquitin-protein ligase RNF8 isoform X2

UniProtKB/Swiss-Prot

Q4KLN8
XM_006256226.5 → XP_006256288.1 E3 ubiquitin-protein ligase RNF8 isoform X3

Conserved Domains (3) summary

COG1716
Location:38 → 109

FHA; Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]

cd00060
Location:17 → 110

FHA; Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins ...

pfam11262
Location:267 → 325

Tho2; Transcription factor/nuclear export subunit protein 2