Rnf128 ring finger protein 128 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Rnf128provided by MGI
Official Full Name: ring finger protein 128provided by MGI
Primary source: MGI:MGI:1914139
See related: Ensembl:ENSMUSG00000031438 AllianceGenome:MGI:1914139
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: GRAIL; Greul1; 1300002C13Rik
Summary: Enables ubiquitin protein ligase activity. Acts upstream of or within negative regulation of cytokine production. Located in Golgi apparatus; endoplasmic reticulum; and late endosome. Is expressed in several structures, including alimentary system; extraembryonic component; genitourinary system; nervous system; and sensory organ. Orthologous to human RNF128 (ring finger protein 128). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in placenta adult (RPKM 42.6), small intestine adult (RPKM 42.3) and 17 other tissues See more
Orthologs: human all
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Genomic context

Location:: X F1; X 61.35 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	X	NC_000086.8 (138464089..138573894)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	X	NC_000086.7 (139563340..139673145)

Chromosome X - NC_000086.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

GRAIL gene knockout mice protect against aging-related and noise-induced hearing loss.
Title: GRAIL gene knockout mice protect against aging-related and noise-induced hearing loss.
RNF128 regulates neutrophil infiltration and myeloperoxidase functions to prevent acute lung injury.
Title: RNF128 regulates neutrophil infiltration and myeloperoxidase functions to prevent acute lung injury.
How GRAIL controls Treg function to maintain self-tolerance.
Title: How GRAIL controls Treg function to maintain self-tolerance.
E3 ubiquitin ligase Grail promotes hepatic steatosis through Sirt1 inhibition.
Title: E3 ubiquitin ligase Grail promotes hepatic steatosis through Sirt1 inhibition.
results indicate that Grail plays a pivotal role in adipogenesis and diet-induced obesity by regulating PPARgamma activity.
Title: Grail is involved in adipocyte differentiation and diet-induced obesity.
Grail contributes to the attenuation of hyperinflammation caused by activated macrophages and prevents organ damage in endotoxemic mice.
Title: Macrophage expression of E3 ubiquitin ligase Grail protects mice from lipopolysaccharide-induced hyperinflammation and organ injury.
loss of Grail enhances anti-tumour reactivity and functionality of CD8(+) T cells.
Title: Absence of Grail promotes CD8(+) T cell anti-tumour activity.
GRAIL expression is regulated by the IL2/mTOR/Otubain-1 axis in CD4 T cells during Trypanosoma cruzi infection.
Title: GRAIL and Otubain-1 are Related to T Cell Hyporesponsiveness during Trypanosoma cruzi Infection.
this study identified RNF128 as an E3 ligase for K63-linked ubiquitination and activation of TBK1 to RNA and DNA viruses
Title: E3 ubiquitin ligase RNF128 promotes innate antiviral immunity through K63-linked ubiquitination of TBK1.
Grail plays a critical role in controlling Th2 cell development through a negative feedback loop by targeting STAT6 for degradation.
Title: Grail controls Th2 cell development by targeting STAT6 for degradation.

Submit: New GeneRIF Correction See all GeneRIFs (21)

Variation

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Alleles

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

Endonuclease-mediated (4) 1 citation
Targeted (6) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI987883 (e-PCR)
- UniSTS:181332

px-58h7 (e-PCR)
- UniSTS:257974

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables metal ion 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	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin protein ligase activity	ISO Inferred from Sequence Orthology more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within negative regulation of cytokine production	IDA Inferred from Direct Assay more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in regulation of protein stability	IEA Inferred from Electronic Annotation more info
involved_in regulation of protein stability	ISO Inferred from Sequence Orthology more info
involved_in ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	IBA Inferred from Biological aspect of Ancestor more info
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
is_active_in late endosome	IBA Inferred from Biological aspect of Ancestor more info
located_in late endosome	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF128

Names: RING-type E3 ubiquitin transferase RNF128; gene related to anergy in lymphocytes protein; goliath-related E3 ubiquitin-protein ligase 1

NP_001241690.1

EC 2.3.2.27

NP_075759.3

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_001254761.1 → NP_001241690.1 E3 ubiquitin-protein ligase RNF128 isoform 2

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate 5' terminal exon, compared to variant 1. It encodes isoform 2, which is shorter and has a distinct N-terminus, compared to isoform 1.

Source sequence(s)

AK004847, AK018582, AL691424, CK380647, DV064262

Consensus CDS

CCDS57776.1

UniProtKB/TrEMBL

A2AGL8

Related

ENSMUSP00000108650.2, ENSMUST00000113027.8

Conserved Domains (2) summary

cd02122
Location:34 → 167

PA_GRAIL_like; PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ...

pfam13639
Location:249 → 292

zf-RING_2; Ring finger domain
NM_023270.5 → NP_075759.3 E3 ubiquitin-protein ligase RNF128 isoform 1 precursor

See identical proteins and their annotated locations for NP_075759.3

Status: VALIDATED

Source sequence(s)

AK004847, AK018582, CK380647

Consensus CDS

CCDS30435.1

UniProtKB/Swiss-Prot

Q3UJY0, Q9CVG1, Q9D304, Q9DBN3, Q9JJF8

Related

ENSMUSP00000108649.2, ENSMUST00000113026.2

Conserved Domains (2) summary

cd02122
Location:48 → 193

PA_GRAIL_like; PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ...

pfam13639
Location:275 → 318

zf-RING_2; Ring finger domain