Rnf135 ring finger protein 135 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Rnf135provided by MGI
Official Full Name: ring finger protein 135provided by MGI
Primary source: MGI:MGI:1919206
See related: Ensembl:ENSMUSG00000020707 AllianceGenome:MGI:1919206
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: Riplet; U 2-3-0; 0610037N03Rik; 2410006N06Rik
Summary: Predicted to enable several functions, including RIG-I binding activity; identical protein binding activity; and ubiquitin protein ligase activity. Involved in RIG-I signaling pathway; antiviral innate immune response; and protein polyubiquitination. Predicted to be located in cytoplasmic stress granule. Predicted to be part of ribonucleoprotein complex. Predicted to be active in cytoplasm. Is expressed in several structures, including central nervous system; heart; and testis. Orthologous to human RNF135 (ring finger protein 135). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in ovary adult (RPKM 5.9), adrenal adult (RPKM 5.2) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 11 B5; 11 47.59 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	11	NC_000077.7 (80074652..80090581)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	11	NC_000077.6 (80183869..80199755)

Chromosome 11 - NC_000077.7 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?

E3 Ubiquitin Ligase Riplet Is Expressed in T Cells and Suppresses T Cell-Mediated Antitumor Immune Responses.
Title: E3 Ubiquitin Ligase Riplet Is Expressed in T Cells and Suppresses T Cell-Mediated Antitumor Immune Responses.
Riplet, and not TRIM25, is required endogenously for the ubiquitination of RIG-I.
Title: RIPLET, and not TRIM25, is required for endogenous RIG-I-dependent antiviral responses.
Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity.
Title: Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity.
Together with Riplet, Ube2D3 promotes covalent conjugation of polyubiquitin chains to RIG-I, while Ube2N preferentially facilitates production of unanchored chains. In the presence of these chains, RIG-I induces MAVS aggregation directly on the mitochondria. Data thus reveal two essential mechanisms underlying the activation of RIG-I and MAVS for triggering innate immune signaling in response to viral infection in cells.
Title: Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation in antiviral innate immunity.
Riplet-mediated K63-linked polyubiquitination released RIG-I RD autorepression, which allowed the access of positive factors to the RIG-I protein.
Title: A distinct role of Riplet-mediated K63-Linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses.
Riplet is essential for regulating RIG-I-mediated innate immune response against RNA virus infection in vivo.
Title: The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection.

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Variation

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Alleles

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

Endonuclease-mediated (5)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Rnf135 (e-PCR), detects polymorphism
- UniSTS:498252

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables RIG-I binding	ISO Inferred from Sequence Orthology more info
enables RIG-I 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 binding	IPI Inferred from Physical Interaction more info	PubMed
enables ribonucleoprotein complex binding	IBA Inferred from Biological aspect of Ancestor more info
enables ribonucleoprotein complex binding	ISO Inferred from Sequence Orthology more info
enables ribonucleoprotein complex binding	ISS Inferred from Sequence or Structural Similarity 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	IBA Inferred from Biological aspect of Ancestor 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

Process	Evidence Code	Pubs
involved_in RIG-I signaling pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in RIG-I signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in RIG-I signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in antiviral innate immune response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in antiviral innate immune response	ISO Inferred from Sequence Orthology more info
involved_in free ubiquitin chain polymerization	ISO Inferred from Sequence Orthology more info
involved_in free ubiquitin chain polymerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of interferon-beta production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interferon-beta production	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 homooligomerization	ISO Inferred from Sequence Orthology more info
involved_in protein homooligomerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein polyubiquitination	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein polyubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of innate immune response	ISO Inferred from Sequence Orthology more info
involved_in regulation of innate immune response	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IC Inferred by Curator 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 cytoplasmic stress granule	ISO Inferred from Sequence Orthology more info
located_in cytoplasmic stress granule	ISS Inferred from Sequence or Structural Similarity more info
part_of ribonucleoprotein complex	ISO Inferred from Sequence Orthology more info
part_of ribonucleoprotein complex	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF135

Names: RING-type E3 ubiquitin transferase RNF135

NP_082295.1

EC 2.3.2.27

XP_036012897.1

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_028019.4 → NP_082295.1 E3 ubiquitin-protein ligase RNF135

See identical proteins and their annotated locations for NP_082295.1

Status: VALIDATED

Source sequence(s)

AL591426

Consensus CDS

CCDS25129.1

UniProtKB/Swiss-Prot

Q3UBK5, Q8R161, Q9CWS1, Q9DCH3

UniProtKB/TrEMBL

B2RRA5

Related

ENSMUSP00000017839.3, ENSMUST00000017839.3

Conserved Domains (2) summary

cd00162
Location:21 → 68

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 ...

cd12902
Location:245 → 413

SPRY_PRY_RNF135; PRY/SPRY domain in RING finger protein RNF135

RNA

NR_157298.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

AK010429, AL591426, BC145236, BY754501

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

Reference GRCm39 C57BL/6J

Genomic

NC_000077.7 Reference GRCm39 C57BL/6J

Range

80074652..80090581

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_036157004.1 → XP_036012897.1 E3 ubiquitin-protein ligase RNF135 isoform X1

Conserved Domains (4) summary

TIGR00599
Location:16 → 140

rad18; DNA repair protein rad18

cd12902
Location:197 → 365

SPRY_PRY_RNF135; PRY/SPRY domain in RING finger protein RNF135

cd00162
Location:21 → 66

RING_Ubox; RING-HC finger (C3HC4-type) [structural motif]

cl17238
Location:21 → 67

RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain