RNF5 ring finger protein 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RNF5provided by HGNC
Official Full Name: ring finger protein 5provided by HGNC
Primary source: HGNC:HGNC:10068
See related: Ensembl:ENSG00000204308 MIM:602677; AllianceGenome:HGNC:10068
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: RMA1; RING5
Summary: The protein encoded by this gene contains a RING finger, which is a motif known to be involved in protein-protein interactions. This protein is a membrane-bound ubiquitin ligase. It can regulate cell motility by targeting paxillin ubiquitination and altering the distribution and localization of paxillin in cytoplasm and cell focal adhesions. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in kidney (RPKM 45.9), small intestine (RPKM 33.9) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 6p21.32

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	6	NC_000006.12 (32178405..32180793)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	6	NC_060930.1 (32031596..32033984)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	6	NC_000006.11 (32146182..32148570)

Chromosome 6 - NC_000006.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Downregulation of EphA2 stability by RNF5 limits its tumor-suppressive function in HER2-negative breast cancers.
Title: Downregulation of EphA2 stability by RNF5 limits its tumor-suppressive function in HER2-negative breast cancers.
The E3 ligase RNF5 restricts SARS-CoV-2 replication by targeting its envelope protein for degradation.
Title: The E3 ligase RNF5 restricts SARS-CoV-2 replication by targeting its envelope protein for degradation.
Suppression of KSHV lytic replication and primary effusion lymphoma by selective RNF5 inhibition.
Title: Suppression of KSHV lytic replication and primary effusion lymphoma by selective RNF5 inhibition.
The E3 Ubiquitin Ligase Ring Finger Protein 5 Ameliorates NASH Through Ubiquitin-Mediated Degradation of 3-Hydroxy-3-Methylglutaryl CoA Reductase Degradation Protein 1.
Title: The E3 Ubiquitin Ligase Ring Finger Protein 5 Ameliorates NASH Through Ubiquitin-Mediated Degradation of 3-Hydroxy-3-Methylglutaryl CoA Reductase Degradation Protein 1.
The ubiquitin ligase RNF5 determines acute myeloid leukemia growth and susceptibility to histone deacetylase inhibitors.
Title: The ubiquitin ligase RNF5 determines acute myeloid leukemia growth and susceptibility to histone deacetylase inhibitors.
RING-finger protein 5 promotes hepatocellular carcinoma progression and predicts poor prognosis.
Title: RING-finger protein 5 promotes hepatocellular carcinoma progression and predicts poor prognosis.
Acetylation Stabilizes Phosphoglycerate Dehydrogenase by Disrupting the Interaction of E3 Ligase RNF5 to Promote Breast Tumorigenesis.
Title: Acetylation Stabilizes Phosphoglycerate Dehydrogenase by Disrupting the Interaction of E3 Ligase RNF5 to Promote Breast Tumorigenesis.
Ring finger protein 5 activates sterol regulatory element-binding protein 2 (SREBP2) to promote cholesterol biosynthesis via inducing polyubiquitination of SREBP chaperone SCAP.
Title: Ring finger protein 5 activates sterol regulatory element-binding protein 2 (SREBP2) to promote cholesterol biosynthesis via inducing polyubiquitination of SREBP chaperone SCAP.
Authors demonstrate that the V proteins of NDV and several other paramyxoviruses target MAVS for ubiquitin-mediated degradation through E3 ubiquitin ligase RING-finger protein 5 (RNF5). MAVS degradation leads to the inhibition of the downstream IFN-beta pathway and therefore benefits virus proliferation.
Title: Newcastle Disease Virus V Protein Degrades Mitochondrial Antiviral Signaling Protein To Inhibit Host Type I Interferon Production via E3 Ubiquitin Ligase RNF5.
we found that RNF5 is differentially expressed in human bronchial epithelia from CF vs. control patients. Our results identify RNF5 as a target for therapeutic modalities to antagonize mutant CFTR proteins.
Title: Genetic Inhibition Of The Ubiquitin Ligase Rnf5 Attenuates Phenotypes Associated To F508del Cystic Fibrosis Mutation.

Submit: New GeneRIF Correction See all GeneRIFs (23)

Phenotypes

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

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Identification of 23 new prostate cancer susceptibility loci using the iCOGS custom genotyping array. EBI GWAS Catalog EBI GWAS CatalogPubMed
Risk HLA-DQA1 and PLA(2)R1 alleles in idiopathic membranous nephropathy. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Knockdown of ring finger protein 5, E3 ubiquitin protein ligase (RNF5) by siRNA has both activating and inhibiting activities on HIV-1 replication in HeLa P4/R5 cells, suggesting a regulatory role in HIV replication	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp160, precursor	env	HIV-1 gp160 is identified to have a physical interaction with ring finger protein 5, E3 ubiquitin protein ligase (RNF5) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH80855 (e-PCR)
- UniSTS:89132

RH67947 (e-PCR)
- UniSTS:87104

RH40485 (e-PCR)
- UniSTS:85336

D6S1871 (e-PCR)
- UniSTS:54378

STS-D60277 (e-PCR)
- UniSTS:54384

MARC_10431-10432:999637141:1 (e-PCR)
- UniSTS:267139

RH124616 (e-PCR)
- UniSTS:161438

RH65115 (e-PCR)
- UniSTS:85939

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IPI Inferred from Physical Interaction more info	PubMed
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin protein ligase activity	TAS Traceable Author Statement more info	PubMed
enables ubiquitin-like protein conjugating enzyme binding	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin-protein transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in ERAD pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of autophagy	IEA Inferred from Electronic Annotation more info
involved_in protein K48-linked ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein K63-linked ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein destabilization	IEA Inferred from Electronic Annotation more info
involved_in regulation of autophagosome assembly	IEA Inferred from Electronic Annotation more info
involved_in response to bacterium	IEA Inferred from Electronic Annotation more info
involved_in transmembrane transport	TAS Traceable Author Statement 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	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info
located_in endoplasmic reticulum membrane	TAS Traceable Author Statement more info
located_in mitochondrial membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF5

Names: RING-type E3 ubiquitin transferase RNF5; protein G16; ram1 homolog; ring finger protein 5, E3 ubiquitin protein ligase

NP_008844.1

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_006913.4 → NP_008844.1 E3 ubiquitin-protein ligase RNF5

See identical proteins and their annotated locations for NP_008844.1

Status: REVIEWED

Source sequence(s)

BC004155, BC127652, BM712189

Consensus CDS

CCDS4745.1

UniProtKB/Swiss-Prot

A2BFI6, B2R4K3, Q0VDB7, Q99942, Q9UMQ2

UniProtKB/TrEMBL

A0A024RCQ4, A0A1U9X8F4, A0A1U9X8G0, B4DJS6

Related

ENSP00000364235.3, ENST00000375094.4

Conserved Domains (2) summary

PLN03208
Location:21 → 116

PLN03208; E3 ubiquitin-protein ligase RMA2; Provisional

cd16743
Location:25 → 70

RING-HC_RNF5; RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins