RNF115 ring finger protein 115 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RNF115provided by HGNC
Official Full Name: ring finger protein 115provided by HGNC
Primary source: HGNC:HGNC:18154
See related: Ensembl:ENSG00000265491 MIM:619535; AllianceGenome:HGNC:18154
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: BCA2; ZFP364; ZNF364; RABRING7
Summary: Enables ubiquitin-protein transferase activity. Involved in negative regulation of epidermal growth factor receptor signaling pathway; protein autoubiquitination; and ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway. Predicted to be located in cytosol. [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in heart (RPKM 16.1), fat (RPKM 8.2) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1q21.1

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (145738868..145824095, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (144855652..144940898, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (145611018..145696218)

Chromosome 1 - NC_000001.11 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: 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?

RNF115 aggravates tumor progression through regulation of CDK10 degradation in thyroid carcinoma.
Title: RNF115 aggravates tumor progression through regulation of CDK10 degradation in thyroid carcinoma.
Roles of RNF126 and BCA2 E3 ubiquitin ligases in DNA damage repair signaling and targeted cancer therapy.
Title: Roles of RNF126 and BCA2 E3 ubiquitin ligases in DNA damage repair signaling and targeted cancer therapy.
RNF115-mediated ubiquitination of p53 regulates lung adenocarcinoma proliferation.
Title: RNF115-mediated ubiquitination of p53 regulates lung adenocarcinoma proliferation.
RNF115 plays dual roles in innate antiviral responses by catalyzing distinct ubiquitination of MAVS and MITA.
Title: RNF115 plays dual roles in innate antiviral responses by catalyzing distinct ubiquitination of MAVS and MITA.
these findings indicate that USP9X is a stabilizer of RNF115 protein and that the USP9X-RNF115 signaling axis is implicated in the breast cancer malignant phenotype.
Title: Deubiquitinase ubiquitin-specific protease 9X regulates the stability and function of E3 ubiquitin ligase ring finger protein 115 in breast cancer cells.
Results from a study on gene expression variability markers in early-stage human embryos shows that RNF115 is a putative expression variability marker for the 3-day, 8-cell embryo stage.
Title: Variability of Gene Expression Identifies Transcriptional Regulators of Early Human Embryonic Development.
Specifically, BCA2 serves as an E3 SUMO ligase in the SUMOylation of IkappaBalpha, which in turn enhances the sequestration of NF-kappaB components in the cytoplasm. Since HIV-1 utilizes NF-kappaB to promote proviral transcription, the BCA2-mediated inhibition of NF-kappaB significantly decreases the transcriptional activity of HIV-1.
Title: BCA2/Rabring7 Interferes with HIV-1 Proviral Transcription by Enhancing the SUMOylation of IκBα.
BCA2 functions as an antiviral factor that targets HIV-1 Gag for degradation, impairing virus assembly and release.
Title: BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin-independent manner.
BCA2 is an endogenous inhibitor of AMPK activation in breast cancer cells and BCA2 inhibition increases the efficacy of metformin.
Title: Regulation of metformin response by breast cancer associated gene 2.
BCA2, a potential oncogenic E3 ubiquitin ligase, promotes breast cancer cell proliferation partially through targeting p21 for ubiquitination and proteasomal degradation.
Title: RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1 for ubiquitin-mediated degradation.

Submit: New GeneRIF Correction See all GeneRIFs (20)

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
A genome-wide association study and biological pathway analysis of epilepsy prognosis in a prospective cohort of newly treated epilepsy. 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 BCA2 by shRNA enhances HIV-1 replication in Jurkat CD4+ T cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Pr55(Gag)	gag	Increased levels of ubiquitinated BCA2 are found in the presence of HIV-1 Gag, suggesting that the auto-ubiquitination activity of BCA2 increases in the absence of target proteins	PubMed
	gag	Replacement of cysteine residues at positions 228 and 231 with alanine in the E3 catalytic domain of BCA2 has no defect in Gag expression or processing, indicating that residues 228 and 231 are required for the antiviral activity of BCA2	PubMed
	gag	A ligase-dead mutant deltaRING-BCA2 has no defect in Gag expression or processing, indicating that the intact RING-domain is required for the antiviral activity of BCA2	PubMed
	gag	BCA2 has tetherin-independent antiviral activity, which results in a defect in either Gag expression or processing, impairing virus assembly and release for both HIV-1 and SIV	PubMed
	gag	BCA2 promotes the lysosomal degradation of HIV-1 and SIV Gag proteins and induces changes in the subcellular distribution of Gag	PubMed
	gag	Results from co-immunoprecipitation assays indicate that the N-terminal region (residues 1-147) of BCA2 physically interacts with the MA region (residues 1-165) of HIV-1 Gag	PubMed
	gag	BCA2 induces ubiquitination of both HIV-1 and SIV Gag proteins, resulting in lysine residues K113, K114, and K418 in HIV-1 Gag, and K360 and K419 residues in SIV Gag that are ubiquinated	PubMed
	gag	BCA2 co-localizes with HIV-1 Gag in in CD63+ endosomes/lysosomes	PubMed
Vpu	vpu	HIV-1 Vpu antagonizes the effects of BCA2 on HIV-1 particle production in ""tetherin-positive"" cells	PubMed
capsid	gag	A significant downregulation in the levels of virion-associated CA is observed in cells expressing BCA2 for both wild-type HIV-1 and Vpu-deficient HIV-1	PubMed
matrix	gag	Results from co-immunoprecipitation assays indicate that the N-terminal region (residues 1-147) of BCA2 physically interacts with HIV-1 MA but not CA and NC proteins	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

D1S442 (e-PCR), detects polymorphism
- UniSTS:2378

RH65408 (e-PCR)
- UniSTS:55125

RH104111 (e-PCR)
- UniSTS:98436

D1S442 (e-PCR), detects polymorphism
- UniSTS:54924

G23710 (e-PCR)
- UniSTS:81323

SHGC-79691 (e-PCR)
- UniSTS:102071

SHGC-56583 (e-PCR)
- UniSTS:954

SHGC-75411 (e-PCR)
- UniSTS:12992

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein 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	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin protein ligase activity	ISS Inferred from Sequence or Structural Similarity more info
enables ubiquitin-protein transferase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in negative regulation of epidermal growth factor receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of toll-like receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in protein K11-linked ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein K48-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein K63-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein autoubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein ubiquitination	IBA Inferred from Biological aspect of Ancestor more info
involved_in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	TAS Traceable Author Statement more info
is_active_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF115

Names: RING-type E3 ubiquitin transferase RNF115; rab7-interacting RING finger protein; rabring 7; zinc finger protein 364

NP_055270.1

EC 2.3.2.27

XP_047273980.1

EC 2.3.2.27

XP_047273981.1

EC 2.3.2.27

XP_047273982.1

EC 2.3.2.27

XP_047273983.1

EC 2.3.2.27

XP_047273984.1

EC 2.3.2.27

XP_054192012.1

EC 2.3.2.27

XP_054192013.1

EC 2.3.2.27

XP_054192014.1

EC 2.3.2.27

XP_054192015.1

EC 2.3.2.27

XP_054192016.1

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_014455.4 → NP_055270.1 E3 ubiquitin-protein ligase RNF115

See identical proteins and their annotated locations for NP_055270.1

Status: VALIDATED

Source sequence(s)

AC242845, AF419857, BG684824, HY099262

Consensus CDS

CCDS72863.1

UniProtKB/Swiss-Prot

A8K3Y4, Q5T2V9, Q7Z2J2, Q9Y4L5

Related

ENSP00000463650.1, ENST00000582693.5

Conserved Domains (2) summary

pfam14369
Location:19 → 49

zinc_ribbon_9; zinc-ribbon

cd16800
Location:226 → 272

RING-H2_RNF115; RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins