RNF138 ring finger protein 138 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RNF138provided by HGNC
Official Full Name: ring finger protein 138provided by HGNC
Primary source: HGNC:HGNC:17765
See related: Ensembl:ENSG00000134758 MIM:616319; AllianceGenome:HGNC:17765
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: NARF; HSD-4; STRIN; hNARF
Summary: The protein encoded by this gene contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
Expression: Broad expression in testis (RPKM 31.9), bone marrow (RPKM 30.7) and 23 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 18q12.1

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	18	NC_000018.10 (32091874..32131561)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	18	NC_060942.1 (32282268..32321925)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	18	NC_000018.9 (29671837..29711524)

Chromosome 18 - NC_000018.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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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?

Ring finger protein 138 inhibits transcription factor C/EBPalpha protein turnover leading to differentiation arrest in acute myeloid leukemia.
Title: Ring finger protein 138 inhibits transcription factor C/EBPα protein turnover leading to differentiation arrest in acute myeloid leukemia.
The role of RNF138 in DNA end resection is regulated by ubiquitylation and CDK phosphorylation.
Title: The role of RNF138 in DNA end resection is regulated by ubiquitylation and CDK phosphorylation.
RNF138 inhibits late inflammatory gene transcription through degradation of SMARCC1 of the SWI/SNF complex.
Title: RNF138 inhibits late inflammatory gene transcription through degradation of SMARCC1 of the SWI/SNF complex.
The Ubiquitin Ligase RNF138 Cooperates with CtIP to Stimulate Resection of Complex DNA Double-Strand Breaks in Human G1-Phase Cells.
Title: The Ubiquitin Ligase RNF138 Cooperates with CtIP to Stimulate Resection of Complex DNA Double-Strand Breaks in Human G1-Phase Cells.
RING finger 138 deregulation distorts NF-small ka, CyrillicB signaling and facilities colitis switch to aggressive malignancy.
Title: RING finger 138 deregulation distorts NF-кB signaling and facilities colitis switch to aggressive malignancy.
African Swine Fever Virus pI215L Negatively Regulates cGAS-STING Signaling Pathway through Recruiting RNF138 to Inhibit K63-Linked Ubiquitination of TBK1.
Title: African Swine Fever Virus pI215L Negatively Regulates cGAS-STING Signaling Pathway through Recruiting RNF138 to Inhibit K63-Linked Ubiquitination of TBK1.
Silencing microRNA29b3p expression protects human trabecular meshwork cells against oxidative injury via upregulation of RNF138 to activate the ERK pathway.
Title: Silencing microRNA‑29b‑3p expression protects human trabecular meshwork cells against oxidative injury via upregulation of RNF138 to activate the ERK pathway.
data suggest that RNF138 modulates the cisplatin resistance in the GC cells, thus serving as a potential drug target to challenge chemotherapy failure. In addition, RNF138 can also be used as a marker to monitor the development of cisplatin resistance in GC treatment.
Title: RNF138 confers cisplatin resistance in gastric cancer cells via activating Chk1 signaling pathway.
The role of RNF138 in glioblastoma and identify rpS3 as a crucial substrate of ubiquitination by RNF138, which underlies the radioresistance of glioblastoma.
Title: RNF138-mediated ubiquitination of rpS3 is required for resistance of glioblastoma cells to radiation-induced apoptosis.
Study suggested that RNF138 was important for the proliferation, migration and invasion of glioma cells. Its downregulation inhibited the process of EMT by suppressing Erk signaling pathway in glioma.
Title: Downregulation of RNF138 inhibits cellular proliferation, migration, invasion and EMT in glioma cells via suppression of the Erk signaling pathway.

Submit: New GeneRIF Correction See all GeneRIFs (18)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH39230 (e-PCR)
- UniSTS:91954

RH47733 (e-PCR)
- UniSTS:90975

G32540 (e-PCR)
- UniSTS:117124

RH39261 (e-PCR)
- UniSTS:92319

RNF138_1666 (e-PCR)
- UniSTS:277679

RH67231 (e-PCR)
- UniSTS:88037

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 protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables single-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables single-stranded DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin protein ligase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA double-strand break processing involved in repair via single-strand annealing	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA double-strand break processing involved in repair via single-strand annealing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in Wnt signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in cellular response to leukemia inhibitory factor	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair via homologous recombination	IBA Inferred from Biological aspect of Ancestor more info
involved_in double-strand break repair via homologous recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in protein ubiquitination	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in nucleus	HDA more info	PubMed
is_active_in site of double-strand break	IBA Inferred from Biological aspect of Ancestor more info
located_in site of double-strand break	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: E3 ubiquitin-protein ligase RNF138

Names: NLK-associated RING finger protein; Nemo-like kinase-associated RING finger protein; RING-type E3 ubiquitin transferase RNF138; nemo-like kinase associated ring finger protein; ring finger protein 138, E3 ubiquitin protein ligase; testicular tissue protein Li 165

NP_001178253.2

EC 2.3.2.27

NP_057355.2

EC 2.3.2.27

NP_937761.1

EC 2.3.2.27

XP_005258342.1

EC 2.3.2.27

XP_005258343.1

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.

Genomic

NG_029944.1 RefSeqGene

Range

5020..44707

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001191324.2 → NP_001178253.2 E3 ubiquitin-protein ligase RNF138 isoform 1

See identical proteins and their annotated locations for NP_001178253.2

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in the 5' UTR compared to variant 1. Variants 1 and 3 encode the same protein (isoform 1).

Source sequence(s)

AK023579, BC018107, DA752192

Consensus CDS

CCDS11903.1

UniProtKB/Swiss-Prot

B2RE17, Q8WVD3, Q9H8K2, Q9UF87, Q9UKI6

UniProtKB/TrEMBL

A0A140VJT9

Conserved Domains (3) summary

cd16544
Location:14 → 59

RING-HC_RNF138; RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins

pfam05605
Location:156 → 215

zf-Di19; Drought induced 19 protein (Di19), zinc-binding

pfam18574
Location:80 → 112

zf_C2HC_14; C2HC Zing finger domain
NM_016271.5 → NP_057355.2 E3 ubiquitin-protein ligase RNF138 isoform 1

See identical proteins and their annotated locations for NP_057355.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript. Variants 1 and 3 encode the same protein (isoform 1).

Source sequence(s)

AC011825, BC018107, DB452430

Consensus CDS

CCDS11903.1

UniProtKB/Swiss-Prot

B2RE17, Q8WVD3, Q9H8K2, Q9UF87, Q9UKI6

UniProtKB/TrEMBL

A0A140VJT9

Related

ENSP00000261593.3, ENST00000261593.8

Conserved Domains (3) summary

cd16544
Location:14 → 59

RING-HC_RNF138; RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins

pfam05605
Location:156 → 215

zf-Di19; Drought induced 19 protein (Di19), zinc-binding

pfam18574
Location:80 → 112

zf_C2HC_14; C2HC Zing finger domain
NM_198128.3 → NP_937761.1 E3 ubiquitin-protein ligase RNF138 isoform 2

See identical proteins and their annotated locations for NP_937761.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and lacks two alternate in-frame exons compared to variant 1. The resulting protein (isoform 2) is shorter compared to isoform 1.

Source sequence(s)

AK023579, BC018107, DB091985

Consensus CDS

CCDS11904.1

UniProtKB/Swiss-Prot

Q8WVD3

Related

ENSP00000257190.5, ENST00000257190.9

Conserved Domains (2) summary

pfam05605
Location:62 → 121

zf-Di19; Drought induced 19 protein (Di19), zinc-binding

cl17238
Location:14 → 37

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

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000018.10 Reference GRCh38.p14 Primary Assembly

Range

32091874..32131561

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_005258286.3 → XP_005258343.1 E3 ubiquitin-protein ligase RNF138 isoform X1

See identical proteins and their annotated locations for XP_005258343.1

UniProtKB/Swiss-Prot

Q8WVD3

Conserved Domains (2) summary

pfam05605
Location:62 → 121

zf-Di19; Drought induced 19 protein (Di19), zinc-binding

cl17238
Location:14 → 37

RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain
XM_005258285.2 → XP_005258342.1 E3 ubiquitin-protein ligase RNF138 isoform X2

See identical proteins and their annotated locations for XP_005258342.1

Conserved Domains (2) summary

pfam05605
Location:110 → 169

zf-Di19; Drought induced 19 protein (Di19), zinc-binding

pfam18574
Location:34 → 66

zf_C2HC_14; C2HC Zing finger domain