TRIM6 tripartite motif containing 6 [Homo sapiens (human)] - Gene

Summary

Official Symbol: TRIM6provided by HGNC
Official Full Name: tripartite motif containing 6provided by HGNC
Primary source: HGNC:HGNC:16277
See related: Ensembl:ENSG00000121236 MIM:607564; AllianceGenome:HGNC:16277
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: RNF89
Summary: The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, B-box type 1 and B-box type 2 domain, and a coiled-coil region. The protein localizes to the nucleus, but its specific function has not been identified. This gene is mapped to chromosome 11p15, where it resides within a TRIM gene cluster. Alternative splicing results in multiple transcript variants. A read-through transcript from this gene into the downstream TRIM34 gene has also been observed, which results in a fusion product from these neighboring family members. [provided by RefSeq, Oct 2010]
Expression: Broad expression in kidney (RPKM 10.6), testis (RPKM 6.4) and 15 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 11p15.4

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	11	NC_000011.10 (5596111..5612952)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	11	NC_060935.1 (5655518..5672393)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	11	NC_000011.9 (5617341..5634182)

Chromosome 11 - NC_000011.10 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 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?

Tripartite motif protein 6 promotes hepatocellular carcinoma progression via multiple pathways.
Title: Tripartite motif protein 6 promotes hepatocellular carcinoma progression via multiple pathways.
TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes.
Title: TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes.
TRIM6 Promotes ROS-Mediated Inflammasome Activation and Pyroptosis in Renal Tubular Epithelial Cells via Ubiquitination and Degradation of GPX3 Protein.
Title: TRIM6 Promotes ROS-Mediated Inflammasome Activation and Pyroptosis in Renal Tubular Epithelial Cells via Ubiquitination and Degradation of GPX3 Protein.
TRIM6: An Upregulated Biomarker with Prognostic Significance and Immune Correlations in Gliomas.
Title: TRIM6: An Upregulated Biomarker with Prognostic Significance and Immune Correlations in Gliomas.
TRIM6 silencing for inhibiting growth and angiogenesis of gliomas by regulating VEGFA.
Title: TRIM6 silencing for inhibiting growth and angiogenesis of gliomas by regulating VEGFA.
TRIM6 Reduces Ferroptosis and Chemosensitivity by Targeting SLC1A5 in Lung Cancer.
Title: TRIM6 Reduces Ferroptosis and Chemosensitivity by Targeting SLC1A5 in Lung Cancer.
Tripartite motif-containing protein 6 facilitates growth and migration of breast cancer through degradation of STUB1.
Title: Tripartite motif-containing protein 6 facilitates growth and migration of breast cancer through degradation of STUB1.
TRIM6 promotes colorectal cancer cells proliferation and response to thiostrepton by TIS21/FoxM1.
Title: TRIM6 promotes colorectal cancer cells proliferation and response to thiostrepton by TIS21/FoxM1.
these results provide evidence that TRIM6 contributes to the antiviral response against WNV and identify VAMP8 as a novel regulator of the IFN-I system.
Title: VAMP8 Contributes to the TRIM6-Mediated Type I Interferon Antiviral Response during West Nile Virus Infection.
Intriguingly, the authors also found that TRIM6 enhances ebola virus polymerase activity in a minigenome assay and TRIM6 knockout cells have reduced replication of infectious ebola virus, suggesting that VP35 hijacks TRIM6 to promote ebola virus replication through ubiquitination.
Title: The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus Replication.

Submit: New GeneRIF Correction See all GeneRIFs (13)

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
Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers. 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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Protein interactions

Protein	Gene	Interaction	Pubs
capsid	gag	Human TRIM6 binds in vitro assembled HIV-1 CA-NC complexes	PubMed
	gag	The RING, B-box 2, and coiled-coil domains of TRIM6 can functionally replace the corresponding domains of rhesus monkey TRIM5alpha with respect to inhibition of HIV-1 infection through the binding of the chimeras to HIV-1 capsid complexes	PubMed
nucleocapsid	gag	Human TRIM6 binds in vitro assembled HIV-1 CA-NC complexes	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

REN98883 (e-PCR)
- UniSTS:423680

ECD22887 (e-PCR)
- UniSTS:303872

REN98884 (e-PCR)
- UniSTS:423681

REN98885 (e-PCR)
- UniSTS:423682

REN98886 (e-PCR)
- UniSTS:423683

REN98887 (e-PCR)
- UniSTS:423684

REN98888 (e-PCR)
- UniSTS:423685

REN98889 (e-PCR)
- UniSTS:423686

REN98890 (e-PCR)
- UniSTS:423687

REN98891 (e-PCR)
- UniSTS:423688

REN98892 (e-PCR)
- UniSTS:423689

REN98893 (e-PCR)
- UniSTS:423690

REN98894 (e-PCR)
- UniSTS:423691

REN98895 (e-PCR)
- UniSTS:423692

REN98896 (e-PCR)
- UniSTS:423693

REN98897 (e-PCR)
- UniSTS:423694

REN98898 (e-PCR)
- UniSTS:423695

REN98899 (e-PCR)
- UniSTS:423696

REN98900 (e-PCR)
- UniSTS:423697

REN98901 (e-PCR)
- UniSTS:423698

REN98902 (e-PCR)
- UniSTS:423699

REN98903 (e-PCR)
- UniSTS:423700

REN98904 (e-PCR)
- UniSTS:423701

REN98905 (e-PCR)
- UniSTS:423702

REN98906 (e-PCR)
- UniSTS:423703

REN98907 (e-PCR)
- UniSTS:423704

REN98908 (e-PCR)
- UniSTS:423705

REN98909 (e-PCR)
- UniSTS:423706

REN98910 (e-PCR)
- UniSTS:423707

REN98911 (e-PCR)
- UniSTS:423708

REN98912 (e-PCR)
- UniSTS:423709

REN98913 (e-PCR)
- UniSTS:423710

REN98914 (e-PCR)
- UniSTS:423711

REN98915 (e-PCR)
- UniSTS:423712

ECD03883 (e-PCR)
- UniSTS:284963

ECD09061 (e-PCR)
- UniSTS:290107

ECD07528 (e-PCR)
- UniSTS:288579

ECD14728 (e-PCR)
- UniSTS:295748

ECD14729 (e-PCR)
- UniSTS:295749

ECD15518 (e-PCR)
- UniSTS:296535

ECD12969 (e-PCR)
- UniSTS:294000

G33046 (e-PCR)
- UniSTS:117623

A010A18 (e-PCR)
- UniSTS:42104

ECD02952 (e-PCR)
- UniSTS:284043

ECD06309 (e-PCR)
- UniSTS:287371

ECD12997 (e-PCR)
- UniSTS:294028

ECD15071 (e-PCR)
- UniSTS:296088

ECD12755 (e-PCR)
- UniSTS:293788

ECD07637 (e-PCR)
- UniSTS:288688

stSG611101 (e-PCR)
- UniSTS:449206

ECD16133 (e-PCR)
- UniSTS:297148

ECD15620 (e-PCR)
- UniSTS:296637

ECD19739 (e-PCR)
- UniSTS:300743

REN98840 (e-PCR)
- UniSTS:423637

REN98841 (e-PCR)
- UniSTS:423638

REN98842 (e-PCR)
- UniSTS:423639

ECD06902 (e-PCR)
- UniSTS:287960

REN98843 (e-PCR)
- UniSTS:423640

REN98844 (e-PCR)
- UniSTS:423641

REN98845 (e-PCR)
- UniSTS:423642

REN98846 (e-PCR)
- UniSTS:423643

REN98847 (e-PCR)
- UniSTS:423644

REN98848 (e-PCR)
- UniSTS:423645

REN98849 (e-PCR)
- UniSTS:423646

REN98850 (e-PCR)
- UniSTS:423647

REN98851 (e-PCR)
- UniSTS:423648

REN98852 (e-PCR)
- UniSTS:423649

REN98853 (e-PCR)
- UniSTS:423650

REN98854 (e-PCR)
- UniSTS:423651

REN98855 (e-PCR)
- UniSTS:423652

REN98856 (e-PCR)
- UniSTS:423653

REN98857 (e-PCR)
- UniSTS:423654

REN98858 (e-PCR)
- UniSTS:423655

REN98859 (e-PCR)
- UniSTS:423656

REN98860 (e-PCR)
- UniSTS:423657

REN98861 (e-PCR)
- UniSTS:423658

REN98862 (e-PCR)
- UniSTS:423659

REN98863 (e-PCR)
- UniSTS:423660

ECD13867 (e-PCR)
- UniSTS:294892

REN98864 (e-PCR)
- UniSTS:423661

REN98865 (e-PCR)
- UniSTS:423662

REN98866 (e-PCR)
- UniSTS:423663

REN98867 (e-PCR)
- UniSTS:423664

REN98868 (e-PCR)
- UniSTS:423665

REN98869 (e-PCR)
- UniSTS:423666

REN98870 (e-PCR)
- UniSTS:423667

REN98871 (e-PCR)
- UniSTS:423668

REN98872 (e-PCR)
- UniSTS:423669

REN98873 (e-PCR)
- UniSTS:423670

REN98874 (e-PCR)
- UniSTS:423671

REN98875 (e-PCR)
- UniSTS:423672

ECD03066 (e-PCR)
- UniSTS:284153

REN98876 (e-PCR)
- UniSTS:423673

REN98877 (e-PCR)
- UniSTS:423674

REN98878 (e-PCR)
- UniSTS:423675

REN98879 (e-PCR)
- UniSTS:423676

REN98880 (e-PCR)
- UniSTS:423677

REN98881 (e-PCR)
- UniSTS:423678

REN98882 (e-PCR)
- UniSTS:423679

Readthrough TRIM6-TRIM34

Readthrough gene: TRIM6-TRIM34, Included gene: TRIM34

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables DNA-binding transcription factor binding	IEA Inferred from Electronic Annotation more info
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 homodimerization activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein kinase binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein tyrosine kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-macromolecule adaptor activity	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	IMP Inferred from Mutant Phenotype more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in antiviral innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to interferon-beta	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to virus	IEA Inferred from Electronic Annotation more info
involved_in free ubiquitin chain polymerization	IDA Inferred from Direct Assay more info	PubMed
involved_in free ubiquitin chain polymerization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of gene expression	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of stem cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of viral genome replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of autophagy	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of canonical NF-kappaB signal transduction	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of cytokine production involved in immune response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of defense response to virus by host	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of peptidyl-serine phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of peptidyl-threonine phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of transcription regulatory region DNA binding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of type I interferon-mediated signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of type I interferon-mediated signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein K48-linked ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of gene expression	IBA Inferred from Biological aspect of Ancestor more info
NOT involved_in regulation of non-canonical NF-kappaB signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of protein localization	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of viral entry into host cell	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to lipopolysaccharide	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleoplasm	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: tripartite motif-containing protein 6

Names: RING finger protein 89; RING-type E3 ubiquitin transferase TRIM6

NP_001003818.1

EC 2.3.2.27

NP_001185573.1

EC 2.3.2.27

NP_001185574.1

EC 2.3.2.27

NP_477514.1

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_001003818.3 → NP_001003818.1 tripartite motif-containing protein 6 isoform 1

See identical proteins and their annotated locations for NP_001003818.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).

Source sequence(s)

AF220030, AK290172, AK316178, BC047564

Consensus CDS

CCDS31389.1

UniProtKB/TrEMBL

E9PFM0

Related

ENSP00000369440.3, ENST00000380097.8

Conserved Domains (4) summary

smart00336
Location:121 → 161

BBOX; B-Box-type zinc finger

cd15823
Location:327 → 514

SPRY_PRY_TRIM6; PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89)

cl17238
Location:43 → 87

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 ...

cl23765
Location:170 → 287

iSH2_PI3K_IA_R; Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits
NM_001198644.2 → NP_001185573.1 tripartite motif-containing protein 6 isoform 3

See identical proteins and their annotated locations for NP_001185573.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an alternate exon in the 5' coding region, and uses a downstream AUG start codon, compared to variant 1. The encoded isoform (3) has a shorter N-terminus, compared to isoform 1. Both variants 3 and 4 encode the same isoform.

Source sequence(s)

AF220030, AK290172, AK293295, AK298301, AK316178, BC047564, DA401634

Consensus CDS

CCDS55738.1

UniProtKB/Swiss-Prot

Q9C030

Related

ENSP00000421079.1, ENST00000506134.5

Conserved Domains (1) summary

cd15823
Location:124 → 311

SPRY_PRY_TRIM6; PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89)
NM_001198645.2 → NP_001185574.1 tripartite motif-containing protein 6 isoform 3

See identical proteins and their annotated locations for NP_001185574.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) lacks two alternate exons in the 5' coding region, and uses a downstream AUG start codon, compared to variant 1. The encoded isoform (3) has a shorter N-terminus, compared to isoform 1. Both variants 3 and 4 encode the same isoform.

Source sequence(s)

AF220030, AK290172, AK293295, BC047564, DA401634

Consensus CDS

CCDS55738.1

UniProtKB/Swiss-Prot

Q9C030

Related

ENSP00000421802.1, ENST00000515022.5

Conserved Domains (1) summary

cd15823
Location:124 → 311

SPRY_PRY_TRIM6; PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89)
NM_058166.5 → NP_477514.1 tripartite motif-containing protein 6 isoform 2

See identical proteins and their annotated locations for NP_477514.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR, lacks a portion of the 5' coding region, and uses a downstream AUG start codon, compared to variant 1. The encoded isoform (2) has a shorter N-terminus, compared to isoform 1.

Source sequence(s)

AF220030, AK027664, AK290172, DC354457

Consensus CDS

CCDS31390.1

UniProtKB/Swiss-Prot

A8K2A7, B4DDQ5, Q86WZ8, Q9C030

UniProtKB/TrEMBL

E9PFM0

Related

ENSP00000278302.5, ENST00000278302.9

Conserved Domains (4) summary

smart00336
Location:93 → 133

BBOX; B-Box-type zinc finger

cd15823
Location:299 → 486

SPRY_PRY_TRIM6; PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89)

cl17238
Location:15 → 59

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 ...

cl23765
Location:142 → 259

iSH2_PI3K_IA_R; Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits