TRIM5 tripartite motif containing 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: TRIM5provided by HGNC
Official Full Name: tripartite motif containing 5provided by HGNC
Primary source: HGNC:HGNC:16276
See related: Ensembl:ENSG00000132256 MIM:608487; AllianceGenome:HGNC:16276
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: RNF88; TRIM5alpha
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, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Dec 2009]
Expression: Ubiquitous expression in urinary bladder (RPKM 5.4), endometrium (RPKM 5.4) and 25 other tissues See more
Orthologs: all
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Genomic context

Location:: 11p15.4

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	11	NC_000011.10 (5588635..5685074, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	11	NC_060935.1 (5647845..5742931, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	11	NC_000011.9 (5684425..5706304, complement)

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?

TRIM5alpha: A Protean Architect of Viral Recognition and Innate Immunity.
Title: TRIM5α: A Protean Architect of Viral Recognition and Innate Immunity.
TBK1 is ubiquitinated by TRIM5alpha to assemble mitophagy machinery.
Title: TBK1 is ubiquitinated by TRIM5α to assemble mitophagy machinery.
The effect of TRIM5 variants on the susceptibility to HIV-1 infection and disease progression in the Polish population.
Title: The effect of TRIM5 variants on the susceptibility to HIV-1 infection and disease progression in the Polish population.
TRIM5alpha restricts poxviruses and is antagonized by CypA and the viral protein C6.
Title: TRIM5α restricts poxviruses and is antagonized by CypA and the viral protein C6.
A frequent SNP in TRIM5alpha strongly enhances the innate immune response against LINE-1 elements.
Title: A frequent SNP in TRIM5α strongly enhances the innate immune response against LINE-1 elements.
The retroviral restriction factor TRIM5/TRIM5alpha regulates mitochondrial quality control.
Title: The retroviral restriction factor TRIM5/TRIM5α regulates mitochondrial quality control.
Interactomic analysis reveals a homeostatic role for the HIV restriction factor TRIM5alpha in mitophagy.
Title: Interactomic analysis reveals a homeostatic role for the HIV restriction factor TRIM5α in mitophagy.
TRIM5alpha Restriction of HIV-1-N74D Viruses in Lymphocytes Is Caused by a Loss of Cyclophilin A Protection.
Title: TRIM5α Restriction of HIV-1-N74D Viruses in Lymphocytes Is Caused by a Loss of Cyclophilin A Protection.
Knockdown of TRIM5alpha or TRIM11 increases lentiviral vector transduction efficiency of human Muller cells.
Title: Knockdown of TRIM5α or TRIM11 increases lentiviral vector transduction efficiency of human Muller cells.
Human TRIM5alpha: Autophagy Connects Cell-Intrinsic HIV-1 Restriction and Innate Immune Sensor Functioning.
Title: Human TRIM5α: Autophagy Connects Cell-Intrinsic HIV-1 Restriction and Innate Immune Sensor Functioning.

Submit: New GeneRIF Correction See all GeneRIFs (135)

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
GWAS of DNA methylation variation within imprinting control regions suggests parent-of-origin association. EBI GWAS Catalog EBI GWAS CatalogPubMed
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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Replication interactions

Interaction	Pubs
HIV-1 replication is inhibited by TRIM5 expression in Jurkat T cells	PubMed
TRIM5 (TRIM5alpha) R332G-R335G mutant protein efficiently restricts HIV-1 IIIB infection spreading/replicaton in CEM.NKR-CCR5 cells	PubMed
Female Pumwani sex workers with the TRIM5 R136Q polymorphism (rs10838525) were less likely to seroconvert despite repeated heavy exposure to HIV-1.	PubMed
Higher TRIM5 (TRIM5alpha) H43Y homozygotes reported in sero-negative Chinese intravenous drug users than in HIV-infected drug users; HIV-1 infection/transmission is restricted by TRIM5 43Y variant [in a Chinese intravenous drug user cohort]	PubMed
TRIM5 (TRIM5alpha) 43Y allele was found less frequently in Japanese and Indian HIV-1-infected individuals relative to ethnicity-matched controls	PubMed
TRIM5 (TRIM5alpha) 43Y vairant protects against HIV-1 transmisssion in African-Americans; HIV-1 is restricted by TRIM5 43Y variant	PubMed
HIV/tuberculosis coinfection upregulates TRIM5 expression in pleural fluid mononuclear cells (PFMC) isolated from antiretroviral-naive coinfected patients (relative to patients infected with tuberculosis only)	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Pr55(Gag)	gag	The viruses expressing Gag proteins from clinical isolates show differences in their sensitivity to TRIM5alpha, which is dependent on the TRIM5alpha alleles that the virus encounters	PubMed
Tat	tat	Overexpression of HIV-1 Tat results in a nonspecific activation of the expression of TRIM5alpha	PubMed
Vpu	vpu	The expression of TRIM5 is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells	PubMed
capsid	gag	HIV-1 infection is modestly restricted by human TRIM5alpha, which acts on the incoming HIV-1 capsid	PubMed
	gag	Removal of a positively charged residue at position 332 of human TRIM5alpha increases its restricting activity by increasing the ability of TRIM5alpha to bind HIV-1 capsid complexes	PubMed
	gag	Intra- and inter-hexamer crosslinking demonstrate the interaction between HIV-1 CA and human TRIM5alpha CC-SPRY domains (residues 132-493)	PubMed
	gag	HIV-1 CA residues 83, 89, 120, 122 and the aromatic residues 117, 130, and 133 modulate its sensitivity to TRIM5alpha	PubMed
	gag	TRIM5alpha disrupts the regular cylindrical hexameric lattice structure of HIV-1 CA-NC complex	PubMed
	gag	HIV-1 capsid is more rapidly degraded in cells expressing monkey TRIM5alpha than in cells expressing human TRIM5alpha	PubMed
	gag	R332G/R335G and R330E/R332G/R335G mutants of TRIM5alpha binds the in vitro-assembled CA-NC complexes and the strength of the interaction correlates with the magnitude of restriction	PubMed
	gag	Mutation G330E in the v1 TRIM5alpha region exhibits a strong level of HIV-1 resistance, while mutations G330A or G330S have little or no effect	PubMed
	gag	The level of susceptibility hTRIM5alpha expressed by viruses carrying HIV-2 CA sequences in the context of HIV-1 NL4-3 is higher than that of HIV-1 NL4-3 and markedly higher than a panel of primary HIV-1 CA sequences	PubMed
	gag	HIV-1 CA-V86M mutant is partially resistant to restriction by hTRIM5alpha mutant R322G/R335G. The restriction of CA-V86M by hTRIM5alpha R322G/R335G is independent of cyclophilin A, but correlates with its sensitivity to cyclosporine A treatment	PubMed
	gag	TRIM5alpha allelic variants R136Q/H419Y and H43Y/G249D are generally inactive for HIV-1 CA inhibition	PubMed
	gag	The T216I mutation in HIV-1 CA restores the ability of P38A CA mutant particles to saturate TRIM5alpha host restrictions in monkey cells	PubMed
	gag	The TAK1 kinase complex (TAK1/TAB2/TAB3) contributes to capsid-specific restriction mediated by TRIM5alpha. TRIM5alpha activates TAK1 autophosphorylation	PubMed
	gag	Human TRIM5-alpha and TRIM5-delta proteins are dominant negative to HIV-1 restriction in rabbit cells	PubMed
	gag	TRIM5alpha associates with HIV-1 capsid-nucleocapsid complexes assembled in vitro, and the TRIM5alpha interaction with these complexes is dependent on its B30.2(SPRY) domains	PubMed
	gag	Cluster I-A and Cluster II-A changes in the B-box 2 domain of TRIM5alpha decrease its binding to HIV-1 Capsid	PubMed
	gag	Two B-box TRIM5alpha mutants (Cluster I-A:Q109E, E110K, V114A, I115L, and L118V; Cluster II-A:E120A, R121Q, Q123R, and E124K) abolish the weak restricting activity against HIV-1 associated with wild-type TRIM5alpha	PubMed
	gag	Human TRIM5alpha modestly, but specifically, inhibits an HIV-1 strain carrying a mutation (G89V) in the cyclophilin binding loop in capsid	PubMed
	gag	The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolates-dependent, which can result in inhibition, no change, or an increase in viral infectivity	PubMed
	gag	TRIM5alpha binds to HIV-1 CA tubular assemblies in a dose-dependent manner, especially at P207/T216 inter-hexamer interfaces	PubMed
nucleocapsid	gag	R332G/R335G and R330E/R332G/R335G mutants of TRIM5alpha binds the in vitro-assembled CA-NC complexes and the strength of the interaction correlates with the magnitude of restriction	PubMed
	gag	TRIM5alpha disrupts the regular cylindrical hexameric lattice structure of HIV-1 CA-NC complex	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

REN99139 (e-PCR)
- UniSTS:423936

REN99140 (e-PCR)
- UniSTS:423937

REN99141 (e-PCR)
- UniSTS:423938

REN99142 (e-PCR)
- UniSTS:423939

REN99143 (e-PCR)
- UniSTS:423940

RH80365 (e-PCR)
- UniSTS:87301

REN99144 (e-PCR)
- UniSTS:423941

REN99145 (e-PCR)
- UniSTS:423942

REN99146 (e-PCR)
- UniSTS:423943

REN99147 (e-PCR)
- UniSTS:423944

REN99148 (e-PCR)
- UniSTS:423945

REN99149 (e-PCR)
- UniSTS:423946

REN99150 (e-PCR)
- UniSTS:423947

REN99151 (e-PCR)
- UniSTS:423948

REN99152 (e-PCR)
- UniSTS:423949

REN99153 (e-PCR)
- UniSTS:423950

REN99154 (e-PCR)
- UniSTS:423951

REN99155 (e-PCR)
- UniSTS:423952

REN99156 (e-PCR)
- UniSTS:423953

REN99157 (e-PCR)
- UniSTS:423954

REN99158 (e-PCR)
- UniSTS:423955

REN99159 (e-PCR)
- UniSTS:423956

REN99160 (e-PCR)
- UniSTS:423957

REN99161 (e-PCR)
- UniSTS:423958

REN99162 (e-PCR)
- UniSTS:423959

REN99163 (e-PCR)
- UniSTS:423960

SHGC-32233 (e-PCR)
- UniSTS:26393

REN99164 (e-PCR)
- UniSTS:423961

REN99165 (e-PCR)
- UniSTS:423962

REN99166 (e-PCR)
- UniSTS:423963

REN99167 (e-PCR)
- UniSTS:423964

REN99168 (e-PCR)
- UniSTS:423965

REN99169 (e-PCR)
- UniSTS:423966

REN99170 (e-PCR)
- UniSTS:423967

REN99171 (e-PCR)
- UniSTS:423968

REN99172 (e-PCR)
- UniSTS:423969

ECD16490 (e-PCR)
- UniSTS:297505

REN99173 (e-PCR)
- UniSTS:423970

ECD06463 (e-PCR)
- UniSTS:287523

REN99174 (e-PCR)
- UniSTS:423971

REN99175 (e-PCR)
- UniSTS:423972

REN99176 (e-PCR)
- UniSTS:423973

REN99177 (e-PCR)
- UniSTS:423974

REN99178 (e-PCR)
- UniSTS:423975

REN99179 (e-PCR)
- UniSTS:423976

REN99180 (e-PCR)
- UniSTS:423977

REN99181 (e-PCR)
- UniSTS:423978

REN99182 (e-PCR)
- UniSTS:423979

REN99183 (e-PCR)
- UniSTS:423980

REN99184 (e-PCR)
- UniSTS:423981

REN99185 (e-PCR)
- UniSTS:423982

REN99186 (e-PCR)
- UniSTS:423983

REN99187 (e-PCR)
- UniSTS:423984

REN99188 (e-PCR)
- UniSTS:423985

REN99189 (e-PCR)
- UniSTS:423986

REN99190 (e-PCR)
- UniSTS:423987

REN99191 (e-PCR)
- UniSTS:423988

REN99192 (e-PCR)
- UniSTS:423989

REN99193 (e-PCR)
- UniSTS:423990

REN99194 (e-PCR)
- UniSTS:423991

REN99195 (e-PCR)
- UniSTS:423992

REN99196 (e-PCR)
- UniSTS:423993

REN99197 (e-PCR)
- UniSTS:423994

REN99198 (e-PCR)
- UniSTS:423995

REN99199 (e-PCR)
- UniSTS:423996

REN99200 (e-PCR)
- UniSTS:423997

REN99201 (e-PCR)
- UniSTS:423998

REN99202 (e-PCR)
- UniSTS:423999

REN99203 (e-PCR)
- UniSTS:424000

ECD00812 (e-PCR)
- UniSTS:281921

REN99204 (e-PCR)
- UniSTS:424001

REN99205 (e-PCR)
- UniSTS:424002

REN99206 (e-PCR)
- UniSTS:424003

REN99207 (e-PCR)
- UniSTS:424004

REN99208 (e-PCR)
- UniSTS:424005

REN99209 (e-PCR)
- UniSTS:424006

ECD14730 (e-PCR)
- UniSTS:295750

REN99210 (e-PCR)
- UniSTS:424007

REN99211 (e-PCR)
- UniSTS:424008

REN99212 (e-PCR)
- UniSTS:424009

ECD16307 (e-PCR)
- UniSTS:297322

RH67864 (e-PCR)
- UniSTS:35182

D11S3114 (e-PCR)
- UniSTS:152207

ECD19427 (e-PCR)
- UniSTS:300432

ECD01668 (e-PCR)
- UniSTS:282769

ECD12489 (e-PCR)
- UniSTS:293522

ECD13261 (e-PCR)
- UniSTS:294291

ECD03497 (e-PCR)
- UniSTS:284579

SHGC-82206 (e-PCR)
- UniSTS:103103

ECD02488 (e-PCR)
- UniSTS:283586

stSG611140 (e-PCR)
- UniSTS:449244

stSG611141 (e-PCR)
- UniSTS:449245

ECD11028 (e-PCR)
- UniSTS:292064

ECD02008 (e-PCR)
- UniSTS:283109

stSG611150 (e-PCR)
- UniSTS:449253

REN99120 (e-PCR)
- UniSTS:423917

REN99121 (e-PCR)
- UniSTS:423918

REN99122 (e-PCR)
- UniSTS:423919

REN99123 (e-PCR)
- UniSTS:423920

REN99124 (e-PCR)
- UniSTS:423921

REN99125 (e-PCR)
- UniSTS:423922

REN99126 (e-PCR)
- UniSTS:423923

REN99127 (e-PCR)
- UniSTS:423924

REN99128 (e-PCR)
- UniSTS:423925

REN99129 (e-PCR)
- UniSTS:423926

REN99130 (e-PCR)
- UniSTS:423927

REN99131 (e-PCR)
- UniSTS:423928

REN99132 (e-PCR)
- UniSTS:423929

REN99133 (e-PCR)
- UniSTS:423930

REN99134 (e-PCR)
- UniSTS:423931

REN99135 (e-PCR)
- UniSTS:423932

REN99136 (e-PCR)
- UniSTS:423933

REN99137 (e-PCR)
- UniSTS:423934

REN99138 (e-PCR)
- UniSTS:423935

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables pattern recognition receptor activity	IDA Inferred from Direct Assay 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 homodimerization activity	IPI Inferred from Physical Interaction more info	PubMed
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-macromolecule adaptor activity	IPI Inferred from Physical Interaction more info	PubMed
enables transcription coactivator activity	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 transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in activation of innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in autophagy	IDA Inferred from Direct Assay more info	PubMed
involved_in defense response to virus	TAS Traceable Author Statement more info	PubMed
involved_in innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of viral entry into host cell	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of DNA-binding transcription factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of MAPK cascade	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of NF-kappaB transcription factor activity	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 canonical NF-kappaB signal transduction	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of canonical NF-kappaB signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein K63-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
involved_in regulation of lipopolysaccharide-mediated signaling pathway	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 protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of viral entry into host cell	IBA Inferred from Biological aspect of Ancestor more info
involved_in suppression of viral release by host	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in P-body	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	TAS Traceable Author Statement more info
is_active_in nucleoplasm	IBA Inferred from Biological aspect of Ancestor more info
colocalizes_with omegasome	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: tripartite motif-containing protein 5

Names: RING-type E3 ubiquitin transferase TRIM5; ring finger protein 88; tripartite motif protein TRIM5; tripartite motif-containing protein 5 alpha

NP_001397887.1

EC 2.3.2.27

NP_149023.2

EC 2.3.2.27

NP_149083.2

EC 2.3.2.27

NP_149084.2

EC 2.3.2.27

XP_005253240.1

EC 2.3.2.27

XP_005253241.1

EC 2.3.2.27

XP_006718421.1

EC 2.3.2.27

XP_011518728.1

EC 2.3.2.27

XP_016873949.1

EC 2.3.2.27

XP_016873950.1

EC 2.3.2.27

XP_047283739.1

EC 2.3.2.27

XP_047283740.1

EC 2.3.2.27

XP_054226288.1

EC 2.3.2.27

XP_054226289.1

EC 2.3.2.27

XP_054226290.1

EC 2.3.2.27

XP_054226291.1

EC 2.3.2.27

XP_054226292.1

EC 2.3.2.27

XP_054226293.1

EC 2.3.2.27

XP_054226294.1

EC 2.3.2.27

XP_054226295.1

EC 2.3.2.27

XP_054226296.1

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_029122.2 RefSeqGene

Range

5000..26879

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001410958.1 → NP_001397887.1 tripartite motif-containing protein 5 isoform 4

Status: REVIEWED

Source sequence(s)

AC015691, AC109341

Consensus CDS

CCDS91425.1

UniProtKB/TrEMBL

A0A804HHS7

Related

ENSP00000506742.1, ENST00000682968.1
NM_033034.3 → NP_149023.2 tripartite motif-containing protein 5 isoform alpha

See identical proteins and their annotated locations for NP_149023.2

Status: REVIEWED

Description

Transcript Variant: This variant (alpha) encodes the longest isoform (alpha).

Source sequence(s)

AC015691, AK027593, CN334837, DA475412

Consensus CDS

CCDS31393.1

UniProtKB/Swiss-Prot

A6NGQ1, A8WFA8, D3DQS8, D3DQS9, G3GJY1, Q2MLV4, Q2MLV8, Q2MLV9, Q2MLW1, Q2MLW3, Q2MLW4, Q2MLW6, Q2MLW7, Q2MLX1, Q2MLX2, Q2MLX3, Q2MLX5, Q2MLY3, Q2MLY4, Q2V6Q6, Q6GX26, Q8WU46, Q96SR5, Q9C031, Q9C032, Q9C033, Q9C034, Q9C035

UniProtKB/TrEMBL

B1Q3L0

Related

ENSP00000369373.3, ENST00000380034.8

Conserved Domains (3) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...

cd15822
Location:288 → 489

SPRY_PRY_TRIM5; PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88)
NM_033092.4 → NP_149083.2 tripartite motif-containing protein 5 isoform gamma

See identical proteins and their annotated locations for NP_149083.2

Status: REVIEWED

Description

Transcript Variant: This variant (gamma) includes an alternate segment in the 3' coding region, compared to variant alpha, which results in a frameshift. The resulting protein (isoform gamma) has a shorter and distinct C-terminus, compared to isoform alpha.

Source sequence(s)

AC015691, AF220027, AK074363, BC021258, CN334837, DA475412

Consensus CDS

CCDS31394.1

UniProtKB/Swiss-Prot

Q9C035

Related

ENSP00000380058.3, ENST00000396847.7

Conserved Domains (4) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

pfam12325
Location:130 → 175

TMF_TATA_bd; TATA element modulatory factor 1 TATA binding

cd16591
Location:12 → 60

RING-HC_TRIM5_like-C-IV; RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins

cl25732
Location:116 → 240

SMC_N; RecF/RecN/SMC N terminal domain
NM_033093.4 → NP_149084.2 tripartite motif-containing protein 5 isoform delta

See identical proteins and their annotated locations for NP_149084.2

Status: REVIEWED

Description

Transcript Variant: This variant (delta) differs in the 5' UTR and uses an alternate splice site in the 3' terminal exon, which results in a frameshift, compared to variant alpha. The encoded isoform (delta) has a shorter and distinct C-terminus, compared to isoform alpha.

Source sequence(s)

AC015691, AC109341, DA475412

Consensus CDS

CCDS31392.1

UniProtKB/Swiss-Prot

Q9C035

Related

ENSP00000369366.1, ENST00000380027.5

Conserved Domains (2) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...

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_000011.10 Reference GRCh38.p14 Primary Assembly

Range

5588635..5685074 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047427783.1 → XP_047283739.1 tripartite motif-containing protein 5 isoform X5
XM_047427784.1 → XP_047283740.1 tripartite motif-containing protein 5 isoform X7

Related

ENSP00000388031.1, ENST00000412903.1
XM_005253183.4 → XP_005253240.1 tripartite motif-containing protein 5 isoform X1

See identical proteins and their annotated locations for XP_005253240.1

UniProtKB/Swiss-Prot

A6NGQ1, A8WFA8, D3DQS8, D3DQS9, G3GJY1, Q2MLV4, Q2MLV8, Q2MLV9, Q2MLW1, Q2MLW3, Q2MLW4, Q2MLW6, Q2MLW7, Q2MLX1, Q2MLX2, Q2MLX3, Q2MLX5, Q2MLY3, Q2MLY4, Q2V6Q6, Q6GX26, Q8WU46, Q96SR5, Q9C031, Q9C032, Q9C033, Q9C034, Q9C035

UniProtKB/TrEMBL

B1Q3L0

Related

ENSP00000507420.1, ENST00000684655.1

Conserved Domains (3) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...

cd15822
Location:288 → 489

SPRY_PRY_TRIM5; PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88)
XM_006718358.4 → XP_006718421.1 tripartite motif-containing protein 5 isoform X6

UniProtKB/TrEMBL

A0A804HHS7

Conserved Domains (2) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...
XM_017018461.3 → XP_016873950.1 tripartite motif-containing protein 5 isoform X4

Conserved Domains (2) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...
XM_011520426.4 → XP_011518728.1 tripartite motif-containing protein 5 isoform X4

Conserved Domains (2) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...
XM_005253184.4 → XP_005253241.1 tripartite motif-containing protein 5 isoform X2

See identical proteins and their annotated locations for XP_005253241.1

UniProtKB/Swiss-Prot

Q9C035

Conserved Domains (2) summary

smart00336
Location:90 → 130

BBOX; B-Box-type zinc finger

cd00162
Location:14 → 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 ...
XM_017018460.3 → XP_016873949.1 tripartite motif-containing protein 5 isoform X3

RNA

XR_007062522.1 RNA Sequence
XR_007062518.1 RNA Sequence
XR_007062519.1 RNA Sequence
XR_001748014.3 RNA Sequence
XR_007062521.1 RNA Sequence
XR_007062520.1 RNA Sequence
XR_007062517.1 RNA Sequence

Alternate T2T-CHM13v2.0

Genomic

NC_060935.1 Alternate T2T-CHM13v2.0

Range

5647845..5742931 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054370319.1 → XP_054226294.1 tripartite motif-containing protein 5 isoform X5
XM_054370318.1 → XP_054226293.1 tripartite motif-containing protein 5 isoform X8
XM_054370313.1 → XP_054226288.1 tripartite motif-containing protein 5 isoform X1
XM_054370321.1 → XP_054226296.1 tripartite motif-containing protein 5 isoform X6
XM_054370317.1 → XP_054226292.1 tripartite motif-containing protein 5 isoform X4
XM_054370316.1 → XP_054226291.1 tripartite motif-containing protein 5 isoform X4
XM_054370314.1 → XP_054226289.1 tripartite motif-containing protein 5 isoform X2
XM_054370320.1 → XP_054226295.1 tripartite motif-containing protein 5 isoform X9
XM_054370315.1 → XP_054226290.1 tripartite motif-containing protein 5 isoform X3