TRIM63 tripartite motif containing 63 [Homo sapiens (human)] - Gene

Summary

Official Symbol: TRIM63provided by HGNC
Official Full Name: tripartite motif containing 63provided by HGNC
Primary source: HGNC:HGNC:16007
See related: Ensembl:ENSG00000158022 MIM:606131; AllianceGenome:HGNC:16007
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: IRF; SMRZ; MURF1; MURF2; RNF28
Summary: This gene encodes a member of the RING zinc finger protein family found in striated muscle and iris. The product of this gene is an E3 ubiquitin ligase that localizes to the Z-line and M-line lattices of myofibrils. This protein plays an important role in the atrophy of skeletal and cardiac muscle and is required for the degradation of myosin heavy chain proteins, myosin light chain, myosin binding protein, and for muscle-type creatine kinase. [provided by RefSeq, Feb 2012]
Expression: Biased expression in heart (RPKM 44.7) and esophagus (RPKM 2.8) See more
Orthologs: mouse all
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Genomic context

Location:: 1p36.11

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (26051301..26067630, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (25888705..25905036, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (26377792..26394121, complement)

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 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?

Evaluation of TRIM63 RNA in situ hybridization (RNA-ISH) as a potential biomarker for alveolar soft-part sarcoma (ASPS).
Title: Evaluation of TRIM63 RNA in situ hybridization (RNA-ISH) as a potential biomarker for alveolar soft-part sarcoma (ASPS).
Myeloma cells shift osteoblastogenesis to adipogenesis by inhibiting the ubiquitin ligase MURF1 in mesenchymal stem cells.
Title: Myeloma cells shift osteoblastogenesis to adipogenesis by inhibiting the ubiquitin ligase MURF1 in mesenchymal stem cells.
Mutations in TRIM63 cause an autosomal-recessive form of hypertrophic cardiomyopathy.
Title: Mutations in TRIM63 cause an autosomal-recessive form of hypertrophic cardiomyopathy.
Doxorubicin induces cardiomyocyte apoptosis and atrophy through cyclin-dependent kinase 2-mediated activation of forkhead box O1.
Title: Doxorubicin induces cardiomyocyte apoptosis and atrophy through cyclin-dependent kinase 2-mediated activation of forkhead box O1.
MuRF1 turned out to be also a target for a new post-translational modification arbitrated by conjugation of SUMO1 and it is mediated by the SUMO ligases E2 UBC9 and the E3 PIASgamma/4. SUMOylation takes place at lysine 238 localized at the second coiled-coil protein domain that is required for efficient substrate interaction for polyubiquitination.
Title: Muscle RING-finger protein-1 (MuRF1) functions and cellular localization are regulated by SUMO1 post-translational modification.
Using a combination of electron paramagnetic resonance, on spin-labeled protein, and disulfide crosslinking, the study shows that TRIM63 follows the structural conservation of the TRIM dimerization domain, observed in other proteins. the COS-box motif folds back onto the dimerization coiled-coil motif, predictably forming a four-helical bundle at the center of the protein and emulating the architecture of canonical TRIMs.
Title: Exploration of the TRIM Fold of MuRF1 Using EPR Reveals a Canonical Antiparallel Structure and Extended COS-Box.
an impaired interaction between titin and MURF1 as a novel mechanism underlying the pathogenesis ofHypertrophic cardiomyopathy (HCM).
Title: Perturbation of the titin/MURF1 signaling complex is associated with hypertrophic cardiomyopathy in a fish model and in human patients.
Our study revealed that TRIM63, acting as an oncogene, is involved in breast cancer progression by activating the Wnt/beta-catenin signaling pathway
Title: A novel oncogene TRIM63 promotes cell proliferation and migration via activating Wnt/β-catenin signaling pathway in breast cancer.
missense single nucleotide polymorphism (A>G, rs2275950 ) within the TRIM63 gene (encoding MuRF-1 and potentially affecting titin mechanical properties) was associated with the variable response to unaccustomed eccentric exercise.
Title: TRIM63 (MuRF-1) gene polymorphism is associated with biomarkers of exercise-induced muscle damage.
role of the muscle specific E3s MuRF-1 and MAFbx in skeletal muscle wasting during various pathologies, as well as their regulation by modifiable lifestyle factors, were explored (review)
Title: The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass.

Submit: New GeneRIF Correction See all GeneRIFs (49)

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

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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Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables titin 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	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 innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in muscle contraction	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of cardiac muscle hypertrophy	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of glycolytic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in response to electrical stimulus involved in regulation of muscle adaptation	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to glucocorticoid	IEA Inferred from Electronic Annotation more info
involved_in response to interleukin-1	IEA Inferred from Electronic Annotation more info
involved_in signal transduction	NAS Non-traceable Author Statement more info	PubMed
involved_in skeletal muscle atrophy	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in M band	IEA Inferred from Electronic Annotation more info
located_in Z disc	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	NAS Non-traceable Author Statement more info	PubMed
located_in microtubule	NAS Non-traceable Author Statement 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 TRIM63

Names: RING-type E3 ubiquitin transferase TRIM63; iris ring finger protein; muscle specific ring finger protein 2; muscle-specific RING finger protein 1; ring finger protein 28; striated muscle RING zinc finger protein; tripartite motif containing 63, E3 ubiquitin protein ligase; tripartite motif-containing protein 63

NP_115977.2

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_033268.1 RefSeqGene

Range

5001..21331

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_757

mRNA and Protein(s)

NM_032588.4 → NP_115977.2 E3 ubiquitin-protein ligase TRIM63

See identical proteins and their annotated locations for NP_115977.2

Status: REVIEWED

Source sequence(s)

AI351421, AL391650, BC080529, DA900348

Consensus CDS

CCDS273.1

UniProtKB/Swiss-Prot

B4DN95, Q5T2I1, Q969Q1, Q96BD3, Q96KD9, Q9BYV4

UniProtKB/TrEMBL

Q6NR77

Related

ENSP00000363390.3, ENST00000374272.4

Conserved Domains (3) summary

smart00336
Location:120 → 159

BBOX; B-Box-type zinc finger

cd00162
Location:23 → 82

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:188 → 283

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