chn-1 E3 ubiquitin-protein ligase CHIP [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: chn-1
Official Full Name: E3 ubiquitin-protein ligase CHIP
Primary source: WormBase:WBGene00000500
Locus tag: CELE_T09B4.10
See related: AllianceGenome:WB:WBGene00000500
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Enables several functions, including Hsp70 protein binding activity; chaperone binding activity; and ubiquitin protein ligase binding activity. Involved in several processes, including oviposition; protein ubiquitination; and sarcomere organization. Located in cytoplasm. Is expressed in several structures, including copulatory spicule; germ line; hermaphrodite distal tip cell; nervous system; and pharynx. Human ortholog(s) of this gene implicated in autosomal recessive spinocerebellar ataxia 16 and cerebellar ataxia type 48. Orthologous to human STUB1 (STIP1 homology and U-box containing protein 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See chn-1 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 7

Sequence:: Chromosome: I; NC_003279.8 (6181314..6183856, complement)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A dimer-monomer switch controls CHIP-dependent substrate ubiquitylation and processing.
Title: A dimer-monomer switch controls CHIP-dependent substrate ubiquitylation and processing.
This suggests a critical role of CHIP/CHN-1-mediated ubiquitylation in the control of muscle wasting and degeneration and identifies a potential new drug target for the treatment of this disease.
Title: A mutation in CHN-1/CHIP suppresses muscle degeneration in Caenorhabditis elegans.
CHIP has a role in development of the animal at the larval stage
Title: Molecular and functional analysis of Caenorhabditis elegans CHIP, a homologue of Mammalian CHIP.
Crystals of the C-terminal 10 kDa lid subdomain from C. elegans chaperone Hsp70 have been obtained that diffract X-rays to 3.5 A. Analysis of X-ray data and initial heavy-atom phasing reveals 24 monomers in the asymmetric unit.
Title: Crystallization and X-ray data analysis of the 10 kDa C-terminal lid subdomain from Caenorhabditis elegans Hsp70.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

T09B4.10 (e-PCR)
- UniSTS:314944

T09B4.2 (e-PCR)
- UniSTS:310753

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables Hsp70 protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed
enables ubiquitin-protein transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin-ubiquitin ligase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to misfolded protein	IBA Inferred from Biological aspect of Ancestor more info
involved_in determination of adult lifespan	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in egg-laying behavior	IGI Inferred from Genetic Interaction more info	PubMed
involved_in locomotion	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of proteasomal ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein autoubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein polyubiquitination	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein polyubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein quality control for misfolded or incompletely synthesized proteins	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein ubiquitination	IDA Inferred from Direct Assay more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in sarcomere organization	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in Z disc	IBA Inferred from Biological aspect of Ancestor 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

General protein information

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Preferred Names: E3 ubiquitin-protein ligase CHIP

NP_491781.2

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

NC_003279.8 Reference assembly

Range

6181314..6183856 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_059380.9 → NP_491781.2 E3 ubiquitin-protein ligase CHIP [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_491781.2

Status: REVIEWED

UniProtKB/TrEMBL

G5ECY6

Conserved Domains (5) summary

smart00028
Location:5 → 36

TPR; Tetratricopeptide repeats

pfam04564
Location:185 → 257

U-box; U-box domain

sd00006
Location:5 → 33

TPR; TPR repeat [structural motif]

pfam00515
Location:38 → 70

TPR_1; Tetratricopeptide repeat

pfam13414
Location:5 → 69

TPR_11; TPR repeat