hsp-60 Chaperonin homolog Hsp-60, mitochondrial;Heat shock protein 60 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: hsp-60
Official Full Name: Chaperonin homolog Hsp-60, mitochondrial;Heat shock protein 60
Primary source: WormBase:WBGene00002025
Locus tag: CELE_Y22D7AL.5
See related: AllianceGenome:WB:WBGene00002025
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 RNA polymerase II-specific DNA-binding transcription factor binding activity. Involved in several processes, including mitochondrial unfolded protein response; mitochondrion organization; and nematode larval development. Located in mitochondrion. Is expressed in hypodermis; intestine; muscle cell; and neurons. Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autistic disorder; glucose intolerance; hereditary spastic paraplegia (multiple); and hypomyelinating leukodystrophy 4. Orthologous to human HSPD1 (heat shock protein family D (Hsp60) member 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See hsp-60 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 6

Sequence:: Chromosome: III; NC_003281.10 (1619742..1625803)

Chromosome III - NC_003281.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

cytosol-localized HSP-60 physically binds and stabilizes SEK-1/MAP kinase kinase 3, which in turn up-regulates p38 MAP kinase and increases immunity.
Title: Mitochondrial chaperone HSP-60 regulates anti-bacterial immunity via p38 MAP kinase signaling.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II-specific DNA-binding transcription factor binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in apoptotic mitochondrial changes	IBA Inferred from Biological aspect of Ancestor more info
involved_in embryo development ending in birth or egg hatching	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial unfolded protein response	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrial unfolded protein response	IEP Inferred from Expression Pattern more info	PubMed
involved_in mitochondrial unfolded protein response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrion organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nematode larval development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial intermembrane space	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein refolding	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in mitochondrial inner membrane	IBA Inferred from Biological aspect of Ancestor more info
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Chaperonin homolog Hsp-60, mitochondrial;Heat shock protein 60

NP_001122723.1

Confirmed by transcript evidence

NP_001293599.1

Confirmed by transcript evidence

NP_497429.1

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_003281.10 Reference assembly

Range

1619742..1625803

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_065028.8 → NP_497429.1 Chaperonin homolog Hsp-60, mitochondrial [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_497429.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P50140, Q965Q0

Conserved Domains (2) summary

PTZ00114
Location:14 → 546

PTZ00114; Heat shock protein 60; Provisional

cd03344
Location:19 → 540

GroEL; GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found ...
NM_001129251.5 → NP_001122723.1 Heat shock protein 60 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001122723.1

Status: REVIEWED

UniProtKB/TrEMBL

G8JYF5

Conserved Domains (2) summary

PTZ00114
Location:14 → 360

PTZ00114; Heat shock protein 60; Provisional

cl02777
Location:19 → 354

chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...
NM_001306670.3 → NP_001293599.1 Chaperonin homolog Hsp-60, mitochondrial [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001293599.1

Status: REVIEWED

UniProtKB/TrEMBL

V6CLG8

Conserved Domains (1) summary

cl02777
Location:1 → 234

chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...