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LOC106464972 60 kDa heat shock protein, mitochondrial-like [ Limulus polyphemus (Atlantic horseshoe crab) ]

Gene ID: 106464972, updated on 21-Dec-2023

Summary

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Gene symbol
LOC106464972
Gene description
60 kDa heat shock protein, mitochondrial-like
See related
EnsemblRapid:LOC106464972
Gene type
protein coding
RefSeq status
MODEL
Organism
Limulus polyphemus
Lineage
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata; Xiphosura; Limulidae; Limulus
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Genomic context

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Location:
chromosome: Un
Exon count:
16
Annotation release Status Assembly Chr Location
101 current Limulus_polyphemus-2.1.2 (GCF_000517525.1) Unplaced Scaffold NW_013667408.1 (4106..38092)

NW_013667408.1Genomic Context describing neighboring genes Neighboring gene 10 kDa heat shock protein, mitochondrial-like Neighboring gene partitioning defective 3 homolog Neighboring gene putative methyltransferase NSUN6

Genomic regions, transcripts, and products

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Genomic Sequence:
NW_013667408 Unplaced Scaffold Reference Limulus_polyphemus-2.1.2 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables protein-folding chaperone binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in apoptotic mitochondrial changes IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in mitochondrial unfolded protein response IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in protein import into mitochondrial intermembrane space IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in protein refolding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in mitochondrial inner membrane IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in mitochondrial matrix IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
60 kDa heat shock protein, mitochondrial-like

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Limulus polyphemus Annotation Release 101 details...Open this link in a new tab

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

Reference Limulus_polyphemus-2.1.2 Primary Assembly

Genomic

  1. NW_013667408.1 Reference Limulus_polyphemus-2.1.2 Primary Assembly

    Range
    4106..38092
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_022392787.1 → XP_022248495.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_022248495.1, XM_022392787.1
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...

  2. XM_022392784.1 → XP_022248492.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_022248492.1, XM_022392784.1
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...

  3. XM_022392785.1 → XP_022248493.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_022248493.1, XM_022392785.1
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...

  4. XM_022392783.1 → XP_022248491.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_022248491.1, XM_022392783.1
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...

  5. XM_013925150.2 → XP_013780604.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_013780604.1, XM_013925150.2
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...

  6. XM_022392786.1 → XP_022248494.1  60 kDa heat shock protein, mitochondrial-like

    Related
    XP_022248494.1, XM_022392786.1
    Conserved Domains (1) summary
    cd03344
    Location:26 → 546
    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 ...
Nucleotide Protein
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