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    HSP60-2 heat shock protein 60-2 [ Arabidopsis thaliana (thale cress) ]

    Gene ID: 817883, updated on 18-Sep-2024

    Summary

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    Official Symbol
    HSP60-2
    Official Full Name
    heat shock protein 60-2
    Primary source
    TAIR:AT2G33210
    Locus tag
    AT2G33210
    See related
    Araport:AT2G33210
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Arabidopsis thaliana (ecotype: Columbia)
    Lineage
    Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
    Also known as
    F25I18.5; F25I18_5; heat shock protein 60-2
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    Genomic context

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    See HSP60-2 in Genome Data Viewer
    Location:
    chromosome: 2
    Exon count:
    17
    Sequence:
    Chromosome: 2; NC_003071.7 (14074767..14078772, complement)

    Chromosome 2 - NC_003071.7Genomic Context describing neighboring genes Neighboring gene F-box family protein Neighboring gene Serinc-domain containing serine and sphingolipid biosynthesis protein Neighboring gene GRIM-19 protein Neighboring gene YUCCA 7 Neighboring gene low-molecular-weight cysteine-rich 49

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003071.7

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Mitochondrial Heat Shock Protein 60s Interact with What's This Factor 9 to Regulate RNA Splicing of ccmFC and rpl2. Hsu YW, et al. Plant Cell Physiol, 2019 Jan 1. PMID 30289547
    2. Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix. Ito J, et al. J Proteome Res, 2006 Dec. PMID 17137349
    3. The Extra-Pathway Interactome of the TCA Cycle: Expected and Unexpected Metabolic Interactions. Zhang Y, et al. Plant Physiol, 2018 Jul. PMID 29794018, Free PMC Article
    4. Analysis of the Arabidopsis mitochondrial proteome. Millar AH, et al. Plant Physiol, 2001 Dec. PMID 11743115, Free PMC Article
    5. The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions. Brugière S, et al. Phytochemistry, 2004 Jun. PMID 15276431

    See all (17) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    NM_001202736.1
    NM_179872.3

    Gene Ontology Provided by TAIR

    Function Evidence Code Pubs
    enables ATP binding HDA PubMed 
    enables ATP-dependent protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables copper ion binding HDA PubMed 
    Process Evidence Code Pubs
    involved_in protein refolding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in chloroplast envelope HDA PubMed 
    located_in chloroplast stroma HDA PubMed 
    located_in cytosol HDA PubMed 
    located_in endoplasmic reticulum HDA PubMed 
    located_in mitochondrion HDA PubMed 
    colocalizes_with mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion ISM
    Inferred from Sequence Model
    more info
    		  
    located_in plant-type vacuole HDA PubMed 

    General protein information

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    Preferred Names
    heat shock protein 60-2
    NP_001189665.1
    • heat shock protein 60-2 (HSP60-2); CONTAINS InterPro DOMAIN/s: Chaperonin Cpn60/TCP-1 (InterPro:IPR002423), Chaperonin Cpn60, conserved site (InterPro:IPR018370), Chaperonin Cpn60 (InterPro:IPR001844); BEST Arabidopsis thaliana protein match is: heat shock protein 60 (TAIR:AT3G23990.1).
    NP_850203.1
    • heat shock protein 60-2 (HSP60-2); FUNCTIONS IN: copper ion binding, ATP binding; INVOLVED IN: inflammatory response, response to salt stress; LOCATED IN: mitochondrion, plasma membrane, chloroplast; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Chaperonin Cpn60/TCP-1 (InterPro:IPR002423), Chaperonin Cpn60, conserved site (InterPro:IPR018370), Chaperonin Cpn60 (InterPro:IPR001844); BEST Arabidopsis thaliana protein match is: heat shock protein 60 (TAIR:AT3G23990.1); Has 33915 Blast hits to 33873 proteins in 8692 species: Archae - 707; Bacteria - 21782; Metazoa - 1680; Fungi - 1548; Plants - 807; Viruses - 2; Other Eukaryotes - 7389 (source: NCBI BLink).

    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

    1. NC_003071.7 Reference assembly

      Range
      14074767..14078772 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_179872.3 → NP_850203.1  heat shock protein 60-2 [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_850203.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      O49314, Q8L7B5
      UniProtKB/TrEMBL
      A0A178VPJ6, A0A5S9X3K3
      Conserved Domains (2) summary
      PTZ00114
      Location:21 → 560
      PTZ00114; Heat shock protein 60; Provisional
      cd03344
      Location:35 → 555
      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. NM_001202736.1 → NP_001189665.1  heat shock protein 60-2 [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_001189665.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      A0A178VPJ6, A0A5S9X3K3, F4IVR2
      Conserved Domains (2) summary
      PTZ00114
      Location:21 → 555
      PTZ00114; Heat shock protein 60; Provisional
      cd03344
      Location:35 → 550
      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
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q8L7B5.1

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