HCSGD entry for HSPD1

1. General information

Official gene symbolHSPD1
Entrez ID3329
Gene full nameheat shock 60kDa protein 1 (chaperonin)
Other gene symbolsCPN60 GROEL HLD4 HSP-60 HSP60 HSP65 HuCHA60 SPG13
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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This gene isn't in Literature mining network.

3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0001530Lipopolysaccharide bindingIDA IEAmolecular_function
GO:0002039P53 bindingIPImolecular_function
GO:0002368B cell cytokine productionIDAbiological_process
GO:0002755MyD88-dependent toll-like receptor signaling pathwayIDAbiological_process
GO:0002842Positive regulation of T cell mediated immune response to tumor cellIDAbiological_process
GO:0003688DNA replication origin bindingISSmolecular_function
GO:0003697Single-stranded DNA bindingISSmolecular_function
GO:0003725Double-stranded RNA bindingIDAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005524ATP bindingIEAmolecular_function
GO:0005615Extracellular spaceIDAcellular_component
GO:0005737CytoplasmIDAcellular_component
GO:0005739MitochondrionIDAcellular_component
GO:0005743Mitochondrial inner membraneIEA ISScellular_component
GO:0005759Mitochondrial matrixTAScellular_component
GO:0005769Early endosomeIDAcellular_component
GO:0005829CytosolIDAcellular_component
GO:0005886Plasma membraneIEAcellular_component
GO:0005905Coated pitIDAcellular_component
GO:0006200ATP catabolic processISSbiological_process
GO:0006458'de novo' protein foldingISSbiological_process
GO:0006919Activation of cysteine-type endopeptidase activity involved in apoptotic processIDAbiological_process
GO:0006950Response to stressIEAbiological_process
GO:0006986Response to unfolded proteinIDAbiological_process
GO:0009986Cell surfaceIDAcellular_component
GO:0016032Viral processIEAbiological_process
GO:0016887ATPase activityISSmolecular_function
GO:0019907Cyclin-dependent protein kinase activating kinase holoenzyme complexIDAcellular_component
GO:0030135Coated vesicleIDAcellular_component
GO:0030141Secretory granuleIEA ISScellular_component
GO:0032727Positive regulation of interferon-alpha productionIDA IEAbiological_process
GO:0032729Positive regulation of interferon-gamma productionIDA IEA ISSbiological_process
GO:0032733Positive regulation of interleukin-10 productionIDAbiological_process
GO:0032735Positive regulation of interleukin-12 productionIDAbiological_process
GO:0032755Positive regulation of interleukin-6 productionIDAbiological_process
GO:0042026Protein refoldingIDAbiological_process
GO:0042100B cell proliferationIDAbiological_process
GO:0042110T cell activationIDA IEAbiological_process
GO:0042113B cell activationIDAbiological_process
GO:0043032Positive regulation of macrophage activationIDAbiological_process
GO:0043065Positive regulation of apoptotic processIMPbiological_process
GO:0043066Negative regulation of apoptotic processIMPbiological_process
GO:0043234Protein complexIDAcellular_component
GO:0044267Cellular protein metabolic processIEAbiological_process
GO:0046696Lipopolysaccharide receptor complexIDAcellular_component
GO:0048291Isotype switching to IgG isotypesIDAbiological_process
GO:0050821Protein stabilizationIMP ISSbiological_process
GO:0050870Positive regulation of T cell activationIDA IEA ISSbiological_process
GO:0051082Unfolded protein bindingIC ISSmolecular_function
GO:0051087Chaperone bindingIPImolecular_function
GO:0051131Chaperone-mediated protein complex assemblyISSbiological_process
GO:0051604Protein maturationISSbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.50668219670.48476132750.99999024731.0000000000

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Up0.0427066067
GSE13712_SHEARUp0.2195586318
GSE13712_STATICUp0.0358895402
GSE19018Down-0.4542412378
GSE19899_A1Up0.0392118465
GSE19899_A2Up0.1024529212
PubMed_21979375_A1Up0.6112883017
PubMed_21979375_A2Down-0.0715066305
GSE35957Down-0.2083167184
GSE36640Down-0.2282189567
GSE54402Up0.1440232250
GSE9593Down-0.1042886073
GSE43922Up0.1763829642
GSE24585Down-0.3440800356
GSE37065Down-0.0268618978
GSE28863_A1Up0.0406182404
GSE28863_A2Up0.3054328772
GSE28863_A3Up0.1425724997
GSE28863_A4Down-0.0213980147
GSE48662Down-0.3957277437

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Not regulated by drugs

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-1MIMAT0000416MIRT003976Luciferase reporter assayFunctional MTI17715156
hsa-miR-1MIMAT0000416MIRT003976Luciferase reporter assayFunctional MTI23226300
hsa-miR-1MIMAT0000416MIRT003976ProteomicsFunctional MTI (Weak)18668040
hsa-miR-214-3pMIMAT0000271MIRT024960Microarray;OtherFunctional MTI (Weak)19859982
hsa-miR-16-5pMIMAT0000069MIRT031799ProteomicsFunctional MTI (Weak)18668040
hsa-miR-744-5pMIMAT0004945MIRT037397CLASHFunctional MTI (Weak)23622248
hsa-miR-324-5pMIMAT0000761MIRT043032CLASHFunctional MTI (Weak)23622248
hsa-miR-331-3pMIMAT0000760MIRT043359CLASHFunctional MTI (Weak)23622248
hsa-miR-125b-5pMIMAT0000423MIRT045988CLASHFunctional MTI (Weak)23622248
hsa-miR-197-3pMIMAT0000227MIRT048142CLASHFunctional MTI (Weak)23622248
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  • mirRecord

MicroRNA name

mirBase ID

Target site number

MiRNA mature ID

Test method inter

MiRNA regulation site

Reporter target site

Pubmed ID

hsa-miR-1MIMAT00004161hsa-miR-117715156
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6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 11 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

26640786RESULTS: Comparison of protein pattern of senescent and young HPMC revealed 29 differentially abundant protein spots, 11 of which were identified to be actin (cytoplasmic 1 and 2), cytokeratin-7, cofilin-2, transgelin-2, Hsp60, Hsc70, proteasome beta-subunits (type-2 and type-3), nucleoside diphosphate kinase A, and cytosolic 5'(3')-deoxyribonucleotidase
256210035%) samples, of which the 53% resulted positive for Hsp60 gene expression
22829758These include COL4A3, CFLAR, GULP1, PDCD1, CASP10, PAX3, BOK, HSPD1, PITX2, and PML
20094032Misfolded proteins deposited at the cell poles lead to selective re-localization of the DnaK/DnaJ/ClpB disaggregating chaperones, but not of GroEL and Lon to these sites
19506556Gene inactivation of components of the cytosolic chaperonin complex that induce increased longevity also causes somatic misexpression of PGL-1
18575266Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10
18575266These proteins include: (i) the major chaperonin Hsp60 (or P1), which was identified in mammalian cells as a protein altered in mutants resistant to microtubule inhibitors and is involved in numerous functions at the cell surface and in other compartments; (ii) the Hspl0 or Cpn10 protein, which is a co-chaperone for Hsp60 in protein folding but also serves as an early pregnancy factor in maternal serum; and (iii) the mHsp70 protein, which plays a central role in mitochondrial protein import but is also important for cellular senescence (mortalin) and antigen presentation processes
18399535Oxidative stress induced a decrease in the mitochondrial Hsp60 levels with a concomitant increase in the cytosolic Hsp60 levels in the early passage HDF, but not in late ones
18399535To show that the resistance to oxidative stress is a specific effect of Hsp60, the levels of Hsp60 were knocked down by siRNA
18399535These findings show that Hsp60 is a key player in the resistance mechanism against oxidative stress and aging
16861898This review reflects recent views on the role of some mitochondrial molecular chaperones as prohibitin, mortalin and HSP60/HSP10 complex and their modifications leading to cell transformation and cancer development
16817317The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins
16804028Mortalin/mtHSP70 and HSP60 are heat-shock proteins that reside in multiple subcellular compartments, mitochondria being the dominant compartment
16804028However, interestingly, whereas an overexpression of mortalin extended in vitro life span of normal fibroblasts (TIG-1), overexpression of HSP60 was neutral
16804028We demonstrate the minute differences in subcellular distribution of mortalin and HSP60, their involvement in tumorigenesis, and functional distinction in pathways involved in senescence
15791579Senescence-associated HSP60 expression in normal human skin fibroblasts
15791579HSP60 has been largely studied in our laboratories and it has been associated with uncontrolled cell proliferation in tumor cells
15791579Since senescence is firmly regulated during cell cycle progression, we wanted to investigate HSP60 protein level during cellular senescence
15791579Our data show that HSP60 increases during the initial stage of senescence and that it is localized in cellular compartments, resembling mitochondria
15791579An increase in HSP60 protein amount is associated with a cell cycle slow-down and it may have a role in cell cycle progression
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