HSPD1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0002755Biological processMyD88-dependent toll-like receptor signaling pathway
GO_0006986Biological processresponse to unfolded protein
GO_0006919Biological processactivation of cysteine-type endopeptidase activity involved in apoptotic process
GO_0050870Biological processpositive regulation of T cell activation
GO_0032755Biological processpositive regulation of interleukin-6 production
GO_0098761Biological processcellular response to interleukin-7
GO_0032735Biological processpositive regulation of interleukin-12 production
GO_0051702Biological processbiological process involved in interaction with symbiont
GO_0032733Biological processpositive regulation of interleukin-10 production
GO_0032727Biological processpositive regulation of interferon-alpha production
GO_0002842Biological processpositive regulation of T cell mediated immune response to tumor cell
GO_0051131Biological processchaperone-mediated protein complex assembly
GO_0043032Biological processpositive regulation of macrophage activation
GO_0045041Biological processprotein import into mitochondrial intermembrane space
GO_0006457Biological processprotein folding
GO_0008637Biological processapoptotic mitochondrial changes
GO_0043066Biological processnegative regulation of apoptotic process
GO_0006458Biological process'de novo' protein folding
GO_0009409Biological processresponse to cold
GO_0050821Biological processprotein stabilization
GO_0042113Biological processB cell activation
GO_0044406Biological processadhesion of symbiont to host
GO_0042026Biological processprotein refolding
GO_0051604Biological processprotein maturation
GO_0042100Biological processB cell proliferation
GO_0032729Biological processpositive regulation of type II interferon production
GO_0043065Biological processpositive regulation of apoptotic process
GO_0042110Biological processT cell activation
GO_0034514Biological processmitochondrial unfolded protein response
GO_0048291Biological processisotype switching to IgG isotypes
GO_0005615Cellular componentextracellular space
GO_0097524Cellular componentsperm plasma membrane
GO_0005886Cellular componentplasma membrane
GO_0016020Cellular componentmembrane
GO_0005739Cellular componentmitochondrion
GO_0005769Cellular componentearly endosome
GO_0070062Cellular componentextracellular exosome
GO_0032991Cellular componentprotein-containing complex
GO_0005743Cellular componentmitochondrial inner membrane
GO_0030135Cellular componentcoated vesicle
GO_0009986Cellular componentcell surface
GO_0005829Cellular componentcytosol
GO_0005759Cellular componentmitochondrial matrix
GO_0005737Cellular componentcytoplasm
GO_0046696Cellular componentlipopolysaccharide receptor complex
GO_0005905Cellular componentclathrin-coated pit
GO_0097225Cellular componentsperm midpiece
GO_0030141Cellular componentsecretory granule
GO_0140494Cellular componentmigrasome
GO_0019899Molecular functionenzyme binding
GO_0003688Molecular functionDNA replication origin binding
GO_0003697Molecular functionsingle-stranded DNA binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0034185Molecular functionapolipoprotein binding
GO_0051082Molecular functionunfolded protein binding
GO_0051087Molecular functionprotein-folding chaperone binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0002039Molecular functionp53 binding
GO_0005524Molecular functionATP binding
GO_0003723Molecular functionRNA binding
GO_0016853Molecular functionisomerase activity
GO_0034186Molecular functionapolipoprotein A-I binding
GO_0001530Molecular functionlipopolysaccharide binding
GO_0008035Molecular functionhigh-density lipoprotein particle binding
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity
GO_0003725Molecular functiondouble-stranded RNA binding

IV. Literature review

[source]
Gene nameHSPD1
Protein name60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (Heat shock protein 60)
Heat shock 60kDa protein 1 isoform 4
60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)
Heat shock 60kDa protein 1 isoform 2
Heat shock protein family D (Hsp60) member 1
60 kDa heat shock protein, mitochondrial
SynonymshCG_2012240
HSP60
DescriptionFUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix . The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. .

AccessionsENST00000677403.1
B9VPB4
A0A7I2V599
B9VP19
A0A0S2Z477
ENST00000428204.6 [P10809-1]
ENST00000440114.2
E7ESH4
ENST00000418022
ENST00000418022.2 [P10809-1]
A0A7I2V369
ENST00000430176.6
Q53QD5
ENST00000679291.1
ENST00000676933.1
A0A7I2YQ71
ENST00000428204
ENST00000677454.1
E7EXB4
Q53SE2
B9VP24
A0A7I2V2X6
A0A7I2V5M1
F8WBB1
C9JCQ4
ENST00000677913.1 [P10809-1]
ENST00000452200
A0A0S2Z415
C9J0S9
ENST00000345042.6 [P10809-1]
C9JL25
ENST00000439605
ENST00000426480
ENST00000678545.1
ENST00000439605.2 [P10809-1]
ENST00000677792.1
P10809
A0A7I2YQK6
C9JL19
ENST00000388968.8 [P10809-1]
A0A7I2V5K3
A0A024R3X4
ENST00000678170.1
ENST00000678621.1
ENST00000426480.2 [P10809-1]
ENST00000678761.1 [P10809-1]
ENST00000452200.6 [P10809-1]
B3GQS7