Search results for HSPA9

Showing 18 results out of 19

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Protein (6 results from a total of 6)

Identifier: R-HSA-5252128
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: HSPA9: P38646
Identifier: R-HSA-5251993
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HSPA9: P38646
Identifier: R-HSA-1252206
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: HSPA9: P38646
Identifier: R-HSA-8878802
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: HSPA9: P38646
Identifier: R-HSA-1267968
Species: Homo sapiens
Compartment: mitochondrial intermembrane space
Primary external reference: UniProt: HSPA9: P38646
Identifier: R-HSA-1267964
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HSPA9: P38646

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-8950249
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: HSPA9: ENSEMBL:ENSG00000113013

Complex (4 results from a total of 4)

Identifier: R-HSA-5252098
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5251963
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5251940
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-5252097
Species: Homo sapiens
Compartment: cytosol

Reaction (6 results from a total of 7)

Identifier: R-HSA-8950389
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
Experiments using human cord blood CD4(+) T cells show 22 protein spots and 20 protein spots, upregulated and downregulated proteins respectively, following Interleukin-12 stimulation (Rosengren et.al, 2005). Among the down-regulated proteins is :HSPA9 protein(HSPA9).
Identifier: R-HSA-1299478
Species: Homo sapiens
Compartment: mitochondrial matrix, mitochondrial inner membrane
As inferred from yeast, the alpha subunit of the mitochondrial processing peptidase (MPP) binds presequences of mitochondrial precursors and the beta subunit cleaves the presequence. After cleavage, proteins destined for the matrix are drawn into the matrix by ATP-dependent interaction with mtHSP70 (HSPA9, homolog of yeast SSC1) of the PAM complex.
Identifier: R-HSA-1299475
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial matrix
As inferred from the yeast TIM23 complex, the human TIMM23 complex transports precursor proteins across the inner membrane and into the matrix. As in yeast, subunits TIMM50, TIMM17, and TIMM23 are probably necessary for initiating translocation while the PAM complex with mtHSP70 (HSPA9, yeast SSC1) provides the motive force that drives the transport. mtHSP70 binding to the precursor pulls the protein into the matrix in a reaction requiring ATP hydrolysis. The yeast reaction appears to use a Brownian ratchet mechanism (Yamano et al. 2008).
In yeast experimentally verified substrates of TIM23 PAM include Hsp60 (HSP60 in human) and Yfh1 (Frataxin, FXN in human). Many other matrix proteins are believed to be substrates of the TIMM23 complex
Identifier: R-HSA-8949145
Species: Homo sapiens
Compartment: mitochondrial outer membrane
VDAC1, VDAC2, and VDAC3 are voltage dependent anion channels that also preferentially transport divalent calcium ions (Ca2+) in their closed state (Rapizzi et al. 2002, De Stefani et al. 2012, Checchetto et al. 2014, and inferred from rat VDAC1). VDAC1, VDAC2, and VDAC3, located in the mitochondrial outer membrane, transport Ca2+ from the cytosol to the mitochondrial intermembrane space. Transfer of cytosolic calcium to the intermembrane space appears to occur preferentially at sites where the endoplasmic reticulum is in close proximity to the mitochondrial outer membrane. This apposition is due to the physical interaction of VDAC channels on the mitochondrial outer membrane with the ITPR1 (IP3R) channel on the endoplasmic reticulum via the chaperone HSPA9 (GRP75) (Szabadkai et al. 2006).
Identifier: R-HSA-8878815
Species: Homo sapiens
Compartment: mitochondrial matrix
Iron-sulfur clusters containing 4Fe-4S are assembled from 2Fe-2S clusters on ISCA1:ISCA2 heterodimers (Banci et al. 2014, Brancaccio et al. 2014, inferred from Saccharomyces cerevisiae in Mühlenhoff et al. 2011). GLRX5:2Fe-2S can donate 2Fe-2S clusters to ISCA1:ISCA2 in vitro (Banci et al. 2014, Brancaccio et al. 2014). It is unclear if other proteins also donate 2Fe-2S clusters. Two conserved C-terminal cysteines of ISCA1:ISCA2 heterodimers extract [2Fe-2S] clusters from GLRX5, forming a ISCA1:ISCA2:GLRX5 intermediate containing two 2Fe-2S clusters (Brancaccio et al. 2017). The physiological electron donor required to convert the two 2Fe-2S clusters bound to the intermediate into a 4Fe-4S cluster is not yet characterized. ISCA1, ISCA2, and IBA57 are required for formation of holoenzymes such as aconitase that contain 4Fe-4S clusters (Sheftel et al. 2012). HSCB (HSC20), the homolog of yeast JAC1, interacts with HSPA9 and appears to facilitate the reaction (Uhrigshardt et al. 2010).
Identifier: R-HSA-1268022
Species: Homo sapiens
Compartment: cytosol, mitochondrial outer membrane, mitochondrial intermembrane space
As inferred from the yeast TOM40:TOM70 complex, the human TOMM40:TOMM70 complex transports precursor proteins from the cytosol, across the outer membrane of the mitochondrion, and into the intermembrane space from where they may be targeted to all locations within the mitochondrion. As inferred from yeast, TOMM40, TOMM22, TOMM5, TOMM6, and TOMM7 probably form the general import pore across the membrane. On the cytosolic side TOMM20 and TOMM22 interact with presequences on mitochondrial precursors while TOMM70 interacts with hydrophobic sequences in mature internal regions of mitochondrial proteins.
In yeast, experimentally verified substrates of the TOM40:TOM70 complex include ATP1 (ATP5A1 in human), ATP2 (ATP5B in human), ATP9 (ATP5G1 in human), TOM40 (TOMM40 in human), SSC1 (mtHsp70, HSPA9 in human), CIT1 (CS in human), ACO1 (ACO2 in human), IDH1 (IDH3G in human), BCS1 (BCS1L in human), CYT1 (CYC1 in human), TIM54 (TIMM54 in human), TIM22 (TIMM22 in human), AAC (ADP/ATP translocase 1, ANT, SLC25A4 in human), HSP60, and CYB2. In humans, TOMM40 has been shown to be a substrate (Humphries et al. 2005). In yeast some proteins such as ACO1, ATP1, CIT1, IDH1, and ATP2 contain both presequences that interact with TOM20 and mature regions that interact with TOM70 (Yamamoto et al. 2009). Most proteins imported into mitochondria are anticipated to be transported through the TOMM40:TOMM70 complex.

Pathway (1 results from a total of 1)

Identifier: R-HSA-8950505
Species: Homo sapiens
Compartment: nucleoplasm
Experiments using human cord blood CD4(+) T cells show 22 protein spots and 20 protein spots, upregulated and downregulated proteins respectively, following Interleukin-12 stimulation (Rosengren et.al, 2005). The identified upregulated proteins are: BOLA2, PSME2, MTAP, CA1, GSTA2, RALA, CNN2, CFL1, TCP1, HNRNPDL, MIF, AIP, SOD1, PPIA and PDCD4.
And the identified downregulated proteins are:
ANXA2, RPLP0, CAPZA1, SOD2, SNRPA1, LMNB1, LCP1, HSPA9, SERPINB2, HNRNPF, TALDO1, PAK2, TCP1, HNRNPA2B1, MSN, PITPNA, ARF1, SOD2, ANXA2, CDC42, RAP1B and GSTO1.
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