Search results for ALAS1

Showing 13 results out of 13

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Protein (2 results from a total of 2)

Identifier: R-HSA-189438
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: ALAS1: P13196
Identifier: R-HSA-1022086
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: ALAS1: P13196

Reaction (5 results from a total of 5)

Identifier: R-HSA-1592238
Species: Homo sapiens
Compartment: nucleoplasm, mitochondrial matrix
The ALAS1 gene is transcribed to yield mRNA and the mRNA is translated in the cytosol to yield precursor protein. The ALAS1 precursor is imported into the mitochodrial matrix where it catalyzes the synthesis of 5-aminolevulinate from glycine and succinyl-CoA as part of heme biosynthesis.
ERR1 (ERRalpha) probably interacts with coactivator PG-1beta to activate ALAS1 (Shao et al. Shao et al. 2010).
Identifier: R-HSA-1592245
Species: Homo sapiens
Compartment: nucleoplasm
As inferred from mouse, PGC-1beta (PPARGC1B) binds NRF1 and coactivates genes regulated by NRF1.
Identifier: R-HSA-9838289
Species: Homo sapiens
Compartment: mitochondrial matrix
The CLPXP complex comprises two heptameric rings of the barrel-shaped CLPP protease and two hexameric rings of the AAA+ CLPX ATPase (Kang et al. 2002, 2005). Though isolated CLPP subunits have peptidase activity, they only have significant protease activity when complexed with CLPX (Kang et al. 2005). The CLPX subunit unfolds proteins so they can enter the axial pore of the CLPP protease (reviewed in Baker and Sauer 2012, Liu et al. 2014). The CLPXP complex binds and degrades several mitochondrial matrix proteins (Lee et al. 2021, Key et al. 2021), including ALAS1 bound to heme (Kubota et al. 2016, Nomura et al. 2021). CLPXP can also regulate proteins involved in bioenergetics such as components of the electron transport chain suggesting that it can regulate proteins in the inner mitochondrial membrane (Seo et al. 2016, Ishizawa et al. 2019, Mabanglo et al. 2022). CLPXP is thought to be involved in the mitochondrial unfolded protein response (inferred from C. elegans homologs in Haynes et al. 2007 and mouse homologs in Lian et al. 2023). Peptides produced by CLPXP are transported from the mitochondria into the cytosol and activate ATF5 (ATFS-1 in C. elegans). ATF5 subsequently translocates to the nucleus where it enhances the expression of mitochondrial proteases (CLPP and LONP1) and chaperones (HSP60 and GRP75) to restore proteostasis (inferred from C. elegans homologs in Haynes et al. 2010, inferred from mouse homologs in Deepa et al. 2016, Fiorese et al. 2016, inferred from rat homologs in Lian et al. 2023). Recessive mutations in the CLPP subunit of the CLPXP complex cause Perreault Syndrome, which is characterized by congenital sensorineural loss, ataxia, azoospermia (male infertility), ovarian failure, psychomotor retardation, ataxia, autism and epilepsy (Jenkinson et al. 2013, Demain et al. 2017, Faridi et al. 2022).
Identifier: R-HSA-9838035
Species: Homo sapiens
Compartment: mitochondrial matrix
The CLPXP complex is an ATP-dependent protease located in the mitochondrial matrix that binds, unfolds, and degrades a specific set of protein substrates. The CLPXP complex comprises two heptameric rings of CLPP protease subunits and two hexameric rings of CLPX ATPase subunits (Kang et al. 2002, 2005). Upon binding the CLPXP complex, substrate proteins are unfolded by CLPX in an ATP-dependent reaction and translocated to the CLPP protease (reviewed in Baker and Sauer 2012, Liu et al. 2014). The CLPXP complex interacts with more than 200 mitochondrial proteins (Cole et al. 2015, Ishizawa et al. 2019, Mabanglo et al. 2022) and degrades several mitochondrial matrix proteins (Lee et al. 2021, Key et al. 2021), including ERAL1, a putative 12S rRNA chaperone (inferred from mouse homologs in Szczepanowska et al. 2016, Key et al. 2022) and heme-bound ALAS1 (Kubota et al. 2016, Nomura et al. 2021). CLPXP can also regulate proteins involved in bioenergetics such as components of the electron transport chain suggesting that it can regulate proteins in the inner mitochondrial membrane (Seo et al. 2016, Ishizawa et al. 2019, Mabanglo et al. 2022). CLPXP is also thought to be involved in the mitochondrial unfolded protein response (inferred from C. elegans homologs in Haynes et al. 2007 and mouse homologs in Lian et al. 2023).
Identifier: R-HSA-189442
Species: Homo sapiens
Compartment: mitochondrial matrix
The committed step for porphyrin synthesis is the formation of 5-aminolevulinate (ALA) by condensation of glycine (from the general amino acid pool) and succinyl-CoA (from the TCA cycle), in the mitochondrial matrix. The reaction is catalyzed by two different ALA synthases, one expressed ubiquitously (ALAS1) and the other only expressed in erythroid precursors (ALAS2). Both enzymes are expressed as homodimers and require pyridoxal 5-phosphate as a cofactor.
No disease-causing mutations of ALAS1 have been recognised in humans. Mutations in ALAS2 cause X-linked sideroblastic anaemia (XLSA), characterised by a microcytic hypochromic anaemia.

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-2466373
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000023330

Complex (3 results from a total of 3)

Identifier: R-HSA-2466384
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-189446
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-9838300
Species: Homo sapiens
Compartment: mitochondrial matrix

Set (2 results from a total of 2)

Identifier: R-HSA-189429
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-9837981
Species: Homo sapiens
Compartment: mitochondrial matrix
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