P23434Q9H1E9GCSH_HUMANGlycine cleavage system H protein, mitochondrialLipoic acid-containing proteinGCSHHomo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoThe glycine cleavage system: structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemias.NUCLEOTIDE SEQUENCE [MRNA]FUNCTIONVARIANT LEU-21LIPOYLATION AT LYS-107COFACTORThe primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning.NUCLEOTIDE SEQUENCE [MRNA]VARIANT LEU-21NUCLEOTIDE SEQUENCE [GENOMIC DNA]VARIANTS LEU-21 AND SER-73The sequence and analysis of duplication-rich human chromosome 16.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]VARIANT LEU-21Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminome analysis of the human mitochondrial proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Biallelic start loss variant, c.1A > G in GCSH is associated with variant nonketotic hyperglycinemia.INVOLVEMENT IN MMDS7Pathogenic variants in GCSH encoding the moonlighting H-protein cause combined nonketotic hyperglycinemia and lipoate deficiency.VARIANTS MMDS7 ARG-57; 76-GLN--GLU-173 DEL; LEU-115 AND PRO-148CHARACTERIZATION OF VARIANTS MMDS7 LEU-115 AND PRO-148INVOLVEMENT IN MMDS7FUNCTIONSUBCELLULAR LOCATIONThe glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST). Has a pivotal role in the lipoylation of enzymes involved in cellular energetics such as the mitochondrial dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (DLAT), and the mitochondrial dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (DLST) (PubMed:36190515).(R)-lipoateBinds 1 lipoyl cofactor covalently.Interacts with GLDC (By similarity). The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH).P23434Q9UHD4false3P23434P43364false3P23434P43360false3P23434Q9P086false3P23434Q9NYP9false3P23434Q13287false4P23434Q6NTF9-3false3MitochondrionMultiple mitochondrial dysfunctions syndrome 7
MMDS7
An autosomal recessive disorder biochemically characterized by glycine accumulation in body fluids, including the cerebrospinal fluid, with an elevated cerebrospinal fluid/plasma glycine ratio. The broad clinical spectrum ranges from neonatal fatal glycine encephalopathy to an attenuated phenotype of developmental delay, limited verbal communication, behavioral problems, seizures and variable movement problems. Death in infancy or early childhood may occur.The disease is caused by variants affecting the gene represented in this entry.Belongs to the GcvH family.Disease variantLipoylMitochondrionNeurodegenerationReference proteomeTransit peptideSLHRNSPLTPMALRVVRSVRALLCTLRAVPSPAAPCPPRPWQLGVGAVRTLRTGPALLSVRKFTEKHEWVTTENGIGTVGISNFAQEALGDVVYCSLPEVGTKLNKQDEFGALESVKAASELYSPLSGEVTEINEALAENPGLVNKSCYEDGWLIKMTLSNPSELDELMSEEAYEKYIKSIEE
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