PYURF
entrez
100996939
canonical
uniprot
Q96I23
canonical
ensembl
ENSG00000145337
resolver
ensp
ENSP00000273968
resolver
enst
ENST00000273968
resolver
genesymbol
PYURF
resolver
genesymbol_syn
NDUFAFQ
resolver
genesymbol_syn
PREY
resolver
hgnc
HGNC:44317
resolver
uniprot
B2R571
resolver
uniprot_entry
PREY_HUMAN
resolver
uniprot_sec
B2R571
resolver
amino_acid_sequence
MLSGARCRLASALRGTRAPPSAVARRCLHASGSRPLADRGKKTEEPPRDFDPALLEFLVCPLSKKPLRYEASTNELINEELGIAYPIIDGIPNMIPQAARMTRQSKKQEEVEQR
uniprot
proteins
disease_involvement
DISEASE: Note=An homozygous frameshift variant in the second exon of PYURF have been found in a patient with profound metabolic acidosis and clinical features including muscle hypotonia, failure to thrive, developmental delay, optic atrophy, persistently elevated lactate levels in the blood and cerebrospinal fluid, and abnormal cerebellar white matter and cerebellar atrophy on magnetic resonance imaging. {ECO:0000269|PubMed:35614220}.
uniprot
proteins
function
FUNCTION: In mitochondria, S-adenosylmethionine-dependent methyltransferase chaperone that supports both coenzyme Q biosynthesis, by stabilizing its components, such as COQ5, and NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) assembly, by stabilizing complex I assembly factors, such as NDUFAF5. {ECO:0000269|PubMed:35614220}.
uniprot
proteins
mass_dalton
12655
uniprot
proteins
mutagenesis
MUTAGEN 58; /note="L->K: Loss of interaction with NDUFAF5."; /evidence="ECO:0000269|PubMed:35614220"; MUTAGEN 60; /note="C->A: Reduces interaction with NDUFAF5."; /evidence="ECO:0000269|PubMed:35614220"; MUTAGEN 91; /note="I->S: Reduces interaction with NDUFAF5."; /evidence="ECO:0000269|PubMed:35614220
uniprot
proteins
protein_family
PREY family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16162815
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
35614220
uniprot
proteins
sequence_length
114
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:35614220}.
uniprot
proteins