Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes.
Defining the membrane proteome of NK cells.
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
CYB5R3:FAD reduces CYB5A:ferriheme to CYB5A:heme
CYB5A:heme reduces Asc.- to AscH-
SGTA binds Tail-anchored protein
Isolated 17,20-lyase deficiency due to the cytochrome b5 mutation W27X.
The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene.
Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5.
Structure of cytochrome b5 and its topology in the microsomal membrane.
A missense mutation in the human cytochrome b5 gene causes 46,XY disorder of sex development due to true isolated 17,20 lyase deficiency.
Evidence that cytochrome b5 acts as a redox donor in CYP17A1 mediated androgen synthesis.
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Redox-inactive manganese-b5 associated with CYP17A1 but did not enhance DHEA production, whereas iron-b5 increased product formation and coupling. Main Methods delegate b5 expression details, so no independently verified human-b5 product is assigned.
"Mn-b5 binds to CYP17A1, but is incapable of enhancing the lyase activity"
Cytochrome b(5) enhances androgen synthesis by rapidly reducing the CYP17A1 oxy-complex in the lyase step.
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Stopped-flow measurements in nanodiscs identified electron donation from full-anchor rabbit cytochrome b5 to human CYP17A1. Rat reductase was the other redox partner; this is mechanistic homolog evidence for human CYB5A, not a direct human-b5 assay.
"direct electron transfer from ferrous b5 to the oxy-complex of CYP17A1"
Substrate-Specific Allosteric Effects on the Enhancement of CYP17A1 Lyase Efficiency by Cytochrome b(5).
NADH-cytochrome b5 reductase and cytochrome b5 isoforms as models for the study of post-translational targeting to the endoplasmic reticulum.
A novel point mutation in a 3' splice site of the NADH-cytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia.
CYB5A source-specific evidence and product scope