Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
UniProtKB P05093 CYP17A1 (CP17A_HUMAN) record
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UniProt describes CYP17A1 as a cytochrome P450 monooxygenase in corticoid and androgen biosynthesis that 17-alpha-hydroxylates C21 steroids and then cleaves the C17-C20 bond to form C19 steroids (DHEA, androstenedione); localizes to the endoplasmic reticulum/microsome membrane; 17,20-lyase is stimulated allosterically by cytochrome b5.
Identification by molecular cloning of an autoantigen associated with Addison's disease as steroid 17 alpha-hydroxylase.
A missense mutation in the human cytochrome b5 gene causes 46,XY disorder of sex development due to true isolated 17,20 lyase deficiency.
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A CYB5A missense mutation causes true isolated 17,20-lyase deficiency, demonstrating that CYP17A1 17,20-lyase activity depends on cytochrome b5 as an allosteric enhancer.
Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001.
A review of the literature on common CYP17A1 mutations in adults with 17-hydroxylase/17,20-lyase deficiency, a case series of such mutations among Koreans and functional characteristics of a novel mutation.
Structures of human steroidogenic cytochrome P450 17A1 with substrates.
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Substrate-bound CYP17A1 structures explain hydroxylase substrate orientation (Asn202) and the basis of 17,20-lyase substrate specificity; CYP17A1 controls mineralocorticoid, glucocorticoid, androgen and estrogen levels.
Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: 18O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN.
Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency.
Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21.
Hydroxylation and lyase reactions of steroids catalyzed by mouse cytochrome P450 17A1 (Cyp17a1).
The genetic and functional basis of isolated 17,20-lyase deficiency.
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Establishes true isolated 17,20-lyase deficiency due to CYP17 mutations that impair interaction with redox partners; fetal testicular androgen (testosterone) production requires CYP17A1 17,20-lyase activity for male sexual differentiation.
Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer.
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Demonstrates that cytochrome b5 augments human P450c17 17,20-lyase activity as an allosteric effector (increasing lyase Vmax) without direct electron transfer, and that POR is necessary/sufficient for microsomal 17,20-lyase activity.
CYP17A1 17-hydroxylates PREG
CYP17A1 cleaves 17aHPREG to DHA
CYP17A1 17-hydroxylates P4 to 17aHPROG
CYP17A1 cleaves 17aHPROG to ANDST
Glucocorticoid biosynthesis
Defective CYP17A1 does not 17-hydroxylate PREG
Defective CYP17A1 does not 17-hydroxylate P4
Defective CYP17A1 does not cleave 17aHPROG