Cytochrome P450 21A2 (P450c21, steroid 21-hydroxylase; EC 1.14.14.16) is a heme-thiolate cytochrome P450 monooxygenase anchored to the endoplasmic reticulum (microsomal) membrane, expressed predominantly in the adrenal cortex. It catalyses hydroxylation at carbon 21 of C21 steroids using molecular oxygen and electrons supplied by NADPH via cytochrome P450 reductase (POR). It acts at the branch point of adrenal corticosteroid biosynthesis, converting progesterone to 11-deoxycorticosterone (DOC) in the mineralocorticoid branch (feeding aldosterone synthesis) and 17alpha-hydroxyprogesterone to 11-deoxycortisol in the glucocorticoid branch (feeding cortisol synthesis), thereby supplying both the mineralocorticoid and glucocorticoid arms of steroidogenesis. Loss-of-function variants cause 21-hydroxylase deficiency, the commonest cause of congenital adrenal hyperplasia (>90-95% of cases), producing cortisol and aldosterone deficiency with adrenal androgen excess across a spectrum from salt-wasting and simple-virilizing classic forms to non-classic late-onset disease; deleterious alleles arise largely by gene conversion with the adjacent CYP21A1P pseudogene.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004509 steroid 21-monooxygenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) assignment of the core catalytic activity, steroid 21-monooxygenase (EC 1.14.14.16), the defining molecular function of CYP21A2. This is well supported by direct enzymology and structure, and represents the core molecular function of the gene. Reason: This is the correct, appropriately specific core molecular-function term for P450c21. UniProt records it as steroid 21-hydroxylase (EC 1.14.14.16) with the two C21-hydroxylation reactions, and direct assays confirm the activity. Supporting Evidence: PMID:25855791 Cytochrome P450 (P450) 21A2 is the major steroid 21-hydroxylase, and deficiency of this enzyme is involved in ∼95% of cases of human congenital adrenal hyperplasia file:human/CYP21A2/CYP21A2-uniprot.txt Catalyzes the hydroxylation at C-21 of |
| GO:0006704 glucocorticoid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) assignment placing CYP21A2 in glucocorticoid biosynthesis. 21-hydroxylation of 17alpha-hydroxyprogesterone yields 11-deoxycortisol, the immediate precursor of cortisol, so CYP21A2 is a committed step in the glucocorticoid branch. Core biological process. Reason: Directly supported by the enzyme's role converting 17alpha-hydroxyprogesterone to 11-deoxycortisol in the cortisol pathway; a core process for this gene. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt the biosynthetic pathway of mineralocorticoids and glucocorticoids PMID:16984992 the conversion of 17-hydroxyprogesterone to 11-deoxycortisol and progesterone to deoxycorticosterone |
| GO:0020037 heme binding | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) assignment of heme binding. CYP21A2 is a heme-thiolate P450; the crystal structure resolves heme b with Cys429 as the axial iron ligand. A correct, essential cofactor-binding function, secondary to the catalytic MF. Reason: The enzyme binds heme b as an obligate cofactor (structure PMID:25855791; UniProt BINDING residues 92/121/366/427/429). Correct but a supporting molecular function rather than the defining catalytic activity. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Name=heme b file:human/CYP21A2/CYP21A2-uniprot.txt axial binding residue |
| GO:0004497 monooxygenase activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro2GO (IEA) mapping from cytochrome P450 domains to the generic parent term monooxygenase activity. Correct in essence but far less informative than the specific steroid 21-monooxygenase activity already annotated. Reason: True but over-general; the specific activity GO:0004509 (steroid 21-monooxygenase) captures the actual function. Retained as a broad IEA parent, marked as over-annotated relative to the core MF. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt A cytochrome P450 monooxygenase that plays a major role in |
| GO:0004509 steroid 21-monooxygenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment (ARBA/EC 1.14.14.16) of the core catalytic activity, identical to the IBA/experimental term. Correct and appropriately specific. Reason: EC 1.14.14.16 maps exactly to steroid 21-monooxygenase activity, the core molecular function; independently supported experimentally. Supporting Evidence: PMID:22014889 More than 90% of all cases of congenital adrenal hyperplasia (CAH) result from steroid 21-hydroxylase gene (CYP21A2) mutations |
| GO:0005506 iron ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (IEA) mapping of iron ion binding, reflecting the catalytic heme iron coordinated by the axial cysteine thiolate. Correct supporting cofactor function. Reason: The heme b iron is coordinated by Cys429 (axial ligand) at the catalytic centre; iron binding is a valid, if generic, supporting molecular function. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt axial binding residue |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic (ARBA / UniProt SubCell SL-0097) assignment of ER-membrane localization. CYP21A2 is a microsomal P450, a peripheral ER-membrane protein anchored by its N-terminal hydrophobic segment. Correct core localization. Reason: Matches the experimentally determined microsomal/ER-membrane localization; correct cellular component. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral |
| GO:0006705 mineralocorticoid biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: Electronic (ARBA) assignment placing CYP21A2 in mineralocorticoid biosynthesis. 21-hydroxylation of progesterone yields 11-deoxycorticosterone (DOC), the precursor of the mineralocorticoid branch leading to aldosterone. Core biological process. Reason: Directly supported by the progesterone-to-DOC reaction feeding aldosterone synthesis; a core process for this gene (also independently annotated TAS by Reactome). Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt the biosynthetic pathway of mineralocorticoids and glucocorticoids PMID:16984992 progesterone to deoxycorticosterone |
| GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro2GO (IEA) mapping to the broad oxidoreductase/monooxygenase parent. Chemically accurate (the enzyme inserts one oxygen atom and reduces the other to water) but far less specific than steroid 21-monooxygenase activity. Reason: Correct high-level chemistry but over-general relative to the annotated core MF GO:0004509; retained as a broad IEA parent. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt with two electrons provided by NADPH via cytochrome P450 |
| GO:0020037 heme binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (IEA) assignment of heme binding, duplicating the IBA/IDA heme-binding annotation. Correct essential cofactor function. Reason: Consistent with the P450 heme-thiolate architecture and the resolved heme b in the structure; correct supporting molecular function. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Name=heme b |
| GO:0034308 primary alcohol metabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA (IEA) process term derived from the chemical class of the products (21-hydroxy steroids bear a primary alcohol). This is a chemistry-generic over-annotation that does not describe the biological role of CYP21A2. Reason: The product hydroxyl is a primary alcohol, but the biologically meaningful process is corticosteroid biosynthesis, already captured by the specific glucocorticoid/mineralocorticoid/cortisol terms. This substrate-chemistry parent adds no functional insight. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Catalyzes the hydroxylation at C-21 of |
| GO:0042180 ketone metabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA (IEA) process term derived from the ketone-containing steroid substrates/products. A chemistry-generic over-annotation that does not describe the enzyme's biological role. Reason: The steroid substrates carry ketone groups, but the biologically relevant process is corticosteroid biosynthesis; this generic parent adds no functional insight. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Catalyzes the hydroxylation at C-21 of |
| GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based (IEA) assignment of the specific reaction 17alpha-hydroxyprogesterone + O2 -> 11-deoxycortisol (RHEA:50308), the glucocorticoid-branch activity of CYP21A2. Correct and appropriately specific; experimentally confirmed. Reason: This is one of the two physiological reactions catalysed by P450c21 and is directly demonstrated by enzyme assays; a core specific molecular function. Supporting Evidence: PMID:16984992 the conversion of 17-hydroxyprogesterone to 11-deoxycortisol |
| GO:0106309 progesterone 21-hydroxylase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea-based (IEA) assignment of the specific reaction progesterone + O2 -> 11-deoxycorticosterone (RHEA:50304), the mineralocorticoid-branch activity of CYP21A2. Correct and appropriately specific; experimentally confirmed. Reason: This is one of the two physiological reactions catalysed by P450c21 and is directly demonstrated by enzyme assays; a core specific molecular function. Supporting Evidence: PMID:16984992 progesterone to deoxycorticosterone |
| GO:0120254 olefinic compound metabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA (IEA) process term derived from the C=C (olefinic) double bond present in the steroid substrates. A chemistry-generic over-annotation unrelated to the enzyme's biological role. Reason: The steroid substrates contain a carbon-carbon double bond, but CYP21A2's biological role is corticosteroid biosynthesis, not olefin metabolism; this parent adds no functional insight. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Catalyzes the hydroxylation at C-21 of |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:10198222 Effects of missense mutations and deletions on membrane anch... | ACCEPT | Summary: Direct experimental (IDA) localization to the ER/microsomal membrane. Lajic et al. studied membrane binding of P450c21 and its N-terminal anchoring segments, showing the protein integrates into microsomal membranes via its first hydrophobic domain. Core cellular location. Reason: Experimentally supports the microsomal/ER-membrane localization where the enzyme is active; consistent with UniProt subcellular location. Core component. Supporting Evidence: PMID:10198222 P450c21 spans the membrane through its first hydrophobic domain only file:human/CYP21A2/CYP21A2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral |
| GO:0006704 glucocorticoid biosynthetic process | TAS Reactome:R-HSA-194002 | ACCEPT | Summary: Reactome (TAS) placement of CYP21A2 in glucocorticoid biosynthesis, consistent with the IBA annotation and the enzyme's role generating 11-deoxycortisol en route to cortisol. Core biological process. Reason: Authoritative pathway (Reactome) annotation matching the demonstrated function; core process. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt the biosynthetic pathway of mineralocorticoids and glucocorticoids |
| GO:0006705 mineralocorticoid biosynthetic process | TAS Reactome:R-HSA-193993 | ACCEPT | Summary: Reactome (TAS) placement of CYP21A2 in mineralocorticoid biosynthesis, consistent with the ARBA IEA and the progesterone-to-DOC reaction feeding aldosterone. Core biological process. Reason: Authoritative pathway (Reactome) annotation matching the demonstrated function; core process. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt the biosynthetic pathway of mineralocorticoids and glucocorticoids |
| GO:0016125 sterol metabolic process | TAS Reactome:R-HSA-211976 | KEEP AS NON CORE | Summary: Reactome (TAS) assignment to the broad sterol metabolic process ("Endogenous sterols"). Steroids are derived from sterols, but this is a broad parent of the specific corticosteroid-biosynthesis processes; not the core term. Reason: Correct at a general level (corticosteroids derive from the sterol cholesterol), but the specific glucocorticoid/mineralocorticoid/cortisol biosynthesis terms are the informative core processes; retain as broad non-core context. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt adrenal steroidogenesis |
| GO:0004509 steroid 21-monooxygenase activity | TAS Reactome:R-HSA-5601976 | ACCEPT | Summary: Reactome (TAS) assignment of the core catalytic activity, in the context of defective CYP21A2 failing to 21-hydroxylate progesterone. Correct core molecular function. Reason: Same appropriately specific core MF as the IBA/EC/experimental annotations. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Catalyzes the hydroxylation at C-21 of |
| GO:0106309 progesterone 21-hydroxylase activity | TAS Reactome:R-HSA-193964 | ACCEPT | Summary: Reactome (TAS) assignment of the specific progesterone 21-hydroxylase reaction (CYP21A2 21-hydroxylates PROG). Correct and appropriately specific. Reason: Matches the demonstrated progesterone-to-DOC reaction; core specific MF. Supporting Evidence: PMID:16984992 progesterone to deoxycorticosterone |
| GO:0106309 progesterone 21-hydroxylase activity | TAS Reactome:R-HSA-193981 | ACCEPT | Summary: Reactome (TAS) assignment of progesterone 21-hydroxylase activity (duplicate of the reaction annotation via a different Reactome event). Correct and appropriately specific. Reason: Same core specific MF as the other progesterone 21-hydroxylase annotations; experimentally supported. Supporting Evidence: PMID:16984992 progesterone to deoxycorticosterone |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5601976 | ACCEPT | Summary: Reactome (TAS) ER-membrane localization, consistent with the IDA and IEA localizations. Correct core cellular component. Reason: Matches the experimentally determined microsomal/ER-membrane localization. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral |
| GO:0034651 cortisol biosynthetic process | IDA PMID:25855791 Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase... | ACCEPT | Summary: Direct experimental (IDA) assignment to cortisol biosynthesis, based on the structural/enzymatic characterization of P450c21 as the major steroid 21-hydroxylase producing 11-deoxycortisol, the cortisol precursor. Specific, core biological process. Reason: The 17alpha-hydroxyprogesterone-to-11-deoxycortisol reaction is the committed 21-hydroxylation step of the cortisol pathway; this is the most specific and informative BP term and is directly supported. Supporting Evidence: PMID:25855791 Cytochrome P450 (P450) 21A2 is the major steroid 21-hydroxylase PMID:16984992 the conversion of 17-hydroxyprogesterone to 11-deoxycortisol |
| GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity | EXP PMID:16984992 Four novel missense mutations in the CYP21A2 gene detected i... | ACCEPT | Summary: Experimental (EXP) assignment of 17-hydroxyprogesterone 21-hydroxylase activity. Grischuk et al. measured conversion of 17-hydroxyprogesterone to 11-deoxycortisol for wild-type and mutant CYP21A2 in vitro. Core specific molecular function. Reason: Directly measured physiological reaction of P450c21; appropriately specific core MF. Supporting Evidence: PMID:16984992 the conversion of 17-hydroxyprogesterone to 11-deoxycortisol |
| GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity | EXP PMID:22014889 p.H282N and p.Y191H: 2 novel CYP21A2 mutations in Italian co... | ACCEPT | Summary: Experimental (EXP) assignment of 17-hydroxyprogesterone 21-hydroxylase activity. Concolino et al. determined residual enzyme activity and apparent kinetic values of CYP21A2 variants toward 17-hydroxyprogesterone. Core specific molecular function. Reason: Directly measured physiological reaction; appropriately specific core MF. Supporting Evidence: PMID:22014889 Functional in vitro assay for mutagenized CYP21A2 enzymes was performed in transiently transfected mammalian cells to test the residual enzyme activity and the apparent kinetic values |
| GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity | EXP PMID:27721825 Functional and Structural Consequences of Nine CYP21A2 Mutat... | ACCEPT | Summary: Experimental (EXP) assignment of 17-hydroxyprogesterone 21-hydroxylase activity. de Paula Michelatto et al. expressed wild-type and mutant CYP21A2 in COS-1 cells and measured enzyme activities toward 17-hydroxyprogesterone and progesterone. Core specific molecular function. Reason: Directly measured physiological reaction; appropriately specific core MF. Supporting Evidence: PMID:27721825 enzyme activities towards 17-hydroxyprogesterone and progesterone were determined |
| GO:0106309 progesterone 21-hydroxylase activity | EXP PMID:16984992 Four novel missense mutations in the CYP21A2 gene detected i... | ACCEPT | Summary: Experimental (EXP) assignment of progesterone 21-hydroxylase activity. Grischuk et al. measured conversion of progesterone to deoxycorticosterone for wild-type and mutant CYP21A2 in vitro. Core specific molecular function. Reason: Directly measured physiological reaction of P450c21; appropriately specific core MF. Supporting Evidence: PMID:16984992 progesterone to deoxycorticosterone |
| GO:0106309 progesterone 21-hydroxylase activity | EXP PMID:22014889 p.H282N and p.Y191H: 2 novel CYP21A2 mutations in Italian co... | ACCEPT | Summary: Experimental (EXP) assignment of progesterone 21-hydroxylase activity. Concolino et al. assayed residual activity and kinetics of CYP21A2 variants, which include the progesterone 21-hydroxylation reaction. Core specific molecular function. Reason: Directly measured physiological reaction; appropriately specific core MF. Supporting Evidence: PMID:22014889 Functional in vitro assay for mutagenized CYP21A2 enzymes was performed in transiently transfected mammalian cells to test the residual enzyme activity and the apparent kinetic values |
| GO:0106309 progesterone 21-hydroxylase activity | EXP PMID:27721825 Functional and Structural Consequences of Nine CYP21A2 Mutat... | ACCEPT | Summary: Experimental (EXP) assignment of progesterone 21-hydroxylase activity. de Paula Michelatto et al. measured CYP21A2 enzyme activities toward progesterone (and 17-hydroxyprogesterone) for wild-type and mutant proteins in COS-1 cells. Core specific molecular function. Reason: Directly measured physiological reaction; appropriately specific core MF. Supporting Evidence: PMID:27721825 enzyme activities towards 17-hydroxyprogesterone and progesterone were determined |
| GO:0103069 17-hydroxyprogesterone 21-hydroxylase activity | IDA PMID:25855791 Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase... | ACCEPT | Summary: Direct experimental (IDA) assignment of 17-hydroxyprogesterone 21-hydroxylase activity from the structural/kinetic study of the human P450 21A2 enzyme, which characterized 21-hydroxylation with 17alpha-hydroxyprogesterone as a substrate. Core specific molecular function. Reason: Directly demonstrated physiological reaction; appropriately specific core MF. Supporting Evidence: PMID:25855791 Cytochrome P450 (P450) 21A2 is the major steroid 21-hydroxylase |
| GO:0106309 progesterone 21-hydroxylase activity | IDA PMID:25855791 Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase... | ACCEPT | Summary: Direct experimental (IDA) assignment of progesterone 21-hydroxylase activity. Pallan et al. solved the human P450 21A2-progesterone complex and characterized 21-hydroxylation of progesterone (kinetics, rate-limiting C-H cleavage). Core specific molecular function. Reason: Directly demonstrated physiological reaction with the enzyme-progesterone structure and kinetics; appropriately specific core MF. Supporting Evidence: PMID:25855791 progesterone, a substrate in adrenal 21-hydroxylation |
| GO:0020037 heme binding | IDA PMID:25855791 Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase... | ACCEPT | Summary: Direct experimental (IDA) assignment of heme binding. The crystal structure of human P450 21A2 (Pallan et al.) resolves the heme b prosthetic group with the axial cysteine iron ligand, directly demonstrating heme binding. Correct essential cofactor function, secondary to the catalytic MF. Reason: The enzyme binds heme b as an obligate cofactor, resolved in the structure; correct supporting molecular function. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt Name=heme b file:human/CYP21A2/CYP21A2-uniprot.txt axial binding residue |
| GO:0006694 steroid biosynthetic process | IDA PMID:25855791 Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase... | KEEP AS NON CORE | Summary: Direct experimental (IDA) assignment to the broad steroid biosynthetic process. Correct but a general parent of the specific corticosteroid-biosynthesis processes that better describe CYP21A2's role. Reason: Accurate but less informative than the specific glucocorticoid/mineralocorticoid/cortisol biosynthesis terms; retain as a broad non-core process. Supporting Evidence: PMID:25855791 Cytochrome P450 (P450) 21A2 is the major steroid 21-hydroxylase |
| GO:0008202 steroid metabolic process | IMP PMID:16984992 Four novel missense mutations in the CYP21A2 gene detected i... | KEEP AS NON CORE | Summary: Mutant-phenotype (IMP) assignment to the broad steroid metabolic process, based on loss of 21-hydroxylation activity in CYP21A2 disease variants. Correct but a general parent of the specific corticosteroid-biosynthesis processes. Reason: Accurate at a general level; the specific corticosteroid biosynthesis terms are the informative core processes. Retain as broad non-core. Supporting Evidence: PMID:16984992 almost absent or negligible CYP21 activity for the conversion of 17-hydroxyprogesterone to 11-deoxycortisol and progesterone to deoxycorticosterone |
| GO:0008395 steroid hydroxylase activity | IMP PMID:16984992 Four novel missense mutations in the CYP21A2 gene detected i... | MODIFY | Summary: Mutant-phenotype (IMP) assignment of the generic steroid hydroxylase activity, inferred from loss of 21-hydroxylation in disease variants. Correct but less specific than steroid 21-monooxygenase activity (GO:0004509). Reason: The essence is correct, but the specific catalytic term steroid 21-monooxygenase activity (GO:0004509) precisely captures the demonstrated function; replace the generic parent with the specific term. Proposed replacements: steroid 21-monooxygenase activity Supporting Evidence: PMID:16984992 almost absent or negligible CYP21 activity for the conversion of 17-hydroxyprogesterone to 11-deoxycortisol and progesterone to deoxycorticosterone |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-193964 | ACCEPT | Summary: Reactome (TAS) ER-membrane localization (progesterone 21-hydroxylation event), consistent with the IDA and other localizations. Correct core cellular component. Reason: Matches the experimentally determined microsomal/ER-membrane localization. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-193981 | ACCEPT | Summary: Reactome (TAS) ER-membrane localization (17-hydroxyprogesterone oxidation event), consistent with the IDA and other localizations. Correct core cellular component. Reason: Matches the experimentally determined microsomal/ER-membrane localization. Supporting Evidence: file:human/CYP21A2/CYP21A2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral |
| GO:0008395 steroid hydroxylase activity | TAS PMID:1406709 R339H and P453S: CYP21 mutations associated with nonclassic ... | MODIFY | Summary: Traceable-author (TAS) assignment of the generic steroid hydroxylase activity from an early CYP21 mutation study. Correct but less specific than steroid 21-monooxygenase activity (GO:0004509). Reason: The essence is correct, but the specific catalytic term steroid 21-monooxygenase activity (GO:0004509) captures the actual demonstrated function; replace the generic parent with the specific term. Proposed replacements: steroid 21-monooxygenase activity Supporting Evidence: PMID:1406709 R339H and P453S CYP21 mutations associated with nonclassic steroid 21-hydroxylase deficiency |
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