Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome P450 11B2, mitochondrial

Gene

CYP11B2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Preferentially catalyzes the conversion of 11-deoxycorticosterone to aldosterone via corticosterone and 18-hydroxycorticosterone.1 Publication

Catalytic activityi

A steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11-beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O.1 Publication
Corticosterone + 2 reduced adrenodoxin + O2 + 2 H+ = 18-hydroxycorticosterone + 2 oxidized adrenodoxin + H2O.1 Publication

Cofactori

heme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi450Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid metabolism, Steroid metabolism, Steroidogenesis
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS11355-MONOMER
BRENDAi1.14.15.4 2681
ReactomeiR-HSA-193993 Mineralocorticoid biosynthesis
R-HSA-194002 Glucocorticoid biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-5579009 Defective CYP11B2 causes Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)
SIGNORiP19099

Chemistry databases

SwissLipidsiSLP:000001198

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 11B2, mitochondrial
Alternative name(s):
Aldosterone synthase (EC:1.14.15.4, EC:1.14.15.5)
Short name:
ALDOS
Aldosterone-synthesizing enzyme
CYPXIB2
Cytochrome P-450Aldo
Cytochrome P-450C18
Steroid 18-hydroxylase
Gene namesi
Name:CYP11B2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000179142.2
HGNCiHGNC:2592 CYP11B2
MIMi124080 gene
neXtProtiNX_P19099

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder of aldosterone biosynthesis. There are two biochemically different forms of selective aldosterone deficiency be termed corticosterone methyloxidase (CMO) deficiency type 1 and type 2. In CMO-1 deficiency, aldosterone is undetectable in plasma, while its immediate precursor, 18-hydroxycorticosterone, is low or normal.
See also OMIM:203400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant dbSNP:rs72554627EnsemblClinVar.1
Corticosterone methyloxidase 2 deficiency (CMO-2 deficiency)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder of aldosterone biosynthesis. In CMO-2 deficiency, aldosterone can be low or normal, but at the expense of increased secretion of 18-hydroxycorticosterone. Consequently, patients have a greatly increased ratio of 18-hydroxycorticosterone to aldosterone and a low ratio of corticosterone to 18-hydroxycorticosterone in serum.
See also OMIM:610600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant dbSNP:rs28931609EnsemblClinVar.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant dbSNP:rs121912978EnsemblClinVar.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs104894072EnsemblClinVar.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone. 5 PublicationsCorresponds to variant dbSNP:rs61757294EnsemblClinVar.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs72554626EnsemblClinVar.1
Hyperaldosteronism, familial, 1 (HALD1)
The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2.
Disease descriptionA disorder characterized by hypertension, variable hyperaldosteronism, and abnormal adrenal steroid production, including 18-oxocortisol and 18-hydroxycortisol. There is significant phenotypic heterogeneity, and some individuals never develop hypertension.
See also OMIM:103900

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1585
MalaCardsiCYP11B2
MIMi103900 phenotype
203400 phenotype
610600 phenotype
OpenTargetsiENSG00000179142
Orphaneti403 Familial hyperaldosteronism type I
99763 Familial hyperreninemic hypoaldosteronism type 1
PharmGKBiPA134

Chemistry databases

ChEMBLiCHEMBL2722
DrugBankiDB04630 Aldosterone
DB00700 Eplerenone
DB00292 Etomidate
DB00741 Hydrocortisone
DB01233 Metoclopramide
DB01011 Metyrapone
DB01388 Mibefradil
DB00421 Spironolactone
GuidetoPHARMACOLOGYi1360

Polymorphism and mutation databases

BioMutaiCYP11B2
DMDMi3041666

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionAdd BLAST24
ChainiPRO_000000359725 – 503Cytochrome P450 11B2, mitochondrialAdd BLAST479

Proteomic databases

PaxDbiP19099
PeptideAtlasiP19099
PRIDEiP19099
ProteomicsDBi53632

PTM databases

iPTMnetiP19099
PhosphoSitePlusiP19099

Expressioni

Gene expression databases

BgeeiENSG00000179142 Expressed in 42 organ(s), highest expression level in left adrenal gland
CleanExiHS_CYP11B2
GenevisibleiP19099 HS

Organism-specific databases

HPAiHPA049171
HPA056348
HPA057752

Interactioni

Protein-protein interaction databases

BioGridi107957, 1 interactor
STRINGi9606.ENSP00000325822

Chemistry databases

BindingDBiP19099

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP19099
SMRiP19099
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159 Eukaryota
COG2124 LUCA
GeneTreeiENSGT00900000140779
HOGENOMiHOG000013161
HOVERGENiHBG051098
InParanoidiP19099
KOiK07433
OMAiPFEAMPQ
OrthoDBiEOG091G0B8F
PhylomeDBiP19099
TreeFamiTF105094

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002399 Cyt_P450_mitochondrial
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 1 hit
PRINTSiPR00408 MITP450
PR00385 P450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19099-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALRAKAEVC VAAPWLSLQR ARALGTRAAR APRTVLPFEA MPQHPGNRWL
60 70 80 90 100
RLLQIWREQG YEHLHLEMHQ TFQELGPIFR YNLGGPRMVC VMLPEDVEKL
110 120 130 140 150
QQVDSLHPCR MILEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPDVLS
160 170 180 190 200
PKAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS
210 220 230 240 250
NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWISP
260 270 280 290 300
KVWKEHFEAW DCIFQYGDNC IQKIYQELAF NRPQHYTGIV AELLLKAELS
310 320 330 340 350
LEAIKANSME LTAGSVDTTA FPLLMTLFEL ARNPDVQQIL RQESLAAAAS
360 370 380 390 400
ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG
410 420 430 440 450
TLVQVFLYSL GRNAALFPRP ERYNPQRWLD IRGSGRNFHH VPFGFGMRQC
460 470 480 490 500
LGRRLAEAEM LLLLHHVLKH FLVETLTQED IKMVYSFILR PGTSPLLTFR

AIN
Length:503
Mass (Da):57,560
Last modified:July 15, 1998 - v3
Checksum:i42BA671704CEE35D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17S → C in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti55I → M in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti119Y → I in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti249S → R in CAA38539 (PubMed:2256920).Curated1
Sequence conflicti342Q → K in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti438F → L in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti470H → R in AAA35741 (PubMed:2592361).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01415129A → T1 PublicationCorresponds to variant dbSNP:rs6438Ensembl.1
Natural variantiVAR_01415230R → Q1 PublicationCorresponds to variant dbSNP:rs6441EnsemblClinVar.1
Natural variantiVAR_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_001266173K → R3 PublicationsCorresponds to variant dbSNP:rs4539EnsemblClinVar.1
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant dbSNP:rs28931609EnsemblClinVar.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant dbSNP:rs121912978EnsemblClinVar.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs104894072EnsemblClinVar.1
Natural variantiVAR_014643222N → T. Corresponds to variant dbSNP:rs5308Ensembl.1
Natural variantiVAR_014153248I → T2 PublicationsCorresponds to variant dbSNP:rs4547Ensembl.1
Natural variantiVAR_014154281N → S2 PublicationsCorresponds to variant dbSNP:rs4537EnsemblClinVar.1
Natural variantiVAR_014155339I → T2 PublicationsCorresponds to variant dbSNP:rs4544EnsemblClinVar.1
Natural variantiVAR_014644383E → V. Corresponds to variant dbSNP:rs5312Ensembl.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone. 5 PublicationsCorresponds to variant dbSNP:rs61757294EnsemblClinVar.1
Natural variantiVAR_014645403V → E. Corresponds to variant dbSNP:rs5315Ensembl.1
Natural variantiVAR_014156435G → S2 PublicationsCorresponds to variant dbSNP:rs4545EnsemblClinVar.1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant dbSNP:rs72554627EnsemblClinVar.1
Natural variantiVAR_014646487F → V. Corresponds to variant dbSNP:rs5317Ensembl.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs72554626EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32881, M32864, M32880 Genomic DNA Translation: AAA35741.1
X54741 mRNA Translation: CAA38539.1
D13752 Genomic DNA Translation: BAA02899.1
EU326306 Genomic DNA Translation: ACA05912.1
CH471162 Genomic DNA Translation: EAW82292.1
CCDSiCCDS6393.1
PIRiB34181
RefSeqiNP_000489.3, NM_000498.3
UniGeneiHs.632054

Genome annotation databases

EnsembliENST00000323110; ENSP00000325822; ENSG00000179142
GeneIDi1585
KEGGihsa:1585
UCSCiuc003yxk.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

CYP11B2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32881, M32864, M32880 Genomic DNA Translation: AAA35741.1
X54741 mRNA Translation: CAA38539.1
D13752 Genomic DNA Translation: BAA02899.1
EU326306 Genomic DNA Translation: ACA05912.1
CH471162 Genomic DNA Translation: EAW82292.1
CCDSiCCDS6393.1
PIRiB34181
RefSeqiNP_000489.3, NM_000498.3
UniGeneiHs.632054

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DVQX-ray2.49A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4FDHX-ray2.71A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4ZGXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L28-503[»]
ProteinModelPortaliP19099
SMRiP19099
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107957, 1 interactor
STRINGi9606.ENSP00000325822

Chemistry databases

BindingDBiP19099
ChEMBLiCHEMBL2722
DrugBankiDB04630 Aldosterone
DB00700 Eplerenone
DB00292 Etomidate
DB00741 Hydrocortisone
DB01233 Metoclopramide
DB01011 Metyrapone
DB01388 Mibefradil
DB00421 Spironolactone
GuidetoPHARMACOLOGYi1360
SwissLipidsiSLP:000001198

PTM databases

iPTMnetiP19099
PhosphoSitePlusiP19099

Polymorphism and mutation databases

BioMutaiCYP11B2
DMDMi3041666

Proteomic databases

PaxDbiP19099
PeptideAtlasiP19099
PRIDEiP19099
ProteomicsDBi53632

Protocols and materials databases

DNASUi1585
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323110; ENSP00000325822; ENSG00000179142
GeneIDi1585
KEGGihsa:1585
UCSCiuc003yxk.1 human

Organism-specific databases

CTDi1585
DisGeNETi1585
EuPathDBiHostDB:ENSG00000179142.2
GeneCardsiCYP11B2
H-InvDBiHIX0034383
HGNCiHGNC:2592 CYP11B2
HPAiHPA049171
HPA056348
HPA057752
MalaCardsiCYP11B2
MIMi103900 phenotype
124080 gene
203400 phenotype
610600 phenotype
neXtProtiNX_P19099
OpenTargetsiENSG00000179142
Orphaneti403 Familial hyperaldosteronism type I
99763 Familial hyperreninemic hypoaldosteronism type 1
PharmGKBiPA134
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0159 Eukaryota
COG2124 LUCA
GeneTreeiENSGT00900000140779
HOGENOMiHOG000013161
HOVERGENiHBG051098
InParanoidiP19099
KOiK07433
OMAiPFEAMPQ
OrthoDBiEOG091G0B8F
PhylomeDBiP19099
TreeFamiTF105094

Enzyme and pathway databases

BioCyciMetaCyc:HS11355-MONOMER
BRENDAi1.14.15.4 2681
ReactomeiR-HSA-193993 Mineralocorticoid biosynthesis
R-HSA-194002 Glucocorticoid biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-5579009 Defective CYP11B2 causes Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)
SIGNORiP19099

Miscellaneous databases

GeneWikiiAldosterone_synthase
GenomeRNAii1585
PROiPR:P19099
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000179142 Expressed in 42 organ(s), highest expression level in left adrenal gland
CleanExiHS_CYP11B2
GenevisibleiP19099 HS

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002399 Cyt_P450_mitochondrial
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 1 hit
PRINTSiPR00408 MITP450
PR00385 P450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiC11B2_HUMAN
AccessioniPrimary (citable) accession number: P19099
Secondary accession number(s): B0ZBE4, Q16726
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 15, 1998
Last modified: September 12, 2018
This is version 193 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again