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Protein

Cytochrome P450 11B1, mitochondrial

Gene

CYP11B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.

Catalytic activityi

A steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11-beta- hydroxysteroid + 2 oxidized adrenodoxin + H2O.

Cofactori

hemeBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi450Iron (heme axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

  • aldosterone biosynthetic process Source: UniProtKB
  • C21-steroid hormone biosynthetic process Source: BHF-UCL
  • cellular response to hormone stimulus Source: UniProtKB
  • cellular response to peptide hormone stimulus Source: GO_Central
  • cellular response to potassium ion Source: UniProtKB
  • cholesterol metabolic process Source: GO_Central
  • cortisol biosynthetic process Source: UniProtKB
  • glucocorticoid biosynthetic process Source: Reactome
  • glucose homeostasis Source: BHF-UCL
  • immune response Source: BHF-UCL
  • regulation of blood pressure Source: BHF-UCL
  • secondary metabolite biosynthetic process Source: GO_Central
  • sterol metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism, Steroidogenesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08547-MONOMER.
ZFISH:HS08547-MONOMER.
BRENDAi1.14.15.4. 2681.
ReactomeiR-HSA-194002. Glucocorticoid biosynthesis.
R-HSA-211976. Endogenous sterols.

Chemistry databases

SwissLipidsiSLP:000001197.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 11B1, mitochondrial
Alternative name(s):
CYPXIB1
Cytochrome P-450c11
Short name:
Cytochrome P450C11
Steroid 11-beta-hydroxylase (EC:1.14.15.4)
Gene namesi
Name:CYP11B1
Synonyms:S11BH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2591. CYP11B1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: BHF-UCL
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Adrenal hyperplasia 4 (AH4)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH)and 'cryptic' (asymptomatic).
See also OMIM:202010
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07449342P → L in AH4; classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs193922538dbSNPEnsembl.1
Natural variantiVAR_00126042P → S in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 3 PublicationsCorresponds to variant rs104894069dbSNPEnsembl.1
Natural variantiVAR_01414643R → Q in AH4; decreases steroid 11-beta-hydroxylase activity. 4 PublicationsCorresponds to variant rs4534dbSNPEnsembl.1
Natural variantiVAR_07449479F → I in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_07449583L → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_07449688M → I in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs193922539dbSNPEnsembl.1
Natural variantiVAR_06566694P → L in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894070dbSNPEnsembl.1
Natural variantiVAR_074497116W → C in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772003869dbSNPEnsembl.1
Natural variantiVAR_074498116W → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772733691dbSNPEnsembl.1
Natural variantiVAR_074499125H → R in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs757389720dbSNPEnsembl.1
Natural variantiVAR_074500129V → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001261133N → H in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894067dbSNPEnsembl.1
Natural variantiVAR_074501135P → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074502139F → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_075553141R → Q in AH4; unknown pathological significance. 1 PublicationCorresponds to variant rs267601810dbSNPEnsembl.1
Natural variantiVAR_074503143R → W in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs140336749dbSNPEnsembl.1
Natural variantiVAR_074504150S → L in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs142484434dbSNPEnsembl.1
Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074506159P → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs370266763dbSNPEnsembl.1
Natural variantiVAR_074507161Missing in AH4. 1 Publication1
Natural variantiVAR_074508165A → D in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074509196T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074510254 – 259Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication6
Natural variantiVAR_074511267G → D in AH4. 1 Publication1
Natural variantiVAR_074512299L → P in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs387907573dbSNPEnsembl.1
Natural variantiVAR_074513306A → V in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs387907572dbSNPEnsembl.1
Natural variantiVAR_074514310E → K in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs387907574dbSNPEnsembl.1
Natural variantiVAR_074515314G → R in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001262318T → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894061dbSNPEnsembl.1
Natural variantiVAR_074516318T → P in AH4. 1 Publication1
Natural variantiVAR_065667318T → R in AH4. 4 Publications1
Natural variantiVAR_001263319T → M in AH4; non-classic; decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894068dbSNPEnsembl.1
Natural variantiVAR_074517321F → V in AH4. 1 Publication1
Natural variantiVAR_074518331A → V in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_075554332R → G in AH4; high reduction of steroid 11-beta-monooxygenase activity. 1 Publication1
Natural variantiVAR_074519332R → Q in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs149881706dbSNPEnsembl.1
Natural variantiVAR_074520341R → S in AH4. 1 PublicationCorresponds to variant rs372115638dbSNPEnsembl.1
Natural variantiVAR_074521366R → C in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs773245244dbSNPEnsembl.1
Natural variantiVAR_074522368A → D in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894071dbSNPEnsembl.1
Natural variantiVAR_074523371E → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs368944209dbSNPEnsembl.1
Natural variantiVAR_001264374R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894062dbSNPEnsembl.1
Natural variantiVAR_065196379G → V in AH4. 1 Publication1
Natural variantiVAR_074524384R → G in AH4. 1 Publication1
Natural variantiVAR_074525384R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs764598023dbSNPEnsembl.1
Natural variantiVAR_074526401T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs201300785dbSNPEnsembl.1
Natural variantiVAR_074527427R → H in AH4. 1 PublicationCorresponds to variant rs754432887dbSNPEnsembl.1
Natural variantiVAR_074528438Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074529441V → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772169059dbSNPEnsembl.1
Natural variantiVAR_074530444G → D in AH4. 1 PublicationCorresponds to variant rs779103938dbSNPEnsembl.1
Natural variantiVAR_074531448R → C in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001265448R → H in AH4; abolishes steroid 11-beta-hydroxylase activity. 5 PublicationsCorresponds to variant rs28934586dbSNPEnsembl.1
Natural variantiVAR_074532453R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_065197454R → C in AH4. 1 Publication1
Natural variantiVAR_074533463L → LL in AH4; classic; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074534489L → S in AH4. 1 PublicationCorresponds to variant rs750428278dbSNPEnsembl.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

Congenital adrenal hyperplasia, Disease mutation

Organism-specific databases

DisGeNETi1584.
MalaCardsiCYP11B1.
MIMi103900. phenotype.
202010. phenotype.
OpenTargetsiENSG00000160882.
Orphaneti90795. Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency.
403. Familial hyperaldosteronism type I.
PharmGKBiPA133.

Chemistry databases

ChEMBLiCHEMBL1908.
DrugBankiDB00501. Cimetidine.
DB00257. Clotrimazole.
DB00292. Etomidate.
DB00196. Fluconazole.
DB00741. Hydrocortisone.
DB01026. Ketoconazole.
DB01233. Metoclopramide.
DB01011. Metyrapone.
DB01110. Miconazole.
DB00648. Mitotane.
DB00252. Phenytoin.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi1359.

Polymorphism and mutation databases

BioMutaiCYP11B1.
DMDMi215274267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionAdd BLAST24
ChainiPRO_000000359625 – 503Cytochrome P450 11B1, mitochondrialAdd BLAST479

Proteomic databases

PaxDbiP15538.
PeptideAtlasiP15538.
PRIDEiP15538.

PTM databases

iPTMnetiP15538.
PhosphoSitePlusiP15538.

Expressioni

Gene expression databases

BgeeiENSG00000160882.
CleanExiHS_CYP11B1.
ExpressionAtlasiP15538. baseline and differential.
GenevisibleiP15538. HS.

Organism-specific databases

HPAiHPA049171.
HPA056348.
HPA057752.

Interactioni

Protein-protein interaction databases

BioGridi107956. 1 interactor.
STRINGi9606.ENSP00000292427.

Chemistry databases

BindingDBiP15538.

Structurei

3D structure databases

ProteinModelPortaliP15538.
SMRiP15538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP15538.
KOiK00497.
PhylomeDBiP15538.
TreeFamiTF105094.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00408. MITP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15538-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALRAKAEVC MAVPWLSLQR AQALGTRAAR VPRTVLPFEA MPRRPGNRWL
60 70 80 90 100
RLLQIWREQG YEDLHLEVHQ TFQELGPIFR YDLGGAGMVC VMLPEDVEKL
110 120 130 140 150
QQVDSLHPHR MSLEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPEVLS
160 170 180 190 200
PNAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS
210 220 230 240 250
NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWTSP
260 270 280 290 300
KVWKEHFEAW DCIFQYGDNC IQKIYQELAF SRPQQYTSIV AELLLNAELS
310 320 330 340 350
PDAIKANSME LTAGSVDTTV FPLLMTLFEL ARNPNVQQAL RQESLAAAAS
360 370 380 390 400
ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVASSDL VLQNYHIPAG
410 420 430 440 450
TLVRVFLYSL GRNPALFPRP ERYNPQRWLD IRGSGRNFYH VPFGFGMRQC
460 470 480 490 500
LGRRLAEAEM LLLLHHVLKH LQVETLTQED IKMVYSFILR PSMFPLLTFR

AIN
Length:503
Mass (Da):57,573
Last modified:November 25, 2008 - v5
Checksum:i0B36D82513960EE9
GO
Isoform 2 (identifier: P15538-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-466: Missing.

Note: No experimental confirmation available.
Show »
Length:437
Mass (Da):49,750
Checksum:iF85180BFB83C9B5A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01414510C → Y.1 PublicationCorresponds to variant rs6405dbSNPEnsembl.1
Natural variantiVAR_07449342P → L in AH4; classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs193922538dbSNPEnsembl.1
Natural variantiVAR_00126042P → S in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 3 PublicationsCorresponds to variant rs104894069dbSNPEnsembl.1
Natural variantiVAR_01414643R → Q in AH4; decreases steroid 11-beta-hydroxylase activity. 4 PublicationsCorresponds to variant rs4534dbSNPEnsembl.1
Natural variantiVAR_01463863D → H.Corresponds to variant rs5282dbSNPEnsembl.1
Natural variantiVAR_07449479F → I in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_07449583L → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_07449688M → I in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs193922539dbSNPEnsembl.1
Natural variantiVAR_06566694P → L in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894070dbSNPEnsembl.1
Natural variantiVAR_074497116W → C in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772003869dbSNPEnsembl.1
Natural variantiVAR_074498116W → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772733691dbSNPEnsembl.1
Natural variantiVAR_074499125H → R in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs757389720dbSNPEnsembl.1
Natural variantiVAR_074500129V → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001261133N → H in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894067dbSNPEnsembl.1
Natural variantiVAR_074501135P → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074502139F → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_075553141R → Q in AH4; unknown pathological significance. 1 PublicationCorresponds to variant rs267601810dbSNPEnsembl.1
Natural variantiVAR_074503143R → W in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs140336749dbSNPEnsembl.1
Natural variantiVAR_074504150S → L in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs142484434dbSNPEnsembl.1
Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074506159P → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs370266763dbSNPEnsembl.1
Natural variantiVAR_014147160M → I.1 PublicationCorresponds to variant rs5287dbSNPEnsembl.1
Natural variantiVAR_074507161Missing in AH4. 1 Publication1
Natural variantiVAR_074508165A → D in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_014639173K → R.Corresponds to variant rs4539dbSNPEnsembl.1
Natural variantiVAR_074509196T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_048462248T → I.Corresponds to variant rs34620645dbSNPEnsembl.1
Natural variantiVAR_074510254 – 259Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication6
Natural variantiVAR_014640257F → L.Corresponds to variant rs5288dbSNPEnsembl.1
Natural variantiVAR_074511267G → D in AH4. 1 Publication1
Natural variantiVAR_014641281S → N.Corresponds to variant rs5291dbSNPEnsembl.1
Natural variantiVAR_014148293L → V.1 PublicationCorresponds to variant rs5292dbSNPEnsembl.1
Natural variantiVAR_074512299L → P in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs387907573dbSNPEnsembl.1
Natural variantiVAR_074513306A → V in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs387907572dbSNPEnsembl.1
Natural variantiVAR_074514310E → K in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs387907574dbSNPEnsembl.1
Natural variantiVAR_074515314G → R in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001262318T → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894061dbSNPEnsembl.1
Natural variantiVAR_074516318T → P in AH4. 1 Publication1
Natural variantiVAR_065667318T → R in AH4. 4 Publications1
Natural variantiVAR_001263319T → M in AH4; non-classic; decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant rs104894068dbSNPEnsembl.1
Natural variantiVAR_074517321F → V in AH4. 1 Publication1
Natural variantiVAR_074518331A → V in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_075554332R → G in AH4; high reduction of steroid 11-beta-monooxygenase activity. 1 Publication1
Natural variantiVAR_074519332R → Q in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs149881706dbSNPEnsembl.1
Natural variantiVAR_074520341R → S in AH4. 1 PublicationCorresponds to variant rs372115638dbSNPEnsembl.1
Natural variantiVAR_014149348A → T.1 PublicationCorresponds to variant rs6407dbSNPEnsembl.1
Natural variantiVAR_074521366R → C in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs773245244dbSNPEnsembl.1
Natural variantiVAR_074522368A → D in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894071dbSNPEnsembl.1
Natural variantiVAR_074523371E → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs368944209dbSNPEnsembl.1
Natural variantiVAR_001264374R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs104894062dbSNPEnsembl.1
Natural variantiVAR_065196379G → V in AH4. 1 Publication1
Natural variantiVAR_074524384R → G in AH4. 1 Publication1
Natural variantiVAR_074525384R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs764598023dbSNPEnsembl.1
Natural variantiVAR_014150386A → V.4 PublicationsCorresponds to variant rs4541dbSNPEnsembl.1
Natural variantiVAR_074526401T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs201300785dbSNPEnsembl.1
Natural variantiVAR_048463404R → H.Corresponds to variant rs4998896dbSNPEnsembl.1
Natural variantiVAR_074527427R → H in AH4. 1 PublicationCorresponds to variant rs754432887dbSNPEnsembl.1
Natural variantiVAR_074528438Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_014642439Y → H.Corresponds to variant rs5294dbSNPEnsembl.1
Natural variantiVAR_074529441V → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant rs772169059dbSNPEnsembl.1
Natural variantiVAR_074530444G → D in AH4. 1 PublicationCorresponds to variant rs779103938dbSNPEnsembl.1
Natural variantiVAR_074531448R → C in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_001265448R → H in AH4; abolishes steroid 11-beta-hydroxylase activity. 5 PublicationsCorresponds to variant rs28934586dbSNPEnsembl.1
Natural variantiVAR_074532453R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_065197454R → C in AH4. 1 Publication1
Natural variantiVAR_074533463L → LL in AH4; classic; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
Natural variantiVAR_074534489L → S in AH4. 1 PublicationCorresponds to variant rs750428278dbSNPEnsembl.1
Natural variantiVAR_008687494F → C.2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043308401 – 466Missing in isoform 2. 1 PublicationAdd BLAST66

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32879, M32863, M32878 Genomic DNA. Translation: AAA52149.1.
X55764 mRNA. Translation: CAA39290.1.
D16153 Genomic DNA. Translation: BAB71992.1.
D16155 Genomic DNA. Translation: BAA03717.1.
EU332839 Genomic DNA. Translation: ABY87528.1.
AC083841 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82293.1.
BC096286 mRNA. Translation: AAH96286.1.
BC096287 mRNA. Translation: AAH96287.1.
M24667 mRNA. Translation: AAA52148.1. Sequence problems.
D10169 Genomic DNA. Translation: BAA01039.1.
CCDSiCCDS34953.1. [P15538-2]
CCDS6392.1. [P15538-1]
PIRiS11338.
RefSeqiNP_000488.3. NM_000497.3. [P15538-1]
NP_001021384.1. NM_001026213.1. [P15538-2]
UniGeneiHs.184927.

Genome annotation databases

EnsembliENST00000292427; ENSP00000292427; ENSG00000160882. [P15538-1]
ENST00000517471; ENSP00000428043; ENSG00000160882. [P15538-2]
GeneIDi1584.
KEGGihsa:1584.
UCSCiuc003yxi.4. human. [P15538-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32879, M32863, M32878 Genomic DNA. Translation: AAA52149.1.
X55764 mRNA. Translation: CAA39290.1.
D16153 Genomic DNA. Translation: BAB71992.1.
D16155 Genomic DNA. Translation: BAA03717.1.
EU332839 Genomic DNA. Translation: ABY87528.1.
AC083841 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82293.1.
BC096286 mRNA. Translation: AAH96286.1.
BC096287 mRNA. Translation: AAH96287.1.
M24667 mRNA. Translation: AAA52148.1. Sequence problems.
D10169 Genomic DNA. Translation: BAA01039.1.
CCDSiCCDS34953.1. [P15538-2]
CCDS6392.1. [P15538-1]
PIRiS11338.
RefSeqiNP_000488.3. NM_000497.3. [P15538-1]
NP_001021384.1. NM_001026213.1. [P15538-2]
UniGeneiHs.184927.

3D structure databases

ProteinModelPortaliP15538.
SMRiP15538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107956. 1 interactor.
STRINGi9606.ENSP00000292427.

Chemistry databases

BindingDBiP15538.
ChEMBLiCHEMBL1908.
DrugBankiDB00501. Cimetidine.
DB00257. Clotrimazole.
DB00292. Etomidate.
DB00196. Fluconazole.
DB00741. Hydrocortisone.
DB01026. Ketoconazole.
DB01233. Metoclopramide.
DB01011. Metyrapone.
DB01110. Miconazole.
DB00648. Mitotane.
DB00252. Phenytoin.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi1359.
SwissLipidsiSLP:000001197.

PTM databases

iPTMnetiP15538.
PhosphoSitePlusiP15538.

Polymorphism and mutation databases

BioMutaiCYP11B1.
DMDMi215274267.

Proteomic databases

PaxDbiP15538.
PeptideAtlasiP15538.
PRIDEiP15538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292427; ENSP00000292427; ENSG00000160882. [P15538-1]
ENST00000517471; ENSP00000428043; ENSG00000160882. [P15538-2]
GeneIDi1584.
KEGGihsa:1584.
UCSCiuc003yxi.4. human. [P15538-1]

Organism-specific databases

CTDi1584.
DisGeNETi1584.
GeneCardsiCYP11B1.
HGNCiHGNC:2591. CYP11B1.
HPAiHPA049171.
HPA056348.
HPA057752.
MalaCardsiCYP11B1.
MIMi103900. phenotype.
202010. phenotype.
610613. gene.
neXtProtiNX_P15538.
OpenTargetsiENSG00000160882.
Orphaneti90795. Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency.
403. Familial hyperaldosteronism type I.
PharmGKBiPA133.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP15538.
KOiK00497.
PhylomeDBiP15538.
TreeFamiTF105094.

Enzyme and pathway databases

BioCyciMetaCyc:HS08547-MONOMER.
ZFISH:HS08547-MONOMER.
BRENDAi1.14.15.4. 2681.
ReactomeiR-HSA-194002. Glucocorticoid biosynthesis.
R-HSA-211976. Endogenous sterols.

Miscellaneous databases

ChiTaRSiCYP11B1. human.
GeneWikiiSteroid_11-beta-hydroxylase.
GenomeRNAii1584.
PROiP15538.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160882.
CleanExiHS_CYP11B1.
ExpressionAtlasiP15538. baseline and differential.
GenevisibleiP15538. HS.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00408. MITP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiC11B1_HUMAN
AccessioniPrimary (citable) accession number: P15538
Secondary accession number(s): Q14095
, Q4VAQ8, Q4VAQ9, Q9UML2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 184 of the entry and version 5 of the sequence. [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

Complete proteome, Direct protein sequencing, 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.