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UniProtKB - Q16850 (CP51A_HUMAN)

Entry version 185 (26 Feb 2020)
Sequence version 3 (15 Dec 1998)
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Protein

Lanosterol 14-alpha demethylase

Gene

CYP51A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid (PubMed:20149798, PubMed:8619637). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:20149798, PubMed:8619637).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

heme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by azalanstat. Inhibited by azole antifungal agents ketoconazole, itraconazole and fluconazole.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.1 Publication
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (CYP51A1)
  2. no protein annotated in this organism
  3. Methylsterol monooxygenase 1 (MSMO1)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (NSDHL)
  5. 3-keto-steroid reductase (HSD17B7)
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi449Iron (heme axial ligand)1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS00076-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.13.70 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-191273 Cholesterol biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00770;UER00754

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001162

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Lanosterol 14-alpha demethylase (EC:1.14.14.1542 Publications)
Short name:
LDM
Alternative name(s):
CYPLI
Cytochrome P450 51A1
Cytochrome P450-14DM
Short name:
Cytochrome P45014DM
Cytochrome P450LI
Sterol 14-alpha demethylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CYP51A1
Synonyms:CYP51
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2649 CYP51A1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601637 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q16850

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei24 – 44HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		1595

MalaCards human disease database

More...MalaCardsi		CYP51A1

Open Targets

More...OpenTargetsi		ENSG00000001630

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		521432 Congenital cataract-severe neonatal hepatopathy-global developmental delay syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27123

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q16850 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3849

Drug and drug target database

More...DrugBanki		DB07705 1-[(2S)-2-[(4-CHLOROBENZYL)OXY]-2-(2,4-DICHLOROPHENYL)ETHYL]-1H-IMIDAZOLE
DB01167 Itraconazole
DB01026 Ketoconazole
DB05667 Levoketoconazole
DB00916 Metronidazole
DB01110 Miconazole
DB01045 Rifampicin
DB01153 Sertaconazole
DB01007 Tioconazole

DrugCentral

More...DrugCentrali		Q16850

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1374

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CYP51A1

Domain mapping of disease mutations (DMDM)

More...DMDMi		3915660

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000519981 – 503Lanosterol 14-alpha demethylaseAdd BLAST503

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q16850

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q16850

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q16850

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q16850

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q16850

PeptideAtlas

More...PeptideAtlasi		Q16850

PRoteomics IDEntifications database

More...PRIDEi		Q16850

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		61101 [Q16850-1]
61102 [Q16850-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q16850

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q16850

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q16850

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed with highest levels in testis, ovary, adrenal, prostate, liver, kidney and lung.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000001630 Expressed in adrenal tissue and 97 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q16850 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q16850 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA041325
HPA043508

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107967, 46 interactors

Protein interaction database and analysis system

More...IntActi		Q16850, 15 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000003100

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q16850

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q16850 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q16850

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q16850

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0684 Eukaryota
COG2124 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00930000151026

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001570_15_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q16850

KEGG Orthology (KO)

More...KOi		K05917

Database of Orthologous Groups

More...OrthoDBi		559299at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q16850

TreeFam database of animal gene trees

More...TreeFami		TF105091

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.630.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002403 Cyt_P450_E_grp-IV
IPR036396 Cyt_P450_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00067 p450, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00465 EP450IV
PR00385 P450

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48264 SSF48264, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q16850-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH 
        60         70         80         90        100
LVQLPAGVKS PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM 
       110        120        130        140        150
VGKTFTYLLG SDAAALLFNS KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP 
       160        170        180        190        200
VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK EYFESWGESG EKNVFEALSE 
       210        220        230        240        250
LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL LPGWLPLPSF 
       260        270        280        290        300
RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE 
       310        320        330        340        350
VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP 
       360        370        380        390        400
PLTYDQLKDL NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ 
       410        420        430        440        450
VCVSPTVNQR LKDSWVERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCI 
       460        470        480        490        500
GENFAYVQIK TIWSTMLRLY EFDLIDGYFP TVNYTTMIHT PENPVIRYKR 

RSK
Length:503
Mass (Da):56,806
Last modified:December 15, 1998 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4FCEC147FB4DED86
GO
Isoform 2 (identifier: Q16850-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Show »
Length:404
Mass (Da):46,312
Checksum:i2D5198C9B55ED478
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0C4DFL7A0A0C4DFL7_HUMAN
Lanosterol 14-alpha demethylase
CYP51A1
509Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C0D0H7C0D0_HUMAN
Lanosterol 14-alpha demethylase
CYP51A1
222Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB39951 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB46356 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAH32322 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence BAA09512 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence BAG36881 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence EAL24154 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence EAW76858 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti270K → E in BAG36881 (PubMed:14702039).Curated1
Sequence conflicti272R → T in AAC50951 (PubMed:8975714).Curated1
Sequence conflicti368K → R in AAC50951 (PubMed:8975714).Curated1
Sequence conflicti377I → V in AAH32322 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02347013V → A. Corresponds to variant dbSNP:rs2229188Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0374131 – 99Missing in isoform 2. 1 PublicationAdd BLAST99

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U23942 mRNA Translation: AAB39951.1 Different initiation.
D55653 mRNA Translation: BAA09512.1 Different initiation.
U51692 U51691 Genomic DNA Translation: AAC50951.1
AK314205 mRNA Translation: BAG36881.1 Different initiation.
AK295932 mRNA Translation: BAG58717.1
AC000120 Genomic DNA Translation: AAB46356.1 Different initiation.
CH236949 Genomic DNA Translation: EAL24154.1 Different initiation.
CH471091 Genomic DNA Translation: EAW76858.1 Different initiation.
CH471091 Genomic DNA Translation: EAW76859.1
BC032322 mRNA Translation: AAH32322.1 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS55123.1 [Q16850-2]

Protein sequence database of the Protein Information Resource

More...PIRi		JC4759
S68855

NCBI Reference Sequences

More...RefSeqi		NP_000777.1, NM_000786.3
NP_001139624.1, NM_001146152.1 [Q16850-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000450723; ENSP00000406757; ENSG00000001630 [Q16850-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1595

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1595

UCSC genome browser

More...UCSCi		uc003ulm.5 human [Q16850-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23942 mRNA Translation: AAB39951.1 Different initiation.
D55653 mRNA Translation: BAA09512.1 Different initiation.
U51692 U51691 Genomic DNA Translation: AAC50951.1
AK314205 mRNA Translation: BAG36881.1 Different initiation.
AK295932 mRNA Translation: BAG58717.1
AC000120 Genomic DNA Translation: AAB46356.1 Different initiation.
CH236949 Genomic DNA Translation: EAL24154.1 Different initiation.
CH471091 Genomic DNA Translation: EAW76858.1 Different initiation.
CH471091 Genomic DNA Translation: EAW76859.1
BC032322 mRNA Translation: AAH32322.1 Different initiation.
CCDSiCCDS55123.1 [Q16850-2]
PIRiJC4759
S68855
RefSeqiNP_000777.1, NM_000786.3
NP_001139624.1, NM_001146152.1 [Q16850-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JUSX-ray2.90A/B54-502[»]
3JUVX-ray3.12A54-502[»]
3LD6X-ray2.80A/B54-502[»]
4UHIX-ray2.04A/B/C/D61-503[»]
4UHLX-ray2.50A/B/C/D/E/F/G/H61-503[»]
6Q2TX-ray2.80A/B61-503[»]
SMRiQ16850
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107967, 46 interactors
IntActiQ16850, 15 interactors
STRINGi9606.ENSP00000003100

Chemistry databases

BindingDBiQ16850
ChEMBLiCHEMBL3849
DrugBankiDB07705 1-[(2S)-2-[(4-CHLOROBENZYL)OXY]-2-(2,4-DICHLOROPHENYL)ETHYL]-1H-IMIDAZOLE
DB01167 Itraconazole
DB01026 Ketoconazole
DB05667 Levoketoconazole
DB00916 Metronidazole
DB01110 Miconazole
DB01045 Rifampicin
DB01153 Sertaconazole
DB01007 Tioconazole
DrugCentraliQ16850
GuidetoPHARMACOLOGYi1374
SwissLipidsiSLP:000001162

PTM databases

iPTMnetiQ16850
PhosphoSitePlusiQ16850
SwissPalmiQ16850

Polymorphism and mutation databases

BioMutaiCYP51A1
DMDMi3915660

Proteomic databases

EPDiQ16850
jPOSTiQ16850
MassIVEiQ16850
MaxQBiQ16850
PaxDbiQ16850
PeptideAtlasiQ16850
PRIDEiQ16850
ProteomicsDBi61101 [Q16850-1]
61102 [Q16850-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1595

Genome annotation databases

EnsembliENST00000450723; ENSP00000406757; ENSG00000001630 [Q16850-2]
GeneIDi1595
KEGGihsa:1595
UCSCiuc003ulm.5 human [Q16850-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1595
DisGeNETi1595

GeneCards: human genes, protein and diseases

More...GeneCardsi		CYP51A1
HGNCiHGNC:2649 CYP51A1
HPAiHPA041325
HPA043508
MalaCardsiCYP51A1
MIMi601637 gene
neXtProtiNX_Q16850
OpenTargetsiENSG00000001630
Orphaneti521432 Congenital cataract-severe neonatal hepatopathy-global developmental delay syndrome
PharmGKBiPA27123

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0684 Eukaryota
COG2124 LUCA
GeneTreeiENSGT00930000151026
HOGENOMiCLU_001570_15_0_1
InParanoidiQ16850
KOiK05917
OrthoDBi559299at2759
PhylomeDBiQ16850
TreeFamiTF105091

Enzyme and pathway databases

UniPathwayiUPA00770;UER00754
BioCyciMetaCyc:HS00076-MONOMER
BRENDAi1.14.13.70 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CYP51A1 human
EvolutionaryTraceiQ16850

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1595
PharosiQ16850 Tchem

Protein Ontology

More...PROi		PR:Q16850
RNActiQ16850 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000001630 Expressed in adrenal tissue and 97 other tissues
ExpressionAtlasiQ16850 baseline and differential
GenevisibleiQ16850 HS

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002403 Cyt_P450_E_grp-IV
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 1 hit
PRINTSiPR00465 EP450IV
PR00385 P450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCP51A_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q16850
Secondary accession number(s): A4D1F8
, B2RAI4, B4DJ55, O00770, O00772, Q16784, Q8N1A8, Q99868
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: February 26, 2020
This is version 185 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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
  7. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
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