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Protein

3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase

Gene

EBP

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

Functioni

Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.3 Publications

Catalytic activityi

5-alpha-cholest-7-en-3-beta-ol = 5-alpha-cholest-8-en-3-beta-ol.3 Publications

Pathwayi: cholesterol biosynthesis

This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.3 Publications
View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.

GO - Molecular functioni

  • C-8 sterol isomerase activity Source: Ensembl
  • cholestenol delta-isomerase activity Source: UniProtKB-EC
  • drug transmembrane transporter activity Source: ProtInc
  • steroid delta-isomerase activity Source: UniProtKB
  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • cholesterol biosynthetic process Source: UniProtKB
  • cholesterol biosynthetic process via desmosterol Source: Reactome
  • cholesterol biosynthetic process via lathosterol Source: Reactome
  • cholesterol metabolic process Source: ProtInc
  • hemopoiesis Source: Ensembl
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000147155-MONOMER.
BRENDAi5.3.3.5. 2681.
ReactomeiR-HSA-6807047. Cholesterol biosynthesis via desmosterol.
R-HSA-6807062. Cholesterol biosynthesis via lathosterol.
SABIO-RKQ15125.
UniPathwayiUPA00063.

Chemistry

SwissLipidsiSLP:000001209.

Names & Taxonomyi

Protein namesi
Recommended name:
3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC:5.3.3.53 Publications)
Alternative name(s):
Cholestenol Delta-isomerase
Delta(8)-Delta(7) sterol isomerase
Short name:
D8-D7 sterol isomerase
Emopamil-binding protein
Gene namesi
Name:EBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3133. EBP.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921HelicalSequence analysisAdd
BLAST
Transmembranei66 – 8621HelicalSequence analysisAdd
BLAST
Transmembranei121 – 14121HelicalSequence analysisAdd
BLAST
Transmembranei185 – 20521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • nuclear envelope Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Chondrodysplasia punctata 2, X-linked dominant (CDPX2)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol in the plasma and tissues.
See also OMIM:302960
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801E → K in CDPX2. 1 Publication
Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
VAR_012105
Natural varianti103 – 1031E → K in CDPX2. 1 Publication
VAR_074637
Natural varianti110 – 1101R → Q in CDPX2. 1 Publication
VAR_012106
Natural varianti147 – 1471R → G in CDPX2. 1 Publication
VAR_012107
Natural varianti147 – 1471R → H in CDPX2. 3 Publications
Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
VAR_012108
MEND syndrome (MEND)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive disorder associated with a defect in sterol biosynthesis. Disease manifestations and severity are highly variable. Clinical features include intellectual disability, short stature, scoliosis, digital abnormalities, cataracts, and dermatologic abnormalities.
See also OMIM:300960
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181L → P in MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation. 1 Publication
Corresponds to variant rs104894795 [ dbSNP | Ensembl ].
VAR_074633
Natural varianti47 – 471W → C in MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation. 1 Publication
Corresponds to variant rs587783599 [ dbSNP | Ensembl ].
VAR_074634
Natural varianti47 – 471W → R in MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication
VAR_074635
Natural varianti75 – 751I → N in MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication
VAR_074636

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681W → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi75 – 751I → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi76 – 761H → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication
Mutagenesisi80 – 801E → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication
Mutagenesisi111 – 1111Y → W: Reduces catalytic activity to less than 2% of wild-type. 1 Publication
Mutagenesisi121 – 1211M → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi121 – 1211M → V: No effect on catalytic activity. 1 Publication
Mutagenesisi122 – 1221E → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication
Mutagenesisi125 – 1251T → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication
Mutagenesisi188 – 1881Y → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi189 – 1891F → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi189 – 1891F → L: No effect on catalytic activity. 1 Publication
Mutagenesisi193 – 1931N → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication
Mutagenesisi196 – 1961W → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication

Keywords - Diseasei

Cataract, Disease mutation, Dwarfism, Ichthyosis

Organism-specific databases

MalaCardsiEBP.
MIMi300960. phenotype.
302960. phenotype.
Orphaneti352487. Digital anomalies - intellectual disability - short stature.
401973. MEND syndrome.
35173. X-linked dominant chondrodysplasia punctata.
PharmGKBiPA27587.

Chemistry

ChEMBLiCHEMBL612409.
DrugBankiDB00675. Tamoxifen.

Polymorphism and mutation databases

BioMutaiEBP.
DMDMi17374795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 2302293-beta-hydroxysteroid-Delta(8),Delta(7)-isomerasePRO_0000174342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ15125.
MaxQBiQ15125.
PaxDbiQ15125.
PeptideAtlasiQ15125.
PRIDEiQ15125.
TopDownProteomicsiQ15125.

PTM databases

iPTMnetiQ15125.
PhosphoSiteiQ15125.

Expressioni

Gene expression databases

BgeeiENSG00000147155.
CleanExiHS_EBP.
ExpressionAtlasiQ15125. baseline and differential.
GenevisibleiQ15125. HS.

Organism-specific databases

HPAiHPA003130.

Interactioni

Protein-protein interaction databases

BioGridi115921. 38 interactions.
IntActiQ15125. 12 interactions.
STRINGi9606.ENSP00000417052.

Chemistry

BindingDBiQ15125.

Structurei

3D structure databases

ProteinModelPortaliQ15125.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 204144EXPERAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the EBP family.Curated
Contains 1 EXPERA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4826. Eukaryota.
ENOG41101ES. LUCA.
GeneTreeiENSGT00530000063715.
HOGENOMiHOG000204543.
HOVERGENiHBG018176.
InParanoidiQ15125.
KOiK01824.
OMAiFVIHHET.
OrthoDBiEOG091G0KCI.
PhylomeDBiQ15125.
TreeFamiTF314716.

Family and domain databases

InterProiIPR007905. EBP.
IPR033118. EXPERA.
[Graphical view]
PANTHERiPTHR14207. PTHR14207. 1 hit.
PfamiPF05241. EBP. 1 hit.
[Graphical view]
PROSITEiPS51751. EXPERA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q15125-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNAGPLHP YWPQHLRLDN FVPNDRPTWH ILAGLFSVTG VLVVTTWLLS
60 70 80 90 100
GRAAVVPLGT WRRLSLCWFA VCGFIHLVIE GWFVLYYEDL LGDQAFLSQL
110 120 130 140 150
WKEYAKGDSR YILGDNFTVC METITACLWG PLSLWVVIAF LRQHPLRFIL
160 170 180 190 200
QLVVSVGQIY GDVLYFLTEH RDGFQHGELG HPLYFWFYFV FMNALWLVLP
210 220 230
GVLVLDAVKH LTHAQSTLDA KATKAKSKKN
Length:230
Mass (Da):26,353
Last modified:January 23, 2007 - v3
Checksum:i3931A9DE3DBAFA04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1882FY → IF in CAG33096 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181L → P in MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation. 1 Publication
Corresponds to variant rs104894795 [ dbSNP | Ensembl ].
VAR_074633
Natural varianti47 – 471W → C in MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation. 1 Publication
Corresponds to variant rs587783599 [ dbSNP | Ensembl ].
VAR_074634
Natural varianti47 – 471W → R in MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication
VAR_074635
Natural varianti75 – 751I → N in MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication
VAR_074636
Natural varianti80 – 801E → K in CDPX2. 1 Publication
Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
VAR_012105
Natural varianti103 – 1031E → K in CDPX2. 1 Publication
VAR_074637
Natural varianti110 – 1101R → Q in CDPX2. 1 Publication
VAR_012106
Natural varianti147 – 1471R → G in CDPX2. 1 Publication
VAR_012107
Natural varianti147 – 1471R → H in CDPX2. 3 Publications
Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
VAR_012108

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37986 mRNA. Translation: CAA86068.1.
CR456815 mRNA. Translation: CAG33096.1.
CR542094 mRNA. Translation: CAG46891.1.
AF196969 Genomic DNA. No translation available.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50773.1.
BC001549 mRNA. Translation: AAH01549.1.
BC001572 mRNA. Translation: AAH01572.1.
BC046501 mRNA. Translation: AAH46501.1.
CCDSiCCDS14300.1.
PIRiB56122.
RefSeqiNP_006570.1. NM_006579.2.
UniGeneiHs.30619.

Genome annotation databases

EnsembliENST00000495186; ENSP00000417052; ENSG00000147155.
GeneIDi10682.
KEGGihsa:10682.
UCSCiuc004djx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37986 mRNA. Translation: CAA86068.1.
CR456815 mRNA. Translation: CAG33096.1.
CR542094 mRNA. Translation: CAG46891.1.
AF196969 Genomic DNA. No translation available.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50773.1.
BC001549 mRNA. Translation: AAH01549.1.
BC001572 mRNA. Translation: AAH01572.1.
BC046501 mRNA. Translation: AAH46501.1.
CCDSiCCDS14300.1.
PIRiB56122.
RefSeqiNP_006570.1. NM_006579.2.
UniGeneiHs.30619.

3D structure databases

ProteinModelPortaliQ15125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115921. 38 interactions.
IntActiQ15125. 12 interactions.
STRINGi9606.ENSP00000417052.

Chemistry

BindingDBiQ15125.
ChEMBLiCHEMBL612409.
DrugBankiDB00675. Tamoxifen.
SwissLipidsiSLP:000001209.

PTM databases

iPTMnetiQ15125.
PhosphoSiteiQ15125.

Polymorphism and mutation databases

BioMutaiEBP.
DMDMi17374795.

Proteomic databases

EPDiQ15125.
MaxQBiQ15125.
PaxDbiQ15125.
PeptideAtlasiQ15125.
PRIDEiQ15125.
TopDownProteomicsiQ15125.

Protocols and materials databases

DNASUi10682.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000495186; ENSP00000417052; ENSG00000147155.
GeneIDi10682.
KEGGihsa:10682.
UCSCiuc004djx.5. human.

Organism-specific databases

CTDi10682.
GeneCardsiEBP.
GeneReviewsiEBP.
HGNCiHGNC:3133. EBP.
HPAiHPA003130.
MalaCardsiEBP.
MIMi300205. gene.
300960. phenotype.
302960. phenotype.
neXtProtiNX_Q15125.
Orphaneti352487. Digital anomalies - intellectual disability - short stature.
401973. MEND syndrome.
35173. X-linked dominant chondrodysplasia punctata.
PharmGKBiPA27587.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4826. Eukaryota.
ENOG41101ES. LUCA.
GeneTreeiENSGT00530000063715.
HOGENOMiHOG000204543.
HOVERGENiHBG018176.
InParanoidiQ15125.
KOiK01824.
OMAiFVIHHET.
OrthoDBiEOG091G0KCI.
PhylomeDBiQ15125.
TreeFamiTF314716.

Enzyme and pathway databases

UniPathwayiUPA00063.
BioCyciMetaCyc:ENSG00000147155-MONOMER.
BRENDAi5.3.3.5. 2681.
ReactomeiR-HSA-6807047. Cholesterol biosynthesis via desmosterol.
R-HSA-6807062. Cholesterol biosynthesis via lathosterol.
SABIO-RKQ15125.

Miscellaneous databases

GenomeRNAii10682.
PROiQ15125.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147155.
CleanExiHS_EBP.
ExpressionAtlasiQ15125. baseline and differential.
GenevisibleiQ15125. HS.

Family and domain databases

InterProiIPR007905. EBP.
IPR033118. EXPERA.
[Graphical view]
PANTHERiPTHR14207. PTHR14207. 1 hit.
PfamiPF05241. EBP. 1 hit.
[Graphical view]
PROSITEiPS51751. EXPERA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEBP_HUMAN
AccessioniPrimary (citable) accession number: Q15125
Secondary accession number(s): Q6FGL3, Q6IBI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 149 of the entry and version 3 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

Miscellaneous

Binds to the phenylalkylamine calcium-ion antagonist emopamil, an anti-ischemic drug.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.