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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.
ZFISH: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 databases

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)DescriptionActionsGraphical viewLength
Transmembranei29 – 49HelicalSequence analysisAdd BLAST21
Transmembranei66 – 86HelicalSequence analysisAdd BLAST21
Transmembranei121 – 141HelicalSequence analysisAdd BLAST21
Transmembranei185 – 205HelicalSequence analysisAdd BLAST21

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01210580E → K in CDPX2. 1 PublicationCorresponds to variant rs28936073dbSNPEnsembl.1
Natural variantiVAR_074637103E → K in CDPX2. 1 Publication1
Natural variantiVAR_012106110R → Q in CDPX2. 1 Publication1
Natural variantiVAR_012107147R → G in CDPX2. 1 Publication1
Natural variantiVAR_012108147R → H in CDPX2. 3 PublicationsCorresponds to variant rs28935174dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07463318L → P in MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation. 1 PublicationCorresponds to variant rs104894795dbSNPEnsembl.1
Natural variantiVAR_07463447W → C in MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation. 1 PublicationCorresponds to variant rs587783599dbSNPEnsembl.1
Natural variantiVAR_07463547W → R in MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication1
Natural variantiVAR_07463675I → N in MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68W → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication1
Mutagenesisi75I → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication1
Mutagenesisi76H → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1
Mutagenesisi80E → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1
Mutagenesisi111Y → W: Reduces catalytic activity to less than 2% of wild-type. 1 Publication1
Mutagenesisi121M → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication1
Mutagenesisi121M → V: No effect on catalytic activity. 1 Publication1
Mutagenesisi122E → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1
Mutagenesisi125T → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1
Mutagenesisi188Y → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication1
Mutagenesisi189F → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication1
Mutagenesisi189F → L: No effect on catalytic activity. 1 Publication1
Mutagenesisi193N → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1
Mutagenesisi196W → A: Reduces catalytic activity to less than 10% of wild-type. 1 Publication1

Keywords - Diseasei

Cataract, Disease mutation, Dwarfism, Ichthyosis

Organism-specific databases

DisGeNETi10682.
MalaCardsiEBP.
MIMi300960. phenotype.
302960. phenotype.
OpenTargetsiENSG00000147155.
Orphaneti352487. Digital anomalies - intellectual disability - short stature.
401973. MEND syndrome.
35173. X-linked dominant chondrodysplasia punctata.
PharmGKBiPA27587.

Chemistry databases

ChEMBLiCHEMBL4931.
DrugBankiDB00675. Tamoxifen.

Polymorphism and mutation databases

BioMutaiEBP.
DMDMi17374795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001743422 – 2303-beta-hydroxysteroid-Delta(8),Delta(7)-isomeraseAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

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

PTM databases

iPTMnetiQ15125.
PhosphoSitePlusiQ15125.

Expressioni

Gene expression databases

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

Organism-specific databases

HPAiHPA003130.

Interactioni

Protein-protein interaction databases

BioGridi115921. 38 interactors.
IntActiQ15125. 14 interactors.
STRINGi9606.ENSP00000417052.

Chemistry databases

BindingDBiQ15125.

Structurei

3D structure databases

ProteinModelPortaliQ15125.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 204EXPERAPROSITE-ProRule annotationAdd BLAST144

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)DescriptionActionsGraphical viewLength
Sequence conflicti187 – 188FY → IF in CAG33096 (Ref. 2) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07463318L → P in MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation. 1 PublicationCorresponds to variant rs104894795dbSNPEnsembl.1
Natural variantiVAR_07463447W → C in MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation. 1 PublicationCorresponds to variant rs587783599dbSNPEnsembl.1
Natural variantiVAR_07463547W → R in MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication1
Natural variantiVAR_07463675I → N in MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation. 1 Publication1
Natural variantiVAR_01210580E → K in CDPX2. 1 PublicationCorresponds to variant rs28936073dbSNPEnsembl.1
Natural variantiVAR_074637103E → K in CDPX2. 1 Publication1
Natural variantiVAR_012106110R → Q in CDPX2. 1 Publication1
Natural variantiVAR_012107147R → G in CDPX2. 1 Publication1
Natural variantiVAR_012108147R → H in CDPX2. 3 PublicationsCorresponds to variant rs28935174dbSNPEnsembl.1

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 interactors.
IntActiQ15125. 14 interactors.
STRINGi9606.ENSP00000417052.

Chemistry databases

BindingDBiQ15125.
ChEMBLiCHEMBL4931.
DrugBankiDB00675. Tamoxifen.
SwissLipidsiSLP:000001209.

PTM databases

iPTMnetiQ15125.
PhosphoSitePlusiQ15125.

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.
DisGeNETi10682.
GeneCardsiEBP.
GeneReviewsiEBP.
HGNCiHGNC:3133. EBP.
HPAiHPA003130.
MalaCardsiEBP.
MIMi300205. gene.
300960. phenotype.
302960. phenotype.
neXtProtiNX_Q15125.
OpenTargetsiENSG00000147155.
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.
ZFISH: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: November 30, 2016
This is version 152 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.