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Q15125 (EBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase

EC=5.3.3.5
Alternative name(s):
Cholestenol Delta-isomerase
Delta(8)-Delta(7) sterol isomerase
Short name=D8-D7 sterol isomerase
Emopamil-binding protein
Gene names
Name:EBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Steroid biosynthesis; cholesterol biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12 Ref.13

Miscellaneous

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

Sequence similarities

Belongs to the EBP family.

Ontologies

Keywords
   Biological processCholesterol biosynthesis
Cholesterol metabolism
Lipid biosynthesis
Lipid metabolism
Steroid biosynthesis
Steroid metabolism
Sterol biosynthesis
Sterol metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DiseaseCataract
Disease mutation
Dwarfism
Ichthyosis
   DomainTransmembrane
Transmembrane helix
   Molecular functionIsomerase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol biosynthetic process

Traceable author statement. Source: Reactome

cholesterol metabolic process

Traceable author statement Ref.11. Source: ProtInc

drug transmembrane transport

Traceable author statement Ref.1. Source: GOC

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: GOC

skeletal system development

Traceable author statement Ref.11. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionC-8 sterol isomerase activity

Inferred from electronic annotation. Source: Ensembl

cholestenol delta-isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

drug transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

steroid delta-isomerase activity

Traceable author statement Ref.11. Source: ProtInc

transmembrane signaling receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2302293-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
PRO_0000174342

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane121 – 14121Helical; Potential
Transmembrane185 – 20521Helical; Potential

Amino acid modifications

Modified residue21N-acetylthreonine By similarity

Natural variations

Natural variant801E → K in CDPX2. Ref.11
Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
VAR_012105
Natural variant1101R → Q in CDPX2. Ref.10
VAR_012106
Natural variant1471R → G in CDPX2. Ref.13
VAR_012107
Natural variant1471R → H in CDPX2. Ref.11 Ref.12
Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
VAR_012108

Experimental info

Mutagenesis681W → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesis751I → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesis761H → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis801E → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis1111Y → W: Reduces catalytic activity to less than 2% of wild-type. Ref.7
Mutagenesis1211M → A: Reduces catalytic activity to less than 35% of wild-type. Ref.7
Mutagenesis1211M → V: No effect on catalytic activity. Ref.7
Mutagenesis1221E → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis1251T → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis1881Y → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesis1891F → A: Reduces catalytic activity to less than 35% of wild-type. Ref.7
Mutagenesis1891F → L: No effect on catalytic activity. Ref.7
Mutagenesis1931N → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis1961W → A: Reduces catalytic activity to less than 10% of wild-type.
Sequence conflict187 – 1882FY → IF in CAG33096. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q15125 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3931A9DE3DBAFA04

FASTA23026,353
        10         20         30         40         50         60 
MTTNAGPLHP YWPQHLRLDN FVPNDRPTWH ILAGLFSVTG VLVVTTWLLS GRAAVVPLGT 

        70         80         90        100        110        120 
WRRLSLCWFA VCGFIHLVIE GWFVLYYEDL LGDQAFLSQL WKEYAKGDSR YILGDNFTVC 

       130        140        150        160        170        180 
METITACLWG PLSLWVVIAF LRQHPLRFIL QLVVSVGQIY GDVLYFLTEH RDGFQHGELG 

       190        200        210        220        230 
HPLYFWFYFV FMNALWLVLP GVLVLDAVKH LTHAQSTLDA KATKAKSKKN 

« Hide

References

« Hide 'large scale' references
[1]"Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning, tissue distribution, and heterologous expression."
Hanner M., Moebius F.F., Weber F., Grabner M., Striessnig J., Glossmann H.
J. Biol. Chem. 270:7551-7557(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix and Placenta.
[6]"Histidine77, glutamic acid81, glutamic acid123, threonine126, asparagine194, and tryptophan197 of the human emopamil binding protein are required for in vivo sterol delta 8-delta 7 isomerization."
Moebius F.F., Soellner K.E.M., Fiechtner B., Huck C.W., Bonn G., Glossmann H.
Biochemistry 38:1119-1127(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol delta8-delta7 isomerase activity."
Moebius F.F., Fitzky B.U., Wietzorrek G., Haidekker A., Eder A., Glossmann H.
Biochem. J. 374:229-237(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-111; MET-121 AND PHE-189.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata."
Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A., Kelley R.I., Boyd Y., Herman G.E.
Nat. Genet. 22:286-290(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDPX2 GLN-110.
[11]"Mutations in the gene encoding 3-beta-hydroxysteroid-delta(8),delta(7)-isomerase cause X-linked dominant Conradi-Hunermann syndrome."
Braverman N., Lin P., Moebius F.F., Obie C., Moser A., Glossmann H., Wilcox W.R., Rimoin D.L., Smith M., Kratz L., Kelley R.I., Valle D.
Nat. Genet. 22:291-294(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDPX2 LYS-80 AND HIS-147.
[12]"The Conradi-Hunermann-Happle syndrome (CDPX2) and emopamil binding protein: novel mutations, and somatic and gonadal mosaicism."
Has C., Bruckner-Tuderman L., Muller D., Floeth M., Folkers E., Donnai D., Traupe H.
Hum. Mol. Genet. 9:1951-1955(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDPX2 HIS-147.
[13]"Identification of a novel mutation in 3beta-hydroxysteroid-Delta8-Delta7-isomerase in a case of Conradi-Hunermann-Happle syndrome."
Becker K., Csikos M., Horvath A., Karpati S.
Exp. Dermatol. 10:286-289(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDPX2 GLY-147.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14300.1.
PIRB56122.
RefSeqNP_006570.1. NM_006579.2.
UniGeneHs.30619.

3D structure databases

ProteinModelPortalQ15125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115921. 7 interactions.
IntActQ15125. 2 interactions.
STRING9606.ENSP00000417052.

Chemistry

BindingDBQ15125.
ChEMBLCHEMBL612409.

PTM databases

PhosphoSiteQ15125.

Polymorphism databases

DMDM17374795.

Proteomic databases

MaxQBQ15125.
PaxDbQ15125.
PeptideAtlasQ15125.
PRIDEQ15125.

Protocols and materials databases

DNASU10682.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000495186; ENSP00000417052; ENSG00000147155.
ENST00000598515; ENSP00000471792; ENSG00000268394.
GeneID10682.
KEGGhsa:10682.
UCSCuc004djx.4. human.

Organism-specific databases

CTD10682.
GeneCardsGC0XP048380.
GeneReviewsEBP.
HGNCHGNC:3133. EBP.
HPAHPA003130.
MIM300205. gene.
302960. phenotype.
neXtProtNX_Q15125.
Orphanet35173. X-linked dominant chondrodysplasia punctata.
PharmGKBPA27587.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331138.
HOGENOMHOG000204543.
HOVERGENHBG018176.
InParanoidQ15125.
KOK01824.
OMAFVIHHET.
PhylomeDBQ15125.
TreeFamTF314716.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000147155-MONOMER.
BRENDA5.3.3.5. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ15125.
UniPathwayUPA00063.

Gene expression databases

ArrayExpressQ15125.
BgeeQ15125.
CleanExHS_EBP.
GenevestigatorQ15125.

Family and domain databases

InterProIPR007905. EBP.
[Graphical view]
PANTHERPTHR14207. PTHR14207. 1 hit.
PfamPF05241. EBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10682.
NextBio40611.
PROQ15125.
SOURCESearch...

Entry information

Entry nameEBP_HUMAN
AccessionPrimary (citable) accession number: Q15125
Secondary accession number(s): Q6FGL3, Q6IBI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM