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Q15125

- EBP_HUMAN

UniProt

Q15125 - EBP_HUMAN

Protein

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

Gene

EBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. C-8 sterol isomerase activity Source: Ensembl
    2. cholestenol delta-isomerase activity Source: UniProtKB-EC
    3. drug transmembrane transporter activity Source: ProtInc
    4. steroid delta-isomerase activity Source: ProtInc
    5. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. cholesterol biosynthetic process Source: Reactome
    2. cholesterol metabolic process Source: ProtInc
    3. drug transmembrane transport Source: GOC
    4. hemopoiesis Source: Ensembl
    5. signal transduction Source: GOC
    6. skeletal system development Source: ProtInc
    7. small molecule metabolic process Source: Reactome

    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.
    ReactomeiREACT_9405. Cholesterol biosynthesis.
    SABIO-RKQ15125.
    UniPathwayiUPA00063.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:EBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3133. EBP.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti80 – 801E → K in CDPX2. 1 Publication
    Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
    VAR_012105
    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. 2 Publications
    Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
    VAR_012108

    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. 2 Publications
    Mutagenesisi121 – 1211M → A: Reduces catalytic activity to less than 35% of wild-type. 2 Publications
    Mutagenesisi121 – 1211M → V: No effect on catalytic activity. 2 Publications
    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. 2 Publications
    Mutagenesisi189 – 1891F → L: No effect on catalytic activity. 2 Publications
    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

    MIMi302960. phenotype.
    Orphaneti35173. X-linked dominant chondrodysplasia punctata.
    PharmGKBiPA27587.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 2302293-beta-hydroxysteroid-Delta(8),Delta(7)-isomerasePRO_0000174342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15125.
    PaxDbiQ15125.
    PeptideAtlasiQ15125.
    PRIDEiQ15125.

    PTM databases

    PhosphoSiteiQ15125.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15125.
    BgeeiQ15125.
    CleanExiHS_EBP.
    GenevestigatoriQ15125.

    Organism-specific databases

    HPAiHPA003130.

    Interactioni

    Protein-protein interaction databases

    BioGridi115921. 7 interactions.
    IntActiQ15125. 2 interactions.
    STRINGi9606.ENSP00000417052.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15125.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the EBP family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG331138.
    HOGENOMiHOG000204543.
    HOVERGENiHBG018176.
    InParanoidiQ15125.
    KOiK01824.
    OMAiFVIHHET.
    PhylomeDBiQ15125.
    TreeFamiTF314716.

    Family and domain databases

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

    MTTNAGPLHP YWPQHLRLDN FVPNDRPTWH ILAGLFSVTG VLVVTTWLLS    50
    GRAAVVPLGT WRRLSLCWFA VCGFIHLVIE GWFVLYYEDL LGDQAFLSQL 100
    WKEYAKGDSR YILGDNFTVC METITACLWG PLSLWVVIAF LRQHPLRFIL 150
    QLVVSVGQIY GDVLYFLTEH RDGFQHGELG HPLYFWFYFV FMNALWLVLP 200
    GVLVLDAVKH LTHAQSTLDA KATKAKSKKN 230
    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. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti80 – 801E → K in CDPX2. 1 Publication
    Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
    VAR_012105
    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. 2 Publications
    Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
    VAR_012108

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.4. human.

    Polymorphism databases

    DMDMi17374795.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14300.1.
    PIRi B56122.
    RefSeqi NP_006570.1. NM_006579.2.
    UniGenei Hs.30619.

    3D structure databases

    ProteinModelPortali Q15125.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115921. 7 interactions.
    IntActi Q15125. 2 interactions.
    STRINGi 9606.ENSP00000417052.

    Chemistry

    BindingDBi Q15125.
    ChEMBLi CHEMBL612409.

    PTM databases

    PhosphoSitei Q15125.

    Polymorphism databases

    DMDMi 17374795.

    Proteomic databases

    MaxQBi Q15125.
    PaxDbi Q15125.
    PeptideAtlasi Q15125.
    PRIDEi Q15125.

    Protocols and materials databases

    DNASUi 10682.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000495186 ; ENSP00000417052 ; ENSG00000147155 .
    GeneIDi 10682.
    KEGGi hsa:10682.
    UCSCi uc004djx.4. human.

    Organism-specific databases

    CTDi 10682.
    GeneCardsi GC0XP048380.
    GeneReviewsi EBP.
    HGNCi HGNC:3133. EBP.
    HPAi HPA003130.
    MIMi 300205. gene.
    302960. phenotype.
    neXtProti NX_Q15125.
    Orphaneti 35173. X-linked dominant chondrodysplasia punctata.
    PharmGKBi PA27587.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331138.
    HOGENOMi HOG000204543.
    HOVERGENi HBG018176.
    InParanoidi Q15125.
    KOi K01824.
    OMAi FVIHHET.
    PhylomeDBi Q15125.
    TreeFami TF314716.

    Enzyme and pathway databases

    UniPathwayi UPA00063 .
    BioCyci MetaCyc:ENSG00000147155-MONOMER.
    BRENDAi 5.3.3.5. 2681.
    Reactomei REACT_9405. Cholesterol biosynthesis.
    SABIO-RK Q15125.

    Miscellaneous databases

    GenomeRNAii 10682.
    NextBioi 40611.
    PROi Q15125.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15125.
    Bgeei Q15125.
    CleanExi HS_EBP.
    Genevestigatori Q15125.

    Family and domain databases

    InterProi IPR007905. EBP.
    [Graphical view ]
    PANTHERi PTHR14207. PTHR14207. 1 hit.
    Pfami PF05241. EBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    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: October 1, 2014
    This is version 130 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

    External Data

    Dasty 3