Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15392

- DHC24_HUMAN

UniProt

Q15392 - DHC24_HUMAN

Protein

Delta(24)-sterol reductase

Gene

DHCR24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis.3 Publications

    Catalytic activityi

    5-alpha-cholest-7-en-3-beta-ol + NADP+ = 5-alpha-cholesta-7,24-dien-3-beta-ol + NADPH.

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei122 – 1232Cleavage; by caspaseSequence Analysis
    Sitei383 – 3842Cleavage; by caspaseSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi163 – 17513FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. delta24-sterol reductase activity Source: UniProtKB-EC
    2. enzyme binding Source: UniProtKB
    3. flavin adenine dinucleotide binding Source: InterPro
    4. oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: MGI
    5. peptide antigen binding Source: UniProtKB
    6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

    GO - Biological processi

    1. amyloid precursor protein catabolic process Source: Ensembl
    2. apoptotic process Source: UniProtKB
    3. cell cycle arrest Source: UniProtKB
    4. cholesterol biosynthetic process Source: UniProtKB
    5. male genitalia development Source: Ensembl
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cell proliferation Source: Ensembl
    8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    9. plasminogen activation Source: Ensembl
    10. protein localization Source: Ensembl
    11. Ras protein signal transduction Source: Ensembl
    12. regulation of neuron death Source: UniProtKB
    13. response to hormone Source: Ensembl
    14. response to oxidative stress Source: UniProtKB
    15. skin development Source: UniProtKB
    16. small molecule metabolic process Source: Reactome
    17. tissue development Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_9405. Cholesterol biosynthesis.
    UniPathwayiUPA00063.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta(24)-sterol reductase (EC:1.3.1.72)
    Alternative name(s):
    24-dehydrocholesterol reductase
    3-beta-hydroxysterol delta-24-reductase
    Diminuto/dwarf1 homolog
    Seladin-1
    Gene namesi
    Name:DHCR24
    Synonyms:KIAA0018
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2859. DHCR24.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB
    5. Golgi membrane Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW
    7. membrane Source: UniProtKB
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Desmosterolosis (DESMOS) [MIM:602398]: Rare autosomal recessive disorder characterized by multiple congenital anomalies and elevated levels of the cholesterol precursor desmosterol in plasma, tissue, and cultured cells.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911E → K in DESMOS. 1 Publication
    Corresponds to variant rs28939093 [ dbSNP | Ensembl ].
    VAR_012732
    Natural varianti294 – 2941N → T in DESMOS. 1 Publication
    VAR_012733
    Natural varianti306 – 3061K → N in DESMOS. 1 Publication
    VAR_012734
    Natural varianti471 – 4711Y → S in DESMOS. 1 Publication
    Corresponds to variant rs28939092 [ dbSNP | Ensembl ].
    VAR_012735

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi602398. phenotype.
    Orphaneti35107. Desmosterolosis.
    PharmGKBiPA27320.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 516494Delta(24)-sterol reductasePRO_0000007230Add
    BLAST

    Proteomic databases

    MaxQBiQ15392.
    PaxDbiQ15392.
    PeptideAtlasiQ15392.
    PRIDEiQ15392.

    PTM databases

    PhosphoSiteiQ15392.

    Expressioni

    Tissue specificityi

    Highly expressed in brain and adrenal gland with moderate expression in liver, lung, spleen, prostate and spinal cord. Low expression in heart, uterus and prostate. Undetectable in blood cells. In the brain, strongly expressed in cortical regions, substantia nigra, caudate nucleus, hippocampus, medulla oblongata and pons. In brains affected by Alzheimer disease, expression in the inferior temporal lobe is substantially lower than in the frontal cortex.2 Publications

    Gene expression databases

    ArrayExpressiQ15392.
    BgeeiQ15392.
    CleanExiHS_DHCR24.
    GenevestigatoriQ15392.

    Organism-specific databases

    HPAiCAB037247.

    Interactioni

    Protein-protein interaction databases

    BioGridi108064. 4 interactions.
    IntActiQ15392. 2 interactions.
    STRINGi9606.ENSP00000360316.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15392.
    SMRiQ15392. Positions 115-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 319LumenalSequence Analysis
    Topological domaini53 – 516464CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 234177FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0277.
    HOGENOMiHOG000243421.
    HOVERGENiHBG051349.
    InParanoidiQ15392.
    KOiK09828.
    OMAiLPNNPGM.
    OrthoDBiEOG7H7920.
    PhylomeDBiQ15392.
    TreeFamiTF313170.

    Family and domain databases

    Gene3Di3.30.465.10. 1 hit.
    InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR006094. Oxid_FAD_bind_N.
    [Graphical view]
    PfamiPF01565. FAD_binding_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56176. SSF56176. 1 hit.
    PROSITEiPS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15392-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' 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

    MEPAVSLAVC ALLFLLWVRL KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY    50
    YVRAWVVFKL SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV 100
    SLRVGKYKKT HKNIMINLMD ILEVDTKKQI VRVEPLVTMG QVTALLTSIG 150
    WTLPVLPELD DLTVGGLIMG TGIESSSHKY GLFQHICTAY ELVLADGSFV 200
    RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL RFEPVRGLEA 250
    ICAKFTHESQ RQENHFVEGL LYSLDEAVIM TGVMTDEAEP SKLNSIGNYY 300
    KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI 350
    FRYLFGWMVP PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCLQQALHT 400
    FQNDIHVYPI WLCPFILPSQ PGLVHPKGNE AELYIDIGAY GEPRVKHFEA 450
    RSCMRQLEKF VRSVHGFQML YADCYMNREE FWEMFDGSLY HKLREKLGCQ 500
    DAFPEVYDKI CKAARH 516
    Length:516
    Mass (Da):60,101
    Last modified:January 31, 2002 - v2
    Checksum:iF9A769446FE19E59
    GO
    Isoform 2 (identifier: Q15392-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: MEPAVSLAVC...HEQRVRDIQK → MGAGEQNRQSAHCVQGICGYLEGDEEGEEGEVRST

    Note: No experimental confirmation available.

    Show »
    Length:475
    Mass (Da):54,750
    Checksum:iC163378CA1E91FC8
    GO

    Sequence cautioni

    The sequence BAA02806.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911E → K in DESMOS. 1 Publication
    Corresponds to variant rs28939093 [ dbSNP | Ensembl ].
    VAR_012732
    Natural varianti294 – 2941N → T in DESMOS. 1 Publication
    VAR_012733
    Natural varianti306 – 3061K → N in DESMOS. 1 Publication
    VAR_012734
    Natural varianti471 – 4711Y → S in DESMOS. 1 Publication
    Corresponds to variant rs28939092 [ dbSNP | Ensembl ].
    VAR_012735

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7676MEPAV…RDIQK → MGAGEQNRQSAHCVQGICGY LEGDEEGEEGEVRST in isoform 2. 1 PublicationVSP_056479Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261758 mRNA. Translation: AAG17288.1.
    AF398342
    , AF398336, AF398337, AF398338, AF398339, AF398340, AF398341 Genomic DNA. Translation: AAL15644.1.
    D13643 mRNA. Translation: BAA02806.3. Different initiation.
    AK302774 mRNA. Translation: BAH13803.1.
    AC096536 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06663.1.
    CH471059 Genomic DNA. Translation: EAX06664.1.
    BC004375 mRNA. Translation: AAH04375.1.
    BC011669 mRNA. Translation: AAH11669.1.
    CCDSiCCDS600.1.
    RefSeqiNP_055577.1. NM_014762.3.
    UniGeneiHs.498727.

    Genome annotation databases

    EnsembliENST00000371269; ENSP00000360316; ENSG00000116133.
    ENST00000535035; ENSP00000440191; ENSG00000116133.
    GeneIDi1718.
    KEGGihsa:1718.
    UCSCiuc001cyc.1. human.

    Polymorphism databases

    DMDMi20141421.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261758 mRNA. Translation: AAG17288.1 .
    AF398342
    , AF398336 , AF398337 , AF398338 , AF398339 , AF398340 , AF398341 Genomic DNA. Translation: AAL15644.1 .
    D13643 mRNA. Translation: BAA02806.3 . Different initiation.
    AK302774 mRNA. Translation: BAH13803.1 .
    AC096536 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06663.1 .
    CH471059 Genomic DNA. Translation: EAX06664.1 .
    BC004375 mRNA. Translation: AAH04375.1 .
    BC011669 mRNA. Translation: AAH11669.1 .
    CCDSi CCDS600.1.
    RefSeqi NP_055577.1. NM_014762.3.
    UniGenei Hs.498727.

    3D structure databases

    ProteinModelPortali Q15392.
    SMRi Q15392. Positions 115-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108064. 4 interactions.
    IntActi Q15392. 2 interactions.
    STRINGi 9606.ENSP00000360316.

    PTM databases

    PhosphoSitei Q15392.

    Polymorphism databases

    DMDMi 20141421.

    Proteomic databases

    MaxQBi Q15392.
    PaxDbi Q15392.
    PeptideAtlasi Q15392.
    PRIDEi Q15392.

    Protocols and materials databases

    DNASUi 1718.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371269 ; ENSP00000360316 ; ENSG00000116133 .
    ENST00000535035 ; ENSP00000440191 ; ENSG00000116133 .
    GeneIDi 1718.
    KEGGi hsa:1718.
    UCSCi uc001cyc.1. human.

    Organism-specific databases

    CTDi 1718.
    GeneCardsi GC01M055315.
    HGNCi HGNC:2859. DHCR24.
    HPAi CAB037247.
    MIMi 602398. phenotype.
    606418. gene.
    neXtProti NX_Q15392.
    Orphaneti 35107. Desmosterolosis.
    PharmGKBi PA27320.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0277.
    HOGENOMi HOG000243421.
    HOVERGENi HBG051349.
    InParanoidi Q15392.
    KOi K09828.
    OMAi LPNNPGM.
    OrthoDBi EOG7H7920.
    PhylomeDBi Q15392.
    TreeFami TF313170.

    Enzyme and pathway databases

    UniPathwayi UPA00063 .
    Reactomei REACT_9405. Cholesterol biosynthesis.

    Miscellaneous databases

    ChiTaRSi DHCR24. human.
    GeneWikii 24-dehydrocholesterol_reductase.
    GenomeRNAii 1718.
    NextBioi 6960.
    PROi Q15392.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15392.
    Bgeei Q15392.
    CleanExi HS_DHCR24.
    Genevestigatori Q15392.

    Family and domain databases

    Gene3Di 3.30.465.10. 1 hit.
    InterProi IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR006094. Oxid_FAD_bind_N.
    [Graphical view ]
    Pfami PF01565. FAD_binding_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56176. SSF56176. 1 hit.
    PROSITEi PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress."
      Greeve I., Hermans-Borgmeyer I., Brellinger C., Kasper D., Gomez-Isla T., Behl C., Levkau B., Nitsch R.M.
      J. Neurosci. 20:7345-7352(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Mutations in the 3beta-hydroxysterol delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis."
      Waterham H.R., Koster J., Romeijn G.J., Hennekam R.C.M., Vreken P., Andersson H.C., FitzPatrick D.R., Kelley R.I., Wanders R.J.A.
      Am. J. Hum. Genet. 69:685-694(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS DESMOS LYS-191; THR-294; ASN-306 AND SER-471.
    3. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    4. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Brain and Placenta.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The membrane topological analysis of 3 {beta}-hydroxysteroid-delta24 reductase (DHCR24) on endoplasmic reticulum."
      Lu X., Li Y., Liu J., Cao X., Wang X., Wang D., Seo H., Gao B.
      J. Mol. Endocrinol. 48:1-9(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.

    Entry informationi

    Entry nameiDHC24_HUMAN
    AccessioniPrimary (citable) accession number: Q15392
    Secondary accession number(s): B7Z817, D3DQ51, Q9HBA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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