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Q15392

- DHC24_HUMAN

UniProt

Q15392 - DHC24_HUMAN

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Protein

Delta(24)-sterol reductase

Gene

DHCR24

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

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

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(24-1) sterol reductase activity Source: UniProtKB
  2. delta24-sterol reductase activity Source: UniProtKB-EC
  3. enzyme binding Source: UniProtKB
  4. flavin adenine dinucleotide binding Source: InterPro
  5. oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: MGI
  6. peptide antigen binding Source: UniProtKB
  7. 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. membrane organization Source: Ensembl
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of cell proliferation Source: Ensembl
  9. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  10. oxidation-reduction process Source: UniProtKB
  11. plasminogen activation Source: Ensembl
  12. protein localization Source: Ensembl
  13. Ras protein signal transduction Source: Ensembl
  14. regulation of neuron death Source: UniProtKB
  15. response to hormone Source: Ensembl
  16. response to oxidative stress Source: UniProtKB
  17. skin development Source: UniProtKB
  18. small molecule metabolic process Source: Reactome
  19. tissue development Source: UniProtKB
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 319LumenalSequence Analysis
Transmembranei32 – 5221HelicalSequence AnalysisAdd
BLAST
Topological domaini53 – 516464CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiQ15392.
CleanExiHS_DHCR24.
ExpressionAtlasiQ15392. baseline and differential.
GenevestigatoriQ15392.

Organism-specific databases

HPAiCAB037247.

Interactioni

Protein-protein interaction databases

BioGridi108064. 11 interactions.
IntActiQ15392. 2 interactions.
STRINGi9606.ENSP00000360316.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00390000008338.
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

        10         20         30         40         50
MEPAVSLAVC ALLFLLWVRL KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY
60 70 80 90 100
YVRAWVVFKL SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV
110 120 130 140 150
SLRVGKYKKT HKNIMINLMD ILEVDTKKQI VRVEPLVTMG QVTALLTSIG
160 170 180 190 200
WTLPVLPELD DLTVGGLIMG TGIESSSHKY GLFQHICTAY ELVLADGSFV
210 220 230 240 250
RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL RFEPVRGLEA
260 270 280 290 300
ICAKFTHESQ RQENHFVEGL LYSLDEAVIM TGVMTDEAEP SKLNSIGNYY
310 320 330 340 350
KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI
360 370 380 390 400
FRYLFGWMVP PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCLQQALHT
410 420 430 440 450
FQNDIHVYPI WLCPFILPSQ PGLVHPKGNE AELYIDIGAY GEPRVKHFEA
460 470 480 490 500
RSCMRQLEKF VRSVHGFQML YADCYMNREE FWEMFDGSLY HKLREKLGCQ
510
DAFPEVYDKI CKAARH
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.Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q15392-1]
RefSeqiNP_055577.1. NM_014762.3. [Q15392-1]
UniGeneiHs.498727.

Genome annotation databases

EnsembliENST00000371269; ENSP00000360316; ENSG00000116133. [Q15392-1]
GeneIDi1718.
KEGGihsa:1718.
UCSCiuc001cyc.1. human. [Q15392-1]

Polymorphism databases

DMDMi20141421.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q15392-1 ]
RefSeqi NP_055577.1. NM_014762.3. [Q15392-1 ]
UniGenei Hs.498727.

3D structure databases

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

Protein-protein interaction databases

BioGridi 108064. 11 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 . [Q15392-1 ]
GeneIDi 1718.
KEGGi hsa:1718.
UCSCi uc001cyc.1. human. [Q15392-1 ]

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.
GeneTreei ENSGT00390000008338.
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 35480367.
PROi Q15392.
SOURCEi Search...

Gene expression databases

Bgeei Q15392.
CleanExi HS_DHCR24.
ExpressionAtlasi Q15392. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 137 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