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Protein

Delta(24)-sterol reductase

Gene

DHCR24

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Pathway: cholesterol biosynthesis

This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.

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

  • delta24(24-1) sterol reductase activity Source: UniProtKB
  • delta24-sterol reductase activity Source: UniProtKB-EC
  • enzyme binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: InterPro
  • oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: MGI
  • peptide antigen binding Source: UniProtKB
  • UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

GO - Biological processi

  • amyloid precursor protein catabolic process Source: Ensembl
  • apoptotic process Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cholesterol biosynthetic process Source: UniProtKB
  • male genitalia development Source: Ensembl
  • membrane organization Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • plasminogen activation Source: Ensembl
  • protein localization Source: Ensembl
  • Ras protein signal transduction Source: Ensembl
  • regulation of neuron death Source: UniProtKB
  • response to hormone Source: Ensembl
  • response to oxidative stress Source: UniProtKB
  • skin development Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • 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

BRENDAi1.3.1.72. 2681.
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 Componenti: 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

  • cytoplasm Source: GO_Central
  • cytoskeleton Source: Ensembl
  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Desmosterolosis (DESMOS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare autosomal recessive disorder characterized by multiple congenital anomalies and elevated levels of the cholesterol precursor desmosterol in plasma, tissue, and cultured cells.

See also OMIM:602398
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.

Polymorphism and mutation databases

BioMutaiDHCR24.
DMDMi20141421.

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.
GenevisibleiQ15392. HS.

Organism-specific databases

HPAiCAB037247.
HPA063005.

Interactioni

Protein-protein interaction databases

BioGridi108064. 13 interactions.
IntActiQ15392. 4 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.
OMAiKFTHESQ.
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. AlignAdd to basket

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]
uc010ook.1. human.

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.
CCDSiCCDS600.1. [Q15392-1]
RefSeqiNP_055577.1. NM_014762.3. [Q15392-1]
UniGeneiHs.498727.

3D structure databases

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

Protein-protein interaction databases

BioGridi108064. 13 interactions.
IntActiQ15392. 4 interactions.
STRINGi9606.ENSP00000360316.

PTM databases

PhosphoSiteiQ15392.

Polymorphism and mutation databases

BioMutaiDHCR24.
DMDMi20141421.

Proteomic databases

MaxQBiQ15392.
PaxDbiQ15392.
PeptideAtlasiQ15392.
PRIDEiQ15392.

Protocols and materials databases

DNASUi1718.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371269; ENSP00000360316; ENSG00000116133. [Q15392-1]
GeneIDi1718.
KEGGihsa:1718.
UCSCiuc001cyc.1. human. [Q15392-1]
uc010ook.1. human.

Organism-specific databases

CTDi1718.
GeneCardsiGC01M055315.
HGNCiHGNC:2859. DHCR24.
HPAiCAB037247.
HPA063005.
MIMi602398. phenotype.
606418. gene.
neXtProtiNX_Q15392.
Orphaneti35107. Desmosterolosis.
PharmGKBiPA27320.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0277.
GeneTreeiENSGT00390000008338.
HOGENOMiHOG000243421.
HOVERGENiHBG051349.
InParanoidiQ15392.
KOiK09828.
OMAiKFTHESQ.
OrthoDBiEOG7H7920.
PhylomeDBiQ15392.
TreeFamiTF313170.

Enzyme and pathway databases

UniPathwayiUPA00063.
BRENDAi1.3.1.72. 2681.
ReactomeiREACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSiDHCR24. human.
GeneWikii24-dehydrocholesterol_reductase.
GenomeRNAii1718.
NextBioi35480367.
PROiQ15392.
SOURCEiSearch...

Gene expression databases

BgeeiQ15392.
CleanExiHS_DHCR24.
ExpressionAtlasiQ15392. baseline and differential.
GenevisibleiQ15392. HS.

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]
ProtoNetiSearch...

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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 143 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

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 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.