Q9UBM7 (DHCR7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
7-dehydrocholesterol reductase
Short name=7-DHC reductase
EC=1.3.1.21

Alternative name(s):
Putative sterol reductase SR-2
Sterol Delta(7)-reductase

Gene names

Name:	DHCR7
Synonyms:	D7SR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).
Catalytic activity	Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH.
Pathway	Steroid biosynthesis; cholesterol biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3.
Tissue specificity	Most abundant in adrenal gland, liver, testis, and brain. Ref.3
Involvement in disease	Smith-Lemli-Opitz syndrome (SLOS) [MIM:270400]: An autosomal recessive frequent inborn disorder of sterol metabolism with characteristic congenital malformations and mental retardation. Children with SLOS have elevated serum 7-dehydrocholesterol (7-DHC) levels and low serum cholesterol levels. SLOS occurs in relatively high frequency: approximately 1 in 20,000 to 30,000 births in populations of northern and central European background. Historically, a clinical distinction often was made between classic ('type I') SLOS and the more severely affected ('type II') patients. There is, in reality, a clinical and biochemical continuum from mild to severe SLOS. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the ERG4/ERG24 family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Cholesterol metabolism Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel development Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: Compara cholesterol biosynthetic process Inferred from mutant phenotype Ref.2. Source: UniProtKB lung development Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of cholesterol biosynthetic process Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear outer membrane Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	7-dehydrocholesterol reductase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 475	475	7-dehydrocholesterol reductase		PRO_0000207502
Regions
	Transmembrane	40 – 60	21	Helical; Potential
	Transmembrane	154 – 174	21	Helical; Potential
	Transmembrane	177 – 197	21	Helical; Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Transmembrane	306 – 326	21	Helical; Potential
	Transmembrane	331 – 351	21	Helical; Potential
	Transmembrane	420 – 440	21	Helical; Potential
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
Natural variations
	Natural variant	5	1	S → L. Ref.2 Ref.4 Corresponds to variant rs1127869 [ dbSNP | Ensembl ].		VAR_067456
	Natural variant	51	1	P → S in SLOS. Ref.13 Ref.14		VAR_012717
	Natural variant	68	1	L → P in SLOS. Ref.19		VAR_023148
	Natural variant	93	1	T → M in SLOS. Ref.13 Ref.14 Ref.16 Ref.17		VAR_012718
	Natural variant	99	1	L → P in SLOS. Ref.13 Ref.14		VAR_012719
	Natural variant	107	1	Q → H in SLOS. Ref.14		VAR_023149
	Natural variant	109	1	L → P in SLOS. Ref.14 Ref.16		VAR_023150
	Natural variant	113	1	S → C in SLOS. Ref.19		VAR_023151
	Natural variant	119	1	H → L in SLOS. Ref.1 Ref.16 Corresponds to variant rs28938174 [ dbSNP | Ensembl ].		VAR_012720
	Natural variant	138	1	G → V in SLOS. Ref.19		VAR_023152
	Natural variant	145	1	I → L in SLOS. Ref.19		VAR_023153
	Natural variant	147	1	G → D in SLOS. Ref.14		VAR_023154
	Natural variant	154	1	T → M in SLOS. Ref.14 Ref.16		VAR_023155
	Natural variant	157	1	L → P in SLOS. Ref.13 Ref.14		VAR_012721
	Natural variant	169	1	S → L in SLOS. Ref.14		VAR_023156
	Natural variant	182	1	W → C in SLOS. Ref.14		VAR_023157
	Natural variant	182	1	W → L in SLOS. Ref.16		VAR_023158
	Natural variant	183	1	C → Y in SLOS. Ref.16		VAR_023159
	Natural variant	198	1	K → E in SLOS. Ref.16		VAR_023160
	Natural variant	235	1	F → S in SLOS. Ref.19		VAR_023161
	Natural variant	242	1	R → C in SLOS. Ref.14 Ref.19		VAR_023162
	Natural variant	242	1	R → H in SLOS. Ref.16		VAR_023163
	Natural variant	244	1	G → R in SLOS. Ref.1 Ref.16		VAR_012722
	Natural variant	247	1	A → V in SLOS. Ref.13 Ref.14		VAR_012723
	Natural variant	248	1	W → C in SLOS. Ref.1 Ref.16 Corresponds to variant rs28939698 [ dbSNP | Ensembl ].		VAR_012724
	Natural variant	255	1	F → L in SLOS. Ref.16		VAR_023164
	Natural variant	281	1	V → M in SLOS. Ref.14		VAR_023165
	Natural variant	289	1	T → I in SLOS. Ref.14 Ref.15		VAR_012725
	Natural variant	297	1	I → T in SLOS. Ref.19		VAR_023166
	Natural variant	311	1	C → G in SLOS. Ref.14		VAR_023167
	Natural variant	311	1	C → Y in SLOS. Ref.14		VAR_023168
	Natural variant	324	1	Y → H in SLOS. Ref.14		VAR_023169
	Natural variant	326	1	V → L in SLOS. Ref.13 Ref.14 Ref.17		VAR_012726
	Natural variant	344	1	G → R in SLOS. Ref.19		VAR_023170
	Natural variant	352	1	R → Q in SLOS. Ref.14		VAR_023171
	Natural variant	352	1	R → W in SLOS. Ref.13 Ref.14 Ref.17		VAR_012727
	Natural variant	353	1	V → A in SLOS. Ref.14		VAR_023172
	Natural variant	362	1	R → C in SLOS. Ref.14		VAR_023173
	Natural variant	380	1	C → R in SLOS. Ref.14		VAR_023174
	Natural variant	380	1	C → S in SLOS. Ref.13 Ref.14		VAR_012728
	Natural variant	380	1	C → Y in SLOS. Ref.14		VAR_023175
	Natural variant	397	1	S → L in SLOS. Ref.14		VAR_023176
	Natural variant	404	1	R → C in SLOS. Ref.13 Ref.14 Ref.17 Ref.19		VAR_012729
	Natural variant	404	1	R → S in SLOS. Ref.14		VAR_023177
	Natural variant	405	1	H → Y in SLOS. Ref.19		VAR_023178
	Natural variant	408	1	Y → H in SLOS. Ref.14 Ref.19		VAR_023179
	Natural variant	410	1	G → R in SLOS. Ref.14		VAR_023180
	Natural variant	410	1	G → S in SLOS. Ref.13 Ref.14		VAR_012730
	Natural variant	425	1	G → S. Corresponds to variant rs760242 [ dbSNP | Ensembl ].		VAR_052154
	Natural variant	426	1	H → P in SLOS. Ref.19		VAR_023181
	Natural variant	443	1	R → C in SLOS. Ref.14		VAR_023182
	Natural variant	446	1	R → Q in SLOS. Ref.14		VAR_023183
	Natural variant	448	1	E → K in SLOS; mild. Ref.14 Ref.18		VAR_016975
	Natural variant	448	1	E → Q in SLOS. Ref.14		VAR_023184
	Natural variant	450	1	R → L in SLOS. Ref.14		VAR_023185
Experimental info
	Sequence conflict	14	1	S → A in AAC18345. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9UBM7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7D726443834C4EEB	FASTA	475	54,489
	10 20 30 40 50 60 MAAKSQPNIP KAKSLDGVTN DRTASQGQWG RAWEVDWFSL ASVIFLLLFA PFIVYYFIMA 70 80 90 100 110 120 CDQYSCALTG PVVDIVTGHA RLSDIWAKTP PITRKAAQLY TLWVTFQVLL YTSLPDFCHK 130 140 150 160 170 180 FLPGYVGGIQ EGAVTPAGVV NKYQINGLQA WLLTHLLWFA NAHLLSWFSP TIIFDNWIPL 190 200 210 220 230 240 LWCANILGYA VSTFAMVKGY FFPTSARDCK FTGNFFYNYM MGIEFNPRIG KWFDFKLFFN 250 260 270 280 290 300 GRPGIVAWTL INLSFAAKQR ELHSHVTNAM VLVNVLQAIY VIDFFWNETW YLKTIDICHD 310 320 330 340 350 360 HFGWYLGWGD CVWLPYLYTL QGLYLVYHPV QLSTPHAVGV LLLGLVGYYI FRVANHQKDL 370 380 390 400 410 420 FRRTDGRCLI WGRKPKVIEC SYTSADGQRH HSKLLVSGFW GVARHFNYVG DLMGSLAYCL 430 440 450 460 470 ACGGGHLLPY FYIIYMAILL THRCLRDEHR CASKYGRDWE RYTAAVPYRL LPGIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene." Waterham H.R., Wijburg F.A., Hennekam R.C.M., Vreken P., Poll-The B.T., Dorland L., Duran M., Jira P.E., Smeitink J.A.M., Wevers R.A., Wanders R.J.A. Am. J. Hum. Genet. 63:329-338(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SLOS LEU-119; ARG-244 AND CYS-248.
[2]	"Molecular cloning and expression of the human delta7-sterol reductase." Moebius F.F., Fitzky B.U., Lee J.N., Paik Y.K., Glossmann H. Proc. Natl. Acad. Sci. U.S.A. 95:1899-1902(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT LEU-5. Tissue: Liver.
[3]	"The human lamin B receptor/sterol reductase multigene family." Holmer L., Pezhman A., Worman H.J. Genomics 54:469-476(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"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], VARIANT LEU-5. Tissue: Testis.
[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: Brain.
[6]	"Mutations in the human sterol delta 7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome." Wassif C.A., Maslen C., Kachilele-Linjewile S., Lin D., Linck L.M., Conner W.E., Steiner R.D., Porter F.D. Am. J. Hum. Genet. 63:55-62(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-475. Tissue: Liver.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY.
[13]	"Mutations in the delta7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome." Fitzky B.U., Witsch-Baumgartner M., Erdel M., Lee J.N., Paik Y.-K., Glossmann H., Utermann G., Moebius F.F. Proc. Natl. Acad. Sci. U.S.A. 95:8181-8186(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SLOS SER-51; MET-93; PRO-99; PRO-157; VAL-247; LEU-326; TRP-352; SER-380; CYS-404 AND SER-410.
[14]	"Mutational spectrum in the Delta7-sterol reductase gene and genotype-phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome." Witsch-Baumgartner M., Fitzky B.U., Ogorelkova M., Kraft H.G., Moebius F.F., Glossmann H., Seedorf U., Gillessen-Kaesbach G., Hoffmann G.F., Clayton P., Kelley R.I., Utermann G. Am. J. Hum. Genet. 66:402-412(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SLOS SER-51; MET-93; PRO-99; HIS-107; PRO-109; ASP-147; MET-154; PRO-157; LEU-169; CYS-182; CYS-242; VAL-247; MET-281; ILE-289; GLY-311; TYR-311; HIS-324; LEU-326; GLN-352; TRP-352; ALA-353; CYS-362; TYR-380; ARG-380; SER-380; LEU-397; CYS-404; SER-404; HIS-408; SER-410; ARG-410; CYS-443; GLN-446; GLN-448; LYS-448 AND LEU-450.
[15]	"Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz syndrome patients: polymerase chain reaction-based assays to simplify genotyping." Krakowiak P.A., Nwokoro N.A., Wassif C.A., Battaile K.P., Nowaczyk M.J.M., Connor W.E., Maslen C., Steiner R.D., Porter F.D. Am. J. Med. Genet. 94:214-227(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SLOS ILE-289.
[16]	"Novel mutations in the 7-dehydrocholesterol reductase gene of 13 patients with Smith-Lemli-Opitz syndrome." Jira P.E., Wanders R.J.A., Smeitink J.A.M., De Jong J., Wevers R.A., Oostheim W., Tuerlings J.H.A.M., Hennekam R.C.M., Sengers R.C.A., Waterham H.R. Ann. Hum. Genet. 65:229-236(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SLOS MET-93; PRO-109; LEU-119; MET-154; LEU-182; TYR-183; GLU-198; HIS-242; ARG-244; CYS-248 AND LEU-255.
[17]	"Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz syndrome in Europe: evidence for different origins of common mutations." Witsch-Baumgartner M., Ciara E., Loffler J., Menzel H.J., Seedorf U., Burn J., Gillessen-Kaesbach G., Hoffmann G.F., Fitzky B.U., Mundy H., Clayton P., Kelley R.I., Krajewska-Walasek M., Utermann G. Eur. J. Hum. Genet. 9:45-50(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SLOS MET-93; LEU-326; TRP-352 AND CYS-404.
[18]	"Identification of three patients with a very mild form of Smith-Lemli-Opitz syndrome." Langius F.A., Waterham H.R., Romeijn G.J., Oostheim W., de Barse M.M., Dorland L., Duran M., Beemer F.A., Wanders R.J., Poll-The B.T. Am. J. Med. Genet. A 122:24-29(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SLOS LYS-448.
[19]	"Identification of nine novel DHCR7 missense mutations in patients with Smith-Lemli-Opitz syndrome (SLOS)." Waye J.S., Krakowiak P.A., Wassif C.A., Sterner A.L., Eng B., Nakamura L.M., Nowaczyk M.J.M., Porter F.D. Hum. Mutat. 26:59-59(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SLOS PRO-68; CYS-113; VAL-138; LEU-145; SER-235; CYS-242; THR-297; ARG-344; CYS-404; TYR-405; HIS-408 AND PRO-426.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF096305 mRNA. Translation: AAD09766.1. AF034544 mRNA. Translation: AAC05086.1. AF110060 Genomic DNA. Translation: AAD24762.1. AF067127 mRNA. Translation: AAD02816.1. AK312775 mRNA. Translation: BAG35639.1. BC000054 mRNA. Translation: AAH00054.1. AF062481 mRNA. Translation: AAC18345.1.
IPI	IPI00294501.
RefSeq	NP_001157289.1. NM_001163817.1. NP_001351.2. NM_001360.2.
UniGene	Hs.503134.
3D structure databases
ProteinModelPortal	Q9UBM7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBM7. 3 interactions.
STRING	9606.ENSP00000347717.
PTM databases
PhosphoSite	Q9UBM7.
Polymorphism databases
DMDM	20138066.
Proteomic databases
PaxDb	Q9UBM7.
PeptideAtlas	Q9UBM7.
PRIDE	Q9UBM7.
Protocols and materials databases
DNASU	1717.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355527; ENSP00000347717; ENSG00000172893. ENST00000407721; ENSP00000384739; ENSG00000172893.
GeneID	1717.
KEGG	hsa:1717.
UCSC	uc001oqk.3. human.
Organism-specific databases
CTD	1717.
GeneCards	GC11M071145.
HGNC	HGNC:2860. DHCR7.
HPA	HPA044280.
MIM	270400. phenotype. 602858. gene.
neXtProt	NX_Q9UBM7.
Orphanet	818. Smith-Lemli-Opitz syndrome.
PharmGKB	PA27321.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG72042.
HOGENOM	HOG000193296.
HOVERGEN	HBG007825.
InParanoid	Q9UBM7.
KO	K00213.
OMA	IIYMTIL.
OrthoDB	EOG4GQQ4Q.
PhylomeDB	Q9UBM7.
Enzyme and pathway databases
BioCyc	MetaCyc:HS10588-MONOMER.
BRENDA	1.3.1.21. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00063.
Gene expression databases
ArrayExpress	Q9UBM7.
Bgee	Q9UBM7.
CleanEx	HS_DHCR7.
Genevestigator	Q9UBM7.
GermOnline	ENSG00000172893. Homo sapiens.
Family and domain databases
InterPro	IPR001171. Ergosterol_biosynth_ERG4_ERG24. IPR018083. Sterol_reductase_CS. [Graphical view]
Pfam	PF01222. ERG4_ERG24. 1 hit. [Graphical view]
PROSITE	PS01017. STEROL_REDUCT_1. 1 hit. PS01018. STEROL_REDUCT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00157. NADH.
GenomeRNAi	1717.
NextBio	6956.
SOURCE	Search...

Entry information

Entry name

DHCR7_HUMAN

Accession

Primary (citable) accession number: Q9UBM7
Secondary accession number(s): B2R6Z2, O60492, O60717

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.