Reviewed, UniProtKB/Swiss-Prot P28845 (DHI1_HUMAN)

Names and origin

Protein names

Recommended name:
    Corticosteroid 11-beta-dehydrogenase isozyme 1
    EC=1.1.1.146
Alternative name(s):
    11-beta-hydroxysteroid dehydrogenase 1
      Short name=11-beta-HSD1
      Short name=11-DH

Gene names

Name:	HSD11B1
Synonyms:	HSD11, HSD11L

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7-ketocholesterol to 7-beta-hydroxycholesterol By similarity.
Catalytic activity	An 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH. Ref.7 Ref.9 Ref.12 Ref.13
Subunit structure	Homodimer. Ref.13 Ref.11
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Ref.7
Tissue specificity	Widely expressed. Highest expression in liver.
Post-translational modification	Glycosylated. Ref.7 Ref.10
Involvement in disease	Defects in HSD11B1 are a cause of cortisone reductase deficiency (CRD) [MIM:604931]. In CRD, activation of cortisone to cortisol does not occur, resulting in adrenocorticotropin-mediated androgen excess and a phenotype resembling polycystic ovary syndrome (PCOS).
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from Experiment. Source: Reactome
Cellular component	endoplasmic reticulum membrane Ref.1 Inferred from Experiment. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 292

291

Corticosteroid 11-beta-dehydrogenase isozyme 1

PRO_0000054619

Regions

Topological domain

2 – 7

6

Cytoplasmic Potential

Transmembrane

8 – 24

17

Signal-anchor for type II membrane protein Potential

Topological domain

25 – 292

268

Lumenal Potential

Nucleotide binding

41 – 67

27

NADP

Nucleotide binding

92 – 93

2

NADP

Nucleotide binding

119 – 121

3

NADP

Nucleotide binding

183 – 187

5

NADP

Nucleotide binding

218 – 222

5

NADP

Sites

Active site

183

1

Proton acceptor

Binding site

170

1

Substrate

Amino acid modifications

Glycosylation

123

1

N-linked (GlcNAc...) Ref.10

Glycosylation

162

1

N-linked (GlcNAc...) Ref.10

Glycosylation

207

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

148

1

V → E in a breast cancer sample; somatic mutation. Ref.18

VAR_035845

Experimental info

Mutagenesis

5 – 6

2

KK → RR: Predominantly inverted topology. No effect on activity. Ref.7

Mutagenesis

5 – 6

2

KK → SS: Inverted topology. Reduced Vmax. Ref.7

Mutagenesis

5

1

K → R: Predominantly inverted topology. No effect on activity. Ref.7

Mutagenesis

5

1

K → S: Inverted topology. No effect on activity. Ref.7

Mutagenesis

6

1

K → R: No effect on topology. Increased Km for corticosterone. Ref.7

Mutagenesis

6

1

K → S: No effect on topology or activity. Ref.7

Mutagenesis

18 – 21

4

YYYY → AAAA: No effect on topology. Reduced Vmax. Ref.7

Mutagenesis

18 – 21

4

YYYY → FFFF: No effect on topology or activity. Ref.7

Mutagenesis

19 – 21

3

YYY → AYA: No effect on topology. Reduced Vmax. Ref.7

Mutagenesis

25 – 26

2

EE → KK: Inverted topology. Reduced Vmax. Ref.9

Mutagenesis

25 – 26

2

EE → KQ: No effect on topology. Reduced Vmax. Ref.9

Mutagenesis

25 – 26

2

EE → QQ: Reduced Vmax. Ref.9

Mutagenesis

25

1

E → K or Q: No effect on activity. Ref.9

Mutagenesis

26

1

E → K: No effect on activity. Ref.9

Mutagenesis

35 – 36

2

KK → SS: Complete loss of activity.

Secondary structure

1

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292

Helix Strand Turn

Details...

Helix

29 – 32

4

Beta strand

36 – 41

6

Helix

45 – 56

12

Beta strand

60 – 63

4

Helix

68 – 81

14

Beta strand

84 – 88

5

Helix

96 – 110

15

Beta strand

114 – 118

5

Helix

133 – 143

11

Helix

145 – 161

17

Beta strand

164 – 170

7

Helix

171 – 173

3

Helix

181 – 203

23

Beta strand

209 – 215

7

Helix

221 – 226

6

Helix

229 – 234

6

Helix

238 – 250

13

Beta strand

254 – 258

5

Helix

262 – 268

7

Helix

271 – 281

11

Sequences

	Sequence		Length	Mass (Da)
	P28845-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4632D0F3BBEFC474	FASTA	292	32,401
	10 20 30 40 50 60 MAFMKKYLLP ILGLFMAYYY YSANEEFRPE MLQGKKVIVT GASKGIGREM AYHLAKMGAH 70 80 90 100 110 120 VVVTARSKET LQKVVSHCLE LGAASAHYIA GTMEDMTFAE QFVAQAGKLM GGLDMLILNH 130 140 150 160 170 180 ITNTSLNLFH DDIHHVRKSM EVNFLSYVVL TVAALPMLKQ SNGSIVVVSS LAGKVAYPMV 190 200 210 220 230 240 AAYSASKFAL DGFFSSIRKE YSVSRVNVSI TLCVLGLIDT ETAMKAVSGI VHMQAAPKEE 250 260 270 280 290 CALEIIKGGA LRQEEVYYDS SLWTTLLIRN PCRKILEFLY STSYNMDRFI NK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization." Tannin G.M., Agarwal A.K., Monder C., New M.I., White P.C. J. Biol. Chem. 266:16653-16658(1991) [PubMed: 1885595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Testis.
[2]	"Association studies between microsatellite markers within the gene encoding human 11beta-hydroxysteroid dehydrogenase type 1 and body mass index, waist to hip ratio, and glucocorticoid metabolism." Draper N., Echwald S.M., Lavery G.G., Walker E.A., Fraser R., Davies E., Soerensen T.I.A., Astrup A., Adamski J., Hewison M., Connell J.M., Pedersen O., Stewart P.M. J. Clin. Endocrinol. Metab. 87:4984-4990(2002) [PubMed: 12414862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane." Odermatt A., Arnold P., Stauffer A., Frey B.M., Frey F.J. J. Biol. Chem. 274:28762-28770(1999) [PubMed: 10497248] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, MUTAGENESIS OF LYS-5; 5-LYS-LYS-6; LYS-6; 18-TYR--TYR-21 AND 19-TYR--TYR-21.
[8]	"Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency." Draper N., Walker E.A., Bujalska I.J., Tomlinson J.W., Chalder S.M., Arlt W., Lavery G.G., Bedendo O., Ray D.W., Laing I., Malunowicz E., White P.C., Hewison M., Mason P.J., Connell J.M., Shackleton C.H.L., Stewart P.M. Nat. Genet. 34:434-439(2003) [PubMed: 12858176] [Abstract] Cited for: INVOLVEMENT IN CDR.
[9]	"Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase." Frick C., Atanasov A.G., Arnold P., Ozols J., Odermatt A. J. Biol. Chem. 279:31131-31138(2004) [PubMed: 15152005] [Abstract] Cited for: CATALYTIC ACTIVITY, TOPOLOGY, MUTAGENESIS OF 5-LYS-LYS-6; GLU-25; 25-GLU-GLU-26; GLU-26 AND 35-LYS-LYS-36.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-123 AND ASN-162, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Conformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation." Hosfield D.J., Wu Y., Skene R.J., Hilgers M., Jennings A., Snell G.P., Aertgeerts K. J. Biol. Chem. 280:4639-4648(2005) [PubMed: 15513927] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND SUBSTRATE ANALOG, SUBUNIT.
[12]	"Adamantane sulfone and sulfonamide 11-beta-HSD1 Inhibitors." Sorensen B., Winn M., Rohde J., Shuai Q., Wang J., Fung S., Monzon K., Chiou W., Stolarik D., Imade H., Pan L., Deng X., Chovan L., Longenecker K., Judge R., Qin W., Brune M., Camp H. , Frevert E.U., Jacobson P., Link J.T. Bioorg. Med. Chem. Lett. 17:527-532(2007) [PubMed: 17070044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-284 IN COMPLEXES WITH ADAMANTANE SULFONE AND SULFONAMIDE INHIBITORS, CATALYTIC ACTIVITY.
[13]	"The discovery of 2-anilinothiazolones as 11beta-HSD1 inhibitors." Yuan C., St Jean D.J. Jr., Liu Q., Cai L., Li A., Han N., Moniz G., Askew B., Hungate R.W., Johansson L., Tedenborg L., Pyring D., Williams M., Hale C., Chen M., Cupples R., Zhang J., Jordan S. , Bartberger M.D., Sun Y., Emery M., Wang M., Fotsch C. Bioorg. Med. Chem. Lett. 17:6056-6061(2007) [PubMed: 17919905] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-292 IN COMPLEX WITH NADP AND INHIBITOR, SUBUNIT, CATALYTIC ACTIVITY.
[14]	"Pyridine amides as potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type 1." Wang H., Ruan Z., Li J.J., Simpkins L.M., Smirk R.A., Wu S.C., Hutchins R.D., Nirschl D.S., Van Kirk K., Cooper C.B., Sutton J.C., Ma Z., Golla R., Seethala R., Salyan M.E.K., Nayeem A., Krystek S.R. Jr., Sheriff S. , Camac D.M., Morin P.E., Carpenter B., Robl J.A., Zahler R., Gordon D.A., Hamann L.G. Bioorg. Med. Chem. Lett. 18:3168-3172(2008) [PubMed: 18485702] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
[15]	"Structural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor." Hale C., Veniant M., Wang Z., Chen M., McCormick J., Cupples R., Hickman D., Min X., Sudom A., Xu H., Matsumoto G., Fotsch C., St Jean D.J. Jr., Wang M. Chem. Biol. Drug Des. 71:36-44(2008) [PubMed: 18069989] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
[16]	"Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo model." Julian L.D., Wang Z., Bostick T., Caille S., Choi R., DeGraffenreid M., Di Y., He X., Hungate R.W., Jaen J.C., Liu J., Monshouwer M., McMinn D., Rew Y., Sudom A., Sun D., Tu H., Ursu S. , Walker N., Yan X., Ye Q., Powers J.P. J. Med. Chem. 51:3953-3960(2008) [PubMed: 18553955] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
[17]	"Discovery and optimization of piperidyl benzamide derivatives as a novel class of 11beta-HSD1 inhibitors." Rew Y., McMinn D.L., Wang Z., He X., Hungate R.W., Jaen J.C., Sudom A., Sun D., Tu H., Ursu S., Villemure E., Walker N.P.C., Yan X., Ye Q., Powers J.P. Bioorg. Med. Chem. Lett. 19:1797-1801(2009) [PubMed: 19217779] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-148.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M76665 , M76661, M76662, M76663, M76664 Genomic DNA. Translation: AAC31757.1.
AY044084, AY044083 Genomic DNA. Translation: AAK83653.1.
AK313973 mRNA. Translation: BAG36688.1.
AL022398, AL031316 Genomic DNA. Translation: CAA18541.2.
AL031316, AL022398 Genomic DNA. Translation: CAI20063.1.
CH471100 Genomic DNA. Translation: EAW93445.1.
BC012593 mRNA. Translation: AAH12593.1.

IPI

IPI00005682.

PIR

DXHUBH. A41173.

RefSeq

NP_005516.1.
NP_861420.1.

UniGene

Hs.195040

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XU7	X-ray	1.80	A/B/C/D	24-292	[»]
1XU9	X-ray	1.55	A/B/C/D	24-292	[»]
2BEL	X-ray	2.11	A/B/C/D	26-284	[»]
2ILT	X-ray	2.30	A	24-284	[»]
2IRW	X-ray	3.10	A/B/C/D/E/F/G/H	26-288	[»]
2RBE	X-ray	1.90	A/B/C/D	25-292	[»]
3BYZ	X-ray	2.69	A/B/C/D	25-292	[»]
3BZU	X-ray	2.25	A/B/C/D	24-292	[»]
3CH6	X-ray	2.35	A/B/D/E	24-292	[»]
3CZR	X-ray	2.35	A/B	24-292	[»]
3D3E	X-ray	2.60	A/B/C/D	24-292	[»]
3D4N	X-ray	2.50	A/B/C/D	24-292	[»]
3D5Q	X-ray	2.55	A/B/C/D	24-292	[»]
3EY4	X-ray	3.00	A/B/C/D	25-292	[»]
3FRJ	X-ray	2.30	A/B	24-292	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P28845.

Proteomic databases

PRIDE

P28845.

Genome annotation databases

Ensembl

ENST00000261465; ENSP00000261465; ENSG00000117594; Homo sapiens. [Genome view]
ENST00000367027; ENSP00000355994; ENSG00000117594; Homo sapiens. [Genome view]
ENST00000367028; ENSP00000355995; ENSG00000117594; Homo sapiens. [Genome view]

GeneID

3290.

KEGG

hsa:3290.

UCSC

uc001hhj.1. human.

Organism-specific databases

CTD

3290.

GeneCards

GC01P207926.

H-InvDB

HIX0001552.

HGNC

HGNC:5208. HSD11B1.

HPA

CAB003788.

MIM

600713. gene.
604931. phenotype.

Orphanet

168588. Hyperandrogenism due to cortisone reductase deficiency.

PharmGKB

PA29476.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P28845.

HOVERGEN

P28845.

OMA

SSIRTEY.

Enzyme and pathway databases

BRENDA

1.1.1.146. 247.

Reactome

REACT_15314. Hormone biosynthesis.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P28845.

Bgee

P28845.

CleanEx

HS_HSD11B1.

Genevestigator

P28845.

GermOnline

ENSG00000117594. Homo sapiens.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

BindingDB

P28845.

DrugBank

DB00157. NADH.

NextBio

13049.

SOURCE

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Entry information

Entry name

DHI1_HUMAN

Accession

Primary (citable) accession number: P28845
Secondary accession number(s): B2R9Z1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.