P28845 (DHI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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-DH
Short name=11-beta-HSD1

Gene names

Name:	HSD11B1
Synonyms:	HSD11, HSD11L

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	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.11 Ref.13
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
Involvement in disease	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). Note: The disease is caused by mutations affecting the gene represented in this entry.
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 Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucocorticoid biosynthetic process Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Traceable author statement. Source: Reactome nucleotide 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

Helical; 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 – 66

7

Helix

68 – 81

14

Beta strand

84 – 90

7

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 – 204

24

Beta strand

209 – 215

7

Helix

221 – 226

6

Helix

229 – 234

6

Helix

238 – 250

13

Beta strand

254 – 258

5

Helix

262 – 267

6

Helix

271 – 280

10

Helix

281 – 283

3

Helix

286 – 288

3

Sequences

	Sequence		Length	Mass (Da)
	P28845 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-148.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CH471100 Genomic DNA. Translation: EAW93446.1.
BC012593 mRNA. Translation: AAH12593.1.

IPI

IPI00005682.

PIR

DXHUBH. A41173.

RefSeq

NP_001193670.1. NM_001206741.1.
NP_005516.1. NM_005525.3.
NP_861420.1. NM_181755.2.

UniGene

Hs.195040.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3FCO	X-ray	2.65	A/B	24-292	[»]
3FRJ	X-ray	2.30	A/B	24-292	[»]
3H6K	X-ray	2.19	A/B/C/D	24-292	[»]
3HFG	X-ray	2.30	A/B/C/D	24-292	[»]
3OQ1	X-ray	2.60	A/B/C/D	24-292	[»]
3PDJ	X-ray	2.30	A/B	24-292	[»]
3QQP	X-ray	2.72	A/B/C/D	24-292	[»]
3TFQ	X-ray	1.80	A/B/D/E	24-292	[»]
4BB5	X-ray	2.20	A/B/C/D	1-292	[»]
4BB6	X-ray	2.55	A/B	1-292	[»]
4HFR	X-ray	2.73	A/B	24-292	[»]

ProteinModelPortal

P28845.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59618N.

IntAct

P28845. 1 interaction.

STRING

9606.ENSP00000261465.

PTM databases

PhosphoSite

P28845.

Polymorphism databases

DMDM

118569.

Proteomic databases

PaxDb

P28845.

PRIDE

P28845.

Protocols and materials databases

DNASU

3290.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000261465; ENSP00000261465; ENSG00000117594.
ENST00000367027; ENSP00000355994; ENSG00000117594.
ENST00000367028; ENSP00000355995; ENSG00000117594.

GeneID

3290.

KEGG

hsa:3290.

UCSC

uc001hhj.3. human.

Organism-specific databases

CTD

3290.

GeneCards

GC01P209859.

HGNC

HGNC:5208. HSD11B1.

HPA

HPA047729.

MIM

600713. gene.
604931. phenotype.

neXtProt

NX_P28845.

Orphanet

168588. Hyperandrogenism due to cortisone reductase deficiency.

PharmGKB

PA29476.

GenAtlas

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Phylogenomic databases

eggNOG

COG1028.

HOGENOM

HOG000010276.

HOVERGEN

HBG005481.

InParanoid

P28845.

KO

K15680.

OMA

SAIRKEH.

OrthoDB

EOG405S1K.

PhylomeDB

P28845.

Enzyme and pathway databases

BRENDA

1.1.1.146. 2681.

Reactome

REACT_111217. Metabolism.
REACT_15493. Steroid hormones.

SABIO-RK

P28845.

Gene expression databases

Bgee

P28845.

CleanEx

HS_HSD11B1.

Genevestigator

P28845.

GermOnline

ENSG00000117594. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

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

BindingDB

P28845.

ChEMBL

CHEMBL4235.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P28845.

GenomeRNAi

3290.

NextBio

13049.

SOURCE

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Entry information

Entry name

DHI1_HUMAN

Accession

Primary (citable) accession number: P28845
Secondary accession number(s): B2R9Z1, D3DT89

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 137 of the entry and version 3 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.