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P28845 (DHI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 292291Corticosteroid 11-beta-dehydrogenase isozyme 1
PRO_0000054619

Regions

Topological domain2 – 76Cytoplasmic Potential
Transmembrane8 – 2417Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 292268Lumenal Potential
Nucleotide binding41 – 6727NADP
Nucleotide binding92 – 932NADP
Nucleotide binding119 – 1213NADP
Nucleotide binding183 – 1875NADP
Nucleotide binding218 – 2225NADP

Sites

Active site1831Proton acceptor
Binding site1701Substrate

Amino acid modifications

Glycosylation1231N-linked (GlcNAc...) Ref.10
Glycosylation1621N-linked (GlcNAc...) Ref.10
Glycosylation2071N-linked (GlcNAc...) Potential

Natural variations

Natural variant1481V → E in a breast cancer sample; somatic mutation. Ref.18
VAR_035845

Experimental info

Mutagenesis5 – 62KK → RR: Predominantly inverted topology. No effect on activity. Ref.7
Mutagenesis5 – 62KK → SS: Inverted topology. Reduced Vmax. Ref.7
Mutagenesis51K → R: Predominantly inverted topology. No effect on activity. Ref.7
Mutagenesis51K → S: Inverted topology. No effect on activity. Ref.7
Mutagenesis61K → R: No effect on topology. Increased Km for corticosterone. Ref.7
Mutagenesis61K → S: No effect on topology or activity. Ref.7
Mutagenesis18 – 214YYYY → AAAA: No effect on topology. Reduced Vmax. Ref.7
Mutagenesis18 – 214YYYY → FFFF: No effect on topology or activity. Ref.7
Mutagenesis19 – 213YYY → AYA: No effect on topology. Reduced Vmax. Ref.7
Mutagenesis25 – 262EE → KK: Inverted topology. Reduced Vmax. Ref.9
Mutagenesis25 – 262EE → KQ: No effect on topology. Reduced Vmax. Ref.9
Mutagenesis25 – 262EE → QQ: Reduced Vmax. Ref.9
Mutagenesis251E → K or Q: No effect on activity. Ref.9
Mutagenesis261E → K: No effect on activity. Ref.9
Mutagenesis35 – 362KK → SS: Complete loss of activity.

Secondary structure

........................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28845 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4632D0F3BBEFC474

FASTA29232,401
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
PIRDXHUBH. A41173.
RefSeqNP_001193670.1. NM_001206741.1.
NP_005516.1. NM_005525.3.
NP_861420.1. NM_181755.2.
UniGeneHs.195040.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XU7X-ray1.80A/B/C/D24-292[»]
1XU9X-ray1.55A/B/C/D24-292[»]
2BELX-ray2.11A/B/C/D26-284[»]
2ILTX-ray2.30A24-284[»]
2IRWX-ray3.10A/B/C/D/E/F/G/H26-288[»]
2RBEX-ray1.90A/B/C/D25-292[»]
3BYZX-ray2.69A/B/C/D25-292[»]
3BZUX-ray2.25A/B/C/D24-292[»]
3CH6X-ray2.35A/B/D/E24-292[»]
3CZRX-ray2.35A/B24-292[»]
3D3EX-ray2.60A/B/C/D24-292[»]
3D4NX-ray2.50A/B/C/D24-292[»]
3D5QX-ray2.55A/B/C/D24-292[»]
3EY4X-ray3.00A/B/C/D25-292[»]
3FCOX-ray2.65A/B24-292[»]
3FRJX-ray2.30A/B24-292[»]
3H6KX-ray2.19A/B/C/D24-292[»]
3HFGX-ray2.30A/B/C/D24-292[»]
3OQ1X-ray2.60A/B/C/D24-292[»]
3PDJX-ray2.30A/B24-292[»]
3QQPX-ray2.72A/B/C/D24-292[»]
3TFQX-ray1.80A/B/D/E24-292[»]
4BB5X-ray2.20A/B/C/D1-292[»]
4BB6X-ray2.55A/B1-292[»]
4C7KX-ray1.91A/B/C/D24-292[»]
4HFRX-ray2.73A/B24-292[»]
4HX5X-ray2.19A/B/C/D24-292[»]
ProteinModelPortalP28845.
SMRP28845. Positions 26-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109523. 2 interactions.
DIPDIP-59618N.
IntActP28845. 1 interaction.
STRING9606.ENSP00000261465.

Chemistry

BindingDBP28845.
ChEMBLCHEMBL4235.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP28845.

Polymorphism databases

DMDM118569.

Proteomic databases

PaxDbP28845.
PRIDEP28845.

Protocols and materials databases

DNASU3290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261465; ENSP00000261465; ENSG00000117594.
ENST00000367027; ENSP00000355994; ENSG00000117594.
ENST00000367028; ENSP00000355995; ENSG00000117594.
GeneID3290.
KEGGhsa:3290.
UCSCuc001hhj.3. human.

Organism-specific databases

CTD3290.
GeneCardsGC01P209859.
HGNCHGNC:5208. HSD11B1.
HPAHPA047729.
MIM600713. gene.
604931. phenotype.
neXtProtNX_P28845.
Orphanet168588. Hyperandrogenism due to cortisone reductase deficiency.
PharmGKBPA29476.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOGENOMHOG000010276.
HOVERGENHBG005481.
InParanoidP28845.
KOK15680.
OMAGLFMAYY.
OrthoDBEOG7353X9.
PhylomeDBP28845.
TreeFamTF329114.

Enzyme and pathway databases

BRENDA1.1.1.146. 2681.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
SABIO-RKP28845.

Gene expression databases

BgeeP28845.
CleanExHS_HSD11B1.
GenevestigatorP28845.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28845.
GeneWiki11%CE%B2-hydroxysteroid_dehydrogenase_type_1.
GenomeRNAi3290.
NextBio13049.
PROP28845.
SOURCESearch...

Entry information

Entry nameDHI1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM