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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

HSD11B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

An 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei170 – 1701Substrate
Active sitei183 – 1831Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 6727NADP6 PublicationsAdd
BLAST
Nucleotide bindingi92 – 932NADP6 Publications
Nucleotide bindingi119 – 1213NADP6 Publications
Nucleotide bindingi183 – 1875NADP6 Publications
Nucleotide bindingi218 – 2225NADP6 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS04154-MONOMER.
BRENDAi1.1.1.146. 2681.
1.1.1.B40. 2681.
ReactomeiREACT_11036. Glucocorticoid biosynthesis.
SABIO-RKP28845.

Names & Taxonomyi

Protein namesi
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
Short chain dehydrogenase/reductase family 26C member 1
Gene namesi
Name:HSD11B1
Synonyms:HSD11, HSD11L, SDR26C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5208. HSD11B1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76CytoplasmicSequence Analysis
Transmembranei8 – 2417Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 292268LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Cortisone reductase deficiency (CRD)

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

Disease descriptionIn CRD, activation of cortisone to cortisol does not occur, resulting in adrenocorticotropin-mediated androgen excess and a phenotype resembling polycystic ovary syndrome (PCOS).

See also OMIM:604931

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 62KK → RR: Predominantly inverted topology. No effect on activity. 2 Publications
Mutagenesisi5 – 62KK → SS: Inverted topology. Reduced Vmax. 2 Publications
Mutagenesisi5 – 51K → R: Predominantly inverted topology. No effect on activity. 1 Publication
Mutagenesisi5 – 51K → S: Inverted topology. No effect on activity. 1 Publication
Mutagenesisi6 – 61K → R: No effect on topology. Increased Km for corticosterone. 1 Publication
Mutagenesisi6 – 61K → S: No effect on topology or activity. 1 Publication
Mutagenesisi18 – 214YYYY → AAAA: No effect on topology. Reduced Vmax. 1 Publication
Mutagenesisi18 – 214YYYY → FFFF: No effect on topology or activity. 1 Publication
Mutagenesisi19 – 213YYY → AYA: No effect on topology. Reduced Vmax. 1 Publication
Mutagenesisi25 – 262EE → KK: Inverted topology. Reduced Vmax. 1 Publication
Mutagenesisi25 – 262EE → KQ: No effect on topology. Reduced Vmax. 1 Publication
Mutagenesisi25 – 262EE → QQ: Reduced Vmax. 1 Publication
Mutagenesisi25 – 251E → K or Q: No effect on activity. 1 Publication
Mutagenesisi26 – 261E → K: No effect on activity. 1 Publication
Mutagenesisi35 – 362KK → SS: Complete loss of activity. 1 Publication

Organism-specific databases

MIMi604931. phenotype.
Orphaneti168588. Hyperandrogenism due to cortisone reductase deficiency.
PharmGKBiPA29476.

Chemistry

DrugBankiDB00635. Prednisone.

Polymorphism and mutation databases

BioMutaiHSD11B1.
DMDMi118569.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 292291Corticosteroid 11-beta-dehydrogenase isozyme 1PRO_0000054619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi123 – 1231N-linked (GlcNAc...)1 Publication
Glycosylationi162 – 1621N-linked (GlcNAc...)1 Publication
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP28845.
PRIDEiP28845.

PTM databases

PhosphoSiteiP28845.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in liver.

Gene expression databases

BgeeiP28845.
CleanExiHS_HSD11B1.
ExpressionAtlasiP28845. baseline and differential.
GenevisibleiP28845. HS.

Organism-specific databases

HPAiHPA047729.

Interactioni

Subunit structurei

Homodimer.6 Publications

Protein-protein interaction databases

BioGridi109523. 11 interactions.
DIPiDIP-59618N.
IntActiP28845. 1 interaction.
STRINGi9606.ENSP00000261465.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Beta strandi36 – 416Combined sources
Helixi45 – 5612Combined sources
Beta strandi60 – 667Combined sources
Helixi68 – 8114Combined sources
Beta strandi84 – 907Combined sources
Helixi96 – 11015Combined sources
Beta strandi114 – 1185Combined sources
Helixi133 – 14311Combined sources
Helixi145 – 16117Combined sources
Beta strandi164 – 1707Combined sources
Helixi171 – 1733Combined sources
Helixi181 – 20424Combined sources
Beta strandi209 – 2157Combined sources
Helixi221 – 2266Combined sources
Helixi229 – 2346Combined sources
Helixi238 – 25013Combined sources
Beta strandi254 – 2585Combined sources
Helixi262 – 2676Combined sources
Helixi271 – 28010Combined sources
Helixi281 – 2833Combined sources
Helixi287 – 2904Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray2.30A24-285[»]
2IRWX-ray3.10A/B/C/D/E/F/G/H26-289[»]
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/B24-291[»]
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[»]
4C7JX-ray2.16A/B/C/D24-292[»]
4C7KX-ray1.91A/B/C/D24-292[»]
4HFRX-ray2.73A/B24-292[»]
4HX5X-ray2.19A/B/C/D24-292[»]
4IJUX-ray2.35A/B/D/E24-292[»]
4IJVX-ray2.35A/B/D/E24-292[»]
4IJWX-ray2.35A/B/D/E24-292[»]
4K1LX-ray1.96A/B/C/D24-292[»]
4P38X-ray2.80A/B26-290[»]
ProteinModelPortaliP28845.
SMRiP28845. Positions 24-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28845.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00800000124140.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP28845.
KOiK15680.
OMAiFMAYYYY.
OrthoDBiEOG7353X9.
PhylomeDBiP28845.
TreeFamiTF329114.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFMKKYLLP ILGLFMAYYY YSANEEFRPE MLQGKKVIVT GASKGIGREM
60 70 80 90 100
AYHLAKMGAH VVVTARSKET LQKVVSHCLE LGAASAHYIA GTMEDMTFAE
110 120 130 140 150
QFVAQAGKLM GGLDMLILNH ITNTSLNLFH DDIHHVRKSM EVNFLSYVVL
160 170 180 190 200
TVAALPMLKQ SNGSIVVVSS LAGKVAYPMV AAYSASKFAL DGFFSSIRKE
210 220 230 240 250
YSVSRVNVSI TLCVLGLIDT ETAMKAVSGI VHMQAAPKEE CALEIIKGGA
260 270 280 290
LRQEEVYYDS SLWTTLLIRN PCRKILEFLY STSYNMDRFI NK
Length:292
Mass (Da):32,401
Last modified:January 23, 2007 - v3
Checksum:i4632D0F3BBEFC474
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481V → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_035845

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1489.1.
PIRiA41173. DXHUBH.
RefSeqiNP_001193670.1. NM_001206741.1.
NP_005516.1. NM_005525.3.
NP_861420.1. NM_181755.2.
UniGeneiHs.195040.

Genome annotation databases

EnsembliENST00000367027; ENSP00000355994; ENSG00000117594.
ENST00000367028; ENSP00000355995; ENSG00000117594.
GeneIDi3290.
KEGGihsa:3290.
UCSCiuc001hhj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1489.1.
PIRiA41173. DXHUBH.
RefSeqiNP_001193670.1. NM_001206741.1.
NP_005516.1. NM_005525.3.
NP_861420.1. NM_181755.2.
UniGeneiHs.195040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray2.30A24-285[»]
2IRWX-ray3.10A/B/C/D/E/F/G/H26-289[»]
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/B24-291[»]
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[»]
4C7JX-ray2.16A/B/C/D24-292[»]
4C7KX-ray1.91A/B/C/D24-292[»]
4HFRX-ray2.73A/B24-292[»]
4HX5X-ray2.19A/B/C/D24-292[»]
4IJUX-ray2.35A/B/D/E24-292[»]
4IJVX-ray2.35A/B/D/E24-292[»]
4IJWX-ray2.35A/B/D/E24-292[»]
4K1LX-ray1.96A/B/C/D24-292[»]
4P38X-ray2.80A/B26-290[»]
ProteinModelPortaliP28845.
SMRiP28845. Positions 24-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109523. 11 interactions.
DIPiDIP-59618N.
IntActiP28845. 1 interaction.
STRINGi9606.ENSP00000261465.

Chemistry

BindingDBiP28845.
ChEMBLiCHEMBL4235.
DrugBankiDB00635. Prednisone.
GuidetoPHARMACOLOGYi2763.

PTM databases

PhosphoSiteiP28845.

Polymorphism and mutation databases

BioMutaiHSD11B1.
DMDMi118569.

Proteomic databases

PaxDbiP28845.
PRIDEiP28845.

Protocols and materials databases

DNASUi3290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367027; ENSP00000355994; ENSG00000117594.
ENST00000367028; ENSP00000355995; ENSG00000117594.
GeneIDi3290.
KEGGihsa:3290.
UCSCiuc001hhj.3. human.

Organism-specific databases

CTDi3290.
GeneCardsiGC01P209859.
HGNCiHGNC:5208. HSD11B1.
HPAiHPA047729.
MIMi600713. gene.
604931. phenotype.
neXtProtiNX_P28845.
Orphaneti168588. Hyperandrogenism due to cortisone reductase deficiency.
PharmGKBiPA29476.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00800000124140.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP28845.
KOiK15680.
OMAiFMAYYYY.
OrthoDBiEOG7353X9.
PhylomeDBiP28845.
TreeFamiTF329114.

Enzyme and pathway databases

BioCyciMetaCyc:HS04154-MONOMER.
BRENDAi1.1.1.146. 2681.
1.1.1.B40. 2681.
ReactomeiREACT_11036. Glucocorticoid biosynthesis.
SABIO-RKP28845.

Miscellaneous databases

ChiTaRSiHSD11B1. human.
EvolutionaryTraceiP28845.
GeneWikii11%CE%B2-hydroxysteroid_dehydrogenase_type_1.
GenomeRNAii3290.
NextBioi13049.
PROiP28845.
SOURCEiSearch...

Gene expression databases

BgeeiP28845.
CleanExiHS_HSD11B1.
ExpressionAtlasiP28845. baseline and differential.
GenevisibleiP28845. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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.
  12. "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.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-284 IN COMPLEXES WITH ADAMANTANE SULFONE AND SULFONAMIDE INHIBITORS, CATALYTIC ACTIVITY.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-292 IN COMPLEX WITH NADP AND INHIBITOR, SUBUNIT, CATALYTIC ACTIVITY.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
  16. "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.
  17. "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.
  18. "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.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-148.

Entry informationi

Entry nameiDHI1_HUMAN
AccessioniPrimary (citable) accession number: P28845
Secondary accession number(s): B2R9Z1, D3DT89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 163 of the entry and version 3 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.