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Q04828

- AK1C1_HUMAN

UniProt

Q04828 - AK1C1_HUMAN

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Protein

Aldo-keto reductase family 1 member C1

Gene

AKR1C1

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

Functioni

Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation.2 Publications

Catalytic activityi

17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H.
Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
Indan-1-ol + NAD(P)+ = indanone + NAD(P)H.

Enzyme regulationi

Inhibited by hexestrol with an IC50 of 9.5 µM, 1,10-phenanthroline with an IC50 of 55 µM, 1,7-phenanthroline with an IC50 of 72 µM, flufenamic acid with an IC50 of 6.0 µM, indomethacin with an IC50 of 140 µM, ibuprofen with an IC50 of 950 µM, lithocholic acid with an IC50 of 25 µM, ursodeoxycholic acid with an IC50 of 340 µM and chenodeoxycholic acid with an IC50 of 570 µM.1 Publication

Kineticsi

  1. KM=5 µM for (s)-tetralol2 Publications
  2. KM=38 µM for (s)-indan-1-ol2 Publications
  3. KM=580 µM for benzene dihydrodiol2 Publications
  4. KM=3 µM for 5-beta-pregnane-3-alpha,20-alpha-diol2 Publications
  5. KM=3 µM for 5-beta-pregnan-20-alpha-ol-3-one2 Publications
  6. KM=12 µM for 4-pregnen-20-alpha-ol-3-one2 Publications
  7. KM=133 µM for 9-alpha,11-beta-PGF22 Publications
  8. KM=2 µM for 5-beta-pregnan-3-alpha-ol-20-one2 Publications
  9. KM=1 µM for 5-beta-androstane-3,17-dione2 Publications
  10. KM=12 µM for PGD22 Publications
  11. KM=0.6 µM for 20-alpha-hydroxyprogesterone (with NADH)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate
Binding sitei50 – 501NADP2 Publications
Sitei54 – 541Important for substrate specificityBy similarity
Active sitei55 – 551Proton donorBy similarity
Sitei84 – 841Lowers pKa of active site TyrBy similarity
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei190 – 1901NADP2 Publications
Binding sitei222 – 2221Substrate
Sitei222 – 2221May be involved in the mediating step between the transformation of progesterone and the release of the cofactor
Binding sitei227 – 2271Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 245NADP2 Publications
Nucleotide bindingi166 – 1672NADP2 Publications
Nucleotide bindingi216 – 2227NADP2 Publications
Nucleotide bindingi270 – 28011NADP2 PublicationsAdd
BLAST

GO - Molecular functioni

  1. 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Source: UniProtKB-EC
  2. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
  3. aldo-keto reductase (NADP) activity Source: UniProtKB
  4. androsterone dehydrogenase (B-specific) activity Source: UniProtKB
  5. bile acid binding Source: UniProtKB
  6. carboxylic acid binding Source: UniProtKB
  7. indanol dehydrogenase activity Source: UniProtKB-EC
  8. ketosteroid monooxygenase activity Source: UniProtKB
  9. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
  10. phenanthrene 9,10-monooxygenase activity Source: UniProtKB
  11. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. bile acid and bile salt transport Source: UniProtKB
  2. bile acid metabolic process Source: UniProtKB
  3. cellular response to jasmonic acid stimulus Source: UniProtKB
  4. cholesterol homeostasis Source: UniProtKB
  5. daunorubicin metabolic process Source: UniProtKB
  6. digestion Source: UniProtKB
  7. doxorubicin metabolic process Source: UniProtKB
  8. epithelial cell differentiation Source: UniProt
  9. intestinal cholesterol absorption Source: UniProtKB
  10. oxidation-reduction process Source: UniProtKB
  11. phototransduction, visible light Source: Reactome
  12. progesterone metabolic process Source: UniProtKB
  13. protein homooligomerization Source: UniProtKB
  14. response to organophosphorus Source: UniProtKB
  15. retinal metabolic process Source: UniProtKB
  16. retinoid metabolic process Source: Reactome
  17. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_24968. Retinoid metabolism and transport.
SABIO-RKQ04828.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldo-keto reductase family 1 member C1 (EC:1.1.1.-)
Alternative name(s):
20-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.149)
Short name:
20-alpha-HSD
Chlordecone reductase homolog HAKRC
Dihydrodiol dehydrogenase 1/2
Short name:
DD1/DD2
High-affinity hepatic bile acid-binding protein
Short name:
HBAB
Indanol dehydrogenase (EC:1.1.1.112)
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
Gene namesi
Name:AKR1C1
Synonyms:DDH, DDH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:384. AKR1C1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271E → D: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value. 1 Publication
Mutagenesisi222 – 2221H → I: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH. 1 Publication
Mutagenesisi222 – 2221H → S: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH. 1 Publication
Mutagenesisi304 – 3041R → L: 70-fold decrease in progesterone reduction. No effect on DHT reduction. 1 Publication
Mutagenesisi305 – 3051Y → F: No effect on progesterone reduction. 1 Publication
Mutagenesisi307 – 3071T → V: No effect on progesterone reduction. 1 Publication
Mutagenesisi309 – 3091D → V: No effect on progesterone reduction. 1 Publication

Organism-specific databases

PharmGKBiPA24677.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Aldo-keto reductase family 1 member C1PRO_0000124633Add
BLAST

Proteomic databases

MaxQBiQ04828.
PaxDbiQ04828.
PRIDEiQ04828.

PTM databases

PhosphoSiteiQ04828.

Expressioni

Tissue specificityi

Expressed in all tissues tested including liver, prostate, testis, adrenal gland, brain, uterus, mammary gland and keratinocytes. Highest levels found in liver, mammary gland and brain.1 Publication

Gene expression databases

BgeeiQ04828.
CleanExiHS_AKR1C1.
ExpressionAtlasiQ04828. baseline and differential.
GenevestigatoriQ04828.

Organism-specific databases

HPAiCAB010874.
CAB047303.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi108012. 8 interactions.
IntActiQ04828. 3 interactions.
MINTiMINT-5001209.
STRINGi9606.ENSP00000370254.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Beta strandi15 – 228
Helixi33 – 4412
Beta strandi48 – 503
Helixi53 – 553
Helixi58 – 7013
Helixi76 – 783
Beta strandi80 – 856
Helixi87 – 893
Helixi92 – 10615
Beta strandi111 – 1166
Beta strandi124 – 1263
Helixi144 – 15613
Beta strandi159 – 1679
Helixi170 – 1778
Beta strandi187 – 1926
Beta strandi194 – 1974
Helixi200 – 2089
Beta strandi212 – 2176
Turni225 – 2273
Helixi235 – 2373
Helixi239 – 24810
Helixi252 – 26211
Beta strandi266 – 2705
Helixi274 – 2807
Helixi281 – 2855
Helixi290 – 2978
Helixi309 – 3113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRQX-ray1.59A2-323[»]
3C3UX-ray1.80A1-323[»]
3GUGX-ray1.90A1-323[»]
3NTYX-ray1.87A1-323[»]
ProteinModelPortaliQ04828.
SMRiQ04828. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04828.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiQ04828.
KOiK00089.
K00212.
OMAiEMREDED.
PhylomeDBiQ04828.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04828-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID
60 70 80 90 100
SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE
110 120 130 140 150
RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA
160 170 180 190 200
VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR
210 220 230 240 250
KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR
260 270 280 290 300
TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
310 320
RNVRYLTLDI FAGPPNYPFS DEY
Length:323
Mass (Da):36,788
Last modified:October 1, 1993 - v1
Checksum:i9CB215478FBD29D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → A no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti95 – 951V → D no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti95 – 951V → D in AAD14012. (PubMed:8274401)Curated
Sequence conflicti158 – 1581G → E no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti158 – 1581G → E in AAD14012. (PubMed:8274401)Curated
Sequence conflicti171 – 1722RQ → ST no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti171 – 1722RQ → ST in AAD14012. (PubMed:8274401)Curated
Sequence conflicti183 – 1842KY → QV no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti183 – 1842KY → QV in AAD14012. (PubMed:8274401)Curated
Sequence conflicti222 – 2221H → L no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti222 – 2221H → L in AAD14012. (PubMed:8274401)Curated
Sequence conflicti319 – 3191F → I no nucleotide entry (PubMed:7626489)Curated
Sequence conflicti319 – 3191F → I in AAD14012. (PubMed:8274401)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701R → H.
Corresponds to variant rs17295755 [ dbSNP | Ensembl ].
VAR_048214
Natural varianti172 – 1721Q → L.
Corresponds to variant rs17354444 [ dbSNP | Ensembl ].
VAR_048215

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86609 mRNA. Translation: AAB02880.1.
U05861
, U05853, U05854, U05855, U05857, U05858, U05859, U05860 Genomic DNA. Translation: AAA18115.1.
U05684 mRNA. Translation: AAA16227.1.
AB031083 mRNA. Translation: BAA92883.1.
AB032150 Genomic DNA. Translation: BAA92886.1.
BT007197 mRNA. Translation: AAP35861.1.
AL713867, AC091817 Genomic DNA. Translation: CAI16409.1.
BC015490 mRNA. Translation: AAH15490.1.
BC020216 mRNA. Translation: AAH20216.1.
BC040210 mRNA. Translation: AAH40210.1.
S68290 mRNA. Translation: AAD14012.1.
D26124 mRNA. Translation: BAA05121.1.
CCDSiCCDS7061.1.
PIRiA53436.
I73675.
S59619.
S61515.
RefSeqiNP_001344.2. NM_001353.5.
UniGeneiHs.460260.

Genome annotation databases

EnsembliENST00000380872; ENSP00000370254; ENSG00000187134.
GeneIDi1645.
KEGGihsa:1645.
UCSCiuc001iho.3. human.

Polymorphism databases

DMDMi416877.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86609 mRNA. Translation: AAB02880.1 .
U05861
, U05853 , U05854 , U05855 , U05857 , U05858 , U05859 , U05860 Genomic DNA. Translation: AAA18115.1 .
U05684 mRNA. Translation: AAA16227.1 .
AB031083 mRNA. Translation: BAA92883.1 .
AB032150 Genomic DNA. Translation: BAA92886.1 .
BT007197 mRNA. Translation: AAP35861.1 .
AL713867 , AC091817 Genomic DNA. Translation: CAI16409.1 .
BC015490 mRNA. Translation: AAH15490.1 .
BC020216 mRNA. Translation: AAH20216.1 .
BC040210 mRNA. Translation: AAH40210.1 .
S68290 mRNA. Translation: AAD14012.1 .
D26124 mRNA. Translation: BAA05121.1 .
CCDSi CCDS7061.1.
PIRi A53436.
I73675.
S59619.
S61515.
RefSeqi NP_001344.2. NM_001353.5.
UniGenei Hs.460260.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MRQ X-ray 1.59 A 2-323 [» ]
3C3U X-ray 1.80 A 1-323 [» ]
3GUG X-ray 1.90 A 1-323 [» ]
3NTY X-ray 1.87 A 1-323 [» ]
ProteinModelPortali Q04828.
SMRi Q04828. Positions 2-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108012. 8 interactions.
IntActi Q04828. 3 interactions.
MINTi MINT-5001209.
STRINGi 9606.ENSP00000370254.

Chemistry

BindingDBi Q04828.
ChEMBLi CHEMBL5905.
DrugBanki DB00945. Acetylsalicylic acid.
DB00936. Salicylic acid.

PTM databases

PhosphoSitei Q04828.

Polymorphism databases

DMDMi 416877.

Proteomic databases

MaxQBi Q04828.
PaxDbi Q04828.
PRIDEi Q04828.

Protocols and materials databases

DNASUi 1645.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380872 ; ENSP00000370254 ; ENSG00000187134 .
GeneIDi 1645.
KEGGi hsa:1645.
UCSCi uc001iho.3. human.

Organism-specific databases

CTDi 1645.
GeneCardsi GC10P004934.
HGNCi HGNC:384. AKR1C1.
HPAi CAB010874.
CAB047303.
MIMi 600449. gene.
neXtProti NX_Q04828.
PharmGKBi PA24677.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
GeneTreei ENSGT00760000119041.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi Q04828.
KOi K00089.
K00212.
OMAi EMREDED.
PhylomeDBi Q04828.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_24968. Retinoid metabolism and transport.
SABIO-RK Q04828.

Miscellaneous databases

EvolutionaryTracei Q04828.
GeneWikii AKR1C1.
GenomeRNAii 1645.
NextBioi 6768.
PROi Q04828.
SOURCEi Search...

Gene expression databases

Bgeei Q04828.
CleanExi HS_AKR1C1.
ExpressionAtlasi Q04828. baseline and differential.
Genevestigatori Q04828.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family."
    Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E.
    J. Biol. Chem. 268:10448-10457(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding."
    Lou H., Hammond L., Sharma V., Sparkes R.S., Lusis A.J., Stolz A.
    J. Biol. Chem. 269:8416-8422(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  3. "Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics."
    Ciaccio P.J., Jaiswal A.K., Tew K.D.
    J. Biol. Chem. 269:15558-15562(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  4. "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans."
    Khanna M., Qin K.-N., Cheng K.-C.
    J. Steroid Biochem. Mol. Biol. 53:41-46(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  5. "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes."
    Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.
    Genes Cells 5:111-125(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  6. "Characterization of a human 20alpha-hydroxysteroid dehydrogenase."
    Zhang Y., Dufort I., Rheault P., Luu-The V.
    J. Mol. Endocrinol. 25:221-228(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Skin fibroblast.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Lung and Testis.
  10. "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase."
    Qin K.-N., New M.I., Cheng K.-C.
    J. Steroid Biochem. Mol. Biol. 46:673-679(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-323.
    Tissue: Liver.
  11. "Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells."
    Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y., Ishida N.
    Biochem. J. 313:373-376(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 10-31; 40-61; 69-126; 137-153; 162-206; 209-230; 250-267; 271-289 AND 295-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder."
    Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K., Hara A.
    Biochem. J. 299:545-552(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-323, PROTEIN SEQUENCE OF 18-31; 105-131; 176-193 AND 271-294.
    Tissue: Liver.
  13. "Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids."
    Couture J.-F., Legrand P., Cantin L., Luu-The V., Labrie F., Breton R.
    J. Mol. Biol. 331:593-604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NADP AND 20ALPHA-HYDROXY-PROGESTERONE, MUTAGENESIS OF GLU-127; HIS-222; ARG-304; TYR-305; THR-307 AND ASP-309.
  14. "Probing the inhibitor selectivity pocket of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and site-directed mutagenesis."
    El-Kabbani O., Dhagat U., Soda M., Endo S., Matsunaga T., Hara A.
    Bioorg. Med. Chem. Lett. 21:2564-2567(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH NADP AND 3-CHLORO-5-PHENYLSALICYLIC ACID.

Entry informationi

Entry nameiAK1C1_HUMAN
AccessioniPrimary (citable) accession number: Q04828
Secondary accession number(s): P52896
, Q5SR15, Q7M4N2, Q9UCX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 157 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

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