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P52895

- AK1C2_HUMAN

UniProt

P52895 - AK1C2_HUMAN

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Protein
Aldo-keto reductase family 1 member C2
Gene
AKR1C2, DDH2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.4 Publications

Catalytic activityi

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.4 Publications
A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.4 Publications

Enzyme regulationi

Inhibited by hexestrol with an IC50 of 2.8 µM, 1,10-phenanthroline with an IC50 of 2100 µM, 1,7-phenanthroline with an IC50 of 1500 µM, flufenamic acid with an IC50 of 0.9 µM, indomethacin with an IC50 of 75 µM, ibuprofen with an IC50 of 6.9 µM, lithocholic acid with an IC50 of 0.07 µM, ursodeoxycholic acid with an IC50 of 0.08 µM and chenodeoxycholic acid with an IC50 of 0.13 µM.1 Publication

Kineticsi

  1. KM=260 µM for (s)-tetralol1 Publication
  2. KM=520 µM for (s)-indan-1-ol
  3. KM=5000 µM for benzene dihydrodiol
  4. KM=1 µM for 5-beta-pregnane-3-alpha,20-alpha-diol
  5. KM=208 µM for 9-alpha,11-beta-PGF2
  6. KM=0.3 µM for 5-beta-androstane-3,17-dione
  7. KM=79 µM for PGD2

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate By similarity
Binding sitei50 – 501NADP
Active sitei55 – 551Proton donor
Sitei84 – 841Lowers pKa of active site Tyr By similarity
Binding sitei117 – 1171Substrate
Binding sitei190 – 1901NADP
Binding sitei222 – 2221Substrate By similarity
Binding sitei227 – 2271Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 245NADP
Nucleotide bindingi166 – 1672NADP
Nucleotide bindingi216 – 2227NADP
Nucleotide bindingi270 – 28011NADP
Add
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
  2. bile acid binding Source: UniProtKB
  3. carboxylic acid binding Source: UniProtKB
  4. ketosteroid monooxygenase activity Source: UniProtKB
  5. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
  6. phenanthrene 9,10-monooxygenase activity Source: UniProtKB
  7. prostaglandin F receptor activity Source: UniProtKB
  8. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: UniProtKB
  2. cellular response to jasmonic acid stimulus Source: UniProtKB
  3. daunorubicin metabolic process Source: UniProtKB
  4. digestion Source: UniProtKB
  5. doxorubicin metabolic process Source: UniProtKB
  6. epithelial cell differentiation Source: UniProt
  7. oxidation-reduction process Source: UniProtKB
  8. positive regulation of cell proliferation Source: UniProtKB
  9. positive regulation of protein kinase B signaling Source: UniProtKB
  10. progesterone metabolic process Source: UniProtKB
  11. prostaglandin metabolic process Source: UniProtKB
  12. response to prostaglandin Source: UniProtKB
  13. steroid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS07754-MONOMER.
BRENDAi1.1.1.213. 2681.
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.
SABIO-RKP52895.
SignaLinkiP52895.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldo-keto reductase family 1 member C2 (EC:1.-.-.-)
Alternative name(s):
3-alpha-HSD3
Chlordecone reductase homolog HAKRD
Dihydrodiol dehydrogenase 2
Short name:
DD-2
Short name:
DD2
Dihydrodiol dehydrogenase/bile acid-binding protein
Short name:
DD/BABP
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
Type III 3-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.357)
Gene namesi
Name:AKR1C2
Synonyms:DDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:385. AKR1C2.

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791I → V in SRXY8; partially impaired activity. 1 Publication
VAR_066632
Natural varianti90 – 901H → Q in SRXY8; partially impaired activity. 1 Publication
VAR_066633
Natural varianti222 – 2221H → Q in SRXY8; partially impaired activity. 1 Publication
VAR_066634
Natural varianti300 – 3001N → T in SRXY8; partially impaired activity. 1 Publication
VAR_066635

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241Y → A: Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold. 1 Publication
Mutagenesisi31 – 311K → A or M: Increases the low androstenedione reductase activity. 1 Publication
Mutagenesisi301 – 3011R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold. 1 Publication
Mutagenesisi304 – 3041R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614279. phenotype.
Orphaneti90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
PharmGKBiPA24678.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Aldo-keto reductase family 1 member C2
PRO_0000124637Add
BLAST

Proteomic databases

MaxQBiP52895.
PaxDbiP52895.
PRIDEiP52895.

PTM databases

PhosphoSiteiP52895.

Expressioni

Tissue specificityi

Expressed in fetal testes. Expressed in fetal and adult adrenal glands.1 Publication

Gene expression databases

ArrayExpressiP52895.
BgeeiP52895.
CleanExiHS_AKR1C2.
GenevestigatoriP52895.

Organism-specific databases

HPAiCAB047304.

Interactioni

Protein-protein interaction databases

BioGridi108013. 1 interaction.
IntActiP52895. 1 interaction.
STRINGi9606.ENSP00000370129.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Beta strandi15 – 228
Helixi32 – 4413
Beta strandi48 – 503
Helixi53 – 553
Helixi58 – 7013
Helixi76 – 783
Beta strandi80 – 856
Helixi87 – 893
Helixi92 – 943
Helixi95 – 10612
Beta strandi111 – 1166
Beta strandi119 – 1224
Beta strandi124 – 1263
Helixi144 – 15613
Beta strandi159 – 1679
Helixi170 – 1778
Beta strandi187 – 1926
Helixi200 – 2089
Beta strandi212 – 2176
Turni225 – 2273
Helixi235 – 2373
Helixi239 – 24810
Helixi252 – 26211
Beta strandi266 – 2705
Helixi274 – 2807
Helixi281 – 2855
Helixi290 – 2978
Helixi309 – 3113
Beta strandi318 – 3214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHIX-ray3.00A/B1-323[»]
1J96X-ray1.25A/B2-323[»]
1XJBX-ray1.90A/B2-323[»]
2HDJX-ray2.00A/B1-323[»]
2IPJX-ray1.80A/B3-323[»]
4JQ1X-ray1.60A/B1-323[»]
4JQ2X-ray1.75A/B1-323[»]
4JQ3X-ray1.75A/B1-323[»]
4JQ4X-ray1.52A/B1-323[»]
4JQAX-ray1.45A/B1-323[»]
4JTQX-ray1.60A/B1-323[»]
4JTRX-ray1.30A/B1-323[»]
4L1WX-ray2.20A/B2-323[»]
4L1XX-ray2.00A/B2-323[»]
ProteinModelPortaliP52895.
SMRiP52895. Positions 2-323.

Miscellaneous databases

EvolutionaryTraceiP52895.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP52895.
KOiK00089.
K00212.
OMAiYTSKLWI.
PhylomeDBiP52895.
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.
PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52895-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID    50
SAHVYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE 100
RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA 150
MEKCKDAGLA KSIGVSNFNH RLLEMILNKP GLKYKPVCNQ VECHPYFNQR 200
KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR 250
TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN 300
RNVRYLTLDI FAGPPNYPFS DEY 323
Length:323
Mass (Da):36,735
Last modified:May 10, 2002 - v3
Checksum:i0D7B6F983FCE85E1
GO
Isoform 2 (identifier: P52895-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-139: PGEEVIPKDENGKILF → EDIGILTWKKSPKHNS
     140-323: Missing.

Note: No experimental confirmation available.

Show »
Length:139
Mass (Da):15,748
Checksum:i11CAE1B299B378AC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461F → Y.1 Publication
Corresponds to variant rs2854482 [ dbSNP | Ensembl ].
VAR_048216
Natural varianti79 – 791I → V in SRXY8; partially impaired activity. 1 Publication
VAR_066632
Natural varianti90 – 901H → Q in SRXY8; partially impaired activity. 1 Publication
VAR_066633
Natural varianti172 – 1721L → Q.
Corresponds to variant rs11474 [ dbSNP | Ensembl ].
VAR_014748
Natural varianti222 – 2221H → Q in SRXY8; partially impaired activity. 1 Publication
VAR_066634
Natural varianti300 – 3001N → T in SRXY8; partially impaired activity. 1 Publication
VAR_066635

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei124 – 13916PGEEV…GKILF → EDIGILTWKKSPKHNS in isoform 2.
VSP_043779Add
BLAST
Alternative sequencei140 – 323184Missing in isoform 2.
VSP_043780Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761R → S AA sequence 1 Publication
Sequence conflicti87 – 871S → C AA sequence 1 Publication
Sequence conflicti93 – 931E → EE AA sequence 1 Publication
Sequence conflicti111 – 1111V → A in AAB38486. 1 Publication
Sequence conflicti164 – 1641G → R in BAF82993. 1 Publication
Sequence conflicti179 – 1791K → E in AAD14013. 1 Publication
Sequence conflicti179 – 1791K → E in AAB38486. 1 Publication
Sequence conflicti185 – 1851K → E in AAD14013. 1 Publication
Sequence conflicti185 – 1851K → E in AAB38486. 1 Publication
Sequence conflicti188 – 1881C → H AA sequence 1 Publication
Sequence conflicti193 – 1931C → H AA sequence 1 Publication
Sequence conflicti319 – 3191F → I in AAD14013. 1 Publication
Sequence conflicti319 – 3191F → I in AAB38486. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68330 mRNA. Translation: AAD14013.1.
U05598 mRNA. Translation: AAA20937.1.
L32592 Genomic DNA. Translation: AAB38486.1.
AB021654 mRNA. Translation: BAA36169.1.
AB031084 mRNA. Translation: BAA92884.1.
AB032153 Genomic DNA. Translation: BAA92891.1.
AK290304 mRNA. Translation: BAF82993.1.
AK296686 mRNA. Translation: BAG59281.1.
BT006653 mRNA. Translation: AAP35299.1.
AL713867, AL391427 Genomic DNA. Translation: CAI16408.1.
BC007024 mRNA. Translation: AAH07024.1.
BC063574 mRNA. Translation: AAH63574.1.
CCDSiCCDS44350.1. [P52895-2]
CCDS7062.1. [P52895-1]
PIRiI73676.
JC5240.
S61516.
RefSeqiNP_001128713.1. NM_001135241.2. [P52895-2]
NP_001345.1. NM_001354.5. [P52895-1]
NP_995317.1. NM_205845.2. [P52895-1]
UniGeneiHs.460260.
Hs.567256.
Hs.734597.

Genome annotation databases

EnsembliENST00000380753; ENSP00000370129; ENSG00000151632. [P52895-1]
ENST00000407674; ENSP00000385221; ENSG00000151632. [P52895-1]
ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
ENST00000580545; ENSP00000464045; ENSG00000265231. [P52895-1]
GeneIDi1646.
KEGGihsa:1646.
UCSCiuc001ihs.3. human. [P52895-1]
uc010qao.2. human. [P52895-2]

Polymorphism databases

DMDMi20532374.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68330 mRNA. Translation: AAD14013.1 .
U05598 mRNA. Translation: AAA20937.1 .
L32592 Genomic DNA. Translation: AAB38486.1 .
AB021654 mRNA. Translation: BAA36169.1 .
AB031084 mRNA. Translation: BAA92884.1 .
AB032153 Genomic DNA. Translation: BAA92891.1 .
AK290304 mRNA. Translation: BAF82993.1 .
AK296686 mRNA. Translation: BAG59281.1 .
BT006653 mRNA. Translation: AAP35299.1 .
AL713867 , AL391427 Genomic DNA. Translation: CAI16408.1 .
BC007024 mRNA. Translation: AAH07024.1 .
BC063574 mRNA. Translation: AAH63574.1 .
CCDSi CCDS44350.1. [P52895-2 ]
CCDS7062.1. [P52895-1 ]
PIRi I73676.
JC5240.
S61516.
RefSeqi NP_001128713.1. NM_001135241.2. [P52895-2 ]
NP_001345.1. NM_001354.5. [P52895-1 ]
NP_995317.1. NM_205845.2. [P52895-1 ]
UniGenei Hs.460260.
Hs.567256.
Hs.734597.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IHI X-ray 3.00 A/B 1-323 [» ]
1J96 X-ray 1.25 A/B 2-323 [» ]
1XJB X-ray 1.90 A/B 2-323 [» ]
2HDJ X-ray 2.00 A/B 1-323 [» ]
2IPJ X-ray 1.80 A/B 3-323 [» ]
4JQ1 X-ray 1.60 A/B 1-323 [» ]
4JQ2 X-ray 1.75 A/B 1-323 [» ]
4JQ3 X-ray 1.75 A/B 1-323 [» ]
4JQ4 X-ray 1.52 A/B 1-323 [» ]
4JQA X-ray 1.45 A/B 1-323 [» ]
4JTQ X-ray 1.60 A/B 1-323 [» ]
4JTR X-ray 1.30 A/B 1-323 [» ]
4L1W X-ray 2.20 A/B 2-323 [» ]
4L1X X-ray 2.00 A/B 2-323 [» ]
ProteinModelPortali P52895.
SMRi P52895. Positions 2-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108013. 1 interaction.
IntActi P52895. 1 interaction.
STRINGi 9606.ENSP00000370129.

Chemistry

BindingDBi P52895.
ChEMBLi CHEMBL5847.
DrugBanki DB00157. NADH.
DB01586. Ursodeoxycholic acid.

PTM databases

PhosphoSitei P52895.

Polymorphism databases

DMDMi 20532374.

Proteomic databases

MaxQBi P52895.
PaxDbi P52895.
PRIDEi P52895.

Protocols and materials databases

DNASUi 1646.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380753 ; ENSP00000370129 ; ENSG00000151632 . [P52895-1 ]
ENST00000407674 ; ENSP00000385221 ; ENSG00000151632 . [P52895-1 ]
ENST00000455190 ; ENSP00000408440 ; ENSG00000151632 . [P52895-2 ]
ENST00000580545 ; ENSP00000464045 ; ENSG00000265231 . [P52895-1 ]
GeneIDi 1646.
KEGGi hsa:1646.
UCSCi uc001ihs.3. human. [P52895-1 ]
uc010qao.2. human. [P52895-2 ]

Organism-specific databases

CTDi 1646.
GeneCardsi GC10M005021.
HGNCi HGNC:385. AKR1C2.
HPAi CAB047304.
MIMi 600450. gene.
614279. phenotype.
neXtProti NX_P52895.
Orphaneti 90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
PharmGKBi PA24678.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P52895.
KOi K00089.
K00212.
OMAi YTSKLWI.
PhylomeDBi P52895.
TreeFami TF106492.

Enzyme and pathway databases

BioCyci MetaCyc:HS07754-MONOMER.
BRENDAi 1.1.1.213. 2681.
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.
SABIO-RK P52895.
SignaLinki P52895.

Miscellaneous databases

EvolutionaryTracei P52895.
NextBioi 6772.
PROi P52895.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52895.
Bgeei P52895.
CleanExi HS_AKR1C2.
Genevestigatori P52895.

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 PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Liver.
  2. "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase."
    Ciaccio P.J., Tew K.D.
    Biochim. Biophys. Acta 1186:129-132(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon.
  3. "Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein."
    Qin K.-N., Khanna M., Cheng K.-C.
    Gene 149:357-361(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT TYR-46.
  4. "Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids."
    Dufort I., Soucy P., Labrie F., Luu-The V.
    Biochem. Biophys. Res. Commun. 228:474-479(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Prostate.
  5. "Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA."
    Shiraishi H., Ishikura S., Matsuura K., Deyashiki Y., Ninomiya M., Sakai S., Hara A.
    Biochem. J. 334:399-405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  6. "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 [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Liver.
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Tongue.
  8. "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] (ISOFORM 1).
  9. "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].
  10. "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] (ISOFORM 1).
    Tissue: Lung and Urinary bladder.
  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 2-31; 40-62; 69-100; 105-131; 137-153; 162-206; 209-231; 250-269 AND 271-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "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: PROTEIN SEQUENCE OF 10-29; 40-55; 76-101; 105-128; 137-146; 162-197; 208-223; 259-270 AND 305-322.
    Tissue: Liver.
  13. "Why boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiation."
    Fluck C.E., Meyer-Boni M., Pandey A.V., Kempna P., Miller W.L., Schoenle E.J., Biason-Lauber A.
    Am. J. Hum. Genet. 89:201-218(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, VARIANTS SRXY8 VAL-79; GLN-90; GLN-222 AND THR-300, CHARACTERIZATION OF VARIANTS SRXY8 VAL-79; GLN-90; GLN-222 AND THR-300.
  14. "Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate."
    Jin Y., Stayrook S.E., Albert R.H., Palackal N.T., Penning T.M., Lewis M.
    Biochemistry 40:10161-10168(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND URSODEOXYCHOLATE.
  15. "Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution."
    Nahoum V., Gangloff A., Legrand P., Zhu D.-W., Cantin L., Zhorov B.S., Luu-The V., Labrie F., Breton R., Lin S.X.
    J. Biol. Chem. 276:42091-42098(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH NADP AND TESTOSTERONE.
  16. "Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an 'induced-fit' mechanism and a conserved basic motif involved in the binding of androgen."
    Couture J.F., de Jesus-Tran K.P., Roy A.M., Cantin L., Cote P.L., Legrand P., Luu-The V., Labrie F., Breton R.
    Protein Sci. 14:1485-1497(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-323 IN COMPLEX WITH NADP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-301 AND ARG-304.
  17. "Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme."
    Faucher F., Pereira de Jesus-Tran K., Cantin L., Luu-The V., Labrie F., Breton R.
    J. Mol. Biol. 364:747-763(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, CATALYTIC ACTIVITY.
  18. "Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding."
    Faucher F., Cantin L., Pereira de Jesus-Tran K., Lemieux M., Luu-The V., Labrie F., Breton R.
    J. Mol. Biol. 369:525-540(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-323 IN COMPLEX WITH NADP AND HYDROXYANDROSTERONE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-24 AND LYS-31.

Entry informationi

Entry nameiAK1C2_HUMAN
AccessioniPrimary (citable) accession number: P52895
Secondary accession number(s): A8K2N9
, B4DKR9, Q14133, Q5SR16, Q7M4N1, Q96A71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: September 3, 2014
This is version 148 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, 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

Dasty 3

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