P52895 (AK1C2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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=1.1.1.213

Gene names

Name:	AKR1C2
Synonyms:	DDH2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Catalytic activity	Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH. Ref.11 A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H. Ref.11
Enzyme regulation	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. Ref.11
Subcellular location	Cytoplasm Potential.
Tissue specificity	Expressed in fetal testes. Expressed in fetal and adult adrenal glands. Ref.13
Involvement in disease	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. Ref.13
Sequence similarities	Belongs to the aldo/keto reductase family.
Biophysicochemical properties	Kinetic parameters: KM=260 µM for (s)-tetralol Ref.11 KM=520 µM for (s)-indan-1-ol KM=5000 µM for benzene dihydrodiol KM=1 µM for 5-beta-pregnane-3-alpha,20-alpha-diol KM=208 µM for 9-alpha,11-beta-PGF2 KM=0.3 µM for 5-beta-androstane-3,17-dione KM=79 µM for PGD2

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to jasmonic acid stimulus Inferred from direct assay PubMed 19487289. Source: UniProtKB daunorubicin metabolic process Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB digestion Inferred from direct assay Ref.11. Source: UniProtKB doxorubicin metabolic process Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB positive regulation of cell proliferation Inferred from direct assay PubMed 18508192. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from direct assay PubMed 18508192. Source: UniProtKB progesterone metabolic process Inferred from direct assay PubMed 21232532. Source: UniProtKB prostaglandin metabolic process Inferred from direct assay Ref.11. Source: UniProtKB response to prostaglandin stimulus Inferred from direct assay PubMed 18508192. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alditol:NADP+ 1-oxidoreductase activity Inferred from direct assay PubMed 21232532. Source: UniProtKB androsterone dehydrogenase (A-specific) activity Inferred from electronic annotation. Source: EC bile acid binding Inferred from direct assay Ref.11. Source: UniProtKB ketosteroid monooxygenase activity Inferred from direct assay PubMed 21232532. Source: UniProtKB oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Inferred from direct assay PubMed 20837989. Source: UniProtKB phenanthrene 9,10-monooxygenase activity Inferred from direct assay PubMed 21851338. Source: UniProtKB prostaglandin F receptor activity Inferred from direct assay PubMed 18508192. Source: UniProtKB trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P52895-1)

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.

Isoform 2 (identifier: P52895-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 323

323

Aldo-keto reductase family 1 member C2

PRO_0000124637

Regions

Nucleotide binding

216 – 280

65

NADP

Sites

Active site

55

1

Proton donor

Binding site

117

1

Substrate

Site

84

1

Lowers pKa of active site Tyr By similarity

Natural variations

Alternative sequence

124 – 139

16

PGEEV…GKILF → EDIGILTWKKSPKHNS in isoform 2.

VSP_043779

Alternative sequence

140 – 323

184

Missing in isoform 2.

VSP_043780

Natural variant

46

1

F → Y. Ref.3
Corresponds to variant rs2854482 [ dbSNP | Ensembl ].

VAR_048216

Natural variant

79

1

I → V in SRXY8; partially impaired activity. Ref.13

VAR_066632

Natural variant

90

1

H → Q in SRXY8; partially impaired activity. Ref.13

VAR_066633

Natural variant

172

1

L → Q.
Corresponds to variant rs11474 [ dbSNP | Ensembl ].

VAR_014748

Natural variant

222

1

H → Q in SRXY8; partially impaired activity. Ref.13

VAR_066634

Natural variant

300

1

N → T in SRXY8; partially impaired activity. Ref.13

VAR_066635

Experimental info

Sequence conflict

76

1

R → S AA sequence Ref.12

Sequence conflict

87

1

S → C AA sequence Ref.12

Sequence conflict

93

1

E → EE AA sequence Ref.12

Sequence conflict

111

1

V → A in AAB38486. Ref.3

Sequence conflict

164

1

G → R in BAF82993. Ref.7

Sequence conflict

179

1

K → E in AAD14013. Ref.1

Sequence conflict

179

1

K → E in AAB38486. Ref.3

Sequence conflict

185

1

K → E in AAD14013. Ref.1

Sequence conflict

185

1

K → E in AAB38486. Ref.3

Sequence conflict

188

1

C → H AA sequence Ref.12

Sequence conflict

193

1

C → H AA sequence Ref.12

Sequence conflict

319

1

F → I in AAD14013. Ref.1

Sequence conflict

319

1

F → I in AAB38486. Ref.3

Secondary structure

1

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323

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

15 – 22

8

Helix

32 – 44

13

Beta strand

48 – 50

3

Helix

53 – 55

3

Helix

58 – 70

13

Helix

76 – 78

3

Beta strand

80 – 85

6

Helix

87 – 89

3

Helix

92 – 94

3

Helix

95 – 106

12

Beta strand

111 – 116

6

Beta strand

119 – 122

4

Beta strand

124 – 126

3

Helix

144 – 156

13

Beta strand

159 – 167

9

Helix

170 – 177

8

Beta strand

187 – 192

6

Helix

200 – 208

9

Beta strand

212 – 217

6

Turn

225 – 227

3

Helix

235 – 237

3

Helix

239 – 248

10

Helix

252 – 262

11

Beta strand

266 – 270

5

Helix

274 – 280

7

Helix

281 – 285

5

Helix

290 – 297

8

Helix

309 – 311

3

Beta strand

318 – 321

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2002. Version 3. Checksum: 0D7B6F983FCE85E1	FASTA	323	36,735
	10 20 30 40 50 60 MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID SAHVYNNEEQ 70 80 90 100 110 120 VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV 130 140 150 160 170 180 SVKPGEEVIP KDENGKILFD TVDLCATWEA MEKCKDAGLA KSIGVSNFNH RLLEMILNKP 190 200 210 220 230 240 GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV 250 260 270 280 290 300 LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN 310 320 RNVRYLTLDI FAGPPNYPFS DEY
	Isoform 2 [UniParc]. Checksum: 11CAE1B299B378AC	FASTA	139	15,748
	10 20 30 40 50 60 MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID SAHVYNNEEQ 70 80 90 100 110 120 VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV 130 SVKEDIGILT WKKSPKHNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005668.

PIR

I73676.
JC5240.
S61516.

RefSeq

NP_001128713.1. NM_001135241.2.
NP_001345.1. NM_001354.5.
NP_995317.1. NM_205845.2.

UniGene

Hs.460260.
Hs.567256.
Hs.734597.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P52895.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52895. 1 interaction.

STRING

9606.ENSP00000370129.

PTM databases

PhosphoSite

P52895.

Polymorphism databases

DMDM

20532374.

Proteomic databases

PaxDb

P52895.

PRIDE

P52895.

Protocols and materials databases

DNASU

1646.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380753; ENSP00000370129; ENSG00000151632.
ENST00000407674; ENSP00000385221; ENSG00000151632.
ENST00000455190; ENSP00000408440; ENSG00000151632.
ENST00000580345; ENSP00000463185; ENSG00000265231.
ENST00000580545; ENSP00000464045; ENSG00000265231.
ENST00000585272; ENSP00000462069; ENSG00000265231.

GeneID

1646.

KEGG

hsa:1646.

UCSC

uc001ihs.3. human.

Organism-specific databases

CTD

1646.

GeneCards

GC10M005021.

HGNC

HGNC:385. AKR1C2.

HPA

CAB047304.

MIM

600450. gene.
614279. phenotype.

neXtProt

NX_P52895.

Orphanet

90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.

PharmGKB

PA24678.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0656.

HOGENOM

HOG000250272.

HOVERGEN

HBG000020.

InParanoid

P52895.

KO

K00089.
K00212.

OMA

HRDPEMV.

OrthoDB

EOG4Q2DG2.

PhylomeDB

P52895.

Enzyme and pathway databases

BioCyc

MetaCyc:HS07754-MONOMER.

BRENDA

1.1.1.213. 2681.

SABIO-RK

P52895.

Gene expression databases

ArrayExpress

P52895.

Bgee

P52895.

CleanEx

HS_AKR1C2.

Genevestigator

P52895.

GermOnline

ENSG00000151632. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. False negative.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P52895.

ChEMBL

CHEMBL5847.

DrugBank

DB00157. NADH.
DB01586. Ursodeoxycholic acid.

EvolutionaryTrace

P52895.

GenomeRNAi

1646.

NextBio

6772.

SOURCE

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Entry information

Entry name

AK1C2_HUMAN

Accession

Primary (citable) accession number: P52895
Secondary accession number(s): A8K2N9 , B4DKR9, Q14133, Q5SR16, Q7M4N1, Q96A71

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 10, 2002
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.