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P52895 (AK1C2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:AKR1C2
Synonyms:DDH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence 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 Ref.16 Ref.17 Ref.18

Catalytic activity

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH. Ref.11 Ref.16 Ref.17 Ref.18

A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H. Ref.11 Ref.16 Ref.17 Ref.18

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 processLipid metabolism
Steroid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 18508192. Source: UniProtKB

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

epithelial cell differentiation

Inferred from expression pattern PubMed 21492153. Source: UniProt

oxidation-reduction process

Inferred from direct assay PubMed 21232532. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 18508192. Source: UniProtKB

positive regulation of protein kinase B signaling

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

Inferred from direct assay PubMed 18508192. Source: UniProtKB

steroid metabolic process

Inferred from direct assay Ref.11. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalditol:NADP+ 1-oxidoreductase activity

Inferred from direct assay PubMed 21232532. Source: UniProtKB

bile acid binding

Inferred from direct assay Ref.11. Source: UniProtKB

carboxylic 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Aldo-keto reductase family 1 member C2
PRO_0000124637

Regions

Nucleotide binding20 – 245NADP
Nucleotide binding166 – 1672NADP
Nucleotide binding216 – 2227NADP
Nucleotide binding270 – 28011NADP

Sites

Active site551Proton donor
Binding site241Substrate By similarity
Binding site501NADP
Binding site1171Substrate
Binding site1901NADP
Binding site2221Substrate By similarity
Binding site2271Substrate
Site841Lowers pKa of active site Tyr By similarity

Natural variations

Alternative sequence124 – 13916PGEEV…GKILF → EDIGILTWKKSPKHNS in isoform 2.
VSP_043779
Alternative sequence140 – 323184Missing in isoform 2.
VSP_043780
Natural variant461F → Y. Ref.3
Corresponds to variant rs2854482 [ dbSNP | Ensembl ].
VAR_048216
Natural variant791I → V in SRXY8; partially impaired activity. Ref.13
VAR_066632
Natural variant901H → Q in SRXY8; partially impaired activity. Ref.13
VAR_066633
Natural variant1721L → Q.
Corresponds to variant rs11474 [ dbSNP | Ensembl ].
VAR_014748
Natural variant2221H → Q in SRXY8; partially impaired activity. Ref.13
VAR_066634
Natural variant3001N → T in SRXY8; partially impaired activity. Ref.13
VAR_066635

Experimental info

Mutagenesis241Y → A: Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold. Ref.18
Mutagenesis311K → A or M: Increases the low androstenedione reductase activity. Ref.18
Mutagenesis3011R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold. Ref.16
Mutagenesis3041R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold. Ref.16
Sequence conflict761R → S AA sequence Ref.12
Sequence conflict871S → C AA sequence Ref.12
Sequence conflict931E → EE AA sequence Ref.12
Sequence conflict1111V → A in AAB38486. Ref.3
Sequence conflict1641G → R in BAF82993. Ref.7
Sequence conflict1791K → E in AAD14013. Ref.1
Sequence conflict1791K → E in AAB38486. Ref.3
Sequence conflict1851K → E in AAD14013. Ref.1
Sequence conflict1851K → E in AAB38486. Ref.3
Sequence conflict1881C → H AA sequence Ref.12
Sequence conflict1931C → H AA sequence Ref.12
Sequence conflict3191F → I in AAD14013. Ref.1
Sequence conflict3191F → I in AAB38486. Ref.3

Secondary structure

........................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2002. Version 3.
Checksum: 0D7B6F983FCE85E1

FASTA32336,735
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 11CAE1B299B378AC
Show »

FASTA13915,748

References

« Hide '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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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.
+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.
PIRI73676.
JC5240.
S61516.
RefSeqNP_001128713.1. NM_001135241.2.
NP_001345.1. NM_001354.5.
NP_995317.1. NM_205845.2.
UniGeneHs.460260.
Hs.567256.
Hs.734597.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP52895.
SMRP52895. Positions 2-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108013. 1 interaction.
IntActP52895. 1 interaction.
STRING9606.ENSP00000370129.

Chemistry

BindingDBP52895.
ChEMBLCHEMBL5847.
DrugBankDB00157. NADH.
DB01586. Ursodeoxycholic acid.

PTM databases

PhosphoSiteP52895.

Polymorphism databases

DMDM20532374.

Proteomic databases

PaxDbP52895.
PRIDEP52895.

Protocols and materials databases

DNASU1646.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380753; ENSP00000370129; ENSG00000151632. [P52895-1]
ENST00000407674; ENSP00000385221; ENSG00000151632. [P52895-1]
ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
ENST00000580545; ENSP00000464045; ENSG00000265231. [P52895-1]
GeneID1646.
KEGGhsa:101930400.
hsa:1646.
UCSCuc001ihs.3. human. [P52895-1]
uc010qao.2. human. [P52895-2]

Organism-specific databases

CTD1646.
GeneCardsGC10M005021.
HGNCHGNC:385. AKR1C2.
HPACAB047304.
MIM600450. gene.
614279. phenotype.
neXtProtNX_P52895.
Orphanet90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
PharmGKBPA24678.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0656.
HOGENOMHOG000250272.
HOVERGENHBG000020.
InParanoidP52895.
KOK00089.
K00212.
OMALWVQDMN.
PhylomeDBP52895.
TreeFamTF106492.

Enzyme and pathway databases

BioCycMetaCyc:HS07754-MONOMER.
BRENDA1.1.1.213. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP52895.
SignaLinkP52895.

Gene expression databases

ArrayExpressP52895.
BgeeP52895.
CleanExHS_AKR1C2.
GenevestigatorP52895.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52895.
NextBio6772.
PROP52895.
SOURCESearch...

Entry information

Entry nameAK1C2_HUMAN
AccessionPrimary (citable) accession number: P52895
Secondary accession number(s): A8K2N9 expand/collapse secondary AC list , B4DKR9, Q14133, Q5SR16, Q7M4N1, Q96A71
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: April 16, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM