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Protein

Aldo-keto reductase family 1 member C2

Gene

AKR1C2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication
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-ol1 Publication
  3. KM=5000 µM for benzene dihydrodiol1 Publication
  4. KM=1 µM for 5-beta-pregnane-3-alpha,20-alpha-diol1 Publication
  5. KM=208 µM for 9-alpha,11-beta-prostaglandin F21 Publication
  6. KM=0.3 µM for 5-beta-androstane-3,17-dione1 Publication
  7. KM=79 µM for prostaglandin D21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei24SubstrateBy similarity1
    Binding sitei50NADP5 Publications1
    Active sitei55Proton donor1
    Sitei84Lowers pKa of active site TyrBy similarity1
    Binding sitei117Substrate1
    Binding sitei190NADP5 Publications1
    Binding sitei222SubstrateBy similarity1
    Binding sitei227Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi20 – 24NADP5 Publications5
    Nucleotide bindingi166 – 167NADP5 Publications2
    Nucleotide bindingi216 – 222NADP5 Publications7
    Nucleotide bindingi270 – 280NADP5 PublicationsAdd BLAST11

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    • bile acid binding Source: UniProtKB
    • carboxylic acid binding Source: UniProtKB
    • ketosteroid monooxygenase activity Source: UniProtKB
    • oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    • phenanthrene 9,10-monooxygenase activity Source: UniProtKB
    • trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • cellular response to jasmonic acid stimulus Source: UniProtKB
    • cellular response to prostaglandin D stimulus Source: UniProtKB
    • daunorubicin metabolic process Source: UniProtKB
    • digestion Source: UniProtKB
    • doxorubicin metabolic process Source: UniProtKB
    • epithelial cell differentiation Source: UniProtKB
    • G-protein coupled receptor signaling pathway Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • positive regulation of cell proliferation Source: UniProtKB
    • positive regulation of protein kinase B signaling Source: UniProtKB
    • progesterone metabolic process Source: UniProtKB
    • prostaglandin metabolic process Source: UniProtKB
    • 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.
    ZFISH:HS07754-MONOMER.
    BRENDAi1.1.1.213. 2681.
    1.1.1.357. 2681.
    1.3.1.20. 2681.
    ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-HSA-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    SABIO-RKP52895.
    SignaLinkiP52895.
    SIGNORiP52895.

    Chemistry databases

    SwissLipidsiSLP:000000803.

    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:1.3.1.201 Publication)
    Type III 3-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.3574 Publications)
    Gene namesi
    Name:AKR1C2
    Synonyms:DDH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:385. AKR1C2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    46,XY sex reversal 8 (SRXY8)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.
    See also OMIM:614279
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06663279I → V in SRXY8; partially impaired activity. 1 PublicationCorresponds to variant rs387906750dbSNPEnsembl.1
    Natural variantiVAR_06663390H → Q in SRXY8; partially impaired activity. 1 Publication1
    Natural variantiVAR_066634222H → Q in SRXY8; partially impaired activity. 1 Publication1
    Natural variantiVAR_066635300N → T in SRXY8; partially impaired activity. 1 PublicationCorresponds to variant rs387906751dbSNPEnsembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi24Y → A: Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold. 1 Publication1
    Mutagenesisi31K → A or M: Increases the low androstenedione reductase activity. 1 Publication1
    Mutagenesisi301R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold. 1 Publication1
    Mutagenesisi304R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi1646.
    MalaCardsiAKR1C2.
    MIMi614279. phenotype.
    OpenTargetsiENSG00000151632.
    Orphaneti90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
    PharmGKBiPA24678.

    Chemistry databases

    ChEMBLiCHEMBL5847.
    DrugBankiDB01586. Ursodeoxycholic acid.

    Polymorphism and mutation databases

    BioMutaiAKR1C2.
    DMDMi20532374.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001246371 – 323Aldo-keto reductase family 1 member C2Add BLAST323

    Proteomic databases

    EPDiP52895.
    MaxQBiP52895.
    PaxDbiP52895.
    PeptideAtlasiP52895.
    PRIDEiP52895.

    PTM databases

    iPTMnetiP52895.
    PhosphoSitePlusiP52895.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000151632.
    CleanExiHS_AKR1C2.
    ExpressionAtlasiP52895. baseline and differential.
    GenevisibleiP52895. HS.

    Organism-specific databases

    HPAiCAB047304.

    Interactioni

    Protein-protein interaction databases

    BioGridi108013. 13 interactors.
    IntActiP52895. 1 interactor.
    STRINGi9606.ENSP00000370129.

    Chemistry databases

    BindingDBiP52895.

    Structurei

    Secondary structure

    1323
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 9Combined sources3
    Beta strandi15 – 22Combined sources8
    Helixi32 – 44Combined sources13
    Beta strandi48 – 50Combined sources3
    Helixi53 – 55Combined sources3
    Helixi58 – 70Combined sources13
    Helixi76 – 78Combined sources3
    Beta strandi80 – 85Combined sources6
    Helixi87 – 89Combined sources3
    Helixi92 – 106Combined sources15
    Beta strandi111 – 116Combined sources6
    Beta strandi119 – 122Combined sources4
    Beta strandi124 – 126Combined sources3
    Helixi144 – 156Combined sources13
    Beta strandi159 – 167Combined sources9
    Helixi170 – 177Combined sources8
    Beta strandi187 – 192Combined sources6
    Helixi200 – 208Combined sources9
    Beta strandi212 – 217Combined sources6
    Turni225 – 227Combined sources3
    Helixi235 – 237Combined sources3
    Helixi239 – 248Combined sources10
    Helixi252 – 262Combined sources11
    Beta strandi266 – 270Combined sources5
    Helixi274 – 281Combined sources8
    Helixi282 – 285Combined sources4
    Helixi290 – 297Combined sources8
    Helixi309 – 311Combined sources3
    Beta strandi319 – 321Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4XO6X-ray1.20A/B2-323[»]
    4XO7X-ray1.75A/B1-323[»]
    ProteinModelPortaliP52895.
    SMRiP52895.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52895.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP52895.
    KOiK00089.
    OMAiRHIDIAY.
    OrthoDBiEOG091G0D69.
    PhylomeDBiP52895.
    TreeFamiTF106492.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID
    60 70 80 90 100
    SAHVYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE
    110 120 130 140 150
    RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA
    160 170 180 190 200
    MEKCKDAGLA KSIGVSNFNH RLLEMILNKP 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):36,735
    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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti76R → S AA sequence (PubMed:8486699).Curated1
    Sequence conflicti87S → C AA sequence (PubMed:8486699).Curated1
    Sequence conflicti93E → EE AA sequence (PubMed:8486699).Curated1
    Sequence conflicti111V → A in AAB38486 (PubMed:7959017).Curated1
    Sequence conflicti164G → R in BAF82993 (PubMed:14702039).Curated1
    Sequence conflicti179K → E in AAD14013 (PubMed:8274401).Curated1
    Sequence conflicti179K → E in AAB38486 (PubMed:7959017).Curated1
    Sequence conflicti185K → E in AAD14013 (PubMed:8274401).Curated1
    Sequence conflicti185K → E in AAB38486 (PubMed:7959017).Curated1
    Sequence conflicti188C → H AA sequence (PubMed:8486699).Curated1
    Sequence conflicti193C → H AA sequence (PubMed:8486699).Curated1
    Sequence conflicti319F → I in AAD14013 (PubMed:8274401).Curated1
    Sequence conflicti319F → I in AAB38486 (PubMed:7959017).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04821646F → Y.1 PublicationCorresponds to variant rs2854482dbSNPEnsembl.1
    Natural variantiVAR_06663279I → V in SRXY8; partially impaired activity. 1 PublicationCorresponds to variant rs387906750dbSNPEnsembl.1
    Natural variantiVAR_06663390H → Q in SRXY8; partially impaired activity. 1 Publication1
    Natural variantiVAR_014748172L → Q.Corresponds to variant rs11474dbSNPEnsembl.1
    Natural variantiVAR_066634222H → Q in SRXY8; partially impaired activity. 1 Publication1
    Natural variantiVAR_066635300N → T in SRXY8; partially impaired activity. 1 PublicationCorresponds to variant rs387906751dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_043779124 – 139PGEEV…GKILF → EDIGILTWKKSPKHNS in isoform 2. 1 PublicationAdd BLAST16
    Alternative sequenceiVSP_043780140 – 323Missing in isoform 2. 1 PublicationAdd BLAST184

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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]
    ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
    GeneIDi1646.
    KEGGihsa:1646.
    UCSCiuc010qao.2. human. [P52895-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4XO6X-ray1.20A/B2-323[»]
    4XO7X-ray1.75A/B1-323[»]
    ProteinModelPortaliP52895.
    SMRiP52895.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108013. 13 interactors.
    IntActiP52895. 1 interactor.
    STRINGi9606.ENSP00000370129.

    Chemistry databases

    BindingDBiP52895.
    ChEMBLiCHEMBL5847.
    DrugBankiDB01586. Ursodeoxycholic acid.
    SwissLipidsiSLP:000000803.

    PTM databases

    iPTMnetiP52895.
    PhosphoSitePlusiP52895.

    Polymorphism and mutation databases

    BioMutaiAKR1C2.
    DMDMi20532374.

    Proteomic databases

    EPDiP52895.
    MaxQBiP52895.
    PaxDbiP52895.
    PeptideAtlasiP52895.
    PRIDEiP52895.

    Protocols and materials databases

    DNASUi1646.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380753; ENSP00000370129; ENSG00000151632. [P52895-1]
    ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
    GeneIDi1646.
    KEGGihsa:1646.
    UCSCiuc010qao.2. human. [P52895-1]

    Organism-specific databases

    CTDi1646.
    DisGeNETi1646.
    GeneCardsiAKR1C2.
    HGNCiHGNC:385. AKR1C2.
    HPAiCAB047304.
    MalaCardsiAKR1C2.
    MIMi600450. gene.
    614279. phenotype.
    neXtProtiNX_P52895.
    OpenTargetsiENSG00000151632.
    Orphaneti90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
    PharmGKBiPA24678.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP52895.
    KOiK00089.
    OMAiRHIDIAY.
    OrthoDBiEOG091G0D69.
    PhylomeDBiP52895.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07754-MONOMER.
    ZFISH:HS07754-MONOMER.
    BRENDAi1.1.1.213. 2681.
    1.1.1.357. 2681.
    1.3.1.20. 2681.
    ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-HSA-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    SABIO-RKP52895.
    SignaLinkiP52895.
    SIGNORiP52895.

    Miscellaneous databases

    EvolutionaryTraceiP52895.
    GenomeRNAii1646.
    PROiP52895.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000151632.
    CleanExiHS_AKR1C2.
    ExpressionAtlasiP52895. baseline and differential.
    GenevisibleiP52895. HS.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 170 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.