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Protein

Aldo-keto reductase family 1 member C1

Gene

AKR1C1

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

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Kineticsi

  1. KM=5 µM for (s)-tetralol2 Publications
  2. KM=38 µM for (s)-indan-1-ol2 Publications
  3. KM=580 µM for benzene dihydrodiol2 Publications
  4. KM=3 µM for 5-beta-pregnane-3-alpha,20-alpha-diol2 Publications
  5. KM=3 µM for 5-beta-pregnan-20-alpha-ol-3-one2 Publications
  6. KM=12 µM for 4-pregnen-20-alpha-ol-3-one2 Publications
  7. KM=133 µM for 9-alpha,11-beta-prostaglandin F22 Publications
  8. KM=2 µM for 5-beta-pregnan-3-alpha-ol-20-one2 Publications
  9. KM=1 µM for 5-beta-androstane-3,17-dione2 Publications
  10. KM=12 µM for prostaglandin D22 Publications
  11. KM=0.6 µM for 20-alpha-hydroxyprogesterone (with NADH)2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei24Substrate1
    Binding sitei50NADP2 Publications1
    Sitei54Important for substrate specificityBy similarity1
    Active sitei55Proton donorBy similarity1
    Sitei84Lowers pKa of active site TyrBy similarity1
    Binding sitei117SubstrateBy similarity1
    Binding sitei190NADP2 Publications1
    Binding sitei222Substrate1
    Sitei222May be involved in the mediating step between the transformation of progesterone and the release of the cofactor1
    Binding sitei227Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi20 – 24NADP2 Publications5
    Nucleotide bindingi166 – 167NADP2 Publications2
    Nucleotide bindingi216 – 222NADP2 Publications7
    Nucleotide bindingi270 – 280NADP2 PublicationsAdd BLAST11

    GO - Molecular functioni

    • 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Source: UniProtKB-EC
    • alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • androsterone dehydrogenase (B-specific) activity Source: UniProtKB
    • bile acid binding Source: UniProtKB
    • carboxylic acid binding Source: UniProtKB
    • indanol dehydrogenase activity Source: UniProtKB-EC
    • 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

    • bile acid and bile salt transport Source: UniProtKB
    • bile acid metabolic process Source: UniProtKB
    • cellular response to jasmonic acid stimulus Source: UniProtKB
    • cholesterol homeostasis Source: UniProtKB
    • daunorubicin metabolic process Source: UniProtKB
    • digestion Source: UniProtKB
    • doxorubicin metabolic process Source: UniProtKB
    • epithelial cell differentiation Source: UniProtKB
    • intestinal cholesterol absorption Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • progesterone metabolic process Source: UniProtKB
    • protein homooligomerization Source: UniProtKB
    • response to organophosphorus Source: UniProtKB
    • retinal metabolic process Source: UniProtKB
    • retinoid metabolic process Source: Reactome
    • xenobiotic metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10741-MONOMER.
    ZFISH:HS10741-MONOMER.
    BRENDAi1.1.1.149. 2681.
    1.1.1.270. 2681.
    1.1.1.50. 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.
    R-HSA-975634. Retinoid metabolism and transport.
    SABIO-RKQ04828.
    SIGNORiQ04828.

    Chemistry databases

    SwissLipidsiSLP:000000802.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member C1 (EC:1.1.1.-)
    Alternative name(s):
    20-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.1492 Publications)
    Short name:
    20-alpha-HSD
    Chlordecone reductase homolog HAKRC
    Dihydrodiol dehydrogenase 1/2
    Short name:
    DD1/DD2
    High-affinity hepatic bile acid-binding protein
    Short name:
    HBAB
    Indanol dehydrogenase (EC:1.1.1.1121 Publication)
    Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.202 Publications)
    Gene namesi
    Name:AKR1C1
    Synonyms:DDH, DDH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:384. AKR1C1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi127E → D: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value. 1 Publication1
    Mutagenesisi222H → I: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH. 1 Publication1
    Mutagenesisi222H → S: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH. 1 Publication1
    Mutagenesisi304R → L: 70-fold decrease in progesterone reduction. No effect on DHT reduction. 1 Publication1
    Mutagenesisi305Y → F: No effect on progesterone reduction. 1 Publication1
    Mutagenesisi307T → V: No effect on progesterone reduction. 1 Publication1
    Mutagenesisi309D → V: No effect on progesterone reduction. 1 Publication1

    Organism-specific databases

    DisGeNETi1645.
    OpenTargetsiENSG00000187134.
    PharmGKBiPA24677.

    Chemistry databases

    ChEMBLiCHEMBL5905.
    DrugBankiDB00945. Acetylsalicylic acid.
    DB00936. Salicylic acid.

    Polymorphism and mutation databases

    BioMutaiAKR1C1.
    DMDMi416877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001246331 – 323Aldo-keto reductase family 1 member C1Add BLAST323

    Proteomic databases

    EPDiQ04828.
    MaxQBiQ04828.
    PaxDbiQ04828.
    PeptideAtlasiQ04828.
    PRIDEiQ04828.

    PTM databases

    iPTMnetiQ04828.
    PhosphoSitePlusiQ04828.
    SwissPalmiQ04828.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000187134.
    CleanExiHS_AKR1C1.
    ExpressionAtlasiQ04828. baseline and differential.
    GenevisibleiQ04828. HS.

    Organism-specific databases

    HPAiCAB047303.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPN3P260455EBI-2116455,EBI-1047946

    Protein-protein interaction databases

    BioGridi108012. 7 interactors.
    IntActiQ04828. 4 interactors.
    MINTiMINT-5001209.
    STRINGi9606.ENSP00000370254.

    Chemistry databases

    BindingDBiQ04828.

    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
    Helixi33 – 44Combined sources12
    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 strandi124 – 126Combined sources3
    Beta strandi133 – 135Combined sources3
    Helixi144 – 156Combined sources13
    Beta strandi159 – 167Combined sources9
    Helixi170 – 177Combined sources8
    Beta strandi187 – 192Combined sources6
    Beta strandi194 – 197Combined sources4
    Helixi200 – 208Combined sources9
    Beta strandi212 – 217Combined sources6
    Turni225 – 227Combined sources3
    Helixi235 – 237Combined sources3
    Helixi239 – 248Combined sources10
    Helixi252 – 262Combined sources11
    Beta strandi266 – 270Combined sources5
    Helixi274 – 280Combined sources7
    Helixi281 – 285Combined sources5
    Helixi290 – 297Combined sources8
    Helixi309 – 311Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MRQX-ray1.59A2-323[»]
    3C3UX-ray1.80A1-323[»]
    3GUGX-ray1.90A1-323[»]
    3NTYX-ray1.87A1-323[»]
    4YVPX-ray2.60A/B1-323[»]
    ProteinModelPortaliQ04828.
    SMRiQ04828.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04828.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ04828.
    KOiK00212.
    PhylomeDBiQ04828.
    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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04828-1 [UniParc]FASTAAdd to basket

    « Hide

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti3S → A no nucleotide entry (PubMed:7626489).Curated1
    Sequence conflicti95V → D no nucleotide entry (PubMed:7626489).Curated1
    Sequence conflicti95V → D in AAD14012 (PubMed:8274401).Curated1
    Sequence conflicti158G → E no nucleotide entry (PubMed:7626489).Curated1
    Sequence conflicti158G → E in AAD14012 (PubMed:8274401).Curated1
    Sequence conflicti171 – 172RQ → ST no nucleotide entry (PubMed:7626489).Curated2
    Sequence conflicti171 – 172RQ → ST in AAD14012 (PubMed:8274401).Curated2
    Sequence conflicti183 – 184KY → QV no nucleotide entry (PubMed:7626489).Curated2
    Sequence conflicti183 – 184KY → QV in AAD14012 (PubMed:8274401).Curated2
    Sequence conflicti222H → L no nucleotide entry (PubMed:7626489).Curated1
    Sequence conflicti222H → L in AAD14012 (PubMed:8274401).Curated1
    Sequence conflicti319F → I no nucleotide entry (PubMed:7626489).Curated1
    Sequence conflicti319F → I in AAD14012 (PubMed:8274401).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_048214170R → H.Corresponds to variant rs139588200dbSNPEnsembl.1
    Natural variantiVAR_048215172Q → L.Corresponds to variant rs17354444dbSNPEnsembl.1

    Sequence databases

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

    Genome annotation databases

    EnsembliENST00000380872; ENSP00000370254; ENSG00000187134.
    GeneIDi1645.
    KEGGihsa:1645.
    UCSCiuc001ihq.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MRQX-ray1.59A2-323[»]
    3C3UX-ray1.80A1-323[»]
    3GUGX-ray1.90A1-323[»]
    3NTYX-ray1.87A1-323[»]
    4YVPX-ray2.60A/B1-323[»]
    ProteinModelPortaliQ04828.
    SMRiQ04828.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108012. 7 interactors.
    IntActiQ04828. 4 interactors.
    MINTiMINT-5001209.
    STRINGi9606.ENSP00000370254.

    Chemistry databases

    BindingDBiQ04828.
    ChEMBLiCHEMBL5905.
    DrugBankiDB00945. Acetylsalicylic acid.
    DB00936. Salicylic acid.
    SwissLipidsiSLP:000000802.

    PTM databases

    iPTMnetiQ04828.
    PhosphoSitePlusiQ04828.
    SwissPalmiQ04828.

    Polymorphism and mutation databases

    BioMutaiAKR1C1.
    DMDMi416877.

    Proteomic databases

    EPDiQ04828.
    MaxQBiQ04828.
    PaxDbiQ04828.
    PeptideAtlasiQ04828.
    PRIDEiQ04828.

    Protocols and materials databases

    DNASUi1645.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380872; ENSP00000370254; ENSG00000187134.
    GeneIDi1645.
    KEGGihsa:1645.
    UCSCiuc001ihq.4. human.

    Organism-specific databases

    CTDi1645.
    DisGeNETi1645.
    GeneCardsiAKR1C1.
    HGNCiHGNC:384. AKR1C1.
    HPAiCAB047303.
    MIMi600449. gene.
    neXtProtiNX_Q04828.
    OpenTargetsiENSG00000187134.
    PharmGKBiPA24677.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ04828.
    KOiK00212.
    PhylomeDBiQ04828.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10741-MONOMER.
    ZFISH:HS10741-MONOMER.
    BRENDAi1.1.1.149. 2681.
    1.1.1.270. 2681.
    1.1.1.50. 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.
    R-HSA-975634. Retinoid metabolism and transport.
    SABIO-RKQ04828.
    SIGNORiQ04828.

    Miscellaneous databases

    EvolutionaryTraceiQ04828.
    GeneWikiiAKR1C1.
    GenomeRNAii1645.
    PROiQ04828.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000187134.
    CleanExiHS_AKR1C1.
    ExpressionAtlasiQ04828. baseline and differential.
    GenevisibleiQ04828. 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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAK1C1_HUMAN
    AccessioniPrimary (citable) accession number: Q04828
    Secondary accession number(s): P52896
    , Q5SR15, Q7M4N2, Q9UCX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: November 30, 2016
    This is version 180 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    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.