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Protein

Aldo-keto reductase family 1 member B10

Gene

AKR1B10

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

Functioni

Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs.1 Publication

Enzyme regulationi

Inhibited by tolrestat.1 Publication

Kineticsi

  1. KM=600 µM for D,L-glyceraldehyde1 Publication
  2. KM=0.6 µM for all-trans-retinaldehyde1 Publication
  3. KM=0.7 µM for 9-cis-retinaldehyde1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441NADP1 Publication
    Active sitei49 – 491Proton donor1 Publication
    Sitei78 – 781Lowers pKa of active site TyrBy similarity
    Binding sitei111 – 1111Substrate1 Publication
    Binding sitei184 – 1841NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 223NADP1 Publication
    Nucleotide bindingi160 – 1612NADP1 Publication
    Nucleotide bindingi210 – 2178NADP1 Publication
    Nucleotide bindingi261 – 27313NADP1 PublicationAdd
    BLAST

    GO - Molecular functioni

    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • geranylgeranyl reductase activity Source: UniProtKB
    • indanol dehydrogenase activity Source: UniProtKB
    • retinal dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • cellular aldehyde metabolic process Source: ProtInc
    • daunorubicin metabolic process Source: UniProtKB
    • digestion Source: ProtInc
    • doxorubicin metabolic process Source: UniProtKB
    • farnesol catabolic process Source: UniProtKB
    • phototransduction, visible light Source: Reactome
    • retinoid metabolic process Source: Reactome
    • steroid metabolic process Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.21. 2681.
    ReactomeiREACT_24968. Retinoid metabolism and transport.
    SABIO-RKO60218.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member B10 (EC:1.1.1.-)
    Alternative name(s):
    ARL-1
    Aldose reductase-like
    Aldose reductase-related protein
    Short name:
    ARP
    Short name:
    hARP
    Small intestine reductase
    Short name:
    SI reductase
    Gene namesi
    Name:AKR1B10
    Synonyms:AKR1B11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:382. AKR1B10.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • lysosome Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251K → L: Increased affinity and reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication
    Mutagenesisi301 – 3011V → L: Reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication

    Organism-specific databases

    PharmGKBiPA24676.

    Polymorphism and mutation databases

    BioMutaiAKR1B10.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Aldo-keto reductase family 1 member B10PRO_0000124632Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251N6-acetyllysine1 Publication
    Modified residuei263 – 2631N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO60218.
    PaxDbiO60218.
    PRIDEiO60218.

    2D gel databases

    DOSAC-COBS-2DPAGEO60218.

    PTM databases

    PhosphoSiteiO60218.

    Expressioni

    Tissue specificityi

    Found in many tissues. Highly expressed in small intestine, colon and adrenal gland.

    Gene expression databases

    BgeeiO60218.
    CleanExiHS_AKR1B10.
    GenevestigatoriO60218.

    Organism-specific databases

    HPAiCAB070163.
    HPA020280.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACACAQ130854EBI-1572139,EBI-717681

    Protein-protein interaction databases

    BioGridi121325. 10 interactions.
    IntActiO60218. 1 interaction.
    STRINGi9606.ENSP00000352584.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Beta strandi12 – 198Combined sources
    Turni25 – 273Combined sources
    Helixi28 – 3710Combined sources
    Beta strandi42 – 443Combined sources
    Helixi47 – 493Combined sources
    Helixi52 – 6413Combined sources
    Helixi70 – 723Combined sources
    Beta strandi74 – 796Combined sources
    Helixi81 – 833Combined sources
    Helixi86 – 10015Combined sources
    Beta strandi105 – 1117Combined sources
    Beta strandi118 – 1203Combined sources
    Beta strandi127 – 1315Combined sources
    Helixi138 – 15013Combined sources
    Beta strandi153 – 1619Combined sources
    Helixi164 – 1718Combined sources
    Beta strandi181 – 1866Combined sources
    Helixi194 – 2029Combined sources
    Beta strandi206 – 2116Combined sources
    Helixi228 – 2303Combined sources
    Helixi232 – 2409Combined sources
    Helixi245 – 25410Combined sources
    Turni255 – 2573Combined sources
    Helixi267 – 2748Combined sources
    Helixi283 – 2908Combined sources
    Helixi302 – 3043Combined sources
    Beta strandi305 – 3073Combined sources
    Helixi311 – 3133Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZUAX-ray1.25X1-316[»]
    4GA8X-ray1.94A1-316[»]
    4GABX-ray1.60A1-316[»]
    4GQ0X-ray2.10A1-316[»]
    4GQGX-ray1.92A1-316[»]
    4I5XX-ray2.10A1-316[»]
    4ICCX-ray1.75X1-316[»]
    4JIHX-ray2.30A1-316[»]
    4JIIX-ray2.20X1-316[»]
    4WEVX-ray1.45X1-316[»]
    ProteinModelPortaliO60218.
    SMRiO60218. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60218.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiO60218.
    KOiK00011.
    OMAiVSNFSHF.
    OrthoDBiEOG70KGQF.
    PhylomeDBiO60218.
    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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60218-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ
    60 70 80 90 100
    NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVR KAFEKTLKDL
    110 120 130 140 150
    KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD
    160 170 180 190 200
    EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC
    210 220 230 240 250
    HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI
    260 270 280 290 300
    RFHIQRNVIV IPKSVTPARI VENIQVFDFK LSDEEMATIL SFNRNWRACN
    310
    VLQSSHLEDY PFNAEY
    Length:316
    Mass (Da):36,020
    Last modified:February 8, 2011 - v2
    Checksum:i0C2FC0E798955A33
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761V → A in AAO13380 (Ref. 3) Curated
    Sequence conflicti100 – 1001L → P in AAO13380 (Ref. 3) Curated
    Sequence conflicti288 – 2881T → I in AAO13380 (Ref. 3) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871P → S.
    Corresponds to variant rs2303312 [ dbSNP | Ensembl ].
    VAR_020077
    Natural varianti286 – 2861M → T.
    Corresponds to variant rs3735042 [ dbSNP | Ensembl ].
    VAR_020078
    Natural varianti313 – 3131N → D.7 Publications
    Corresponds to variant rs4728329 [ dbSNP | Ensembl ].
    VAR_013287

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U37100 mRNA. Translation: AAC17469.1.
    AF052577 mRNA. Translation: AAC36465.1.
    AF524864 mRNA. Translation: AAO13380.1.
    BT006794 mRNA. Translation: AAP35440.1.
    CR541801 mRNA. Translation: CAG46600.1.
    AC078847 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24069.1.
    CH471070 Genomic DNA. Translation: EAW83816.1.
    BC008837 mRNA. Translation: AAH08837.1.
    AF044961 mRNA. Translation: AAC15671.1.
    CCDSiCCDS5832.1.
    RefSeqiNP_064695.3. NM_020299.4.
    UniGeneiHs.116724.

    Genome annotation databases

    EnsembliENST00000359579; ENSP00000352584; ENSG00000198074.
    GeneIDi57016.
    KEGGihsa:57016.
    UCSCiuc003vrr.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U37100 mRNA. Translation: AAC17469.1.
    AF052577 mRNA. Translation: AAC36465.1.
    AF524864 mRNA. Translation: AAO13380.1.
    BT006794 mRNA. Translation: AAP35440.1.
    CR541801 mRNA. Translation: CAG46600.1.
    AC078847 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24069.1.
    CH471070 Genomic DNA. Translation: EAW83816.1.
    BC008837 mRNA. Translation: AAH08837.1.
    AF044961 mRNA. Translation: AAC15671.1.
    CCDSiCCDS5832.1.
    RefSeqiNP_064695.3. NM_020299.4.
    UniGeneiHs.116724.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZUAX-ray1.25X1-316[»]
    4GA8X-ray1.94A1-316[»]
    4GABX-ray1.60A1-316[»]
    4GQ0X-ray2.10A1-316[»]
    4GQGX-ray1.92A1-316[»]
    4I5XX-ray2.10A1-316[»]
    4ICCX-ray1.75X1-316[»]
    4JIHX-ray2.30A1-316[»]
    4JIIX-ray2.20X1-316[»]
    4WEVX-ray1.45X1-316[»]
    ProteinModelPortaliO60218.
    SMRiO60218. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121325. 10 interactions.
    IntActiO60218. 1 interaction.
    STRINGi9606.ENSP00000352584.

    Chemistry

    BindingDBiO60218.
    ChEMBLiCHEMBL5983.

    PTM databases

    PhosphoSiteiO60218.

    Polymorphism and mutation databases

    BioMutaiAKR1B10.

    2D gel databases

    DOSAC-COBS-2DPAGEO60218.

    Proteomic databases

    MaxQBiO60218.
    PaxDbiO60218.
    PRIDEiO60218.

    Protocols and materials databases

    DNASUi57016.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000359579; ENSP00000352584; ENSG00000198074.
    GeneIDi57016.
    KEGGihsa:57016.
    UCSCiuc003vrr.3. human.

    Organism-specific databases

    CTDi57016.
    GeneCardsiGC07P134212.
    H-InvDBHIX0007102.
    HIX0033661.
    HGNCiHGNC:382. AKR1B10.
    HPAiCAB070163.
    HPA020280.
    MIMi604707. gene.
    neXtProtiNX_O60218.
    PharmGKBiPA24676.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiO60218.
    KOiK00011.
    OMAiVSNFSHF.
    OrthoDBiEOG70KGQF.
    PhylomeDBiO60218.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BRENDAi1.1.1.21. 2681.
    ReactomeiREACT_24968. Retinoid metabolism and transport.
    SABIO-RKO60218.

    Miscellaneous databases

    EvolutionaryTraceiO60218.
    GeneWikiiAKR1B10.
    GenomeRNAii57016.
    NextBioi62758.
    PROiO60218.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO60218.
    CleanExiHS_AKR1B10.
    GenevestigatoriO60218.

    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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and characterization of a novel human aldose reductase-like gene."
      Cao D., Fan S.T., Chung S.S.M.
      J. Biol. Chem. 273:11429-11435(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-313.
      Tissue: Liver tumor.
    2. "Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family."
      Hyndman D.J., Flynn T.G.
      Biochim. Biophys. Acta 1399:198-202(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Small intestine.
    3. "Representational difference analysis based identification and full-length sequencing of a gene of the aldo-ketoreductase family strongly overexpressed in hepatocellular carcinoma."
      Heringlake S.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-313.
    4. "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], VARIANT ASP-313.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-313.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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], VARIANT ASP-313.
      Tissue: Pancreas.
    10. "New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma."
      Scuric Z., Stain S.C., Anderson W.F., Hwang J.-J.
      Hepatology 27:943-950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 232-316, VARIANT ASP-313.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway."
      Luo D.X., Huang M.C., Ma J., Gao Z., Liao D.F., Cao D.
      Biochem. J. 438:71-80(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10."
      Gallego O., Ruiz F.X., Ardevol A., Dominguez M., Alvarez R., de Lera A.R., Rovira C., Farres J., Fita I., Pares X.
      Proc. Natl. Acad. Sci. U.S.A. 104:20764-20769(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH TOLRESTAT AND NADP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF LYS-125 AND VAL-301.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAK1BA_HUMAN
    AccessioniPrimary (citable) accession number: O60218
    Secondary accession number(s): A4D1P1
    , O75890, Q6FHF3, Q8IWZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2002
    Last sequence update: February 8, 2011
    Last modified: May 27, 2015
    This is version 138 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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

    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 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.