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O60218

- AK1BA_HUMAN

UniProt

O60218 - AK1BA_HUMAN

Protein

Aldo-keto reductase family 1 member B10

Gene

AKR1B10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (08 Feb 2011)
      Previous versions | rss
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    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 donor
    Sitei78 – 781Lowers pKa of active site TyrBy similarity
    Binding sitei111 – 1111Substrate
    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

    1. aldo-keto reductase (NADP) activity Source: UniProtKB
    2. geranylgeranyl reductase activity Source: UniProtKB
    3. indanol dehydrogenase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. retinal dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. cellular aldehyde metabolic process Source: ProtInc
    2. daunorubicin metabolic process Source: UniProtKB
    3. digestion Source: ProtInc
    4. doxorubicin metabolic process Source: UniProtKB
    5. farnesol catabolic process Source: UniProtKB
    6. phototransduction, visible light Source: Reactome
    7. retinoid metabolic process Source: Reactome
    8. steroid metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    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: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:382. AKR1B10.

    Subcellular locationi

    Lysosome 1 Publication. Secreted 1 Publication
    Note: Secreted through a lysosome-mediated non-classical pathway.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB-SubCell

    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.

    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

    HPAiHPA020280.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi121325. 3 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 – 63
    Beta strandi12 – 198
    Turni25 – 273
    Helixi28 – 3710
    Beta strandi42 – 443
    Helixi47 – 493
    Helixi52 – 6413
    Helixi70 – 723
    Beta strandi74 – 796
    Helixi81 – 833
    Helixi86 – 10015
    Beta strandi105 – 1117
    Beta strandi118 – 1203
    Beta strandi127 – 1315
    Helixi138 – 15013
    Beta strandi153 – 1619
    Helixi164 – 1718
    Beta strandi181 – 1866
    Helixi194 – 2029
    Beta strandi206 – 2116
    Helixi228 – 2303
    Helixi232 – 2409
    Helixi245 – 25410
    Turni255 – 2573
    Helixi267 – 2748
    Helixi283 – 2908
    Helixi302 – 3043
    Beta strandi305 – 3073
    Helixi311 – 3133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiO60218.
    KOiK00011.
    OMAiTSKLWLQ.
    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

    MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ    50
    NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVR KAFEKTLKDL 100
    KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD 150
    EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC 200
    HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI 250
    RFHIQRNVIV IPKSVTPARI VENIQVFDFK LSDEEMATIL SFNRNWRACN 300
    VLQSSHLEDY PFNAEY 316
    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. 1 PublicationCurated
    Sequence conflicti100 – 1001L → P in AAO13380. 1 PublicationCurated
    Sequence conflicti288 – 2881T → I in AAO13380. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5832.1.
    RefSeqi NP_064695.3. NM_020299.4.
    UniGenei Hs.116724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZUA X-ray 1.25 X 1-316 [» ]
    4GA8 X-ray 1.94 A 1-316 [» ]
    4GAB X-ray 1.60 A 1-316 [» ]
    4GQ0 X-ray 2.10 A 1-316 [» ]
    4GQG X-ray 1.92 A 1-316 [» ]
    4I5X X-ray 2.10 A 1-316 [» ]
    4ICC X-ray 1.75 X 1-316 [» ]
    4JIH X-ray 2.30 A 1-316 [» ]
    4JII X-ray 2.20 X 1-316 [» ]
    ProteinModelPortali O60218.
    SMRi O60218. Positions 1-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121325. 3 interactions.
    IntActi O60218. 1 interaction.
    STRINGi 9606.ENSP00000352584.

    Chemistry

    BindingDBi O60218.
    ChEMBLi CHEMBL5983.

    PTM databases

    PhosphoSitei O60218.

    2D gel databases

    DOSAC-COBS-2DPAGE O60218.

    Proteomic databases

    MaxQBi O60218.
    PaxDbi O60218.
    PRIDEi O60218.

    Protocols and materials databases

    DNASUi 57016.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359579 ; ENSP00000352584 ; ENSG00000198074 .
    GeneIDi 57016.
    KEGGi hsa:57016.
    UCSCi uc003vrr.3. human.

    Organism-specific databases

    CTDi 57016.
    GeneCardsi GC07P134212.
    H-InvDB HIX0007102.
    HIX0033661.
    HGNCi HGNC:382. AKR1B10.
    HPAi HPA020280.
    MIMi 604707. gene.
    neXtProti NX_O60218.
    PharmGKBi PA24676.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi O60218.
    KOi K00011.
    OMAi TSKLWLQ.
    OrthoDBi EOG70KGQF.
    PhylomeDBi O60218.
    TreeFami TF106492.

    Enzyme and pathway databases

    Reactomei REACT_24968. Retinoid metabolism and transport.
    SABIO-RK O60218.

    Miscellaneous databases

    EvolutionaryTracei O60218.
    GeneWikii AKR1B10.
    GenomeRNAii 57016.
    NextBioi 62758.
    PROi O60218.
    SOURCEi Search...

    Gene expression databases

    Bgeei O60218.
    CleanExi HS_AKR1B10.
    Genevestigatori O60218.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    PANTHERi PTHR11732. PTHR11732. 1 hit.
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000097. AKR. 1 hit.
    PRINTSi PR00069. ALDKETRDTASE.
    SUPFAMi SSF51430. SSF51430. 1 hit.
    PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 131 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

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