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Protein

Aflatoxin B1 aldehyde reductase member 2

Gene

AKR7A2

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

Functioni

Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.2 Publications

Catalytic activityi

4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH.1 Publication

Kineticsi

  1. KM=20 µM for succinic semialdehyde1 Publication
  2. KM=17 µM for 2-carboxybenzaldehyde1 Publication
  3. KM=8 µM for 9,10-phenanthrenequinone1 Publication
  4. KM=102 µM for 1,2-naphthoquinone1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721NADP1 Publication
    Active sitei77 – 771Proton donorBy similarity
    Sitei105 – 1051Lowers pKa of active site TyrBy similarity
    Binding sitei141 – 1411SubstrateBy similarity
    Binding sitei197 – 1971NADP1 Publication
    Binding sitei250 – 2501NADP1 Publication
    Binding sitei260 – 2601SubstrateBy similarity
    Binding sitei263 – 2631SubstrateBy similarity
    Binding sitei359 – 3591SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi171 – 1722NADP1 Publication
    Nucleotide bindingi226 – 23611NADP1 PublicationAdd
    BLAST
    Nucleotide bindingi318 – 3269NADP1 Publication

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: ProtInc
    • electron carrier activity Source: UniProtKB
    • phenanthrene-9,10-epoxide hydrolase activity Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: ProtInc
    • cellular aldehyde metabolic process Source: ProtInc
    • daunorubicin metabolic process Source: UniProtKB
    • doxorubicin metabolic process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • xenobiotic metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_264461. Aflatoxin activation and detoxification.
    SABIO-RKO43488.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aflatoxin B1 aldehyde reductase member 2 (EC:1.1.1.n11)
    Alternative name(s):
    AFB1 aldehyde reductase 1
    Short name:
    AFB1-AR 1
    Aldoketoreductase 7
    Succinic semialdehyde reductase
    Short name:
    SSA reductase
    Gene namesi
    Name:AKR7A2
    Synonyms:AFAR, AFAR1, AKR7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:389. AKR7A2.

    Subcellular locationi

    • Golgi apparatus By similarity
    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • Golgi apparatus Source: UniProtKB-SubCell
    • mitochondrion Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24682.

    Polymorphism and mutation databases

    BioMutaiAKR7A2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Aflatoxin B1 aldehyde reductase member 2PRO_0000070375Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281N6-acetyllysineBy similarity
    Modified residuei236 – 2361N6-succinyllysineBy similarity
    Modified residuei255 – 2551Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO43488.
    PRIDEiO43488.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00305978.
    O43488.
    UCD-2DPAGEO43488.

    PTM databases

    PhosphoSiteiO43488.

    Miscellaneous databases

    PMAP-CutDBO43488.

    Expressioni

    Tissue specificityi

    Detected in brain, liver, small intestine and testis, and at lower levels in heart, prostate, skeletal muscle and spleen. Detected in kidney proximal and distal tubules, endothelial cells lining the Bowman's capsules and some cysts. Detected at low levels in lung and pancreas (at protein level). Widely expressed.2 Publications

    Gene expression databases

    BgeeiO43488.
    CleanExiHS_AKR7A2.
    ExpressionAtlasiO43488. baseline and differential.
    GenevestigatoriO43488.

    Organism-specific databases

    HPAiCAB032587.
    CAB032841.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi114142. 6 interactions.
    IntActiO43488. 2 interactions.
    MINTiMINT-5002225.
    STRINGi9606.ENSP00000235835.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 435Combined sources
    Turni48 – 503Combined sources
    Helixi53 – 6513Combined sources
    Beta strandi70 – 723Combined sources
    Helixi77 – 804Combined sources
    Helixi81 – 877Combined sources
    Beta strandi101 – 1066Combined sources
    Helixi116 – 13015Combined sources
    Beta strandi135 – 1406Combined sources
    Helixi149 – 16113Combined sources
    Beta strandi164 – 1729Combined sources
    Helixi175 – 18814Combined sources
    Beta strandi193 – 1997Combined sources
    Helixi206 – 2083Combined sources
    Helixi211 – 2188Combined sources
    Beta strandi221 – 2255Combined sources
    Helixi229 – 2346Combined sources
    Helixi239 – 2424Combined sources
    Turni243 – 2453Combined sources
    Beta strandi252 – 2543Combined sources
    Helixi257 – 2648Combined sources
    Helixi267 – 28418Combined sources
    Helixi285 – 2873Combined sources
    Helixi291 – 30212Combined sources
    Helixi307 – 3093Combined sources
    Beta strandi312 – 3154Combined sources
    Helixi320 – 33011Combined sources
    Helixi337 – 35014Combined sources
    Helixi351 – 3533Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BP1X-ray2.40A/B/C/D30-359[»]
    ProteinModelPortaliO43488.
    SMRiO43488. Positions 37-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43488.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0667.
    HOGENOMiHOG000250286.
    HOVERGENiHBG050576.
    InParanoidiO43488.
    KOiK15303.
    OMAiCTVKIAT.
    OrthoDBiEOG77127F.
    PhylomeDBiO43488.
    TreeFamiTF329173.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF51430. SSF51430. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O43488-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLSAASRVVS RAAVHCALRS PPPEARALAM SRPPPPRVAS VLGTMEMGRR
    60 70 80 90 100
    MDAPASAAAV RAFLERGHTE LDTAFMYSDG QSETILGGLG LGLGGGDCRV
    110 120 130 140 150
    KIATKANPWD GKSLKPDSVR SQLETSLKRL QCPQVDLFYL HAPDHGTPVE
    160 170 180 190 200
    ETLHACQRLH QEGKFVELGL SNYASWEVAE ICTLCKSNGW ILPTVYQGMY
    210 220 230 240 250
    NATTRQVETE LFPCLRHFGL RFYAYNPLAG GLLTGKYKYE DKDGKQPVGR
    260 270 280 290 300
    FFGNSWAETY RNRFWKEHHF EAIALVEKAL QAAYGASAPS VTSAALRWMY
    310 320 330 340 350
    HHSQLQGAHG DAVILGMSSL EQLEQNLAAT EEGPLEPAVV DAFNQAWHLV

    AHECPNYFR
    Length:359
    Mass (Da):39,589
    Last modified:November 14, 2003 - v3
    Checksum:i2C9775FE4B977D2A
    GO

    Sequence cautioni

    The sequence AAC52104.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAH04111.3 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAH10852.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAH11586.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAH12171.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAH13996.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAP36011.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA76347.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAB72321.1 differs from that shown. Reason: Erroneous initiation. Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351V → M.
    Corresponds to variant rs6670759 [ dbSNP | Ensembl ].
    VAR_048209
    Natural varianti142 – 1421A → T.2 Publications
    Corresponds to variant rs1043657 [ dbSNP | Ensembl ].
    VAR_017413
    Natural varianti157 – 1571Q → H.1 Publication
    Corresponds to variant rs859208 [ dbSNP | Ensembl ].
    VAR_017414
    Natural varianti180 – 1801E → K.
    Corresponds to variant rs859210 [ dbSNP | Ensembl ].
    VAR_060222
    Natural varianti198 – 1981G → S.
    Corresponds to variant rs2231200 [ dbSNP | Ensembl ].
    VAR_048210
    Natural varianti214 – 2141C → Y.
    Corresponds to variant rs2235794 [ dbSNP | Ensembl ].
    VAR_017415
    Natural varianti255 – 2551S → N.
    Corresponds to variant rs2231203 [ dbSNP | Ensembl ].
    VAR_048211

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035413 Genomic DNA. Translation: CAB72321.1. Different initiation.
    BC004111 mRNA. Translation: AAH04111.3. Different initiation.
    BC007352 mRNA. Translation: AAH07352.2.
    BC010852 mRNA. Translation: AAH10852.1. Different initiation.
    BC011586 mRNA. Translation: AAH11586.1. Different initiation.
    BC012171 mRNA. Translation: AAH12171.1. Different initiation.
    BC013996 mRNA. Translation: AAH13996.1. Different initiation.
    AF026947 mRNA. Translation: AAC52104.1. Different initiation.
    Y16675 mRNA. Translation: CAA76347.1. Different initiation.
    BT007347 mRNA. Translation: AAP36011.1. Different initiation.
    BK000395 mRNA. Translation: DAA00088.1.
    CCDSiCCDS194.1.
    RefSeqiNP_003680.2. NM_003689.3.
    UniGeneiHs.571886.

    Genome annotation databases

    EnsembliENST00000235835; ENSP00000235835; ENSG00000053371.
    GeneIDi8574.
    KEGGihsa:8574.
    UCSCiuc001bbw.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035413 Genomic DNA. Translation: CAB72321.1. Different initiation.
    BC004111 mRNA. Translation: AAH04111.3. Different initiation.
    BC007352 mRNA. Translation: AAH07352.2.
    BC010852 mRNA. Translation: AAH10852.1. Different initiation.
    BC011586 mRNA. Translation: AAH11586.1. Different initiation.
    BC012171 mRNA. Translation: AAH12171.1. Different initiation.
    BC013996 mRNA. Translation: AAH13996.1. Different initiation.
    AF026947 mRNA. Translation: AAC52104.1. Different initiation.
    Y16675 mRNA. Translation: CAA76347.1. Different initiation.
    BT007347 mRNA. Translation: AAP36011.1. Different initiation.
    BK000395 mRNA. Translation: DAA00088.1.
    CCDSiCCDS194.1.
    RefSeqiNP_003680.2. NM_003689.3.
    UniGeneiHs.571886.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BP1X-ray2.40A/B/C/D30-359[»]
    ProteinModelPortaliO43488.
    SMRiO43488. Positions 37-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114142. 6 interactions.
    IntActiO43488. 2 interactions.
    MINTiMINT-5002225.
    STRINGi9606.ENSP00000235835.

    PTM databases

    PhosphoSiteiO43488.

    Polymorphism and mutation databases

    BioMutaiAKR7A2.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00305978.
    O43488.
    UCD-2DPAGEO43488.

    Proteomic databases

    PaxDbiO43488.
    PRIDEiO43488.

    Protocols and materials databases

    DNASUi8574.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000235835; ENSP00000235835; ENSG00000053371.
    GeneIDi8574.
    KEGGihsa:8574.
    UCSCiuc001bbw.3. human.

    Organism-specific databases

    CTDi8574.
    GeneCardsiGC01M019630.
    H-InvDBHIX0000198.
    HGNCiHGNC:389. AKR7A2.
    HPAiCAB032587.
    CAB032841.
    MIMi603418. gene.
    neXtProtiNX_O43488.
    PharmGKBiPA24682.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0667.
    HOGENOMiHOG000250286.
    HOVERGENiHBG050576.
    InParanoidiO43488.
    KOiK15303.
    OMAiCTVKIAT.
    OrthoDBiEOG77127F.
    PhylomeDBiO43488.
    TreeFamiTF329173.

    Enzyme and pathway databases

    ReactomeiREACT_264461. Aflatoxin activation and detoxification.
    SABIO-RKO43488.

    Miscellaneous databases

    EvolutionaryTraceiO43488.
    GeneWikiiAKR7A2.
    GenomeRNAii8574.
    NextBioi32161.
    PMAP-CutDBO43488.
    PROiO43488.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO43488.
    CleanExiHS_AKR7A2.
    ExpressionAtlasiO43488. baseline and differential.
    GenevestigatoriO43488.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF51430. SSF51430. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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] OF 2-359.
      Tissue: Pancreas, Skin and Uterus.
    3. "Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase."
      Ireland L.S., Harrison D.J., Neal G.E., Hayes J.D.
      Biochem. J. 332:21-34(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-359, PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT THR-142.
      Tissue: Liver.
    4. "Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a region frequently altered in human tumor cells."
      Praml C., Savelyeva L., Perri P., Schwab M.
      Cancer Res. 58:5014-5018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-359.
      Tissue: Brain.
    5. "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] OF 30-359.
    6. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 222-236; 251-261 AND 279-297, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    7. "Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members."
      O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D.
      Biochem. J. 343:487-504(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    8. "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins."
      Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.
      Biochem. J. 366:847-861(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE.
    9. "Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2."
      Lyon R.C., Johnston S.M., Watson D.G., McGarvie G., Ellis E.M.
      J. Biol. Chem. 282:25986-25992(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Structure of the aflatoxin aldehyde reductase in complex with NADPH."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
    13. "Genetic variation of aflatoxin B1 aldehyde reductase genes (AFAR) in human tumour cells."
      Praml C., Schulz W., Claas A., Mollenhauer J., Poustka A., Ackermann R., Schwab M., Henrich K.-O.
      Cancer Lett. 272:160-166(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-142 AND HIS-157.

    Entry informationi

    Entry nameiARK72_HUMAN
    AccessioniPrimary (citable) accession number: O43488
    Secondary accession number(s): O75749, Q5TG63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 14, 2003
    Last modified: May 27, 2015
    This is version 148 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

    Caution

    It is uncertain whether Met-1 or Met-30 is the initiator.Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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.