Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P14550

- AK1A1_HUMAN

UniProt

P14550 - AK1A1_HUMAN

Protein

Alcohol dehydrogenase [NADP(+)]

Gene

AKR1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN).3 Publications

    Catalytic activityi

    An alcohol + NADP+ = an aldehyde + NADPH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501Proton donor
    Sitei80 – 801Lowers pKa of active site Tyr
    Binding sitei113 – 1131Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi211 – 27363NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. alditol:NADP+ 1-oxidoreductase activity Source: ProtInc
    2. electron carrier activity Source: UniProtKB
    3. L-glucuronate reductase activity Source: Ensembl

    GO - Biological processi

    1. aldehyde catabolic process Source: Ensembl
    2. cellular aldehyde metabolic process Source: ProtInc
    3. D-glucuronate catabolic process Source: Ensembl
    4. glucose metabolic process Source: ProtInc
    5. L-ascorbic acid biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    SABIO-RKP14550.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
    Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member A1
    Gene namesi
    Name:AKR1A1
    Synonyms:ALDR1, ALR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:380. AKR1A1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. cytosol Source: Ensembl
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501Y → F: Complete loss of enzymatic activity. 1 Publication
    Mutagenesisi50 – 501Y → H: Complete loss of enzymatic activity. 1 Publication
    Mutagenesisi80 – 801K → M: Complete loss of enzymatic activity. 1 Publication
    Mutagenesisi113 – 1131H → Q: Strong decrease in enzymatic activity. 1 Publication
    Mutagenesisi299 – 2991I → A: No change in enzymatic activity. 1 Publication
    Mutagenesisi299 – 2991I → C: No change in enzymatic activity. 1 Publication
    Mutagenesisi300 – 3001V → C: No change in enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24674.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 325324Alcohol dehydrogenase [NADP(+)]PRO_0000124617Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei127 – 1271N6-acetyllysine; alternateBy similarity
    Modified residuei127 – 1271N6-succinyllysine; alternateBy similarity
    Modified residuei145 – 1451N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP14550.
    PaxDbiP14550.
    PeptideAtlasiP14550.
    PRIDEiP14550.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00220271.
    P14550.
    SWISS-2DPAGEP14550.
    UCD-2DPAGEP14550.

    PTM databases

    PhosphoSiteiP14550.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in kidney, salivary gland and liver. Detected in trachea, stomach, brain, lung, prostate, placenta, mammary gland, small intestine and lung.2 Publications

    Gene expression databases

    ArrayExpressiP14550.
    BgeeiP14550.
    CleanExiHS_AKR1A1.
    GenevestigatoriP14550.

    Organism-specific databases

    HPAiCAB006246.
    HPA017919.
    HPA019649.
    HPA027734.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi115610. 4 interactions.
    IntActiP14550. 2 interactions.
    MINTiMINT-5001699.
    STRINGi9606.ENSP00000312606.

    Structurei

    Secondary structure

    1
    325
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Beta strandi13 – 175
    Helixi26 – 3914
    Beta strandi43 – 453
    Helixi48 – 503
    Helixi53 – 6311
    Beta strandi68 – 703
    Helixi72 – 743
    Beta strandi76 – 816
    Helixi83 – 853
    Helixi88 – 10215
    Beta strandi107 – 1137
    Beta strandi115 – 1184
    Beta strandi120 – 1223
    Helixi140 – 15314
    Beta strandi155 – 1639
    Helixi166 – 1738
    Beta strandi182 – 1865
    Helixi194 – 20310
    Beta strandi206 – 2105
    Helixi232 – 24110
    Helixi245 – 25511
    Helixi267 – 2748
    Helixi283 – 2908
    Beta strandi302 – 3054
    Beta strandi308 – 3136
    Beta strandi320 – 3234

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ALRX-ray2.48A2-325[»]
    ProteinModelPortaliP14550.
    SMRiP14550. Positions 2-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14550.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP14550.
    KOiK00002.
    OMAiWPYAFER.
    OrthoDBiEOG70KGQF.
    PhylomeDBiP14550.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY    50
    GNEPEIGEAL KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA 100
    DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTICYDSTHY KETWKALEAL 150
    VAKGLVQALG LSNFNSRQID DILSVASVRP AVLQVECHPY LAQNELIAHC 200
    QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEK YGRSPAQILL 250
    RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV 300
    PMLTVDGKRV PRDAGHPLYP FNDPY 325
    Length:325
    Mass (Da):36,573
    Last modified:January 23, 2007 - v3
    Checksum:iF6B27517EB754E37
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3051V → A in BAF85772. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521N → S Reduced activity towards daunorubicin.
    Corresponds to variant rs2229540 [ dbSNP | Ensembl ].
    VAR_048212
    Natural varianti55 – 551E → D Reduced activity towards daunorubicin.
    Corresponds to variant rs6690497 [ dbSNP | Ensembl ].
    VAR_058909

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04794 mRNA. Translation: AAA51711.1.
    AF036683
    , AF036680, AF036681, AF036682 Genomic DNA. Translation: AAB92369.1.
    AF112485, AF112484 Genomic DNA. Translation: AAF01260.1.
    AK293083 mRNA. Translation: BAF85772.1.
    CR457010 mRNA. Translation: CAG33291.1.
    BT007003 mRNA. Translation: AAP35649.1.
    AL355480 Genomic DNA. Translation: CAI22459.1.
    CH471059 Genomic DNA. Translation: EAX06970.1.
    CH471059 Genomic DNA. Translation: EAX06971.1.
    CH471059 Genomic DNA. Translation: EAX06972.1.
    CH471059 Genomic DNA. Translation: EAX06974.1.
    BC000670 mRNA. Translation: AAH00670.1.
    BC005394 mRNA. Translation: AAH05394.1.
    CCDSiCCDS523.1.
    PIRiA33851.
    RefSeqiNP_001189342.1. NM_001202413.1.
    NP_001189343.1. NM_001202414.1.
    NP_006057.1. NM_006066.3.
    NP_697021.1. NM_153326.2.
    UniGeneiHs.474584.
    Hs.721160.

    Genome annotation databases

    EnsembliENST00000351829; ENSP00000312606; ENSG00000117448.
    ENST00000372070; ENSP00000361140; ENSG00000117448.
    GeneIDi10327.
    KEGGihsa:10327.
    UCSCiuc001cod.3. human.

    Polymorphism databases

    DMDMi113600.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04794 mRNA. Translation: AAA51711.1 .
    AF036683
    , AF036680 , AF036681 , AF036682 Genomic DNA. Translation: AAB92369.1 .
    AF112485 , AF112484 Genomic DNA. Translation: AAF01260.1 .
    AK293083 mRNA. Translation: BAF85772.1 .
    CR457010 mRNA. Translation: CAG33291.1 .
    BT007003 mRNA. Translation: AAP35649.1 .
    AL355480 Genomic DNA. Translation: CAI22459.1 .
    CH471059 Genomic DNA. Translation: EAX06970.1 .
    CH471059 Genomic DNA. Translation: EAX06971.1 .
    CH471059 Genomic DNA. Translation: EAX06972.1 .
    CH471059 Genomic DNA. Translation: EAX06974.1 .
    BC000670 mRNA. Translation: AAH00670.1 .
    BC005394 mRNA. Translation: AAH05394.1 .
    CCDSi CCDS523.1.
    PIRi A33851.
    RefSeqi NP_001189342.1. NM_001202413.1.
    NP_001189343.1. NM_001202414.1.
    NP_006057.1. NM_006066.3.
    NP_697021.1. NM_153326.2.
    UniGenei Hs.474584.
    Hs.721160.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ALR X-ray 2.48 A 2-325 [» ]
    ProteinModelPortali P14550.
    SMRi P14550. Positions 2-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115610. 4 interactions.
    IntActi P14550. 2 interactions.
    MINTi MINT-5001699.
    STRINGi 9606.ENSP00000312606.

    Chemistry

    BindingDBi P14550.
    ChEMBLi CHEMBL2246.
    DrugBanki DB00997. Doxorubicin.

    PTM databases

    PhosphoSitei P14550.

    Polymorphism databases

    DMDMi 113600.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00220271.
    P14550.
    SWISS-2DPAGE P14550.
    UCD-2DPAGE P14550.

    Proteomic databases

    MaxQBi P14550.
    PaxDbi P14550.
    PeptideAtlasi P14550.
    PRIDEi P14550.

    Protocols and materials databases

    DNASUi 10327.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351829 ; ENSP00000312606 ; ENSG00000117448 .
    ENST00000372070 ; ENSP00000361140 ; ENSG00000117448 .
    GeneIDi 10327.
    KEGGi hsa:10327.
    UCSCi uc001cod.3. human.

    Organism-specific databases

    CTDi 10327.
    GeneCardsi GC01P046017.
    HGNCi HGNC:380. AKR1A1.
    HPAi CAB006246.
    HPA017919.
    HPA019649.
    HPA027734.
    MIMi 103830. gene.
    neXtProti NX_P14550.
    PharmGKBi PA24674.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi P14550.
    KOi K00002.
    OMAi WPYAFER.
    OrthoDBi EOG70KGQF.
    PhylomeDBi P14550.
    TreeFami TF106492.

    Enzyme and pathway databases

    SABIO-RK P14550.

    Miscellaneous databases

    ChiTaRSi AKR1A1. human.
    EvolutionaryTracei P14550.
    GeneWikii Aldo-keto_reductase_family_1,_member_A1.
    GenomeRNAii 10327.
    NextBioi 39151.
    PROi P14550.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14550.
    Bgeei P14550.
    CleanExi HS_AKR1A1.
    Genevestigatori P14550.

    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. "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases."
      Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.
      J. Biol. Chem. 264:9547-9551(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32."
      Fujii J., Hamaoka R., Matsumoto A., Fujii T., Yamaguchi Y., Egashira M., Miyoshi O., Niikawa N., Taniguchi N.
      Cytogenet. Cell Genet. 84:230-232(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Characterization of the human aldehyde reductase gene and promoter."
      Barski O.A., Gabbay K.H., Bohren K.M.
      Genomics 60:188-198(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    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].
    6. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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].
    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].
      Tissue: Colon and Kidney.
    10. "Primary structure of aldehyde reductase from human liver."
      Wermuth B., Omar A., Forster A., di Francesco C., Wolf M., von Wartburg J.-P., Bullock B., Gabbay K.H.
      Prog. Clin. Biol. Res. 232:297-307(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-325.
      Tissue: Liver.
    11. "Mechanism of human aldehyde reductase: characterization of the active site pocket."
      Barski O.A., Gabbay K.H., Grimshaw C.E., Bohren K.M.
      Biochemistry 34:11264-11275(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-50; LYS-80; HIS-113; ILE-299 AND VAL-300.
    12. "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: FUNCTION, TISSUE SPECIFICITY.
    13. "Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1)."
      Palackal N.T., Burczynski M.E., Harvey R.G., Penning T.M.
      Chem. Biol. Interact. 130:815-824(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    14. "Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin."
      Bains O.S., Takahashi R.H., Pfeifer T.A., Grigliatti T.A., Reid R.E., Riggs K.W.
      Drug Metab. Dispos. 36:904-910(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS SER-52 AND ASP-55.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications."
      El-Kabbani O., Green N.C., Lin G., Carson M., Narayana S.V.L., Moore K.M., Flynn T.G., DeLucas L.J.
      Acta Crystallogr. D 50:859-868(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).

    Entry informationi

    Entry nameiAK1A1_HUMAN
    AccessioniPrimary (citable) accession number: P14550
    Secondary accession number(s): A8KAL8, D3DQ04, Q6IAZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 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 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