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P15121

- ALDR_HUMAN

UniProt

P15121 - ALDR_HUMAN

Protein

Aldose reductase

Gene

AKR1B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.

    Catalytic activityi

    Alditol + NAD(P)+ = aldose + NAD(P)H.

    Enzyme regulationi

    Cys-299 may regulate the kinetic and inhibition properties of the enzyme, but does not participate in catalysis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei49 – 491Proton donor1 Publication
    Sitei78 – 781Lowers pKa of active site Tyr
    Binding sitei111 – 1111Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 1910NADPSequence Analysis
    Nucleotide bindingi211 – 27363NADP6 PublicationsAdd
    BLAST

    GO - Molecular functioni

    1. alditol:NADP+ 1-oxidoreductase activity Source: ProtInc
    2. aldo-keto reductase (NADP) activity Source: UniProtKB
    3. electron carrier activity Source: UniProtKB
    4. glyceraldehyde oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. C21-steroid hormone biosynthetic process Source: Reactome
    2. carbohydrate metabolic process Source: ProtInc
    3. daunorubicin metabolic process Source: UniProtKB
    4. doxorubicin metabolic process Source: UniProtKB
    5. response to stress Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. steroid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01502-MONOMER.
    BRENDAi1.1.1.21. 2681.
    ReactomeiREACT_11038. Pregnenolone biosynthesis.
    SABIO-RKP15121.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldose reductase (EC:1.1.1.21)
    Short name:
    AR
    Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member B1
    Gene namesi
    Name:AKR1B1
    Synonyms:ALDR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:381. AKR1B1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular space Source: ProtInc
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441D → N: Reduced enzymatic activity. 1 Publication
    Mutagenesisi49 – 491Y → F: Complete loss of enzymatic activity. 1 Publication
    Mutagenesisi78 – 781K → M: Reduced enzymatic activity. 1 Publication
    Mutagenesisi111 – 1111H → N: Reduced enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24675.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 316315Aldose reductasePRO_0000124623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei95 – 951N6-acetyllysine1 Publication
    Modified residuei222 – 2221N6-acetyllysine1 Publication
    Modified residuei263 – 2631N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP15121.
    PaxDbiP15121.
    PeptideAtlasiP15121.
    PRIDEiP15121.

    2D gel databases

    DOSAC-COBS-2DPAGEP15121.
    REPRODUCTION-2DPAGEIPI00413641.
    P15121.
    UCD-2DPAGEP15121.

    PTM databases

    PhosphoSiteiP15121.

    Expressioni

    Tissue specificityi

    Highly expressed in embryonic epithelial cells (EUE) in response to osmotic stress.1 Publication

    Gene expression databases

    ArrayExpressiP15121.
    BgeeiP15121.
    CleanExiHS_AKR1B1.
    GenevestigatoriP15121.

    Organism-specific databases

    HPAiCAB018773.
    CAB027391.
    CAB047353.
    HPA026425.
    HPA052751.

    Interactioni

    Subunit structurei

    Monomer.6 Publications

    Protein-protein interaction databases

    BioGridi106732. 8 interactions.
    IntActiP15121. 2 interactions.
    MINTiMINT-1196717.
    STRINGi9606.ENSP00000285930.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi12 – 165
    Helixi25 – 3814
    Beta strandi42 – 443
    Helixi47 – 493
    Helixi52 – 6413
    Helixi70 – 723
    Beta strandi74 – 796
    Helixi81 – 833
    Turni86 – 883
    Helixi89 – 10012
    Beta strandi105 – 1139
    Beta strandi118 – 1203
    Beta strandi127 – 1293
    Helixi138 – 15013
    Beta strandi153 – 1553
    Beta strandi157 – 1615
    Helixi164 – 1718
    Beta strandi181 – 1866
    Helixi194 – 2029
    Beta strandi206 – 2116
    Beta strandi223 – 2253
    Turni228 – 2303
    Helixi232 – 24110
    Helixi245 – 25511
    Beta strandi259 – 2613
    Helixi267 – 2748
    Helixi283 – 2908
    Helixi302 – 3043
    Beta strandi307 – 3093
    Beta strandi311 – 3144

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ABNX-ray2.40A2-316[»]
    1ADSX-ray1.65A2-316[»]
    1AZ1X-ray1.80A2-316[»]
    1AZ2X-ray2.90A2-316[»]
    1EF3X-ray2.80A/B2-316[»]
    1EL3X-ray1.70A1-316[»]
    1IEIX-ray2.50A1-316[»]
    1MARX-ray1.80A2-316[»]
    1PWLX-ray1.10A1-316[»]
    1PWMX-ray0.92A1-316[»]
    1T40X-ray1.80A1-316[»]
    1T41X-ray1.05A1-316[»]
    1US0X-ray0.66A1-316[»]
    1X96X-ray1.40A1-316[»]
    1X97X-ray1.40A1-316[»]
    1X98X-ray1.30A1-316[»]
    1XGDX-ray2.10A2-316[»]
    1Z3NX-ray1.04A1-316[»]
    1Z89X-ray1.43A1-316[»]
    1Z8AX-ray0.95A1-316[»]
    2ACQX-ray1.76A2-316[»]
    2ACRX-ray1.76A2-316[»]
    2ACSX-ray1.76A2-316[»]
    2ACUX-ray1.76A2-316[»]
    2AGTX-ray1.00A1-316[»]
    2DUXX-ray1.60A1-316[»]
    2DUZX-ray1.60A1-316[»]
    2DV0X-ray1.62A1-316[»]
    2F2KX-ray1.94A1-316[»]
    2FZ8X-ray1.48A1-316[»]
    2FZ9X-ray1.60A1-316[»]
    2FZBX-ray1.50A6-316[»]
    2FZDX-ray1.08A6-316[»]
    2HV5X-ray1.59A1-316[»]
    2HVNX-ray1.58A1-316[»]
    2HVOX-ray1.65A1-316[»]
    2I16X-ray0.81A1-316[»]
    2I17X-ray0.81A1-316[»]
    2IKGX-ray1.43A1-316[»]
    2IKHX-ray1.55A1-316[»]
    2IKIX-ray1.47A1-316[»]
    2IKJX-ray1.55A1-316[»]
    2INEX-ray1.90A2-316[»]
    2INZX-ray1.95A2-316[»]
    2IPWX-ray2.00A2-316[»]
    2IQ0X-ray1.95A2-316[»]
    2IQDX-ray2.00A2-316[»]
    2IS7X-ray1.70A2-316[»]
    2ISFX-ray2.00A2-316[»]
    2J8TX-ray0.82A6-316[»]
    2NVCX-ray1.65A1-316[»]
    2NVDX-ray1.55A1-316[»]
    2PD5X-ray1.60A1-316[»]
    2PD9X-ray1.55A1-316[»]
    2PDBX-ray1.60A1-316[»]
    2PDCX-ray1.65A1-316[»]
    2PDFX-ray1.56A1-316[»]
    2PDGX-ray1.42A1-316[»]
    2PDHX-ray1.45A1-316[»]
    2PDIX-ray1.55A1-316[»]
    2PDJX-ray1.57A1-316[»]
    2PDKX-ray1.55A1-316[»]
    2PDLX-ray1.47A1-316[»]
    2PDMX-ray1.75A1-316[»]
    2PDNX-ray1.70A1-316[»]
    2PDPX-ray1.65A1-316[»]
    2PDQX-ray1.73A1-316[»]
    2PDUX-ray1.55A1-316[»]
    2PDWX-ray1.55A1-316[»]
    2PDXX-ray1.65A1-316[»]
    2PDYX-ray1.65A1-316[»]
    2PEVX-ray0.90A1-316[»]
    2PF8X-ray0.85A1-316[»]
    2PFHX-ray0.85A1-316[»]
    2PZNX-ray1.00A1-316[»]
    2QXWX-ray0.80A1-316[»]
    2R24X-ray1.75A1-316[»]
    3BCJX-ray0.78A1-316[»]
    3DN5X-ray1.45A1-316[»]
    3G5EX-ray1.80A1-316[»]
    3GHRX-ray1.00A1-316[»]
    3GHSX-ray1.00A1-316[»]
    3GHTX-ray1.10A1-316[»]
    3GHUX-ray1.20A1-316[»]
    3LBOX-ray1.10A1-316[»]
    3LD5X-ray1.27A1-316[»]
    3LENX-ray1.21A1-316[»]
    3LEPX-ray0.99A1-316[»]
    3LQGX-ray1.35A1-316[»]
    3LQLX-ray1.13A1-316[»]
    3LZ3X-ray1.03A1-316[»]
    3LZ5X-ray0.95A1-316[»]
    3M0IX-ray1.07A1-316[»]
    3M4HX-ray0.94A1-316[»]
    3M64X-ray1.30A1-316[»]
    3MB9X-ray1.65A1-316[»]
    3MC5X-ray1.14A1-316[»]
    3ONBX-ray1.45A2-316[»]
    3ONCX-ray1.06A2-316[»]
    3P2VX-ray1.69A1-316[»]
    3Q65X-ray2.09A/B1-316[»]
    3Q67X-ray1.55A/B1-316[»]
    3RX2X-ray1.90A1-316[»]
    3RX3X-ray1.90A1-316[»]
    3RX4X-ray2.00A1-316[»]
    3S3GX-ray1.80A1-316[»]
    3T42X-ray1.28A1-316[»]
    3U2CX-ray1.00A1-316[»]
    3V35X-ray1.90A1-316[»]
    3V36X-ray2.00A1-316[»]
    4GCAX-ray0.90A2-316[»]
    4GQ0X-ray2.10A1-316[»]
    4IGSX-ray0.85A1-316[»]
    4JIRX-ray2.00A1-316[»]
    4LAUX-ray0.84A1-316[»]
    4LAZX-ray0.85A1-316[»]
    4LB3X-ray0.80A1-316[»]
    4LB4X-ray0.80A1-316[»]
    4LBRX-ray0.80A1-316[»]
    4LBSX-ray0.76A1-316[»]
    ProteinModelPortaliP15121.
    SMRiP15121. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15121.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    HOVERGENiHBG000020.
    InParanoidiP15121.
    KOiK00011.
    OMAiDFLDTWT.
    OrthoDBiEOG70KGQF.
    PhylomeDBiP15121.
    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.

    P15121-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ    50
    NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL 100
    KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD 150
    EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC 200
    QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI 250
    RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA 300
    LLSCTSHKDY PFHEEF 316
    Length:316
    Mass (Da):35,853
    Last modified:January 23, 2007 - v3
    Checksum:i1852E8616B5DCEAE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51L → I in AAA51714. (PubMed:2504709)Curated
    Sequence conflicti114 – 1141T → I in CAG47000. 1 PublicationCurated
    Sequence conflicti117 – 1171K → R in CAG29347. 1 PublicationCurated
    Sequence conflicti142 – 1421W → R in AAH05387. (PubMed:15489334)Curated
    Sequence conflicti172 – 1721N → S in CAG29347. 1 PublicationCurated
    Sequence conflicti270 – 2723IAE → EAA AA sequence (PubMed:2492527)Curated
    Sequence conflicti307 – 3071H → M AA sequence (PubMed:8343525)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151I → F.
    Corresponds to variant rs5054 [ dbSNP | Ensembl ].
    VAR_014743
    Natural varianti42 – 421H → L.
    Corresponds to variant rs5056 [ dbSNP | Ensembl ].
    VAR_014744
    Natural varianti73 – 731L → V.
    Corresponds to variant rs5057 [ dbSNP | Ensembl ].
    VAR_014745
    Natural varianti90 – 901K → E.
    Corresponds to variant rs2229542 [ dbSNP | Ensembl ].
    VAR_048213
    Natural varianti204 – 2041G → S.
    Corresponds to variant rs5061 [ dbSNP | Ensembl ].
    VAR_014746
    Natural varianti288 – 2881T → I.
    Corresponds to variant rs5062 [ dbSNP | Ensembl ].
    VAR_014747

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04795 mRNA. Translation: AAA51713.1.
    J05017 mRNA. Translation: AAA51714.1.
    X15414 mRNA. Translation: CAA33460.1.
    M34720 mRNA. Translation: AAA35560.1.
    M34721 Genomic DNA. Translation: AAA35561.1.
    J05474 mRNA. Translation: AAA51715.1.
    M59783, M59856 Genomic DNA. Translation: AAA51712.1.
    AF032455 Genomic DNA. Translation: AAB88851.1.
    AF328729 mRNA. Translation: AAN09721.1.
    AK313439 mRNA. Translation: BAG36230.1.
    CR450351 mRNA. Translation: CAG29347.1.
    CR542203 mRNA. Translation: CAG47000.1.
    BT019859 mRNA. Translation: AAV38662.1.
    CH236950 Genomic DNA. Translation: EAL24070.1.
    CH471070 Genomic DNA. Translation: EAW83814.1.
    BC000260 mRNA. Translation: AAH00260.1.
    BC005387 mRNA. Translation: AAH05387.1.
    BC010391 mRNA. Translation: AAH10391.1.
    CCDSiCCDS5831.1.
    PIRiA39763.
    RefSeqiNP_001619.1. NM_001628.2.
    UniGeneiHs.521212.

    Genome annotation databases

    EnsembliENST00000285930; ENSP00000285930; ENSG00000085662.
    GeneIDi231.
    KEGGihsa:231.
    UCSCiuc003vrp.1. human.

    Polymorphism databases

    DMDMi113596.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04795 mRNA. Translation: AAA51713.1 .
    J05017 mRNA. Translation: AAA51714.1 .
    X15414 mRNA. Translation: CAA33460.1 .
    M34720 mRNA. Translation: AAA35560.1 .
    M34721 Genomic DNA. Translation: AAA35561.1 .
    J05474 mRNA. Translation: AAA51715.1 .
    M59783 , M59856 Genomic DNA. Translation: AAA51712.1 .
    AF032455 Genomic DNA. Translation: AAB88851.1 .
    AF328729 mRNA. Translation: AAN09721.1 .
    AK313439 mRNA. Translation: BAG36230.1 .
    CR450351 mRNA. Translation: CAG29347.1 .
    CR542203 mRNA. Translation: CAG47000.1 .
    BT019859 mRNA. Translation: AAV38662.1 .
    CH236950 Genomic DNA. Translation: EAL24070.1 .
    CH471070 Genomic DNA. Translation: EAW83814.1 .
    BC000260 mRNA. Translation: AAH00260.1 .
    BC005387 mRNA. Translation: AAH05387.1 .
    BC010391 mRNA. Translation: AAH10391.1 .
    CCDSi CCDS5831.1.
    PIRi A39763.
    RefSeqi NP_001619.1. NM_001628.2.
    UniGenei Hs.521212.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ABN X-ray 2.40 A 2-316 [» ]
    1ADS X-ray 1.65 A 2-316 [» ]
    1AZ1 X-ray 1.80 A 2-316 [» ]
    1AZ2 X-ray 2.90 A 2-316 [» ]
    1EF3 X-ray 2.80 A/B 2-316 [» ]
    1EL3 X-ray 1.70 A 1-316 [» ]
    1IEI X-ray 2.50 A 1-316 [» ]
    1MAR X-ray 1.80 A 2-316 [» ]
    1PWL X-ray 1.10 A 1-316 [» ]
    1PWM X-ray 0.92 A 1-316 [» ]
    1T40 X-ray 1.80 A 1-316 [» ]
    1T41 X-ray 1.05 A 1-316 [» ]
    1US0 X-ray 0.66 A 1-316 [» ]
    1X96 X-ray 1.40 A 1-316 [» ]
    1X97 X-ray 1.40 A 1-316 [» ]
    1X98 X-ray 1.30 A 1-316 [» ]
    1XGD X-ray 2.10 A 2-316 [» ]
    1Z3N X-ray 1.04 A 1-316 [» ]
    1Z89 X-ray 1.43 A 1-316 [» ]
    1Z8A X-ray 0.95 A 1-316 [» ]
    2ACQ X-ray 1.76 A 2-316 [» ]
    2ACR X-ray 1.76 A 2-316 [» ]
    2ACS X-ray 1.76 A 2-316 [» ]
    2ACU X-ray 1.76 A 2-316 [» ]
    2AGT X-ray 1.00 A 1-316 [» ]
    2DUX X-ray 1.60 A 1-316 [» ]
    2DUZ X-ray 1.60 A 1-316 [» ]
    2DV0 X-ray 1.62 A 1-316 [» ]
    2F2K X-ray 1.94 A 1-316 [» ]
    2FZ8 X-ray 1.48 A 1-316 [» ]
    2FZ9 X-ray 1.60 A 1-316 [» ]
    2FZB X-ray 1.50 A 6-316 [» ]
    2FZD X-ray 1.08 A 6-316 [» ]
    2HV5 X-ray 1.59 A 1-316 [» ]
    2HVN X-ray 1.58 A 1-316 [» ]
    2HVO X-ray 1.65 A 1-316 [» ]
    2I16 X-ray 0.81 A 1-316 [» ]
    2I17 X-ray 0.81 A 1-316 [» ]
    2IKG X-ray 1.43 A 1-316 [» ]
    2IKH X-ray 1.55 A 1-316 [» ]
    2IKI X-ray 1.47 A 1-316 [» ]
    2IKJ X-ray 1.55 A 1-316 [» ]
    2INE X-ray 1.90 A 2-316 [» ]
    2INZ X-ray 1.95 A 2-316 [» ]
    2IPW X-ray 2.00 A 2-316 [» ]
    2IQ0 X-ray 1.95 A 2-316 [» ]
    2IQD X-ray 2.00 A 2-316 [» ]
    2IS7 X-ray 1.70 A 2-316 [» ]
    2ISF X-ray 2.00 A 2-316 [» ]
    2J8T X-ray 0.82 A 6-316 [» ]
    2NVC X-ray 1.65 A 1-316 [» ]
    2NVD X-ray 1.55 A 1-316 [» ]
    2PD5 X-ray 1.60 A 1-316 [» ]
    2PD9 X-ray 1.55 A 1-316 [» ]
    2PDB X-ray 1.60 A 1-316 [» ]
    2PDC X-ray 1.65 A 1-316 [» ]
    2PDF X-ray 1.56 A 1-316 [» ]
    2PDG X-ray 1.42 A 1-316 [» ]
    2PDH X-ray 1.45 A 1-316 [» ]
    2PDI X-ray 1.55 A 1-316 [» ]
    2PDJ X-ray 1.57 A 1-316 [» ]
    2PDK X-ray 1.55 A 1-316 [» ]
    2PDL X-ray 1.47 A 1-316 [» ]
    2PDM X-ray 1.75 A 1-316 [» ]
    2PDN X-ray 1.70 A 1-316 [» ]
    2PDP X-ray 1.65 A 1-316 [» ]
    2PDQ X-ray 1.73 A 1-316 [» ]
    2PDU X-ray 1.55 A 1-316 [» ]
    2PDW X-ray 1.55 A 1-316 [» ]
    2PDX X-ray 1.65 A 1-316 [» ]
    2PDY X-ray 1.65 A 1-316 [» ]
    2PEV X-ray 0.90 A 1-316 [» ]
    2PF8 X-ray 0.85 A 1-316 [» ]
    2PFH X-ray 0.85 A 1-316 [» ]
    2PZN X-ray 1.00 A 1-316 [» ]
    2QXW X-ray 0.80 A 1-316 [» ]
    2R24 X-ray 1.75 A 1-316 [» ]
    3BCJ X-ray 0.78 A 1-316 [» ]
    3DN5 X-ray 1.45 A 1-316 [» ]
    3G5E X-ray 1.80 A 1-316 [» ]
    3GHR X-ray 1.00 A 1-316 [» ]
    3GHS X-ray 1.00 A 1-316 [» ]
    3GHT X-ray 1.10 A 1-316 [» ]
    3GHU X-ray 1.20 A 1-316 [» ]
    3LBO X-ray 1.10 A 1-316 [» ]
    3LD5 X-ray 1.27 A 1-316 [» ]
    3LEN X-ray 1.21 A 1-316 [» ]
    3LEP X-ray 0.99 A 1-316 [» ]
    3LQG X-ray 1.35 A 1-316 [» ]
    3LQL X-ray 1.13 A 1-316 [» ]
    3LZ3 X-ray 1.03 A 1-316 [» ]
    3LZ5 X-ray 0.95 A 1-316 [» ]
    3M0I X-ray 1.07 A 1-316 [» ]
    3M4H X-ray 0.94 A 1-316 [» ]
    3M64 X-ray 1.30 A 1-316 [» ]
    3MB9 X-ray 1.65 A 1-316 [» ]
    3MC5 X-ray 1.14 A 1-316 [» ]
    3ONB X-ray 1.45 A 2-316 [» ]
    3ONC X-ray 1.06 A 2-316 [» ]
    3P2V X-ray 1.69 A 1-316 [» ]
    3Q65 X-ray 2.09 A/B 1-316 [» ]
    3Q67 X-ray 1.55 A/B 1-316 [» ]
    3RX2 X-ray 1.90 A 1-316 [» ]
    3RX3 X-ray 1.90 A 1-316 [» ]
    3RX4 X-ray 2.00 A 1-316 [» ]
    3S3G X-ray 1.80 A 1-316 [» ]
    3T42 X-ray 1.28 A 1-316 [» ]
    3U2C X-ray 1.00 A 1-316 [» ]
    3V35 X-ray 1.90 A 1-316 [» ]
    3V36 X-ray 2.00 A 1-316 [» ]
    4GCA X-ray 0.90 A 2-316 [» ]
    4GQ0 X-ray 2.10 A 1-316 [» ]
    4IGS X-ray 0.85 A 1-316 [» ]
    4JIR X-ray 2.00 A 1-316 [» ]
    4LAU X-ray 0.84 A 1-316 [» ]
    4LAZ X-ray 0.85 A 1-316 [» ]
    4LB3 X-ray 0.80 A 1-316 [» ]
    4LB4 X-ray 0.80 A 1-316 [» ]
    4LBR X-ray 0.80 A 1-316 [» ]
    4LBS X-ray 0.76 A 1-316 [» ]
    ProteinModelPortali P15121.
    SMRi P15121. Positions 1-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106732. 8 interactions.
    IntActi P15121. 2 interactions.
    MINTi MINT-1196717.
    STRINGi 9606.ENSP00000285930.

    Chemistry

    BindingDBi P15121.
    ChEMBLi CHEMBL1900.
    DrugBanki DB00605. Sulindac.
    GuidetoPHARMACOLOGYi 2768.

    PTM databases

    PhosphoSitei P15121.

    Polymorphism databases

    DMDMi 113596.

    2D gel databases

    DOSAC-COBS-2DPAGE P15121.
    REPRODUCTION-2DPAGE IPI00413641.
    P15121.
    UCD-2DPAGE P15121.

    Proteomic databases

    MaxQBi P15121.
    PaxDbi P15121.
    PeptideAtlasi P15121.
    PRIDEi P15121.

    Protocols and materials databases

    DNASUi 231.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285930 ; ENSP00000285930 ; ENSG00000085662 .
    GeneIDi 231.
    KEGGi hsa:231.
    UCSCi uc003vrp.1. human.

    Organism-specific databases

    CTDi 231.
    GeneCardsi GC07M134127.
    HGNCi HGNC:381. AKR1B1.
    HPAi CAB018773.
    CAB027391.
    CAB047353.
    HPA026425.
    HPA052751.
    MIMi 103880. gene.
    neXtProti NX_P15121.
    PharmGKBi PA24675.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOVERGENi HBG000020.
    InParanoidi P15121.
    KOi K00011.
    OMAi DFLDTWT.
    OrthoDBi EOG70KGQF.
    PhylomeDBi P15121.
    TreeFami TF106492.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01502-MONOMER.
    BRENDAi 1.1.1.21. 2681.
    Reactomei REACT_11038. Pregnenolone biosynthesis.
    SABIO-RK P15121.

    Miscellaneous databases

    ChiTaRSi AKR1B1. human.
    EvolutionaryTracei P15121.
    GeneWikii AKR1B1.
    GenomeRNAii 231.
    NextBioi 938.
    PROi P15121.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15121.
    Bgeei P15121.
    CleanExi HS_AKR1B1.
    Genevestigatori P15121.

    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.
    2. "Cloning and sequence determination of human placental aldose reductase gene."
      Chung S., Lamendola J.
      J. Biol. Chem. 264:14775-14777(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetus.
    4. "Cloning and prokaryotic expression of a biologically active human placental aldose reductase."
      Grundmann U., Bohn H., Obermeier R., Amann E.
      DNA Cell Biol. 9:149-157(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Placenta.
    5. "Cloning and expression of human aldose reductase."
      Nishimura C., Matsuura Y., Kokai Y., Akera T., Carper D., Morjana N., Lyons C., Flynn T.G.
      J. Biol. Chem. 265:9788-9792(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Structure of the human aldose reductase gene."
      Graham A., Brown L., Hedge P.J., Gammack A.J., Markham A.F.
      J. Biol. Chem. 266:6872-6877(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene."
      Ko B.C.B., Ruepp B., Bohren K.M., Gabbay K.H., Chung S.S.
      J. Biol. Chem. 272:16431-16437(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
      Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
      Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoma.
    9. "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: Brain cortex.
    10. "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].
    11. "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].
    12. "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].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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: Brain, Eye and Urinary bladder.
    15. "Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress."
      Ferraretto A., Negri A., Giuliani A., De Grada L., Fuhrman Conti A.M., Ronchi S.
      Biochim. Biophys. Acta 1175:283-288(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 131-162, TISSUE SPECIFICITY.
    16. "Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine."
      Morjana N.A., Lyons C., Flynn T.G.
      J. Biol. Chem. 264:2912-2919(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 244-275.
    17. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 276-294, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    18. "Identification of the reactive cysteine residue in human placenta aldose reductase."
      Liu S.Q., Bhatnagar A., Ansari N.H., Srivastava S.K.
      Biochim. Biophys. Acta 1164:268-272(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 298-316, ENZYME REGULATION.
    19. "Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes."
      Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A.
      Eur. J. Biochem. 218:893-903(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2.
      Tissue: Muscle.
    20. "Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110."
      Tarle I., Borhani D.W., Wilson D.K., Quiocho F.A., Petrash J.M.
      J. Biol. Chem. 268:25687-25693(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111.
    21. "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].
    22. "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-95; LYS-222 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications."
      Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A.
      Science 257:81-84(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    25. "The crystal structure of the aldose reductase.NADPH binary complex."
      Borhani D.W., Harter T.M., Pertrash J.M.
      J. Biol. Chem. 267:24841-24847(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
    26. "Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat."
      Wilson D.K., Tarle I., Petrash J.M., Quiocho F.A.
      Proc. Natl. Acad. Sci. U.S.A. 90:9847-9851(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    27. "The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant."
      Harrison D.H., Bohren K.M., Petsko G.A., Ringe D., Gabbay K.H.
      Biochemistry 36:16134-16140(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    28. "The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48."
      Ruiz F., Hazemann I., Mitschler A., Joachimiak A., Schneider T., Karplus M., Podjarny A.
      Acta Crystallogr. D 60:1347-1354(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR, ACTIVE SITE.
    29. "Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A."
      Howard E.I., Sanishvili R., Cachau R.E., Mitschler A., Chevrier B., Barth P., Lamour V., Van Zandt M., Sibley E., Bon C., Moras D., Schneider T.R., Joachimiak A., Podjarny A.
      Proteins 55:792-804(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
    30. "High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group."
      Steuber H., Zentgraf M., Podjarny A., Heine A., Klebe G.
      J. Mol. Biol. 356:45-56(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE ANALOG.
    31. "The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop."
      Biadene M., Hazemann I., Cousido A., Ginell S., Joachimiak A., Sheldrick G.M., Podjarny A., Schneider T.R.
      Acta Crystallogr. D 63:665-672(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
    32. "Evidence for a novel binding site conformer of aldose reductase in ligand-bound state."
      Steuber H., Zentgraf M., La Motta C., Sartini S., Heine A., Klebe G.
      J. Mol. Biol. 369:186-197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
    33. "Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution."
      Steuber H., Heine A., Klebe G.
      J. Mol. Biol. 368:618-638(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.

    Entry informationi

    Entry nameiALDR_HUMAN
    AccessioniPrimary (citable) accession number: P15121
    Secondary accession number(s): B2R8N3
    , Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 173 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 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