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P00915

- CAH1_HUMAN

UniProt

P00915 - CAH1_HUMAN

Protein

Carbonic anhydrase 1

Gene

CA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.1 Publication

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Activated by histamine, imidazole, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide, benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR15, BR17, BR22 and BR30. Activated by a short exposition to Foscarnet (phosphonoformate trisodium salt), but inhibited by a long one. Esterase activity weakly reduced by cyanamide.9 Publications

    Kineticsi

    1. KM=4.0 mM for CO22 Publications
    2. KM=15 mM for 4-nitrophenyl acetate2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Proton acceptorBy similarity
    Metal bindingi65 – 651Zinc 2; variant Michigan-1
    Metal bindingi68 – 681Zinc 2; variant Michigan-1
    Metal bindingi95 – 951Zinc 1; catalytic1 Publication
    Metal bindingi97 – 971Zinc 1; catalytic1 Publication
    Metal bindingi120 – 1201Zinc 1; catalytic1 Publication
    Active sitei129 – 1291By similarity
    Binding sitei200 – 2001Substrate
    Metal bindingi201 – 2011Zinc 2; variant Michigan-1

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: ProtInc
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. one-carbon metabolic process Source: InterPro
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
    REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    SABIO-RKP00915.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 1 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase I
    Carbonic anhydrase B
    Short name:
    CAB
    Carbonic anhydrase I
    Short name:
    CA-I
    Gene namesi
    Name:CA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1368. CA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25984.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 261260Carbonic anhydrase 1PRO_0000077409Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00915.
    PeptideAtlasiP00915.
    PRIDEiP00915.

    2D gel databases

    DOSAC-COBS-2DPAGEP00915.
    REPRODUCTION-2DPAGEIPI00215983.
    P00915.
    UCD-2DPAGEP00915.

    PTM databases

    PhosphoSiteiP00915.

    Expressioni

    Gene expression databases

    ArrayExpressiP00915.
    BgeeiP00915.
    CleanExiHS_CA1.
    GenevestigatoriP00915.

    Organism-specific databases

    HPAiCAB025790.
    HPA006558.

    Interactioni

    Protein-protein interaction databases

    BioGridi107214. 2 interactions.
    IntActiP00915. 2 interactions.
    STRINGi9606.ENSP00000256119.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123
    Helixi14 – 196
    Helixi22 – 254
    Beta strandi26 – 283
    Beta strandi32 – 343
    Turni36 – 383
    Beta strandi48 – 514
    Helixi54 – 563
    Beta strandi57 – 626
    Beta strandi67 – 715
    Beta strandi74 – 829
    Beta strandi89 – 9810
    Beta strandi100 – 1045
    Beta strandi107 – 1104
    Beta strandi116 – 12510
    Turni126 – 1283
    Helixi132 – 1354
    Beta strandi141 – 15313
    Helixi156 – 1583
    Helixi159 – 1646
    Helixi165 – 1673
    Beta strandi174 – 1763
    Helixi182 – 1854
    Beta strandi192 – 1976
    Beta strandi208 – 2158
    Beta strandi217 – 2193
    Helixi221 – 2288
    Beta strandi230 – 2334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AZMX-ray2.00A2-261[»]
    1BZMX-ray2.00A2-261[»]
    1CRMX-ray2.00A2-261[»]
    1CZMX-ray2.00A2-261[»]
    1HCBX-ray1.60A2-261[»]
    1HUGX-ray2.00A2-261[»]
    1HUHX-ray2.20A2-261[»]
    1J9WX-ray2.60A/B2-261[»]
    1JV0X-ray2.00A/B2-261[»]
    2CABX-ray2.00A2-261[»]
    2FOYX-ray1.55A/B2-261[»]
    2FW4X-ray2.00A/B2-261[»]
    2IT4X-ray2.00A/B6-261[»]
    2NMXX-ray1.55A/B2-261[»]
    2NN1X-ray1.65A/B2-261[»]
    2NN7X-ray1.85A/B2-261[»]
    3LXEX-ray1.90A/B2-261[»]
    3W6HX-ray2.96A/B2-261[»]
    3W6IX-ray2.69A/E2-261[»]
    ProteinModelPortaliP00915.
    SMRiP00915. Positions 4-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00915.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 2012Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP00915.
    KOiK01672.
    OMAiVTWIICK.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiP00915.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018442. Carbonic_anhydrase_CA1.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF82. PTHR18952:SF82. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00915-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV    50
    SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS 100
    TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK 150
    VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT 200
    HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ 250
    PLKGRTVRAS F 261
    Length:261
    Mass (Da):28,870
    Last modified:January 23, 2007 - v2
    Checksum:i4959E5FA25E374F8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 762DN → ND AA sequence (PubMed:4217196)Curated
    Sequence conflicti75 – 762DN → ND AA sequence (PubMed:4625868)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681H → R in variant Michigan-1; confers enhanced esterase activity and an additional zinc binding site. 2 Publications
    VAR_001378
    Natural varianti143 – 1431A → V.
    Corresponds to variant rs7821248 [ dbSNP | Ensembl ].
    VAR_048679
    Natural varianti254 – 2541G → R in Guam. 1 Publication
    VAR_001379

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05014 mRNA. Translation: CAA28663.1.
    M33987 mRNA. Translation: AAA51910.1.
    BC027890 mRNA. Translation: AAH27890.1.
    CCDSiCCDS6237.1.
    PIRiJQ0786. CRHU1.
    RefSeqiNP_001122301.1. NM_001128829.3.
    NP_001122302.1. NM_001128830.3.
    NP_001122303.1. NM_001128831.3.
    NP_001158302.1. NM_001164830.1.
    NP_001729.1. NM_001738.4.
    UniGeneiHs.23118.

    Genome annotation databases

    EnsembliENST00000431316; ENSP00000392338; ENSG00000133742.
    ENST00000523022; ENSP00000429798; ENSG00000133742.
    ENST00000523953; ENSP00000430656; ENSG00000133742.
    ENST00000542576; ENSP00000443517; ENSG00000133742.
    GeneIDi759.
    KEGGihsa:759.
    UCSCiuc003ydh.3. human.

    Polymorphism databases

    DMDMi115449.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05014 mRNA. Translation: CAA28663.1 .
    M33987 mRNA. Translation: AAA51910.1 .
    BC027890 mRNA. Translation: AAH27890.1 .
    CCDSi CCDS6237.1.
    PIRi JQ0786. CRHU1.
    RefSeqi NP_001122301.1. NM_001128829.3.
    NP_001122302.1. NM_001128830.3.
    NP_001122303.1. NM_001128831.3.
    NP_001158302.1. NM_001164830.1.
    NP_001729.1. NM_001738.4.
    UniGenei Hs.23118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AZM X-ray 2.00 A 2-261 [» ]
    1BZM X-ray 2.00 A 2-261 [» ]
    1CRM X-ray 2.00 A 2-261 [» ]
    1CZM X-ray 2.00 A 2-261 [» ]
    1HCB X-ray 1.60 A 2-261 [» ]
    1HUG X-ray 2.00 A 2-261 [» ]
    1HUH X-ray 2.20 A 2-261 [» ]
    1J9W X-ray 2.60 A/B 2-261 [» ]
    1JV0 X-ray 2.00 A/B 2-261 [» ]
    2CAB X-ray 2.00 A 2-261 [» ]
    2FOY X-ray 1.55 A/B 2-261 [» ]
    2FW4 X-ray 2.00 A/B 2-261 [» ]
    2IT4 X-ray 2.00 A/B 6-261 [» ]
    2NMX X-ray 1.55 A/B 2-261 [» ]
    2NN1 X-ray 1.65 A/B 2-261 [» ]
    2NN7 X-ray 1.85 A/B 2-261 [» ]
    3LXE X-ray 1.90 A/B 2-261 [» ]
    3W6H X-ray 2.96 A/B 2-261 [» ]
    3W6I X-ray 2.69 A/E 2-261 [» ]
    ProteinModelPortali P00915.
    SMRi P00915. Positions 4-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107214. 2 interactions.
    IntActi P00915. 2 interactions.
    STRINGi 9606.ENSP00000256119.

    Chemistry

    BindingDBi P00915.
    ChEMBLi CHEMBL2095180.
    DrugBanki DB00819. Acetazolamide.
    DB00381. Amlodipine.
    DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB01194. Brinzolamide.
    DB00880. Chlorothiazide.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB01144. Dichlorphenamide.
    DB01031. Ethinamate.
    DB00311. Ethoxzolamide.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB01202. Levetiracetam.
    DB00703. Methazolamide.
    DB00232. Methyclothiazide.
    DB01325. Quinethazone.
    DB01021. Trichlormethiazide.
    DB00661. Verapamil.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi 2597.

    PTM databases

    PhosphoSitei P00915.

    Polymorphism databases

    DMDMi 115449.

    2D gel databases

    DOSAC-COBS-2DPAGE P00915.
    REPRODUCTION-2DPAGE IPI00215983.
    P00915.
    UCD-2DPAGE P00915.

    Proteomic databases

    PaxDbi P00915.
    PeptideAtlasi P00915.
    PRIDEi P00915.

    Protocols and materials databases

    DNASUi 759.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000431316 ; ENSP00000392338 ; ENSG00000133742 .
    ENST00000523022 ; ENSP00000429798 ; ENSG00000133742 .
    ENST00000523953 ; ENSP00000430656 ; ENSG00000133742 .
    ENST00000542576 ; ENSP00000443517 ; ENSG00000133742 .
    GeneIDi 759.
    KEGGi hsa:759.
    UCSCi uc003ydh.3. human.

    Organism-specific databases

    CTDi 759.
    GeneCardsi GC08M086315.
    HGNCi HGNC:1368. CA1.
    HPAi CAB025790.
    HPA006558.
    MIMi 114800. gene.
    neXtProti NX_P00915.
    PharmGKBi PA25984.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P00915.
    KOi K01672.
    OMAi VTWIICK.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P00915.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.
    REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    SABIO-RK P00915.

    Miscellaneous databases

    EvolutionaryTracei P00915.
    GeneWikii CA1_(gene).
    GenomeRNAii 759.
    NextBioi 3070.
    PROi P00915.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00915.
    Bgeei P00915.
    CleanExi HS_CA1.
    Genevestigatori P00915.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018442. Carbonic_anhydrase_CA1.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF82. PTHR18952:SF82. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure and methylation patterns of the gene encoding human carbonic anhydrase I."
      Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., Butterworth P.H.W.
      Gene 93:277-283(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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: Pancreas and Spleen.
    4. "Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)."
      Giraud N., Marriq C., Laurent-Tabusse G.
      Biochimie 56:1031-1043(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-261, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    5. "Amino acid sequence of human erythrocyte carbonic anhydrase B."
      Andersson B., Nyman P.O., Strid L.
      Biochem. Biophys. Res. Commun. 48:670-677(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-261.
    6. "Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B."
      Lin K.-T.D., Deutsch H.F.
      J. Biol. Chem. 248:1885-1893(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 12-261.
    7. "Human carbonic anhydrases. XII. The complete primary structure of the C isozyme."
      Lin K.-T.D., Deutsch H.F.
      J. Biol. Chem. 249:2329-2337(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    8. "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?"
      Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.
      J. Biol. Inorg. Chem. 4:528-536(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    11. "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
      Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
      Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
      Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
      J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    14. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
      Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
      Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications."
      Kannan K.K., Fridborg K., Bergsten P.C., Liljas A., Loevgren S., Petef M., Strandberg B., Waara I., Adler L., Falkbring S.O., Goethe P.O., Nyman P.O.
      J. Mol. Biol. 63:601-604(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260.
    17. "Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution."
      Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M.
      Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    18. "Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I."
      Kannan K.K., Ramanadham M., Jones T.A.
      Ann. N. Y. Acad. Sci. 429:49-60(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
    19. "Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes."
      Kumar V., Kannan K.K., Sathyamurthi P.
      Acta Crystallogr. D 50:731-738(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS.
    20. "Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate."
      Kumar V., Kannan K.K.
      J. Mol. Biol. 241:226-232(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND BICARBONATE.
    21. "Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme."
      Chakravarty S., Kannan K.K.
      J. Mol. Biol. 243:298-309(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS.
    22. "Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination."
      Ferraroni M., Tilli S., Briganti F., Chegwidden W.R., Supuran C.T., Wiebauer K.E., Tashian R.E., Scozzafava A.
      Biochemistry 41:6237-6244(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION, VARIANT MICHIGAN-1 ARG-68.
    23. "Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I."
      Temperini C., Scozzafava A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 16:5152-5156(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND ACTIVATORS, ACTIVATION BY IMIDAZOLE AND HISTIDINE.
    24. "Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity."
      Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., Srivastava D.K., Christianson D.W.
      J. Am. Chem. Soc. 128:3011-3018(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
    25. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
      Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-260 IN COMPLEX WITH ZINC ION AND THE ANTIVIRAL FOSCARNET, ENZYME REGULATION.
    26. "Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II."
      Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W.
      J. Am. Chem. Soc. 129:5528-5537(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
    27. "Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam."
      Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G.
      Am. J. Hum. Genet. 33:105-111(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GUAM ARG-254.
    28. "Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I."
      Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., Tashian R.E.
      Hum. Mutat. 4:294-296(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MICHIGAN-1 ARG-68.

    Entry informationi

    Entry nameiCAH1_HUMAN
    AccessioniPrimary (citable) accession number: P00915
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 160 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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