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Protein

Carbonic anhydrase 1

Gene

CA1

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

Functioni

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

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

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

    • arylesterase activity Source: CACAO
    • carbonate dehydratase activity Source: CACAO
    • hydro-lyase activity Source: CACAO
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1368. CA1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25984.

    Chemistry

    DrugBankiDB00819. Acetazolamide.
    DB00381. Amlodipine.
    DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB01194. Brinzolamide.
    DB00880. Chlorothiazide.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB01144. Diclofenamide.
    DB00869. Dorzolamide.
    DB01031. Ethinamate.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00703. Methazolamide.
    DB00423. Methocarbamol.
    DB00232. Methyclothiazide.
    DB01325. Quinethazone.
    DB01021. Trichlormethiazide.
    DB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA1.
    DMDMi115449.

    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

    BgeeiP00915.
    CleanExiHS_CA1.
    ExpressionAtlasiP00915. baseline and differential.
    GenevisibleiP00915. HS.

    Organism-specific databases

    HPAiCAB025790.
    HPA006558.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFCP2Q128003EBI-3912102,EBI-717422

    Protein-protein interaction databases

    BioGridi107214. 3 interactions.
    IntActiP00915. 3 interactions.
    STRINGi9606.ENSP00000256119.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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

            10         20         30         40         50
    MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV
    60 70 80 90 100
    SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS
    110 120 130 140 150
    TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK
    160 170 180 190 200
    VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT
    210 220 230 240 250
    HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ
    260
    PLKGRTVRAS F
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi107214. 3 interactions.
    IntActiP00915. 3 interactions.
    STRINGi9606.ENSP00000256119.

    Chemistry

    BindingDBiP00915.
    ChEMBLiCHEMBL2095180.
    DrugBankiDB00819. Acetazolamide.
    DB00381. Amlodipine.
    DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB01194. Brinzolamide.
    DB00880. Chlorothiazide.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB01144. Diclofenamide.
    DB00869. Dorzolamide.
    DB01031. Ethinamate.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00703. Methazolamide.
    DB00423. Methocarbamol.
    DB00232. Methyclothiazide.
    DB01325. Quinethazone.
    DB01021. Trichlormethiazide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2597.

    PTM databases

    PhosphoSiteiP00915.

    Polymorphism and mutation databases

    BioMutaiCA1.
    DMDMi115449.

    2D gel databases

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

    Proteomic databases

    PaxDbiP00915.
    PeptideAtlasiP00915.
    PRIDEiP00915.

    Protocols and materials databases

    DNASUi759.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi759.
    GeneCardsiGC08M086315.
    HGNCiHGNC:1368. CA1.
    HPAiCAB025790.
    HPA006558.
    MIMi114800. gene.
    neXtProtiNX_P00915.
    PharmGKBiPA25984.
    GenAtlasiSearch...

    Phylogenomic databases

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

    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.

    Miscellaneous databases

    EvolutionaryTraceiP00915.
    GeneWikiiCA1_(gene).
    GenomeRNAii759.
    NextBioi3070.
    PROiP00915.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP00915.
    CleanExiHS_CA1.
    ExpressionAtlasiP00915. baseline and differential.
    GenevisibleiP00915. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "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.
    18. "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).
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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: June 24, 2015
    This is version 169 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

    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.