Details for: CA1

Gene ID: 759

Symbol: CA1

Ensembl ID: ENSG00000133742

Description: carbonic anhydrase 1

Associated with

Other Information

Genular Protein ID: 1718426029

Symbol: CAH1_HUMAN

Name: Carbonic anhydrase 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 3104879

Title: Human carbonic anhydrase I cDNA.

PubMed ID: 3104879

DOI: 10.1093/nar/15.5.2386

PubMed ID: 2121614

Title: Structure and methylation patterns of the gene encoding human carbonic anhydrase I.

PubMed ID: 2121614

DOI: 10.1016/0378-1119(90)90236-k

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 4217196

Title: Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260).

PubMed ID: 4217196

DOI: 10.1016/s0300-9084(74)80093-3

PubMed ID: 4625868

Title: Amino acid sequence of human erythrocyte carbonic anhydrase B.

PubMed ID: 4625868

DOI: 10.1016/0006-291x(72)90400-7

PubMed ID: 4632246

Title: Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.

PubMed ID: 4632246

DOI: 10.1016/s0021-9258(19)44161-6

PubMed ID: 4207120

Title: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.

PubMed ID: 4207120

DOI: 10.1016/s0021-9258(19)42734-8

PubMed ID: 10550681

Title: Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?

PubMed ID: 10550681

DOI: 10.1007/s007750050375

PubMed ID: 16807956

Title: 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.

PubMed ID: 16807956

DOI: 10.1002/chem.200600159

PubMed ID: 16686544

Title: 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.

PubMed ID: 16686544

DOI: 10.1021/jm0603320

PubMed ID: 17127057

Title: Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.

PubMed ID: 17127057

DOI: 10.1016/j.bmcl.2006.11.027

PubMed ID: 19186056

Title: A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases.

PubMed ID: 19186056

DOI: 10.1016/j.bmcl.2009.01.038

PubMed ID: 19206230

Title: Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors.

PubMed ID: 19206230

DOI: 10.1021/ja809683v

PubMed ID: 18618712

Title: Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide.

PubMed ID: 18618712

DOI: 10.1002/prot.22144

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 4622589

Title: Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications.

PubMed ID: 4622589

DOI: 10.1016/0022-2836(72)90452-4

PubMed ID: 804171

Title: Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.

PubMed ID: 804171

DOI: 10.1073/pnas.72.1.51

PubMed ID: 6430186

Title: Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.

PubMed ID: 6430186

DOI: 10.1111/j.1749-6632.1984.tb12314.x

PubMed ID: 15299369

Title: Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes.

PubMed ID: 15299369

DOI: 10.1107/s0907444994001873

PubMed ID: 8057362

Title: Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate.

PubMed ID: 8057362

DOI: 10.1006/jmbi.1994.1491

PubMed ID: 7932756

Title: Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme.

PubMed ID: 7932756

DOI: 10.1006/jmbi.1994.1655

PubMed ID: 12009884

Title: 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.

PubMed ID: 12009884

DOI: 10.1021/bi0120446

PubMed ID: 16870440

Title: Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.

PubMed ID: 16870440

DOI: 10.1016/j.bmcl.2006.07.021

PubMed ID: 16506782

Title: Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity.

PubMed ID: 16506782

DOI: 10.1021/ja057257n

PubMed ID: 17314045

Title: 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.

PubMed ID: 17314045

DOI: 10.1016/j.bmcl.2007.01.113

PubMed ID: 17407288

Title: Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II.

PubMed ID: 17407288

DOI: 10.1021/ja068359w

PubMed ID: 6781336

Title: Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam.

PubMed ID: 6781336

PubMed ID: 7866410

Title: Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I.

PubMed ID: 7866410

DOI: 10.1002/humu.1380040411

Sequence Information:

  • Length: 261
  • Mass: 28870
  • Checksum: 4959E5FA25E374F8
  • Sequence:
  • MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI 
    INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH 
    VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF 
    DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV 
    PMQHNNRPTQ PLKGRTVRAS F

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.