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P00915

- CAH1_HUMAN

UniProt

P00915 - CAH1_HUMAN

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Protein

Carbonic anhydrase 1

Gene

CA1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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
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: Chromosome 8

Organism-specific databases

HGNCiHGNC:1368. CA1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiP00915.
CleanExiHS_CA1.
ExpressionAtlasiP00915. baseline and differential.
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

        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:
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. Diclofenamide.
DB00869. Dorzolamide.
DB01031. Ethinamate.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00703. Methazolamide.
DB00423. Methocarbamol.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB01021. Trichlormethiazide.
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

Bgeei P00915.
CleanExi HS_CA1.
ExpressionAtlasi P00915. baseline and differential.
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

« 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. "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 29, 2014
This is version 161 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