Catalytic
P00915CA1
Carbonic anhydrase 1
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Evidence cards are admitted only after source identity, construct, measurement and provenance checks.
Open the dossierProtein dossiers
One dossier per UniProt accession for the human carbonic anhydrase family in this release. Each keeps the protein’s identity, sequence and location separate from the experimental records linked to it.
15 dossiers in this view.
Catalytic
P00918CA2
Carbonic anhydrase 2
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Dense upstream coverage is stratified by method, resolution band, assay, and fixed per-protein quotas so this paralog does not dominate the collection.
Open the dossierCatalytic
P07451CA3
Carbonic anhydrase 3
UniProt-reviewed human alpha-carbonic-anhydrase scope record. This release admits five experimental structure mappings, two direct assay activities, and one protein-specific reaction assignment with record-local comparison boundaries retained.
Open the dossierCatalytic
P22748CA4
Carbonic anhydrase 4
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Ten experimental structure mappings, two direct assay activities, and one reaction assignment retain membrane attachment and construct boundaries.
Open the dossierCatalytic
P35218CA5A
Carbonic anhydrase 5A, mitochondrial
UniProt-reviewed mitochondrial alpha-carbonic-anhydrase scope record. The pathway map shows its reaction context without making tissue, rate or flux claims.
Open the dossierCatalytic
Q9Y2D0CA5B
Carbonic anhydrase 5B, mitochondrial
UniProt-reviewed mitochondrial alpha-carbonic-anhydrase scope record. It remains distinct from CA5A and from the boundary record CA5BP1.
Open the dossierCatalytic
P23280CA6
Carbonic anhydrase 6
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Secreted and soluble experimental contexts are not silently pooled.
Open the dossierCatalytic
P43166CA7
Carbonic anhydrase 7
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Exact protein and construct identity controls evidence admission.
Open the dossierAcatalytic related
P35219CA8
Carbonic anhydrase-related protein
UniProt-reviewed acatalytic carbonic-anhydrase-related scope record. It is never placed on catalytic-rate plots or treated as reaction evidence.
Open the dossierCatalytic
Q16790CA9
Carbonic anhydrase 9
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Ectodomain constructs, full-length protein and cell-based contexts remain separate.
Open the dossierAcatalytic related
Q9NS85CA10
Carbonic anhydrase-related protein 10
UniProt-reviewed acatalytic carbonic-anhydrase-related scope record. Its admitted protein identity remains visible even though this release selects no structure, assay-activity, or reaction-assignment evidence for CA10.
Open the dossierAcatalytic related
O75493CA11
Carbonic anhydrase-related protein 11
UniProt-reviewed acatalytic carbonic-anhydrase-related scope record. It remains visible as a family boundary but outside catalytic comparisons.
Open the dossierCatalytic
O43570CA12
Carbonic anhydrase 12
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Construct and assay context remain first-class comparison fields.
Open the dossierCatalytic
Q8N1Q1CA13
Carbonic anhydrase 13
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Seven experimental structure mappings, two direct assay activities, and one reaction assignment remain tied to CA13 rather than backfilled from nearby paralogs.
Open the dossierCatalytic
Q9ULX7CA14
Carbonic anhydrase 14
UniProt-reviewed human alpha-carbonic-anhydrase scope record. Membrane context and protein identity are preserved across sources.
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