20/chembl/api/data/protein_classification?limit=20&offset=20905Root of the ChEMBL protein family classificationProtein classprotein classProtein class1Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified. [MESH:D004798]Enzymeenzyme1Enzyme11Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis. [MESH:D015815]Adhesionadhesion2Adhesion61Secreted proteinsecreted3Secreted91Structural proteinstructural4Structural101Other nuclear proteinnuclear other5Nuclear other142A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. [MESH:D010770]1Kinaseenzyme kinase6Kinase1Other membrane proteinmembrane other7Membrane other131Other cytosolic proteincytosolic other8Cytosolic other121Antigens on surfaces of cells, including infectious or foreign cells or viruses. They are usually protein-containing groups on cell membranes or walls and may be isolated. [MESH:D000954]Surface antigensurface antigen9Surface antigen112The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) [MESH:D010088]1Oxidoreductaseenzyme reductase10Reductase1Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. [MESH:D011956]Membrane receptormembrane receptor11Membrane receptor21Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. [MESH:D014157]Transcription factortranscription factor12Transcription Factor53A soluble cytochrome P-450 enzyme that catalyzes camphor monooxygenation in the presence of putidaredoxin, putidaredoxin reductase, and molecular oxygen. This enzyme, encoded by the CAMC gene also known as CYP101, has been crystallized from bacteria and the structure is well defined. Under anaerobic conditions, this enzyme reduces the polyhalogenated compounds bound at the camphor-binding site. [MESH:D019475]1031Cytochrome P450 CAM familyenzyme cytochrome p450 cyp_cam13CYP_CAM51136Serine protease S6 familyenzyme protease serine pas s614S65A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62. [MESH:D020860]1119Serine protease S8A subfamilyenzyme protease serine sb s8a15S8A51119Serine protease S8B subfamilyenzyme protease serine sb s8b16S8B5A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13. [MESH:D043402]1120Serine protease S10 familyenzyme protease serine sc s1018S1051120Serine protease S28 familyenzyme protease serine sc s2819S2851120Serine protease S33 familyenzyme protease serine sc s3320S33