Search results for CAD

Showing 19 results out of 72

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Protein (4 results from a total of 10)

CAD

Identifier: R-HSA-73452
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: CAD: P27708
Identifier: R-HSA-198169
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CADM3: Q8N126
Identifier: R-HSA-420589
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CADM1: Q9BY67
Identifier: R-HSA-433734
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CADM2: Q8N3J6

Complex (4 results from a total of 18)

Identifier: R-HSA-73457
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-448876
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-376008
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-418976
Species: Homo sapiens
Compartment: plasma membrane

Reaction (4 results from a total of 37)

Identifier: R-HSA-73577
Species: Homo sapiens
Compartment: cytosol
The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).
Identifier: R-HSA-73573
Species: Homo sapiens
Compartment: cytosol
The synthesis of N-carbamoyl L-aspartate from carbamoyl phosphate and L-aspartate is catalyzed by the aspartate carbamoyltansferase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).
Identifier: R-HSA-73571
Species: Homo sapiens
Compartment: cytosol
The synthesis of dihydroorotate from N-carbamoyl L-aspartate is catalyzed by the dihydroorotase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein. This activity has not been directly demonstrated in experimental studies of the purified human protein, but has been inferred from the behavior of the purified hamster protein and the high degree of sequence similarity between the cloned hamster and human genes (Iwahana et al. 1996). Also on the basis of this similarity, the active human protein is annotated as a hexamer (Lee et al. 1985).
Identifier: R-HSA-5357477
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Activated PAK then phosphorylates a serene residue (S665) within a conserved motif in the cytoplasmic tail of VE-cadherin. VE-cadherin is also phosphorylated by c-Src in a manner dependent on TSAD (Sun et al. 2012, Lambeng et al. 2005). Serine-phosphorylated VE-cadherin recruits beta-arrestin 2 which promotes the internalization of VE-cadherin into clathrin-coated pits. This process leads to the disassembly of endothelial-cell junctions, resulting in the enhanced permeability of the blood-vessel wall (Gavard & Gutkind 2006).

Interactor (1 results from a total of 1)

Identifier: Q9ULU8-4
Species: Homo sapiens
Primary external reference: UniProt: Q9ULU8-4

Set (2 results from a total of 2)

Identifier: R-HSA-418977
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-375081
Species: Homo sapiens
Compartment: plasma membrane

Pathway (2 results from a total of 2)

Identifier: R-HSA-9764260
Species: Homo sapiens
Type II classical cadherins are comprised of five extracellular cadherin (EC) repeats in their ectodomain. The first cadherin repeat (EC1) of type II classical cadherins has two conserved tryptophan residues, at positions 2 and 4. The conserved tryptophan residues are critical for dimerization. Trans dimerization of classical cadherins occurs through a unique mechanism, called 'strand swapping', where one set of interactions in two monomers is replaced with an equivalent set of interactions in a dimer, through exchange of an N-terminal beta-strand facilitating docking of the Trp residues into a hydrophobic receptor pocket of the binding partner. This strand-swapping mechanism is aided by an intermediate non-swapped dimer, called X dimer, in accordance with the induced fit model. Type II classical cadherins include CDH5 (cadherin-5, also known as VE-cadherin, an atypical type II cadherin), CDH6 (cadherin-6, also known as K-cadherin), CDH7 (cadherin-7), CDH8 (cadherin-8), CDH9 (cadherin-9, also known as T1-cadherin), CDH10 (cadherin-10, also known as T2-cadherin), CDH11 (cadherin-11, also known as OB-cadherin), CDH12 (cadherin-12, also known as N-cadherin 2), CDH18 (cadherin-18), CDH19 (cadherin-19), CDH20 (cadherin-20), CDH22 (cadherin-22), and CDH24 (cadherin-24). For review, refer to Brasch et al. 2012, Gul et al. 2017.

Type II classical cadherins are predominantly expressed in the nervous system where they govern formation of neuronal circuits (e.g. cold perception, motor neuron bundling). In addition to homotypic dimer formation, type II classical cadherins form heterotypic dimers with other type II classical cadherins and can be divided into three specificity subgroups based on their binding preferences. The specificity subgroups correspond to the branches of the phylogenetic tree where binding between members has been retained. The first specificity subgroup includes CDH8 and CDH11, and likely CDH24, the second specificity subgroup includes CDH6, CDH9 and CDH10, and the third specificity subgroup includes CDH7, CDH12, CDH18, CDH20 and CDH22. The CDH8, CDH11, and CDH24 group does not bind to the others, while binding interactions are found within the other branches of the phylogenetic tree. Divergent type II cadherin CDH5 and CDH19 could not be placed in these specificity subgroups (Brasch et al. 2018).
Identifier: R-HSA-140342
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
DNA fragmentation in response to apoptotic signals is achieved, in part, through the activity of apoptotic nucleases, termed DNA fragmentation factor (DFF) or caspase-activated DNase (CAD) (reviewed in Widlak and Garrard, 2005). In non-apoptotic cells, DFF is a nuclear heterodimer consisting of a 45 kD chaperone and inhibitor subunit (DFF45)/inhibitor of CAD (ICAD-L)] and a 40 kD nuclease subunit (DFF40/CAD)( Liu et al. 1997, 1998; Enari et al. 1998). During apoptosis, activated caspase-3 or -7 cleave DFF45/ICAD releasing active DFF40/CAD nuclease. The activity of DFF is tightly controlled at multiple stages. During translation, DFF45/ICAD, Hsp70, and Hsp40 proteins play a role in insuring the appropriate folding of DFF40 during translation(Sakahira and Nagata, 2002). The nuclease activity of DFF40 is enhanced by the chromosomal proteins histone H1, Topoisomerase II and HMGB1/2(Widlak et al., 2000). In addition, the inhibitors (DFF45/35; ICAD-S/L) are produced in stoichiometric excess (Widlak et al., 2003).

Icon (2 results from a total of 2)

Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
Cadherins icon
Generic representation of Calcium-dependent adhesion proteins
Curator: Bruce May
Designer: Cristoffer Sevilla
Cadmium icon
Cadmium
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