Search results for ATP7A

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Protein (3 results from a total of 3)

Identifier: R-HSA-6803546
Species: Homo sapiens
Compartment: phagocytic vesicle membrane
Primary external reference: UniProt: ATP7A: Q04656
Identifier: R-HSA-3697896
Species: Homo sapiens
Compartment: trans-Golgi network membrane
Primary external reference: UniProt: ATP7A: Q04656
Identifier: R-HSA-936841
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: ATP7A: Q04656

Reaction (5 results from a total of 5)

Identifier: R-HSA-3697838
Species: Homo sapiens
Compartment: Golgi lumen, cytosol, trans-Golgi network membrane
As inferred from mouse, ATP7A (Menke's ATPase, MNK) transports copper from ATOX in the cytosol to SOD3 in the lumen of the trans golgi network. ATP7A and SOD3 directly interact. Mutations in ATP7A cause Menke's disease, a neurodegenerative condition.
Identifier: R-HSA-936802
Species: Homo sapiens
Compartment: plasma membrane
The human gene ATP7A (MNK) encodes the copper-transporting ATPase 1 (ATP7A, ATPase1, Menkes protein) which is expressed in most tissues except the liver (Vulpe et al, 1993; Chelly et al, 1993). Normally, ATP7A resides on the trans-Golgi membrane (Dierick et al, 1997). When cells are exposed to excessive copper levels, it is rapidly relocalized to the plasma membrane where it functions in copper efflux (Petris and Mercer, 1999). Defects in ATP7A are the cause of Menkes disease (MNKD), an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency (Ambrosini and Mercer, 1999).
Identifier: R-HSA-6803545
Species: Homo sapiens
Compartment: cytosol, phagocytic vesicle lumen, phagocytic vesicle membrane
Copper is an essential cofactor of key metabolic enzymes (Linder MC & Hazegh-Azam M 1996). Under normal conditions, the biosynthetic incorporation of copper into secreted and plasma membrane-bound proteins requires activity of the copper-transporting P1B-type ATPases (Cu-ATPases), ATP7A and ATP7B (Camakaris J et al. 1999; La Fontaine S & Mercer JF 2007; Lutsenko S et al. 2007). The Cu-ATPases also export excess copper from the cell and thus critically contribute to the homeostatic control of copper (Camakaris J et al. 1999; La Fontaine S & Mercer JF 2007). However, during bacterial infection phagocytic cells accumulate copper Cu(I) in cytoplasmic vesicles that partially fuse with the phagolysosome, attacking invading microbes with toxic levels of Cu (Festa RA & Thiele DJ 2012). The accumulation of Cu(I) in the phagosome may be dependent upon the trafficking of ATP7A to the membranes of these vesicles (Fu Y et al. 2014). Silencing of ATP7A expression in mouse RAW264.7 macrophages attenuated bacterial killing, suggesting a role for ATP7A-dependent copper transport in the bactericidal activity of macrophages (White C et al. 2009). Copper toxicity targets iron-sulfur containing proteins via iron displacement from solvent-exposed iron-sulfur clusters (Macomber L & Imlay JA 2009; Chillappagari S et al. 2010; Djoko KY & McEwan AG 2013). Copper resistance has been shown to be required for virulence in two animal models of mycobacterial infection (Wolschendorf F et al. 2011; Shi X et al. 2014).

Mutations in the gene encoding ATP7A results in a severe copper-deficiency known as Menkes disease (Kaler SG 2011).

Identifier: R-HSA-8955289
Species: Homo sapiens
Compartment: cytosol
COMMD1 is a member of a family of 10 copper metabolism MURR1 domain-containing proteins that have pleiotropic roles in copper metabolism, NF kappa beta-mediated transcription, the hypoxic response and electrolyte transport (Burstein et al, 2005; reviewed in Maine and Burstein, 2007). COMMD proteins have differential tissue and expression levels, but appear to have partially overlapping function and form homo- and heterodimers through the shared COMM domain (Burstein et al, 2005). COMMD1 and other family members interact with the cullin subunit of CRL E3 ubiquitin ligase complexes, as well as with CCDC22, a protein implicated in X-linked intellectual disability that may regulate COMMD localization. Together, COMMD proteins and CCDC22 activate the ubiquitin ligase activity of CRL complexes by displacing the CAND1 inhibitor (Burstein et al, 2005; Maine et al, 2007; Mao et al, 2011; Starokadomskyy et al, 2013;Phillips-Krawczak et al, 2015). The specificity of interaction between various COMMD and CUL family members may serve to fine tune the regulation of CRL activation, although these details remain to be determined.
Identifier: R-HSA-8955285
Species: Homo sapiens
Compartment: nucleoplasm
COMMD1 is a member of a family of 10 copper metabolism MURR1 domain-containing proteins that have pleiotropic roles in copper metabolism, NF kappa beta-mediated transcription, the hypoxic response and electrolyte transport (Burstein et al, 2005; reviewed in Maine and Burstein, 2007). COMMD proteins have differential tissue and expression levels, but appear to have partially overlapping function and form homo- and heterodimers through the shared COMM domain (Burstein et al, 2005). COMMD1 and other family members interact with the cullin subunit of CRL E3 ubiquitin ligase complexes, as well as with CCDC22, a protein implicated in X-linked intellectual disability that may regulate COMMD localization. Together, COMMD proteins and CCDC22 activate the ubiquitin ligase activity of CRL complexes by displacing the CAND1 inhibitor (Burstein et al, 2005; Maine et al, 2007; Mao et al, 2011; Starokadomskyy et al, 2013;Phillips-Krawczak et al, 2015). The specificity of interaction between various COMMD and CUL family members may serve to fine tune the regulation of CRL activation, although these details remain to be determined.

Complex (2 results from a total of 2)

Identifier: R-HSA-6803541
Species: Homo sapiens
Compartment: phagocytic vesicle membrane
Identifier: R-HSA-5358995
Species: Homo sapiens
Compartment: plasma membrane
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