Amine oxidase.

annotation not available

Aquaporin-1 isoform X2.

AQP2 isoform 1; Belongs to the MIP/aquaporin (TC 1.A.8) family.

AQP2 isoform 1; Belongs to the MIP/aquaporin (TC 1.A.8) family.

Aquaporin-1 isoform X2.

ATPase, Cu++ transporting, alpha polypeptide.

ATPase copper transporting beta.

ATPase, Cu++ transporting, alpha polypeptide.

MT1E isoform 3; Belongs to the metallothionein superfamily. Type 1 family.

ATPase, Cu++ transporting, alpha polypeptide.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase, Cu++ transporting, alpha polypeptide.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase, Cu++ transporting, alpha polypeptide.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase, Cu++ transporting, alpha polypeptide.

PARK7 isoform 1.

ATPase, Cu++ transporting, alpha polypeptide.

Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family.

ATPase copper transporting beta.

ATPase, Cu++ transporting, alpha polypeptide.

ATPase copper transporting beta.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase copper transporting beta.

MT1E isoform 3; Belongs to the metallothionein superfamily. Type 1 family.

ATPase copper transporting beta.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase copper transporting beta.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase copper transporting beta.

Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.

ATPase copper transporting beta.

Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family.

Beta-site APP-cleaving enzyme 1; Belongs to the peptidase A1 family.

Major prion protein; Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan s [...]

Beta-site APP-cleaving enzyme 1; Belongs to the peptidase A1 family.

Alpha-synuclein; Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs [...]

Beta-site APP-cleaving enzyme 1; Belongs to the peptidase A1 family.

Transferrin receptor (P90, CD71).