Underlined values are claims re-computed from the knowledge base each time this page is built. The tables below are the source of truth.

ATP7B (copper-transporting ATPase 2) is a P1B-type ATPase (EC 7.2.2.8) predominantly expressed in hepatocytes. It has two main physiological roles: (1) biosynthetic copper delivery to cuproenzymes (particularly ceruloplasmin) at the trans-Golgi network, and (2) biliary copper excretion via copper-responsive vesicular trafficking. Under basal copper conditions, ATP7B resides in the TGN where it loads copper into the secretory pathway. When intracellular copper rises, ATP7B traffics to pericanalicular vesicles that sequester excess copper and subsequently undergo exocytosis to excrete copper into bile. This vesicular sequestration mechanism (not direct plasma membrane transport) is the primary route for biliary copper elimination. ATP7B contains six N-terminal heavy metal-associated (HMA) domains, each with a GMXCXXC copper-binding motif, eight transmembrane domains with a conserved CPC motif essential for transport, and cytoplasmic nucleotide-binding and phosphorylation domains. The copper chaperone ATOX1 delivers copper to ATP7B and stimulates its catalytic activity. Loss-of-function mutations cause Wilson disease (MIM:277900), an autosomal recessive disorder of hepatic copper accumulation leading to liver cirrhosis and neurological damage.

Disorders

Relationship is the entry's genetic[].relationship_type. untyped means the entry has a genetic record for the gene but does not type it; its free-text association is shown instead.

An entry matches when ClinGen's MONDO disease is the entry's own disease term, a subtype term, or an exact-match mapping. An amber status marks an entry ClinGen supports the gene for (Definitive, Strong or Moderate) whose own record does not type it. A Limited, Disputed or Refuted tier on such an entry is not a gap.