SCUBA

COX4I2 — Cytochrome c oxidase subunit 4I2

COX4I2 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

COX4I2's module in each cell type

Cell typeModuleShares the module with
PericytesHypoxia NO Signaling
Mitochondrial & OxPhos
CAMK2N1, CDH6, EPS8, FAM162B, GUCY1A2, NDUFA4L2, PMEPA1View in SCUBA
Smooth muscle cellsPericyte Signature
Development
AC100803.3, CCND1, CPM, ENTPD3, GPR20, GPRIN3, GRIP2, ISYNA1 +8 moreView in SCUBA

About the gene

SynonymsCOX4-2, COX4B, COX4L2, COXIV-2, dJ857M17.2
Chromosome20: 31637912-31645006
Predicted locationMembrane
Essential geneNo
Protein classDisease related genes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted membrane proteins, Transporters

Function

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.