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Overview

Uniprot IDP14854
Protein NameCytochrome c oxidase subunit 6B1
Gene NameCOX6B1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 ETKIKNYKTAPFDSR

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

Protein Sequence

10 MAEDMETKIK 20 NYKTAPFDSR 30 FPNQNQTRNC 40 WQNYLDFHRC 50 QKAMTAKGGD 60 ISVCEWYQRV 70 YQSLCPTSWV 80 TDWDEQRAEG TFPGKI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0045277 respiratory chain complex IV
Molecular Function GO:0004129 cytochrome-c oxidase activity
Biological Process GO:0045333 cellular respiration
Biological Process GO:0006123 mitochondrial electron transport, cytochrome c to oxygen
Biological Process GO:0021762 substantia nigra development

Reference

[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.