Type | Description |
---|---|
Definition | cytochrome c oxidase assembly factor 6 |
Date | Results | Publications |
---|---|---|
2021-02-27 13:47:00 | What Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both? | 32977416 |
2020-09-19 16:30:00 | COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase. | 31851937 |
2020-08-29 12:46:00 | COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria. | 32061935 |
2020-07-04 12:24:00 | Data present the crystal structures of human Coa6 and the pathogenic (W59C)Coa6-mutant protein. These structures show that Coa6 has a 3-helical bundle structure, with the first 2 helices tethered by disulfide bonds, one of which likely provides the copper-binding site. Disulfide-mediated oligomerization of the (W59C)Coa6 protein provides a structural explanation for the loss-of-function mutation. | 31515291 |
2016-07-16 10:47:00 | Results find that COA6 associates with COX2 and is crucial for its maturation and complex IV biogenesis. Also, COA6 interacts with the copper chaperone SCO1 which indicates that COA6 is intrinsically involved in the copper delivery process for COX2. | 26160915 |
Type | IDs |
---|---|
Synonymous | C1orf31, CEMCOX4 |
Gene |
UniProtKB-ID:
COA6_HUMAN
UniprotKB:
Q5JTJ3
UniParc:
UPI000015FF99,
UPI000020607F,
UPI00001D7D6B
EMBL:
BC116455,
BC025793,
AL355472
Ensembl:
ENSG00000168275
KO:
hsa:388753
|
Nucleutide sequences |
EMBL-CDS:
AAI16456.1,
AAH25793.1
Ensembl_TRS:
ENST00000366613,
ENST00000619305,
ENST00000366615,
ENST00000366612
|
Protein sequencees |
Ensembl_PRO:
ENSP00000355572,
ENSP00000355571,
ENSP00000355574,
ENSP00000479686
RefSeq:
NP_001288662.1,
NP_001013003.1,
NP_001193570.2
|
Others |
UniRef100:
UniRef100_Q5JTJ3
UniRef90:
UniRef90_Q5JTJ3
UniRef50:
UniRef50_Q5JTJ3
UniGene:
Hs.23198
CCDS:
CCDS31059.1,
CCDS55690.1,
CCDS76275.1
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
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