| Type | Description |
|---|---|
| Definition | copper metallochaperone ATX1 |
| Date | Results | Publications |
|---|---|---|
| 2013-08-03 11:28:00 | different effects of ATX1 unfolding on Cu(I) affinity | 23169585 |
| 2010-01-21 00:00:00 | The possible role of electrostatic potential surfaces in the docking of Ccc2 with these Atx1-homologues is discussed | 15710399 |
| 2010-01-21 00:00:00 | structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase | 16732294 |
| 2010-01-21 00:00:00 | evidence of a dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, thereby activating the ATPase | 19678841 |
| 2010-01-21 00:00:00 | results suggest that in vivo the high GSH concentration favors Atx1 dimerization and that Cu (2) (I) (GS(-))(2)(Atx1)(2) is the major conformation of Atx1 in the cytosol | 17957393 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
ATX1_YEAST
UniprotKB:
P38636
UniParc:
UPI0000110BE0
EMBL:
BK006947,
AY558367,
Z71535,
L35270,
X96722
EnsemblGenome:
YNL259C
KO:
sce:YNL259C
|
| Nucleutide sequences |
EMBL-CDS:
AAC37428.1,
CAA96166.1,
CAA65485.1,
DAA10300.1,
AAS56693.1
Gene_ORFName:
N0840
EnsemblGenome_TRS:
YNL259C_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YNL259C
RefSeq:
NP_014140.1
|
| Others |
UniRef100:
UniRef100_P38636
UniRef90:
UniRef90_P38636
UniRef50:
UniRef50_P38636
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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