Type | Description |
---|---|
Definition | Fic domain-containing protein |
Date | Results | Publications |
---|---|---|
2019-03-16 11:21:00 | These findings show that Fic-mediated AMPylation of BiP is required for neurons to adapt to transient stress demands. | 30015618 |
2018-11-17 10:43:00 | Data (including data from studies using transgenic animals) suggest that dual enzymatic activity of Fic is, in part, regulated by Fic dimerization, as loss of this dimerization increases AMPylation and reduces deAMPylation of BiP/Grp78. (Fic = Fic domain-containing protein; BiP/Grp78 = molecular chaperone BiP) | 29089387 |
2015-04-18 10:52:00 | The inactive conformation of BiP is the preferred substrate for dFic. | 25395623 |
2012-09-22 10:09:00 | Our data are consistent with the idea that Fic's enzymatic activity is involved in the regulation of the distribution of the visual neurotransmitter histamine | 22544313 |
Type | IDs |
---|---|
Synonymous | CG9523, Dmel\CG9523, l(2)k11101 |
Gene |
UniProtKB-ID:
FICD_DROME
UniprotKB:
Q8SWV6
UniParc:
UPI000007F6D1
EMBL:
AE014134,
AY095059
EnsemblGenome:
FBgn0263278
KO:
dme:Dmel_CG9523
|
Nucleutide sequences |
EMBL-CDS:
AAM11387.1,
AAF52381.2
Gene_ORFName:
CG9523
EnsemblGenome_TRS:
FBtr0079257
|
Protein sequencees |
EnsemblGenome_PRO:
FBpp0078887
RefSeq:
NP_609026.1
|
Others |
UniRef100:
UniRef100_Q8SWV6
UniRef90:
UniRef90_Q8SWV6
UniRef50:
UniRef50_Q8SWV6
UniGene:
Dm.11352
|
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Refseq |
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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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