FICD report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of FICD at tissue level.

III. Associated gene sets

GO_1903894Biological processregulation of IRE1-mediated unfolded protein response
GO_0006986Biological processresponse to unfolded protein
GO_0034260Biological processnegative regulation of GTPase activity
GO_0044602Biological processprotein deadenylylation
GO_0018117Biological processprotein adenylylation
GO_0034976Biological processresponse to endoplasmic reticulum stress
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0042803Molecular functionprotein homodimerization activity
GO_0030544Molecular functionHsp70 protein binding
GO_0051087Molecular functionprotein-folding chaperone binding
GO_0044603Molecular functionprotein adenylylhydrolase activity
GO_0042802Molecular functionidentical protein binding
GO_0005515Molecular functionprotein binding
GO_0070733Molecular functionAMPylase activity
GO_0005524Molecular functionATP binding

IV. Literature review

[source]
Gene nameFICD
Protein nameProtein adenylyltransferase FICD (EC 2.7.7.108) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin yeast partner E) (Huntingtin-interacting protein 13) (HIP-13) (Huntingtin-interacting protein E)
FIC domain protein adenylyltransferase
SynonymsHIP13
UNQ3041/PRO9857
HYPE
DescriptionFUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP . In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates . .

AccessionsENST00000549641.1
ENST00000552758.1
F8VZ74
Q9BVA6
ENST00000552695.6
H0YIR6
J3KP49
ENST00000361549.2