TRIM23 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0016567Biological processprotein ubiquitination
GO_0045087Biological processinnate immune response
GO_0006886Biological processintracellular protein transport
GO_0016192Biological processvesicle-mediated transport
GO_0010508Biological processpositive regulation of autophagy
GO_0005886Cellular componentplasma membrane
GO_0000139Cellular componentGolgi membrane
GO_0005737Cellular componentcytoplasm
GO_0005765Cellular componentlysosomal membrane
GO_0005634Cellular componentnucleus
GO_0019003Molecular functionGDP binding
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0008047Molecular functionenzyme activator activity
GO_0042802Molecular functionidentical protein binding
GO_0005525Molecular functionGTP binding
GO_0008270Molecular functionzinc ion binding
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0005515Molecular functionprotein binding
GO_0003924Molecular functionGTPase activity

IV. Literature review

[source]
Gene nameTRIM23
Protein nameE3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) (ADP-ribosylation factor domain-containing protein 1) (GTP-binding protein ARD-1) (RING finger protein 46) (RING-type E3 ubiquitin transferase TRIM23) (Tripartite motif-containing protein 23)
Tripartite motif containing 23
SynonymsRNF46
ARD1
ARFD1
DescriptionFUNCTION: Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes . .; FUNCTION: (Microbial infection) Mediates TRAF6 auto-ubiquitination in the presence of human cytomegalovirus protein UL144, resulting in the virally controlled activation of NF-kappa-B stimulation at early times of HCMV infection. .

AccessionsD6RBN4
P36406
ENST00000274327.11 [P36406-3]
ENST00000505205.1
D6RD22
ENST00000506400.1
ENST00000513794.1
D6R9E9
ENST00000381018.7 [P36406-2]
ENST00000231524.14 [P36406-1]