HERC5 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of HERC5 at tissue level.

III. Associated gene sets

GO_0000079Biological processregulation of cyclin-dependent protein serine/threonine kinase activity
GO_0051607Biological processdefense response to virus
GO_0016567Biological processprotein ubiquitination
GO_0006511Biological processubiquitin-dependent protein catabolic process
GO_0032020Biological processISG15-protein conjugation
GO_0050688Biological processregulation of defense response to virus
GO_0000209Biological processprotein polyubiquitination
GO_0039585Biological processPKR/eIFalpha signaling
GO_0045087Biological processinnate immune response
GO_0005829Cellular componentcytosol
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0005737Cellular componentcytoplasm
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0042296Molecular functionISG15 transferase activity
GO_0005515Molecular functionprotein binding
GO_0003723Molecular functionRNA binding

IV. Literature review

[source]
Gene nameHERC5
Protein nameHECT and RLD domain containing E3 ubiquitin protein ligase 5
E3 ISG15--protein ligase HERC5 (HECT And RLD domain-containing E3 ubiquitin protein ligase 5)
E3 ISG15--protein ligase HERC5 (HECT and RLD domain-containing E3 ubiquitin protein ligase 5)
E3 ISG15--protein ligase HERC5
E3 ISG15--protein ligase HERC5 (EC 2.3.2.-) (Cyclin-E-binding protein 1) (HECT domain and RCC1-like domain-containing protein 5)
SynonymsCEB1
CEBP1
DescriptionFUNCTION: Major E3 ligase for ISG15 conjugation . Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Mediates ISGylation of the phosphatase PTEN leading to its degradation, thus alleviating its suppression of the PI3K-AKT signaling pathway and promoting the production of cytokines that facilitate bacterial clearance . Interferes with the function of key viral structural proteins such as ebolavirus structural protein VP40 or HIV-1 protein GAG . Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15. Promotes parkin/PRKN ubiquitin E3 ligase activity by suppressing the intramolecular interaction that maintains its autoinhibited conformation . .; FUNCTION: (Microbial infection) Functions as an E3 ligase for ISGylation of hepatitis B virus protein X leading to enhanced viral replication due to increased interferon resistance. .

AccessionsA0A222UC57
A0A222UBP8
A0A222UC18
A0A222UBL1
A0A222UBG1
A0A1B1H4K9
ENST00000264350.8
A0A222UBT1
A0A222UC07
A0A222UBI2
A0A222UBQ9
A0A222UBU1
A0A222UBJ3
Q9UII4
A0A222UBR9
A0A222UBP1
A0A222UBN9
E9PBL0
A0A221SLY6
A0A222UC38
A0A222UBN1
A0A222UBQ7
A0A222UBK9
A0A222UBU5
A0A222UBS8
A0A222UBZ4
A0A222UBP0
ENST00000508159.1
A0A222UBL0
A0A222UBN3
A0A222UBN6
A0A222UBS7
A0A222UC53
A0A222UBK6
A0A222UBP7
A0A222UBQ8
A0A222UBK0