HERC5
entrez
51191
canonical
uniprot
Q9UII4
canonical
ensembl
ENSG00000138646
resolver
ensp
ENSP00000264350
resolver
ensp
ENSP00000582912
resolver
enst
ENST00000264350
resolver
genesymbol
HERC5
resolver
genesymbol_syn
CEB1
resolver
genesymbol_syn
CEBP1
resolver
hgnc
HGNC:24368
resolver
uniprot
B2RTQ1
resolver
uniprot
B4DXV3
resolver
uniprot
Q69G20
resolver
uniprot_entry
B4DXV3_HUMAN
resolver
uniprot_entry
HERC5_HUMAN
resolver
uniprot_sec
B2RTQ1
resolver
uniprot_sec
Q69G20
resolver
amino_acid_sequence
MERRSRRKSRRNGRSTAGKAAATQPAKSPGAQLWLFPSAAGLHRALLRRVEVTRQLCCSPGRLAVLERGGAGVQVHQLLAGSGGARTPKCIKLGKNMKIHSVDQGAEHMLILSSDGKPFEYDNYSMKHLRFESILQEKKIIQITCGDYHSLALSKGGELFAWGQNLHGQLGVGRKFPSTTTPQIVEHLAGVPLAQISAGEAHSMALSMSGNIYSWGKNECGQLGLGHTESKDDPSLIEGLDNQKVEFVACGGSHSALLTQDGLLFTFGAGKHGQLGHNSTQNELRPCLVAELVGYRVTQIACGRWHTLAYVSDLGKVFSFGSGKDGQLGNGGTRDQLMPLPVKVSSSEELKLESHTSEKELIMIAGGNQSILLWIKKENSYVNLKRTIPTLNEGTVKRWIADVETKRWQSTKREIQEIFSSPACLTGSFLRKRRTTEMMPVYLDLNKARNIFKELTQKDWITNMITTCLKDNLLKRLPFHSPPQEALEIFFLLPECPMMHISNNWESLVVPFAKVVCKMSDQSSLVLEEYWATLQESTFSKLVQMFKTAVICQLDYWDESAEENGNVQALLEMLKKLHRVNQVKCQLPESIFQVDELLHRLNFFVEVCRRYLWKMTVDASENVQCCVIFSHFPFIFNNLSKIKLLHTDTLLKIESKKHKAYLRSAAIEEERESEFALRPTFDLTVRRNHLIEDVLNQLSQFENEDLRKELWVSFSGEIGYDLGGVKKEFFYCLFAEMIQPEYGMFMYPEGASCMWFPVKPKFEKKRYFFFGVLCGLSLFNCNVANLPFPLALFKKLLDQMPSLEDLKELSPDLGKNLQTLLDDEGDNFEEVFYIHFNVHWDRNDTNLIPNGSSITVNQTNKRDYVSKYINYIFNDSVKAVYEEFRRGFYKMCDEDIIKLFHPEELKDVIVGNTDYDWKTFEKNARYEPGYNSSHPTIVMFWKAFHKLTLEEKKKFLVFLTGTDRLQMKDLNNMKITFCCPESWNERDPIRALTCFSVLFLPKYSTMETVEEALQEAINNNRGFG
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
FUNCTION: Major E3 ligase for ISG15 conjugation (PubMed:16407192, PubMed:16815975, PubMed:16884686, PubMed:20308324, PubMed:20542004, PubMed:26355087, PubMed:27534820, PubMed:27564865, PubMed:37279284, PubMed:38421872, PubMed:38652662, PubMed:40184173). Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner (PubMed:16407192, PubMed:16815975, PubMed:16884686, PubMed:20308324, PubMed:20542004, PubMed:26355087, PubMed:27534820, PubMed:27564865, PubMed:37279284). Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner (PubMed:20542004). Acts as a positive regulator of innate antiviral response in cells induced by interferon by mediating ISGylation of proteins involved in innate immunity, such as CGAS, IRF3, IFIH1/MDA5 and STING1 (PubMed:16815975, PubMed:20308324, PubMed:38421872, PubMed:38652662, PubMed:40184173). 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 (PubMed:20308324). Also regulates innate antiviral response by mediating ISGylation of CGAS and STING1, thereby promoting activation of cGAS-STING signaling (PubMed:38421872, PubMed:38652662). Catalyzes ISGylation of IFIH1/MDA5, promoting IFIH1/MDA5 oligomerization and immune signal transduction (PubMed:40184173). Also regulates innate immunity by catalyzing ISGylation of viral proteins: newly translated viral proteins are primary targets of ISG15 in interferon-stimulated cells (PubMed:20133869, PubMed:20385878, PubMed:20542004, PubMed:22093708, PubMed:34572049). Interferes with the function of key viral structural proteins such as ebolavirus structural protein VP40 or HIV-1 protein GAG (PubMed:22093708, PubMed:34572049). Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets (PubMed:20133869, PubMed:20385878). Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity (PubMed:20542004). 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 (PubMed:37279284). Promotes parkin/PRKN ubiquitin E3 ligase activity by suppressing the intramolecular interaction that maintains its autoinhibited conformation (PubMed:27534820). {ECO:0000269|PubMed:16407192, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:16884686, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20385878, ECO:0000269|PubMed:20542004, ECO:0000269|PubMed:22093708, ECO:0000269|PubMed:26355087, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:27564865, ECO:0000269|PubMed:34572049, ECO:0000269|PubMed:37279284, ECO:0000269|PubMed:38421872, ECO:0000269|PubMed:38652662, ECO:0000269|PubMed:40184173}.; 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. {ECO:0000269|PubMed:34661519}.
uniprot
proteins
mass_dalton
116852
uniprot
proteins
mutagenesis
MUTAGEN 994; /note="C->A: Loss of E3 ISG15--protein ligase activity; no effect on IRF3 interaction."; /evidence="ECO:0000269|PubMed:15331633, ECO:0000269|PubMed:16407192, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20385878, ECO:0000269|PubMed:20542004, ECO:0000269|PubMed:22093708, ECO:0000269|PubMed:34661519, ECO:0000269|PubMed:38421872, ECO:0000269|PubMed:38652662
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000305|PubMed:16815975}.
uniprot
proteins
pubmed
10581175
uniprot
proteins
pubmed
15331633
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16407192
uniprot
proteins
pubmed
16815975
uniprot
proteins
pubmed
16884686
uniprot
proteins
pubmed
20133869
uniprot
proteins
pubmed
20308324
uniprot
proteins
pubmed
20385878
uniprot
proteins
pubmed
20542004
uniprot
proteins
pubmed
22093708
uniprot
proteins
pubmed
26355087
uniprot
proteins
pubmed
27534820
uniprot
proteins
pubmed
27564865
uniprot
proteins
pubmed
34572049
uniprot
proteins
pubmed
34661519
uniprot
proteins
pubmed
37279284
uniprot
proteins
pubmed
38421872
uniprot
proteins
pubmed
38652662
uniprot
proteins
pubmed
40184173
uniprot
proteins
sequence_length
1024
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20542004}. Cytoplasm {ECO:0000269|PubMed:22093708, ECO:0000269|PubMed:38421872}. Note=Associated with the polyribosomes, probably via the 60S subunit. {ECO:0000269|PubMed:20542004}.
uniprot
proteins