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E3 ISG15--protein ligase HERC5 (EC 2.3.2.-) (Cyclin-E-binding protein 1) (HECT domain and RCC1-like domain-containing protein 5)

 HERC5_HUMAN             Reviewed;        1024 AA.
Q9UII4; B2RTQ1; Q69G20;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
10-OCT-2018, entry version 150.
RecName: Full=E3 ISG15--protein ligase HERC5;
EC=2.3.2.-;
AltName: Full=Cyclin-E-binding protein 1;
AltName: Full=HECT domain and RCC1-like domain-containing protein 5;
Name=HERC5; Synonyms=CEB1, CEBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
CCNA1; CCNB1; CCND1 AND CCNE1.
TISSUE=Embryonic kidney;
PubMed=10581175; DOI=10.1006/bbrc.1999.1777;
Mitsui K., Nakanishi M., Ohtsuka S., Norwood T.H., Okabayashi K.,
Miyamoto C., Tanaka K., Yoshimura A., Ohtsubo M.;
"A novel human gene encoding HECT domain and RCC1-like repeats
interacts with cyclins and is potentially regulated by the tumor
suppressor proteins.";
Biochem. Biophys. Res. Commun. 266:115-122(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-994, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=15331633; DOI=10.1242/jcs.01338;
Kroismayr R., Baranyi U., Stehlik C., Dorfleutner A., Binder B.R.,
Lipp J.;
"HERC5, a HECT E3 ubiquitin ligase tightly regulated in LPS activated
endothelial cells.";
J. Cell Sci. 117:4749-4756(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076;
Takeuchi T., Inoue S., Yokosawa H.;
"Identification and Herc5-mediated ISGylation of novel target
proteins.";
Biochem. Biophys. Res. Commun. 348:473-477(2006).
[6]
FUNCTION, AND MUTAGENESIS OF CYS-994.
PubMed=16407192; DOI=10.1074/jbc.M512830200;
Dastur A., Beaudenon S., Kelley M., Krug R.M., Huibregtse J.M.;
"Herc5, an interferon-induced HECT E3 enzyme, is required for
conjugation of ISG15 in human cells.";
J. Biol. Chem. 281:4334-4338(2006).
[7]
FUNCTION, MUTAGENESIS OF CYS-994, ISGYLATION, INDUCTION BY IFNB1, AND
INTERACTION WITH ISGYLATED HSPA8 AND TXNRD1.
PubMed=16815975; DOI=10.1073/pnas.0600397103;
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
type I IFN-induced ISGylation of protein targets.";
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-994.
PubMed=20385878; DOI=10.4049/jimmunol.0903588;
Tang Y., Zhong G., Zhu L., Liu X., Shan Y., Feng H., Bu Z., Chen H.,
Wang C.;
"Herc5 attenuates influenza A virus by catalyzing ISGylation of viral
NS1 protein.";
J. Immunol. 184:5777-5790(2010).
[9]
FUNCTION, MUTAGENESIS OF CYS-994, AND INTERACTION WITH IRF3.
PubMed=20308324; DOI=10.1128/MCB.01466-09;
Shi H.X., Yang K., Liu X., Liu X.Y., Wei B., Shan Y.F., Zhu L.H.,
Wang C.;
"Positive regulation of interferon regulatory factor 3 activation by
Herc5 via ISG15 modification.";
Mol. Cell. Biol. 30:2424-2436(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH 60S SUBUNIT, AND
MUTAGENESIS OF CYS-994.
PubMed=20542004; DOI=10.1016/j.molcel.2010.05.002;
Durfee L.A., Lyon N., Seo K., Huibregtsesend J.M.;
"The ISG15 conjugation system broadly targets newly synthesized
proteins: implications for the antiviral function of ISG15.";
Mol. Cell 38:722-732(2010).
[11]
FUNCTION, AND INTERACTION WITH INFLUENZA A VIRUS NS1.
PubMed=20133869; DOI=10.1073/pnas.0909144107;
Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.;
"ISG15 conjugation system targets the viral NS1 protein in influenza A
virus-infected cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010).
-!- FUNCTION: 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. 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.
{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}.
-!- SUBUNIT: Binds to CCNA1, CCNB1, CCND1 and CCNE1. Interacts with
UBE2L6. Interacts with IRF3, this interaction is marginal in
resting cells but enhanced upon viral infection. Interacts with
influenza A virus NS1. {ECO:0000269|PubMed:10581175,
ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:20133869,
ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20542004}.
-!- INTERACTION:
P03495:NS (xeno); NbExp=3; IntAct=EBI-2339540, EBI-2548993;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:20542004}. Note=Associated with the
polyribosomes, probably via the 60S subunit.
-!- TISSUE SPECIFICITY: Expressed in testis and to a lesser degree in
brain, ovary and placenta. Found in most tissues at low levels.
{ECO:0000269|PubMed:10581175, ECO:0000269|PubMed:15331633}.
-!- INDUCTION: By IFNB1/IFN-beta. In endothelial cells, by TNF,
IL1B/interleukin-1B and by bacterial lipopolysaccharides (LPS),
hardly induced in other cells of the vascular wall such as primary
smooth muscle cells and fibroblasts. By viral infection.
{ECO:0000269|PubMed:15331633, ECO:0000269|PubMed:16815975}.
-!- PTM: ISGylated. {ECO:0000305|PubMed:16815975}.
-!- CAUTION: Was thought to be a ubiquitin ligase ubiquitinated by
UBE2D1, but was confirmed by numerous studies that it's main
function is as E3 ISG15 ligase. {ECO:0000305|PubMed:15331633}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB027289; BAA88519.1; -; mRNA.
EMBL; AY337518; AAR00320.1; -; mRNA.
EMBL; AC083829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC140716; AAI40717.1; -; mRNA.
CCDS; CCDS3630.1; -.
RefSeq; NP_057407.2; NM_016323.3.
UniGene; Hs.26663; -.
ProteinModelPortal; Q9UII4; -.
SMR; Q9UII4; -.
BioGrid; 119365; 53.
DIP; DIP-44200N; -.
IntAct; Q9UII4; 19.
MINT; Q9UII4; -.
STRING; 9606.ENSP00000264350; -.
iPTMnet; Q9UII4; -.
PhosphoSitePlus; Q9UII4; -.
BioMuta; HERC5; -.
DMDM; 296434523; -.
EPD; Q9UII4; -.
MaxQB; Q9UII4; -.
PaxDb; Q9UII4; -.
PeptideAtlas; Q9UII4; -.
PRIDE; Q9UII4; -.
ProteomicsDB; 84527; -.
Ensembl; ENST00000264350; ENSP00000264350; ENSG00000138646.
GeneID; 51191; -.
KEGG; hsa:51191; -.
UCSC; uc003hrt.5; human.
CTD; 51191; -.
DisGeNET; 51191; -.
EuPathDB; HostDB:ENSG00000138646.8; -.
GeneCards; HERC5; -.
H-InvDB; HIX0200636; -.
HGNC; HGNC:24368; HERC5.
HPA; HPA043929; -.
MIM; 608242; gene.
neXtProt; NX_Q9UII4; -.
OpenTargets; ENSG00000138646; -.
PharmGKB; PA134973940; -.
eggNOG; KOG0941; Eukaryota.
eggNOG; COG5021; LUCA.
eggNOG; COG5184; LUCA.
GeneTree; ENSGT00910000144004; -.
HOGENOM; HOG000208452; -.
HOVERGEN; HBG050878; -.
InParanoid; Q9UII4; -.
KO; K22372; -.
OMA; SGNIYSW; -.
OrthoDB; EOG091G028I; -.
PhylomeDB; Q9UII4; -.
TreeFam; TF315189; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
GeneWiki; HERC5; -.
GenomeRNAi; 51191; -.
PRO; PR:Q9UII4; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138646; Expressed in 201 organ(s), highest expression level in female gonad.
CleanEx; HS_HERC5; -.
ExpressionAtlas; Q9UII4; baseline and differential.
Genevisible; Q9UII4; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042296; F:ISG15 transferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032020; P:ISG15-protein conjugation; IDA:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
CDD; cd00078; HECTc; 1.
Gene3D; 2.130.10.30; -; 1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
Pfam; PF00632; HECT; 1.
Pfam; PF00415; RCC1; 4.
PRINTS; PR00633; RCCNDNSATION.
SMART; SM00119; HECTc; 1.
SUPFAM; SSF50985; SSF50985; 1.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS00626; RCC1_2; 2.
PROSITE; PS50012; RCC1_3; 4.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Polymorphism; Reference proteome; Repeat;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1024 E3 ISG15--protein ligase HERC5.
/FTId=PRO_0000206641.
REPEAT 96 155 RCC1 1.
REPEAT 156 208 RCC1 2.
REPEAT 209 260 RCC1 3.
REPEAT 262 312 RCC1 4.
REPEAT 314 364 RCC1 5.
DOMAIN 702 1024 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ACT_SITE 994 994 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
VARIANT 301 301 A -> T (in dbSNP:rs17014143).
/FTId=VAR_057123.
MUTAGEN 994 994 C->A: Loss of activity; no effect on IRF3
interaction.
{ECO:0000269|PubMed:15331633,
ECO:0000269|PubMed:16407192,
ECO:0000269|PubMed:16815975,
ECO:0000269|PubMed:20308324,
ECO:0000269|PubMed:20385878,
ECO:0000269|PubMed:20542004}.
CONFLICT 204 204 M -> T (in Ref. 2; AAR00320).
{ECO:0000305}.
CONFLICT 419 419 F -> S (in Ref. 2; AAR00320).
{ECO:0000305}.
CONFLICT 453 453 K -> R (in Ref. 1; BAA88519).
{ECO:0000305}.
CONFLICT 498 498 M -> V (in Ref. 1; BAA88519, 2; AAR00320
and 3; AAI40717). {ECO:0000305}.
CONFLICT 513 513 A -> T (in Ref. 2; AAR00320).
{ECO:0000305}.
SEQUENCE 1024 AA; 116852 MW; 1449C51A58269A6C CRC64;
MERRSRRKSR RNGRSTAGKA AATQPAKSPG AQLWLFPSAA GLHRALLRRV EVTRQLCCSP
GRLAVLERGG AGVQVHQLLA GSGGARTPKC IKLGKNMKIH SVDQGAEHML ILSSDGKPFE
YDNYSMKHLR FESILQEKKI IQITCGDYHS LALSKGGELF AWGQNLHGQL GVGRKFPSTT
TPQIVEHLAG VPLAQISAGE AHSMALSMSG NIYSWGKNEC GQLGLGHTES KDDPSLIEGL
DNQKVEFVAC GGSHSALLTQ DGLLFTFGAG KHGQLGHNST QNELRPCLVA ELVGYRVTQI
ACGRWHTLAY VSDLGKVFSF GSGKDGQLGN GGTRDQLMPL PVKVSSSEEL KLESHTSEKE
LIMIAGGNQS ILLWIKKENS YVNLKRTIPT LNEGTVKRWI ADVETKRWQS TKREIQEIFS
SPACLTGSFL RKRRTTEMMP VYLDLNKARN IFKELTQKDW ITNMITTCLK DNLLKRLPFH
SPPQEALEIF FLLPECPMMH ISNNWESLVV PFAKVVCKMS DQSSLVLEEY WATLQESTFS
KLVQMFKTAV ICQLDYWDES AEENGNVQAL LEMLKKLHRV NQVKCQLPES IFQVDELLHR
LNFFVEVCRR YLWKMTVDAS ENVQCCVIFS HFPFIFNNLS KIKLLHTDTL LKIESKKHKA
YLRSAAIEEE RESEFALRPT FDLTVRRNHL IEDVLNQLSQ FENEDLRKEL WVSFSGEIGY
DLGGVKKEFF YCLFAEMIQP EYGMFMYPEG ASCMWFPVKP KFEKKRYFFF GVLCGLSLFN
CNVANLPFPL ALFKKLLDQM PSLEDLKELS PDLGKNLQTL LDDEGDNFEE VFYIHFNVHW
DRNDTNLIPN GSSITVNQTN KRDYVSKYIN YIFNDSVKAV YEEFRRGFYK MCDEDIIKLF
HPEELKDVIV GNTDYDWKTF EKNARYEPGY NSSHPTIVMF WKAFHKLTLE EKKKFLVFLT
GTDRLQMKDL NNMKITFCCP ESWNERDPIR ALTCFSVLFL PKYSTMETVE EALQEAINNN
RGFG


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