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P10220

- DEN_HHV11

UniProt

P10220 - DEN_HHV11

Protein

Deneddylase

Gene

UL36

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Deneddylase that deregulates the host cell cycle S phase to create a favorable environment allowing efficient viral genome replication. Interacts with and deneddylates host cullins including CUL1 and CUL4A, thereby reducing their E3 ubiquitin ligase activity. Inhibition of cullins leads to the stabilization of cullin-RING ligase substrates such as host CDN1A/p21, CDKN1B/p27kip and CDC25A, preventing S phase progression. Additionally, acts as a deubiquitinase and cleaves both 'Lys-48' and 'Lys-63'-linked ubiquitin chains By similarity.By similarity

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei52 – 521Important for catalytic activityPROSITE-ProRule annotation
    Active sitei65 – 6511 PublicationPROSITE-ProRule annotation
    Active sitei197 – 1971PROSITE-ProRule annotation
    Active sitei199 – 1991PROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. omega peptidase activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. modulation by virus of host protein ubiquitination Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Host-virus interaction, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC76.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deneddylase (EC:3.4.19.12, EC:3.4.22.-)
    Alternative name(s):
    Tegument protein VP1-2
    Tegument protein VP1/2
    Gene namesi
    ORF Names:UL36
    OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
    Taxonomic identifieri10299 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000009294: Genome

    Subcellular locationi

    Virion tegument. Host cytoplasm. Host nucleus
    Note: Tightly associated with the capsid.

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. viral tegument Source: CACAO

    Keywords - Cellular componenti

    Host cytoplasm, Host nucleus, Virion, Virion tegument

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651C → A: Complete loss of deubiquitination activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31643164DeneddylasePRO_0000116035Add
    BLAST

    Post-translational modificationi

    Proteolytically processed, possibly into several polypeptides. Enzymatic activity is only detectable following cleavage of the UL36 protein, which occurs late during viral replication.1 Publication

    Interactioni

    Subunit structurei

    Interacts with host CUL1 and CUL4A; these interactions inhibit the E3 ligase activity of cullins By similarity. Interacts with UL37.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UL37P102212EBI-7694334,EBI-6880600

    Protein-protein interaction databases

    IntActiP10220. 2 interactions.
    MINTiMINT-6732711.

    Structurei

    3D structure databases

    ProteinModelPortaliP10220.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 263219Peptidase C76PROSITE-ProRule annotationAdd
    BLAST
    Repeati2911 – 291221
    Repeati2913 – 291422
    Repeati2915 – 291623
    Repeati2917 – 291824
    Repeati2919 – 292025
    Repeati2921 – 292226
    Repeati2923 – 292427
    Repeati2925 – 292628
    Repeati2927 – 292829
    Repeati2929 – 2930210
    Repeati2931 – 2932211
    Repeati2933 – 2934212
    Repeati2935 – 2936213
    Repeati2937 – 2938214
    Repeati2939 – 2940215
    Repeati2941 – 2942216
    Repeati2943 – 2944217
    Repeati2945 – 2946218
    Repeati2947 – 2948219
    Repeati2949 – 2950220
    Repeati2951 – 2952221
    Repeati2953 – 2954222
    Repeati2955 – 2956223
    Repeati2957 – 2958224
    Repeati2959 – 2960225
    Repeati2961 – 2962226
    Repeati2963 – 2964227
    Repeati2965 – 2966228
    Repeati2967 – 2968229
    Repeati2969 – 2970230
    Repeati2971 – 2972231
    Repeati2973 – 2974232
    Repeati2975 – 2976233
    Repeati2977 – 2978234
    Repeati2979 – 2980235

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 273273Deubiquitination activityBy similarityAdd
    BLAST
    Regioni579 – 60931Interaction with UL37Add
    BLAST
    Regioni2911 – 29807035 X 2 AA tandem repeats of P-QAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1020 – 105334Sequence AnalysisAdd
    BLAST
    Coiled coili1317 – 135438Sequence AnalysisAdd
    BLAST
    Coiled coili1741 – 176929Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi426 – 4338Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi307 – 494188Pro-richAdd
    BLAST
    Compositional biasi1161 – 1288128Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the herpesviridae deneddylase family.Curated
    Contains 1 peptidase C76 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Family and domain databases

    InterProiIPR005210. Herpes_UL36.
    IPR006928. Pept_C76_UL36-USP.
    [Graphical view]
    PfamiPF04843. Herpes_teg_N. 1 hit.
    PF03586. Herpes_UL36. 1 hit.
    [Graphical view]
    PROSITEiPS51521. HTUSP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10220-1 [UniParc]FASTAAdd to Basket

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    MGGGNNTNPG GPVHKQAGSL ASRAHMIAGT PPHSTMERGG DRDIVVTGAR     50
    NQFAPDLEPG GSVSCMRSSL SFLSLIFDVG PRDVLSAEAI EGCLVEGGEW 100
    TRATAGPGPP RMCSIVELPN FLEYPGARGG LRCVFSRVYG EVGFFGEPAA 150
    GLLETQCPAH TFFAGPWALR PLSYTLLTIG PLGMGLFRDG DTAYLFDPHG 200
    LPEGTPAFIA KVRAGDMYPY LTYYTRDRPD VRWAGAMVFF VPSGPEPAAP 250
    ADLTAAALHL YGASETYLQD EAFSERRVAI THPLRGEIAG LGEPCVGVGP 300
    REGVGGPGPH PPTAAQSPPP TRARRDDRAS ETSRGTAGPS AKPEAKRPNR 350
    APDDVWAVAL KGTPPTDPPS ADPPSADPPS AIPPPPPSAP KTPAAEAAEE 400
    DDDDMRVLEM GVVPVGRHRA RYSAGLPKRR RPTWTPPSSV EDLTSGEKTK 450
    RSAPPAKTKK KSTPKGKTPV GAAVPASVPE PVLASAPPDP AGPPVAEAGE 500
    DDGPTVPASS QALEALKTRR SPEPPGADLA QLFEAHPNVA ATAVKFTACS 550
    AALAREVAAC SRLTISALRS PYPASPGLLE LCVIFFFERV LAFLIENGAR 600
    THTQAGVAGP AAALLEFTLN MLPWKTAVGD FLASTRLSLA DVAAHLPLVQ 650
    HVLDENSLIG RLALAKLILV ARDVIRETDA FYGELADLEL QLRAAPPANL 700
    YTRLGEWLLE RSQAHPDTLF APATPTHPEP LLYRVQALAK FARGEEIRVE 750
    AEDRQMREAL DALARGVDAV SQHAGPLGVM PAPAGAAPQG APRPPPLGPE 800
    AVQVRLEEVR TQARRAIEGA VKEYFYRGAV YSAKALQASD NNDRRFHVAS 850
    AAVVPVVQLL ESLPVFDQHT RDIAQRAAIP APPPIATSPT AILLRDLIQR 900
    GQTLDAPEDL AAWLSVLTDA ANQGLIERKP LDELARSIRD INDQQARRSS 950
    GLAELRRFDA LDAALGQQLD SDAAFVPAPG ASPYPDDGGL SPEATRMAEE 1000
    ALRQARAMDA AKLTAELAPD ARARLRERAR SLEAMLEGAR ERAKVARDAR 1050
    EKFLHKLQGV LRPLPDFVGL KACPAVLATL RASLPAGWSD LPEAVRGAPP 1100
    EVTAALRADM WGLLGQYRDA LEHPTPDTAT ALSGLHPSFV VVLKNLFADA 1150
    PETPFLLQFF ADHAPIIAHA VSNAINAGSA AVATADPAST VDAAVRAHRV 1200
    LVDAVTALGA AASDPASPLA FLAAMADSAA GYVKATRLAL DARVAIAQLT 1250
    TLGSAAADLV VQVRRAANQP EGEHASLIQA ATRATTGARE SLAGHEGRFG 1300
    GLLHAEGTAG DHSPSGRALQ ELGKVIGATR RRADELEAAT ADLREKMAAQ 1350
    RARSSHERWA ADVEAVLDRV ESGAEFDVVE LRRLQALAGT HGYNPRDFRK 1400
    RAEQALGTNA KAVTLALETA LAFNPYTPEN QRHPMLPPLA AIHRIDWSAA 1450
    FGAAADTYAD MFRVDTEPLA RLLRLAGGLL ERAQANDGFI DYHEAVLHLS 1500
    EDLGGVPALR QYVPFFQKGY AEYVDIRDRL DALRADARRA IGSVALDLAA 1550
    AAEEISAVRN DPAAAAELVR AGVTLPCPSE DALVACVAAL ERVDQSPVKD 1600
    TAYAHYVAFV TRQDLADTKD AVVRAKQQRA EATERVTAGL REVLAARERR 1650
    AQLEAEGLAN LKTLLKVVAV PATVAKTLDQ ARSAEEIADQ VEILVDQTEK 1700
    ARELDVQAVA WLEHAQRTFE THPLSAASGD GPGLLTRQGA RLQALFDTRR 1750
    RVEALRRSLE EAEAEWDEVW GRFGRVRGGA WKSPEGFRAA CEQLRALQDT 1800
    TNTVSGLRAQ RDYERLPAKY QGVLGAKSAE RAGAVEELGG RVAQHADLSA 1850
    RLRDEVVPRV AWEMNFDTLG GLLAEFDAVA GDLAPWAVEE FRGARELIQR 1900
    RMGLYSAYAK ATGQTGAGAA AAPAPLLVDL RALDARARAS APPGQEADPQ 1950
    MLRRRGEAYL RVSGGPGPLV LREATSTLDR PFAPSFLVPD GTPLQYALCF 2000
    PAVTDKLGAL LMCPEAACIR PPLPTDTLES ASTVTAMYVL TVINRLQLAL 2050
    SDAQAANFQL FGRFVRHRQA RWGASMDAAA ELYVALVATT LTREFGCRWA 2100
    QLEWGGDAAA PGPPLGPQSS TRHRVSFNEN DVLVALVASS PEHIYTFWRL 2150
    DLVRQHEYMH LTLPRAFQNA ADSMLFVQRL TPHPDARIRV LPAFSAGGPP 2200
    TRGLMFGTRL ADWRRGKLSE TDPLAPWRSV PELGTERGAA LGKLSPAQAL 2250
    AAVSVLGRMC LPSTALVALW TCMFPDDYTE YDSFDALLTA RLESGQTLSP 2300
    SGGREASPPA PPNALYRPTG QHVAVPAAAT HRTPAARVTA MDLVLAAVLL 2350
    GAPVVVALRN TTAFSRESEL ELCLTLFDSR ARGPDAALRD AVSSDIETWA 2400
    VRLLHADLNP IENACLAAQL PRLSALIAER PLARGPPCLV LVDISMTPVA 2450
    VLWENPDPPG PPDVRFVGSE ATEELPFVAG GEDVLAASAT DEDPFLARAI 2500
    LGRPFDASLL SGELFPGHPV YQRAPDDQSP SVPNPTPGPV DLVGAEGSLG 2550
    PGSLAPTLFT DATPGEPVPP RMWAWIHGLE ELASDDSGGP APLLAPDPLS 2600
    PTADQSVPTS QCAPRPPGPA VTAREARPGV PAESTRPAPV GPRDDFRRLP 2650
    SPQSSPAPPD ATAPRPPASS RASAASSSGS RARRHRRARS LARATQASAT 2700
    TQGWRPPALP DTVAPVTDFA RPPAPPKPPE PAPHALVSGV PLPLGPQAAG 2750
    QASPALPIDP VPPPVATGTV LPGGENRRPP LTSGPAPTPP RVPVGGPQRR 2800
    LTRPAVASLS ESRESLPSPW DPADPTAPVL GRNPAEPTSS SPAGPSPPPP 2850
    AVQPVAPPPT SGPPPTYLTL EGGVAPGGPV SRRPTTRQPV ATPTTSARPR 2900
    GHLTVSRLSA PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ 2950
    PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ NGHVAPGEYP AVRFRAPQNR 3000
    PSVPASASST NPRTGSSLSG VSSWASSLAL HIDATPPPVS LLQTLYVSDD 3050
    EDSDATSLFL SDSEAEALDP LPGEPHSPIT NEPFSALSAD DSQEVTRLQF 3100
    GPPPVSANAV LSRRYVQRTG RSALAVLIRA CYRLQQQLQR TRRALLHHSD 3150
    AVLTSLHHVR MLLG 3164
    Length:3,164
    Mass (Da):335,862
    Last modified:July 1, 1989 - v1
    Checksum:iCC5D31FF4F9FE3F4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti307 – 3071P → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti375 – 3795Missing in strain: Nonneuroinvasive mutant HF10.
    Natural varianti392 – 3921T → P in strain: Nonneuroinvasive mutant HF10.
    Natural varianti620 – 6201N → S in strain: Nonneuroinvasive mutant HF10.
    Natural varianti624 – 6241W → R in strain: Nonneuroinvasive mutant HF10.
    Natural varianti671 – 6711A → V in strain: Nonneuroinvasive mutant HF10.
    Natural varianti885 – 8851I → M in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1023 – 10231A → V in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1244 – 12441V → G in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1373 – 13731G → S in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1389 – 13891G → D in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1419 – 14191T → M in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1470 – 14701A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1604 – 16041A → S in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1605 – 16051H → D in strain: 17 syn+ and Nonneuroinvasive mutant HF10.
    Natural varianti1642 – 16421E → D in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1695 – 16951V → L in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1729 – 17291G → S in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1777 – 17771R → C in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1888 – 18881V → M in strain: Nonneuroinvasive mutant HF10.
    Natural varianti1973 – 19731E → K in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2267 – 22671V → A in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2540 – 25401V → A in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2545 – 25451A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2646 – 26461F → V in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2666 – 26661P → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2748 – 27481A → S in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2856 – 28561A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2875 – 28751A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2894 – 28941T → A in strain: Nonneuroinvasive mutant HF10.
    Natural varianti2973 – 29786Missing in strain: Nonneuroinvasive mutant HF10.
    Natural varianti3095 – 30951V → A in strain: Nonneuroinvasive mutant HF10.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32311.1.
    DQ889502 Genomic DNA. Translation: ABI63498.1.
    FJ593289 Genomic DNA. Translation: ACM62259.1.
    PIRiI30085. WMBEH6.
    RefSeqiNP_044638.2. NC_001806.1.

    Genome annotation databases

    GeneIDi2703357.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32311.1 .
    DQ889502 Genomic DNA. Translation: ABI63498.1 .
    FJ593289 Genomic DNA. Translation: ACM62259.1 .
    PIRi I30085. WMBEH6.
    RefSeqi NP_044638.2. NC_001806.1.

    3D structure databases

    ProteinModelPortali P10220.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P10220. 2 interactions.
    MINTi MINT-6732711.

    Protein family/group databases

    MEROPSi C76.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703357.

    Family and domain databases

    InterProi IPR005210. Herpes_UL36.
    IPR006928. Pept_C76_UL36-USP.
    [Graphical view ]
    Pfami PF04843. Herpes_teg_N. 1 hit.
    PF03586. Herpes_UL36. 1 hit.
    [Graphical view ]
    PROSITEi PS51521. HTUSP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
      McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
      J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
      Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
      Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Nonneuroinvasive mutant HF10.
    3. "Herpes simplex virus type 1 bacterial artificial chromosome."
      Cunningham C., Davison A.J.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 17 syn+.
    4. "A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae."
      Kattenhorn L.M., Korbel G.A., Kessler B.M., Spooner E., Ploegh H.L.
      Mol. Cell 19:547-557(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, ACTIVE SITES, MUTAGENESIS OF CYS-65.
      Strain: KOS.
    5. "A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae."
      Schlieker C., Korbel G.A., Kattenhorn L.M., Ploegh H.L.
      J. Virol. 79:15582-15585(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures."
      Desai P., Sexton G.L., Huang E., Person S.
      J. Virol. 82:11354-11361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL37.
      Strain: KOS.
    7. "Comprehensive characterization of extracellular herpes simplex virus type 1 virions."
      Loret S., Guay G., Lippe R.
      J. Virol. 82:8605-8618(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: F.
    8. "Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus."
      Jovasevic V., Liang L., Roizman B.
      J. Virol. 82:3311-3319(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE.
      Strain: F.
    9. "UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules."
      Shanda S.K., Wilson D.W.
      J. Virol. 82:7388-7394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein."
      Abaitua F., O'Hare P.
      J. Virol. 82:5234-5244(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
    11. "Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1."
      Roberts A.P., Abaitua F., O'Hare P., McNab D., Rixon F.J., Pasdeloup D.
      J. Virol. 83:105-116(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 17 syn+.
    12. "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases."
      Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M., Di Guglielmo C., Masucci M.G.
      Nat. Cell Biol. 12:351-361(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiDEN_HHV11
    AccessioniPrimary (citable) accession number: P10220
    Secondary accession number(s): B9VQG4, Q09I97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3