IE2_HHV6G
ID IE2_HHV6G Reviewed; 1466 AA.
AC Q8BB47;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 29-SEP-2021, entry version 48.
DE RecName: Full=Immediate-early protein 2;
DE Short=IE2;
GN Name=U90/U86;
OS Human herpesvirus 6A (strain GS) (HHV-6 variant A) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10369;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12706083; DOI=10.1016/s0042-6822(03)00007-2;
RA Gravel A., Tomoiu A., Cloutier N., Gosselin J., Flamand L.;
RT "Characterization of the immediate-early 2 protein of human herpesvirus 6,
RT a promiscuous transcriptional activator.";
RL Virology 308:340-353(2003).
RN [2]
RP FUNCTION.
RX PubMed=16884756; DOI=10.1016/j.virol.2006.06.030;
RA Tomoiu A., Gravel A., Flamand L.;
RT "Mapping of human herpesvirus 6 immediate-early 2 protein transactivation
RT domains.";
RL Virology 354:91-102(2006).
RN [3]
RP INTERACTION WITH UBE2I, AND SUBCELLULAR LOCATION.
RX PubMed=17005699; DOI=10.1128/jvi.00375-06;
RA Tomoiu A., Gravel A., Tanguay R.M., Flamand L.;
RT "Functional interaction between human herpesvirus 6 immediate-early 2
RT protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation.";
RL J. Virol. 80:10218-10228(2006).
CC -!- FUNCTION: Transcriptional transactivator.
CC {ECO:0000269|PubMed:16884756}.
CC -!- SUBUNIT: Interacts with human UBE2I in the nucleus. Although this
CC interaction does not promote IE2 sumoylation, it represses
CC transactivation activity. {ECO:0000269|PubMed:17005699}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:17005699}.
CC -!- SIMILARITY: Belongs to the herpesviridae IE2 family. {ECO:0000305}.
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DR EMBL; AY037931; AAK67493.1; -; mRNA.
DR SMR; Q8BB47; -.
DR PRIDE; Q8BB47; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR005028; Herpes_IE2_3.
DR InterPro; IPR005507; HHV6-IE.
DR Pfam; PF03361; Herpes_IE2_3; 1.
DR Pfam; PF03753; HHV6-IE; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Host nucleus; Host-virus interaction; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1466
FT /note="Immediate-early protein 2"
FT /id="PRO_0000260223"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1037
FT /note="Interaction with human UBE2I"
FT REGION 1005..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 165268 MW; B19243F7EBDAC4D6 CRC64;
MEPAKPSGNN MGSNDERMQD YRPDPMMEES IQQILEDSLM CDTSFDDLIL PGLESFGLII
PESSNNIESN NVEEGSNEDL KTLAEHKCKQ GNDNDVIQSA MKLSGLYCDA DITHTQPLSD
NTHQDPIYSQ ETRIFSKTIQ DPRIAAQTHR QCTSSASNLP SNESGSTQVR FASELPNQLL
QPMYTSHNQN ANLQNNFTSL PYQPYHDPYR DIESSYRESR NTNRGYDYNF RHHSYRPRGG
NGKYNYYNPN SKYQQPYKRC FTRTYNRRGR GHRSYDCSDR SADLPYEHYT YPNYEQQNPD
PRMNNYKDFT QLTNKFNFGA NDYSMAFSTD STHVQSDNYN HPTKAQTIPE TTKTKKHKAT
KDNETSRGNQ VLTSNDAISL SYRPSPIKLD IIKKIYDTDV IPLPKEALTA NGSNRDVDIQ
KYKKAHIRCR SVQKKKERSS QTNKHDENHA SSRSDLKERK SNEHEDKAVT KARDFSKLDP
LLSPLPLTPE PAIDFADHTD KFYSTPEFNQ IKQNLHRSKT SLQDTVPISK HTPRAPTKDN
SYKKHHDSKD NYPKMKHSPG RTTSKKNTTN SNGHQNFKDV SVKNVSGKAT STSPKSKTHH
YSSSSDEEGQ YKSPVKTITP SPSPYCKLKN PSIMDKNSAK NHTASADKNL TDNSPIRSNL
NPTAFNKSNN NKSITNSTSN SDECTDKKPN CNSTKNESKD PNRTCGKNSD KHLSKSCTMA
SKRAPSRASS RTSSRASSRA SSRASSRASS RASSRASSRD SSRASSRAPS RASSRDSSRA
SSRDSSRDSN RASSKASSRA SSRDSSRASS RDSSRASSKA SRKASSRASS RASSRASSKA
SGKASSKASS RASSRAFSRN SSRASSRASS RASSRASSRA SSRASSRDSS RALSRAFGRD
SSRASSRASS RDSSRASSKA SRKASSRASS RASSRASSRA SSRELRQIYC DSNKRQTPPH
DTSINTKFEI SEIKFRCGED LNFYKNTAAR LQCFNHNDQF YNPRFRPHIR TNRKKSESTN
DTDSESSMSR CKSHCRNSPD SLTIVRRKKH KSGSSSISSS IEENCRSNSH IVTGKEKFTP
FYYQSSRTRS SSSSSSSSSA SLSCSKSTLK TCRKTQNRDN KQIKSKSDSK HKTTNMSSDY
ESNRHADVFR NSPEAGEKFP LHNSSPFNTH EQSNHSENAI DEEQKKAPNI TTSHLHQKQN
VKLHNTKKCK KKRPRDDDSD SSIKNFCKKR ISGAQKTESE VSEIDDLCYR DYVRLKERKV
SEKFKIHRGR VATKDFQKLF RNTMRAFEYK QIPKKPCNDK NLKEAVYNIC CNGLSNNAAI
IMYFTRSKKV AQNIKIMQKE LMIRPNITVS EAFKMNHAPP KYYDKDEIKR FIQLQKQGPQ
ELWDKFENNT THDLFTRHSD VKTMIIYAAT PIDFVGAVKT CNKYAKDNPK EIVLRVCSII
DGDNPISIYN PISKDFKSKF STLSKC
