VE2_HPV24
ID VE2_HPV24 Reviewed; 467 AA.
AC P50770;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 02-JUN-2021, entry version 82.
DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS Human papillomavirus 24.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=37956;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the initiation of viral DNA replication. A
CC dimer of E2 interacts with a dimer of E1 in order to improve
CC specificity of E1 DNA binding activity. Once the complex recognizes and
CC binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also
CC regulates viral transcription through binding to the E2RE response
CC element (5'-ACCNNNNNNGGT-3') present in multiple copies in the
CC regulatory regions of the viral genome. Activates or represses
CC transcription depending on E2RE's position with regards to proximal
CC promoter elements including the TATA-box. Repression occurs by
CC sterically hindering the assembly of the transcription initiation
CC complex. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC -!- SUBUNIT: Binds DNA as homodimer. Interacts with protein E1; this
CC interaction greatly increases E1 DNA-binding activity. Interacts with
CC protein L1; this interaction enhances E2-dependent replication and
CC transcription activation. Interacts with protein L2; this interaction
CC inhibits E2 transcriptional activity but not DNA replication function
CC E2. Interacts with protein E7; this interaction inhibits E7 oncogenic
CC activity. Interacts with host TAF1; this interaction modulates E2-
CC dependent transcriptional regulation. Interacts with host BRD4; this
CC interaction mediates E2 transcriptional activation function.
CC Additionally, the interaction with host BRD4 on mitotic chromosomes
CC mediates tethering of the viral genome. Interacts with host TOPBP1;
CC this interaction is required for optimal viral DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_04001}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04001}.
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DR EMBL; U31782; AAA79418.1; -; Genomic_DNA.
DR SMR; P50770; -.
DR PRIDE; P50770; -.
DR Proteomes; UP000158064; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.30; -; 1.
DR Gene3D; 2.170.200.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_04001; PPV_E2; 1.
DR InterPro; IPR035975; E2/EBNA1_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR000427; Papillomavirus_E2_C.
DR InterPro; IPR001866; Papillomavirus_E2_N.
DR InterPro; IPR033668; Reg_prot_E2.
DR InterPro; IPR036050; Regulatory_protein_E2_N.
DR InterPro; IPR042503; Regulatory_protein_E2_N_1.
DR InterPro; IPR042504; Regulatory_protein_E2_N_2.
DR Pfam; PF00511; PPV_E2_C; 1.
DR Pfam; PF00508; PPV_E2_N; 1.
DR SUPFAM; SSF51332; SSF51332; 1.
DR SUPFAM; SSF54957; SSF54957; 1.
PE 3: Inferred from homology;
KW Activator; DNA replication; DNA-binding; Early protein; Host nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..467
FT /note="Regulatory protein E2"
FT /id="PRO_0000133203"
FT REGION 1..201
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 196..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..467
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT COMPBIAS 196..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52856 MW; 8E04B454AD44CB63 CRC64;
MENLKKRFDV LQDLLMNIYE QGSDTLESQI EHWQALRREA VLLYYARQNG VLRLGYLPVP
PLATSEAKAK QAISMVLQLQ SLQQSPYGTE KWTLVDTSIE TFKNTPENHF KKGPINVEVI
YDGDPDNANL YTMWKYVYYM DDNDQWQKTE SGANHTGIYY LIGEFKHYYV LFADDANRYS
KSGQWEVRIN KETVFAPVTS STPPDSPGGS RELPGSTANS KASSPTQQPQ QACSDETTKR
KRYGRRESSP TDSRCRRRSS SRQKKQGRRA RSRTRSRCSS TQTRSRSTSR RSRSTSRGNR
RCRGDTPRGQ RGVSTSSRGR GRGSRRSSSS SSPTPRTKAS QRGCDTRSVR DSGISPGDVG
RKLQTVSGRN SGRLGRLLEE ALDPPVILLR GGANTLKCFR NRAKLRYRGH YKAFSTSWSW
VAADGTERLG RSRLLVSFTS FKQRSGFLDL VRFPKGVDWS LGSFDKL
