ID M0QU77_9ADEN Unreviewed; 495 AA.
AC M0QU77;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E1B 55 kDa protein {ECO:0000256|ARBA:ARBA00022118};
DE AltName: Full=E1B protein, large T-antigen {ECO:0000256|ARBA:ARBA00030428};
DE AltName: Full=E1B-495R {ECO:0000256|ARBA:ARBA00031863};
GN Name=E1B {ECO:0000313|EMBL:AFK92245.1};
OS Human adenovirus 20.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus D.
OX NCBI_TaxID=46923 {ECO:0000313|EMBL:AFK92245.1, ECO:0000313|Proteomes:UP000162243};
RN [1] {ECO:0000313|EMBL:AFK92245.1, ECO:0000313|Proteomes:UP000162243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24027303; DOI=10.1128/JVI.01927-13;
RA Singh G., Robinson C.M., Dehghan S., Jones M.S., Dyer D.W., Seto D.,
RA Chodosh J.;
RT "Homologous recombination in e3 genes of human adenovirus species d.";
RL J. Virol. 87:12481-12488(2013).
CC -!- FUNCTION: Plays a major role to prevent cellular inhibition of viral
CC genome replication. Assembles an SCF-like E3 ubiquitin ligase complex
CC based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in
CC cooperation with viral E4orf6. This viral RING-type ligase
CC ubiquitinates cellular substrates and targets them to proteasomal
CC degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3,
CC DAXX and BLM. Degradation of host TP53/p53 activity is essential for
CC preventing E1A-induced TP53 accumulation that would otherwise lead to
CC cell apoptosis and growth arrest. E1B-55K also inactivates TP53
CC transcription-factor activity by binding its transactivation domain.
CC E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the
CC latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies
CC thereby contributing to maximal inhibition of TP53 function.
CC {ECO:0000256|ARBA:ARBA00002808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC {ECO:0000256|ARBA:ARBA00008605}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN226749; AFK92245.1; -; Genomic_DNA.
DR Proteomes; UP000162243; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039526; P:perturbation by virus of host apoptosis; IEA:UniProtKB-KW.
DR InterPro; IPR006717; Adeno_E1B_55K_N.
DR InterPro; IPR002612; Adeno_E1B_55kDa.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF01696; Adeno_E1B_55K; 1.
DR Pfam; PF04623; Adeno_E1B_55K_N; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Modulation of host cell apoptosis by virus {ECO:0000256|ARBA:ARBA00023323}.
FT DOMAIN 1..69
FT /note="Adenovirus E1B protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04623"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55291 MW; 01AF2AEB080686B5 CRC64;
MEPEHPTEQG LHSGLRSHAP VEGMGEAAGT ENLELLAYTA SSSGSSSSTQ TNIHVGGRNE
AGHGREPEER PGPSVGRGAG LNQVSSLYPE LSKVLTSMAR GVKRERSDGG NTGMMTELTA
SLMNRKRPER ITWHELQMEC RDELGLMQDK YGLEQIKTHW LNPDEDWEEA IKKYAKIALR
PDCKYIVTKT VNIRHACYIS GNGAEVVIDT LDKAAFRCCM MGMRAGVMNM NSMIFMNMKF
NGEKFNGVLF MANSHMTLHG CSFFGFNNMC AEVWGASKIR GCKFYGCWMG VVGRPKSEMS
VKQCVFEKCY LGVSTEGNAR VRHCSSLDTG CFCLVKGTAS LKHNMVKGCT DERMYNMLTC
DSGVCHILKN IHVTSHPRKK WPVFENNLLI KCHMHLGARR GTFQPYQCNF SQTKLLLEND
AFSRVNLNGI FDMDVSVYKI LRYDETRSRV RACECGGRHT RMQPVALDVT EELRPDHLVM
ACTGTEFSSS GEDTD
//
