ID M0QUF4_9ADEN Unreviewed; 495 AA.
AC M0QUF4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:AFK92324.1};
OS Human adenovirus 24.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus D.
OX NCBI_TaxID=46926 {ECO:0000313|EMBL:AFK92324.1, ECO:0000313|Proteomes:UP000160117};
RN [1] {ECO:0000313|EMBL:AFK92324.1, ECO:0000313|Proteomes:UP000160117}
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}.
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DR EMBL; JN226751; AFK92324.1; -; Genomic_DNA.
DR Proteomes; UP000160117; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; 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; 55336 MW; 24E14C323D1D90D7 CRC64;
MEPEHPTEQG LHSGLRSHAP VEGMGEAAGT ENLELLAYTA SSSGSSSSTQ TNIHVGGRNE
AGHGREPEER PGPSVGRGAG LNQVSSLYPE LSRVLTSMAR GVKRERSDGG NTGMMTELTA
SLMNRKRPER ITWHELQMEC RDEVGLMQDK YGLEQIKTHW LNPDEDWEEA IKKYAKIALR
PDCKYRVTKT VNIRHACYIS GNGAEVVIDT LDKAAFRCCM MGMRAGVMNM NSMIFMNMKF
NGEKFNGVMF MANSHMTLHG CSFFGFNNMC AEVWGAAKIR GCKFYGCWMG VVGRPKSEMS
VKQCVFEKCY LGVSTEGNAR VRHCSSLETG CFCLVKGTAS LKHNMVKGCT DERMYNMLTC
DSGVCHILKN IHVTSHPRKK WPVFENNLLI KCHMHLGARR GTFQPYQCNF SQTKLLLEND
AFSRVNLNGI FDMDVSVYKI LRYDETKSRV RACECGGRHT RMQPVALDVT EELRPDHLVM
ACTGTEFSSS GEDTD
//
