E1B55_ADE12
ID E1B55_ADE12 Reviewed; 482 AA.
AC P04491; Q64837;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 02-JUN-2021, entry version 80.
DE RecName: Full=E1B 55 kDa protein;
DE Short=E1B-55K;
DE AltName: Full=E1B protein, large T-antigen;
DE AltName: Full=E1B-495R;
OS Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6275367; DOI=10.1093/nar/9.23.6571;
RA Kimura T., Sawada Y., Shinawawa M., Shimizu Y., Shiroki K., Shimojo H.,
RA Sugisaki H., Takanami M., Uemizu Y., Fujinaga K.;
RT "Nucleotide sequence of the transforming early region E1b of adenovirus
RT type 12 DNA: structure and gene organization, and comparison with those of
RT adenovirus type 5 DNA.";
RL Nucleic Acids Res. 9:6571-6589(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7326748; DOI=10.1016/0092-8674(81)90366-4;
RA Bos J.L., Polder L.J., Bernards R., Schrier P.I., van den Elsen P.J.,
RA van der Eb A.J., van Ormondt H.;
RT "The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens
RT starting at different AUG triplets.";
RL Cell 27:121-131(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kimura T.;
RT "Structure and sequence analysis of the transforming region E1B of human
RT adenovirus type 12.";
RL Sapporo Igaku Zasshi 52:253-267(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
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:0000250|UniProtKB:P03243}.
CC -!- SUBUNIT: Interacts with the transactivation domain of TP53 (via N-
CC terminus); this interaction leads to the inhibition of TP53 function
CC and/or its degradation. Interacts with host PML-4 and PML-5; this
CC interaction promotes efficient subnuclear targeting of E1B-55K to PML
CC nuclear bodies. Interacts with E4-ORF3 protein (By similarity)
CC Interacts with E4-ORF6 protein. Interacts with host DAXX protein; this
CC interaction might alterate the normal interactions of DAXX, PML, and
CC p53, which may contribute to cell transformation.
CC {ECO:0000250|UniProtKB:P03243, ECO:0000250|UniProtKB:P03244}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03243}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03243}. Note=Colocalizes with host
CC TP53 to host PML nuclear bodies. PML localization of E1B-55K is
CC necessary for E1B-55K-dependent SUMOylation of TP53.
CC {ECO:0000250|UniProtKB:P03243}.
CC -!- DOMAIN: Contains a PML interaction motif that allows the subnuclear PML
CC localization. {ECO:0000250|UniProtKB:P03243}.
CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC {ECO:0000305}.
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DR EMBL; V00004; CAA23407.1; -; Genomic_DNA.
DR EMBL; M55003; AAA42499.1; -; Genomic_DNA.
DR EMBL; X73487; CAA51879.1; -; Genomic_DNA.
DR PIR; A03812; ERAD24.
DR RefSeq; NP_040912.1; NC_001460.1.
DR SMR; P04491; -.
DR IntAct; P04491; 1.
DR DNASU; 1460854; -.
DR GeneID; 1460854; -.
DR KEGG; vg:1460854; -.
DR Proteomes; UP000004993; Genome.
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:modulation by virus of host apoptotic process; 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; SSF51126; 1.
PE 3: Inferred from homology;
KW Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Modulation of host cell apoptosis by virus.
FT CHAIN 1..482
FT /note="E1B 55 kDa protein"
FT /id="PRO_0000221727"
FT REGION 73..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75..76
FT /note="DS -> ER (in Ref. 3; AAA42499)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="I -> E (in Ref. 3; AAA42499)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..301
FT /note="LIV -> ILN (in Ref. 3; AAA42499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53936 MW; 359E8082B7EF3659 CRC64;
MEREIPPELG LHAGLHVNAA VEGMAEEEGL HLLAGAAFDH AAAADVARGE GGGAEPCGGG
EVNMEQQVQE GHVLDSGEGP SCADDRDKQE KKESLKEAAV LSRLTVNLMS RPRLETVYWQ
ELQDEFQRGD MHLQYKYSFE QLKTHWLEPW EDMECAIKAF AKLALRPDCS YRITKTVTIT
SCAYIIGNGA IVEVDTSDRV AFRCRMQGMG PGVVGLDGIT FINVRFAGDK FKGIMFEANT
CLVLHGVYFL NFSNICVESW NKVSARGCTF YGCWKGLVGR PKSKLSVKKC LFEKCVLALI
VEGDAHIRHN AASENACFVL LKGMAILKHN MVCGVSDQTM RRFVTCADGN CHTLKTVHIV
SHSRHCWPVC DHNMFMRCTI HLGLRRGMFR PSQCNFSHSN IMLEPEVFSR VCLNGVFDLS
VELCKVIRYN DDTRHRCRQC ECGSSHLELR PIVLNVTEEL RSDHLTLSCL RTDYESSDED
DN
