ID   E1B55_ADE07             Reviewed;         492 AA.
AC   P03245;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 64.
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 B serotype 7 (HAdV-7) (Human adenovirus 7).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX   NCBI_TaxID=10519;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Gomen;
RX   PubMed=6290319; DOI=10.1016/0378-1119(82)90112-3;
RA   Dijkema R., Dekker B.M.M., van Ormondt H.;
RT   "Gene organization of the transforming region of adenovirus type 7 DNA.";
RL   Gene 18:143-156(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
RC   STRAIN=Grider;
RA   Yoshida K., Fujinaga K.;
RT   "The nucleotide sequence of the transforming HindIII-I.J fragment of
RT   adenovirus type 7 DNA.";
RL   Tumor Res. 19:39-47(1984).
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. Interacts with E4-ORF6
CC       protein. Interacts with host DAXX protein; this interaction might
CC       alterate the normal interactions of DAXX, PML, and p53, which may
CC       contribute to cell transformation. {ECO:0000250|UniProtKB:P03243,
CC       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; X03000; CAA26763.1; -; Genomic_DNA.
DR   EMBL; M38648; AAA42457.1; -; Genomic_DNA.
DR   PIR; A03810; WMAD55.
DR   SMR; P03245; -.
DR   PRIDE; P03245; -.
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..492
FT                   /note="E1B 55 kDa protein"
FT                   /id="PRO_0000221726"
FT   REGION          22..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         42
FT                   /note="G -> R (in strain: Grider)"
FT   VARIANT         52
FT                   /note="D -> Y (in strain: Grider)"
FT   VARIANT         230
FT                   /note="I -> V (in strain: Grider)"
FT   VARIANT         259
FT                   /note="S -> R (in strain: Grider)"
FT   VARIANT         268
FT                   /note="V -> E (in strain: Grider)"
SQ   SEQUENCE   492 AA;  54702 MW;  68511E135ADF2ACD CRC64;
     MDPPNSLQQG IRFGFHSSSF VENMEGSQDE DNLRLLASAA SGSSRDTETP TDHASGSAGG
     AAGGQSESRP GPSGGGVADL FPELRRVLTR STTSGQNRGI KRERNPSGNN SRTELALSLM
     SRRRPETVWW HEVQSEGRDE VSILQEKYSL EQLKTCWLEP EDDWEVAIRN YAKISLRPDK
     QYRITKKINI RNACYISGNG AEVIIDTQDK AAFRCCMMGM WPGVVGMEAI TLMNIRFRGD
     GYNGIVFMAN TKLILHGCSF FGFNNTCVEA WGQVSVRGCS FYACWIATSG RVKSQLSVKK
     CMFERCNLGI LNEGEARVRH CAATETACFI LIKGNASVKH NMICGHSDER PYQMLTCAGG
     HCNILATVHI VSHARKKWPV FEHNVITKCT MHIGGRRGMF MPYQCNMNHV KVMLEPDAFS
     RVSVTGIFDM NIQLWKILRY DDTKPRVRAC ECGGKHARFQ PVCVDVTEDL RPDHLVLACT
     GAEFGSSGEE TD