ID E1B55_ADECR Reviewed; 444 AA. AC Q96679; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-NOV-2016, entry version 42. 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 Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine OS adenovirus 1 (strain RI261)). OC Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus; OC Canine mastadenovirus A. OX NCBI_TaxID=69151; OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9129661; RA Morrison M.D., Onions D.E., Nicolson L.; RT "Complete DNA sequence of canine adenovirus type 1."; RL J. Gen. Virol. 78:873-878(1997). CC -!- FUNCTION: Plays a major role to prevent cellular inhibition of CC viral genome replication. Assembles an SCF-like E3 ubiquitin CC ligase complex based on the cellular proteins TCEB2, TCEB1, CUL5 CC and RBX1, in cooperation with viral E4orf6. This viral RING-type CC ligase ubiquitinates cellular substrates and targets them to CC proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) CC complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 CC activity is essential for preventing E1A-induced TP53 accumulation CC that would otherwise lead to cell apoptosis and growth arrest. CC E1B-55K also inactivates TP53 transcription-factor activity by CC binding its transactivation domain. E1B-55K also functions as a CC SUMO1 E3 ligase for TP53 which causes the latter to be sequestered CC in promyelocytic leukemia (PML) nuclear bodies thereby CC 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 CC function and/or its degradation. Interacts with host PML-4 and CC PML-5; this interaction promotes efficient subnuclear targeting of CC E1B-55K to PML nuclear bodies. Interacts with E4-ORF3 protein. CC Interacts with E4-ORF6 protein. Interacts with host DAXX protein; CC this interaction might alterate the normal interactions of DAXX, CC PML, and 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}. CC Host cytoplasm {ECO:0000250|UniProtKB:P03243}. Note=Colocalizes CC with host TP53 to host PML nuclear bodies. PML localization of CC E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53. CC {ECO:0000250|UniProtKB:P03243}. CC -!- DOMAIN: Contains a PML interaction motif that allows the CC subnuclear PML localization. {ECO:0000250|UniProtKB:P03243}. CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family. CC {ECO:0000305}. 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; Y07760; CAA69054.1; -; Genomic_DNA. DR RefSeq; AP_000047.1; AC_000003.1. DR RefSeq; NP_044186.1; NC_001734.1. DR ProteinModelPortal; Q96679; -. DR GeneID; 1488948; -. DR KEGG; vg:1488948; -. 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; IPR002612; Adeno_E1B_55kDa. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF01696; Adeno_E1B_55K; 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 1 444 E1B 55 kDa protein. FT /FTId=PRO_0000221731. SQ SEQUENCE 444 AA; 49200 MW; 01073C78F1AC8736 CRC64; MEQDSDLESG RATNQRPPRV RVRGAGVRGR GRVRRRALSE GQRRSLFRLD DLQLPDSLYV TRALQRDHAL EMPRGQVDFS LIEAEERRAG PTDEWYFESV KTYRAKPGDD LQTLIKNYAK ISLECGAVYE INSKIVVTGA CYIIGNCAVL RANLPVGTAM FEVLNVDVIP SIGFMERIVF SNILFDCRST TAVVCCISER NTLFHNCVFS GPHMLCLDIR AGAEVRGCHF VGAVCALRSK GLYSVRVRNS IFEKCAFGVV SGSKASISHS MFKDCACCIM LGGQGTIAHS HFMATTCTDT PMNLQLCTCE GNGSHVVPLG NIHFASNREA PWPTFNANVL VRVRLYMGRR RGVFHPKQST FSMCVIAAPR GVVQRIYLFS VYDATCAILQ LGEAGDAATE RLCTCGMRHN TPSLRAAYVT DTRIDREINS QDTAEFFSSD EDNL //