E1B55_ADE05
ID E1B55_ADE05 Reviewed; 496 AA.
AC P03243; Q64827;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6260576; DOI=10.1016/0378-1119(80)90070-0;
RA van Ormondt H., Maat J., van Beveren C.P.;
RT "The nucleotide sequence of the transforming early region E1 of adenovirus
RT type 5 DNA.";
RL Gene 11:299-309(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS E1B-496R; E1B-176R; E1B-156R; E1B-93R AND
RP E1B-84R).
RX PubMed=551290; DOI=10.1038/281694a0;
RA Perricaudet M., Akusjaervi G., Virtanen A., Pettersson U.;
RT "Structure of two spliced mRNAs from the transforming region of human
RT subgroup C adenoviruses.";
RL Nature 281:694-696(1979).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORMS E1B-496R; E1B-176R; E1B-156R; E1B-93R AND
RP E1B-84R).
RX PubMed=8151295; DOI=10.1099/0022-1317-75-4-789;
RA Takayesu D., Teodoro J.G., Whalen S.G., Branton P.E.;
RT "Characterization of the 55K adenovirus type 5 E1B product and related
RT proteins.";
RL J. Gen. Virol. 75:789-798(1994).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH E4-ORF3 PROTEIN.
RX PubMed=10211970; DOI=10.1099/0022-1317-80-4-997;
RA Leppard K.N., Everett R.D.;
RT "The adenovirus type 5 E1b 55K and E4 Orf3 proteins associate in infected
RT cells and affect ND10 components.";
RL J. Gen. Virol. 80:997-1008(1999).
RN [7]
RP INTERACTION WITH HOST DAXX.
RX PubMed=14557665; DOI=10.1128/jvi.77.21.11809-11821.2003;
RA Zhao L.Y., Colosimo A.L., Liu Y., Wan Y., Liao D.;
RT "Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates
RT enhancement of p53-dependent transcription by DAXX.";
RL J. Virol. 77:11809-11821(2003).
RN [8]
RP INTERACTION WITH HOST PML-4, AND INTERACTION WITH HOST PML-5.
RX PubMed=20639899; DOI=10.1038/onc.2010.284;
RA Wimmer P., Schreiner S., Everett R.D., Sirma H., Groitl P., Dobner T.;
RT "SUMO modification of E1B-55K oncoprotein regulates isoform-specific
RT binding to the tumour suppressor protein PML.";
RL Oncogene 29:5511-5522(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20861261; DOI=10.1128/jvi.01442-10;
RA Pennella M.A., Liu Y., Woo J.L., Kim C.A., Berk A.J.;
RT "Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that
RT represses p53 and stimulates its nuclear export through interactions with
RT promyelocytic leukemia nuclear bodies.";
RL J. Virol. 84:12210-12225(2010).
RN [10]
RP FUNCTION.
RX PubMed=20484509; DOI=10.1128/jvi.00074-10;
RA Schreiner S., Wimmer P., Sirma H., Everett R.D., Blanchette P., Groitl P.,
RA Dobner T.;
RT "Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in
RT human adenovirus-infected cells.";
RL J. Virol. 84:7029-7038(2010).
RN [11]
RP FUNCTION, INTERACTION WITH HOST TP53, INTERACTION WITH HOST PML-4, AND
RP INTERACTION WITH HOST PML-5.
RX PubMed=25772236; DOI=10.1038/onc.2015.63;
RA Wimmer P., Berscheminski J., Blanchette P., Groitl P., Branton P.E.,
RA Hay R.T., Dobner T., Schreiner S.;
RT "PML isoforms IV and V contribute to adenovirus-mediated oncogenic
RT transformation by functionally inhibiting the tumor-suppressor p53.";
RL Oncogene 35:69-82(2016).
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:0000269|PubMed:20484509, ECO:0000269|PubMed:20861261,
CC ECO:0000269|PubMed:25772236}.
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 (PubMed:25772236). Interacts with host PML-4 and
CC PML-5; this interaction promotes efficient subnuclear targeting of E1B-
CC 55K to PML nuclear bodies (PubMed:20639899, PubMed:25772236). Interacts
CC with E4-ORF3 protein (PubMed:10211970). Interacts with E4-ORF6 protein
CC (By similarity). Interacts with host DAXX protein; this interaction
CC might alterate the normal interactions of DAXX, PML, and p53, which may
CC contribute to cell transformation (PubMed:14557665).
CC {ECO:0000250|UniProtKB:P03244, ECO:0000269|PubMed:10211970,
CC ECO:0000269|PubMed:14557665, ECO:0000269|PubMed:20639899,
CC ECO:0000269|PubMed:25772236}.
CC -!- INTERACTION:
CC P03243; Q9UER7: DAXX; Xeno; NbExp=4; IntAct=EBI-1561361, EBI-77321;
CC P03243-1; P49959: MRE11; Xeno; NbExp=2; IntAct=EBI-1927377, EBI-396513;
CC P03243-1; F1M589: Pml; Xeno; NbExp=6; IntAct=EBI-1927377, EBI-2941391;
CC P03243-1; P29590: PML; Xeno; NbExp=3; IntAct=EBI-1927377, EBI-295890;
CC P03243-1; P29590-2: PML; Xeno; NbExp=3; IntAct=EBI-1927377, EBI-303996;
CC P03243-1; P29590-5: PML; Xeno; NbExp=3; IntAct=EBI-1927377, EBI-304008;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10211970,
CC ECO:0000269|PubMed:20861261}. Host cytoplasm
CC {ECO:0000269|PubMed:10211970}. Note=Colocalizes with host TP53 to host
CC PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-
CC 55K-dependent SUMOylation of TP53. {ECO:0000269|PubMed:20861261}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=At least five different polypeptides are generated by
CC alternative splicing of a common mRNA precursor.;
CC Name=E1B-496R; Synonyms=E1B-55K;
CC IsoId=P03243-1; Sequence=Displayed;
CC Name=E1B-156R; Synonyms=E1B-18K;
CC IsoId=P03243-2; Sequence=VSP_033960;
CC Name=E1B-93R; Synonyms=E1B-16K;
CC IsoId=P03243-3; Sequence=VSP_033961, VSP_033964;
CC Name=E1B-84R; Synonyms=E1B-15K;
CC IsoId=P03243-4; Sequence=VSP_033962, VSP_033963;
CC Name=E1B-176R; Synonyms=E1B-19K;
CC IsoId=P03246-1; Sequence=External;
CC -!- DOMAIN: Contains a PML interaction motif that allows the subnuclear PML
CC localization. {ECO:0000269|PubMed:25772236}.
CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC {ECO:0000305}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02996; CAA26743.1; -; Genomic_DNA.
DR EMBL; X02996; CAB40666.1; -; Genomic_DNA.
DR PIR; A03809; Q1AD55.
DR RefSeq; AP_000199.1; AC_000008.1. [P03243-1]
DR SMR; P03243; -.
DR DIP; DIP-569N; -.
DR IntAct; P03243; 11.
DR PRIDE; P03243; -.
DR Proteomes; UP000004992; 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:0061665; F:SUMO ligase activity; IDA:UniProtKB.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR006717; Adeno_E1B_55K_N.
DR InterPro; IPR002612; Adeno_E1B_55kDa.
DR InterPro; IPR012334; Pectin_lyas_fold.
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 1: Evidence at protein level;
KW Alternative splicing; Early protein; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Modulation of host cell apoptosis by virus.
FT CHAIN 1..496
FT /note="E1B 55 kDa protein"
FT /id="PRO_0000221725"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 80..419
FT /note="Missing (in isoform E1B-156R)"
FT /evidence="ECO:0000305"
FT /id="VSP_033960"
FT VAR_SEQ 80..93
FT /note="VAELYPELRRILTI -> EGGVPTLPMQFESH (in isoform E1B-
FT 93R)"
FT /evidence="ECO:0000305"
FT /id="VSP_033961"
FT VAR_SEQ 80..84
FT /note="VAELY -> QPPPP (in isoform E1B-84R)"
FT /evidence="ECO:0000305"
FT /id="VSP_033962"
FT VAR_SEQ 85..496
FT /note="Missing (in isoform E1B-84R)"
FT /evidence="ECO:0000305"
FT /id="VSP_033963"
FT VAR_SEQ 94..495
FT /note="Missing (in isoform E1B-93R)"
FT /evidence="ECO:0000305"
FT /id="VSP_033964"
SQ SEQUENCE 496 AA; 55000 MW; 31EE3E4B9762DCE8 CRC64;
MERRNPSERG VPAGFSGHAS VESGCETQES PATVVFRPPG DNTDGGAAAA AGGSQAAAAG
AEPMEPESRP GPSGMNVVQV AELYPELRRI LTITEDGQGL KGVKRERGAC EATEEARNLA
FSLMTRHRPE CITFQQIKDN CANELDLLAQ KYSIEQLTTY WLQPGDDFEE AIRVYAKVAL
RPDCKYKISK LVNIRNCCYI SGNGAEVEID TEDRVAFRCS MINMWPGVLG MDGVVIMNVR
FTGPNFSGTV FLANTNLILH GVSFYGFNNT CVEAWTDVRV RGCAFYCCWK GVVCRPKSRA
SIKKCLFERC TLGILSEGNS RVRHNVASDC GCFMLVKSVA VIKHNMVCGN CEDRASQMLT
CSDGNCHLLK TIHVASHSRK AWPVFEHNIL TRCSLHLGNR RGVFLPYQCN LSHTKILLEP
ESMSKVNLNG VFDMTMKIWK VLRYDETRTR CRPCECGGKH IRNQPVMLDV TEELRPDHLV
LACTRAEFGS SDEDTD
