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Database: UniProt
Entry: T1UK63_9ADEN
LinkDB: T1UK63_9ADEN
Original site: T1UK63_9ADEN 
ID   T1UK63_9ADEN            Unreviewed;       495 AA.
AC   T1UK63;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:AGT77810.1};
GN   ORFNames=H648_40380gpE1B {ECO:0000313|EMBL:AGT77810.1};
OS   Human mastadenovirus D.
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=130310 {ECO:0000313|EMBL:AGT77810.1, ECO:0000313|Proteomes:UP000099673};
RN   [1] {ECO:0000313|EMBL:AGT77810.1, ECO:0000313|Proteomes:UP000099673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Human/DEU/HEIM_00083/1986/17[P17H17F17]
RC   {ECO:0000313|EMBL:AGT77810.1};
RA   Madupu R., Halpin R., Fedorova N., Tsitrin T., Stockwell T., Amedeo P.,
RA   Appalla L., Bishop B., Edworthy P., Gupta N., Hoover J., Katzel D., Li K.,
RA   Schobel S., Shrivastava S., Thovarai V., Wang S., Dehghan S., Singh S.,
RA   Liu E.B., Seto J., Jones M.S., Kajon A., Gray G., Kowalski R.,
RA   Romanowski E., Chodosh J., Wentworth D.E., Seto D.;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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; KF268330; AGT77810.1; -; Genomic_DNA.
DR   Proteomes; UP000099673; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039526; P:perturbation by virus of host apoptosis; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; 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        32..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  55163 MW;  B560BA3AF1C885F3 CRC64;
     MEPANPLNQG LHPGLHGHAP VEGLGQAAGT ENLELLASTA SSSGSSSSTQ TNIHVGGRDE
     GGHGREPEER PGPSVGRGAG LNQVSSLYPE LSKVLTTMAR GVKRERSDGG NTGMMTELTA
     SLMNRRRPER ITWHELQQEC RDEIGLMQDK YGLEQIKTHW LNPDEDWEEA IKKYAKIALR
     PDCKYRVTKT VNIRHACYIS GNGAEVIIDT LDKAAFRCCM MGMRAGVMNM NSMIFMNIKF
     NGEKFNGVLF MANSHMTLHG CNFFGFNNMC AEVWGASKIR GCKFYGCWMG VVGRPKSEMS
     VKQCVFEKCY LAVSTEGNAR VRHCSSMETG CFCLVKGTAS IKHNVIKGCT DERMYNMLTC
     DSGVCHILKN IHVTSHPRKR WPSFENNVLI KCHVHLGARR GTFQPYQCNF SQTKLLLEND
     AFSRVNLNGI FDMDVSVYKI LRYDETRSRV RACECGGRHT RMQPVALDVT EELRPDHLVM
     ACTGTEFSSS GEDTD
//
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