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Protein

E1B 55 kDa protein

Gene
N/A
Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins TCEB2, TCEB1, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function.3 Publications

GO - Molecular functioni

  • SUMO ligase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Modulation of host cell apoptosis by virus

Names & Taxonomyi

Protein namesi
Recommended name:
E1B 55 kDa protein
Short name:
E1B-55K
Alternative name(s):
E1B protein, large T-antigen
E1B-495R
OrganismiHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic identifieri28285 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000004992 Componenti: Genome

Subcellular locationi

  • Host nucleus 2 Publications
  • Host cytoplasm 1 Publication

  • Note: Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496E1B 55 kDa proteinPRO_0000221725Add
BLAST

Proteomic databases

PRIDEiP03243.

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Interacts with the transactivation domain of TP53 (via N-terminus); this interaction leads to the inhibition of TP53 function and/or its degradation (PubMed:25772236). Interacts with host PML-4 and PML-5; this interaction promotes efficient subnuclear targeting of E1B-55K to PML nuclear bodies (PubMed:20639899, PubMed:25772236). Interacts with E4-ORF3 protein (PubMed:10211970). Interacts with E4-ORF6 protein (By similarity). Interacts with host DAXX protein; this interaction might alterate the normal interactions of DAXX, PML, and p53, which may contribute to cell transformation (PubMed:14557665).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAXXQ9UER74EBI-1561361,EBI-77321From a different organism.
PMLP29590-22EBI-1927377,EBI-303996From a different organism.
PMLP29590-52EBI-1927377,EBI-304008From a different organism.
PmlF1M5896EBI-1927377,EBI-2941391From a different organism.

Protein-protein interaction databases

DIPiDIP-569N.
IntActiP03243. 7 interactions.
MINTiMINT-1521034.

Structurei

3D structure databases

ProteinModelPortaliP03243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 515Poly-Ala
Compositional biasi56 – 616Poly-Ala

Domaini

Contains a PML interaction motif that allows the subnuclear PML localization.1 Publication

Sequence similaritiesi

Family and domain databases

InterProiIPR006717. Adeno_E1B_55K_N.
IPR002612. Adeno_E1B_55kDa.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF01696. Adeno_E1B_55K. 1 hit.
PF04623. Adeno_E1B_55K_N. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: At least five different polypeptides are generated by alternative splicing of a common mRNA precursor.

Isoform E1B-496R (identifier: P03243-1) [UniParc]FASTAAdd to basket

Also known as: E1B-55K

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERRNPSERG VPAGFSGHAS VESGCETQES PATVVFRPPG DNTDGGAAAA
60 70 80 90 100
AGGSQAAAAG AEPMEPESRP GPSGMNVVQV AELYPELRRI LTITEDGQGL
110 120 130 140 150
KGVKRERGAC EATEEARNLA FSLMTRHRPE CITFQQIKDN CANELDLLAQ
160 170 180 190 200
KYSIEQLTTY WLQPGDDFEE AIRVYAKVAL RPDCKYKISK LVNIRNCCYI
210 220 230 240 250
SGNGAEVEID TEDRVAFRCS MINMWPGVLG MDGVVIMNVR FTGPNFSGTV
260 270 280 290 300
FLANTNLILH GVSFYGFNNT CVEAWTDVRV RGCAFYCCWK GVVCRPKSRA
310 320 330 340 350
SIKKCLFERC TLGILSEGNS RVRHNVASDC GCFMLVKSVA VIKHNMVCGN
360 370 380 390 400
CEDRASQMLT CSDGNCHLLK TIHVASHSRK AWPVFEHNIL TRCSLHLGNR
410 420 430 440 450
RGVFLPYQCN LSHTKILLEP ESMSKVNLNG VFDMTMKIWK VLRYDETRTR
460 470 480 490
CRPCECGGKH IRNQPVMLDV TEELRPDHLV LACTRAEFGS SDEDTD
Length:496
Mass (Da):55,000
Last modified:July 21, 1986 - v1
Checksum:i31EE3E4B9762DCE8
GO
Isoform E1B-156R (identifier: P03243-2) [UniParc]FASTAAdd to basket

Also known as: E1B-18K

The sequence of this isoform differs from the canonical sequence as follows:
     80-419: Missing.

Show »
Length:156
Mass (Da):16,649
Checksum:iF9517CEFCEC9DC2D
GO
Isoform E1B-93R (identifier: P03243-3) [UniParc]FASTAAdd to basket

Also known as: E1B-16K

The sequence of this isoform differs from the canonical sequence as follows:
     80-93: VAELYPELRRILTI → EGGVPTLPMQFESH
     94-495: Missing.

Show »
Length:94
Mass (Da):9,420
Checksum:i19EED86F2E3FB123
GO
Isoform E1B-84R (identifier: P03243-4) [UniParc]FASTAAdd to basket

Also known as: E1B-15K

The sequence of this isoform differs from the canonical sequence as follows:
     80-84: VAELY → QPPPP
     85-496: Missing.

Show »
Length:84
Mass (Da):8,311
Checksum:i6BE10C242CDB494C
GO
Isoform E1B-176R (identifier: P03246-1) [UniParc]FASTAAdd to basket

Also known as: E1B-19K

The sequence of this isoform can be found in the external entry P03246.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:176
Mass (Da):20,614
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei80 – 419340Missing in isoform E1B-156R. CuratedVSP_033960Add
BLAST
Alternative sequencei80 – 9314VAELY…RILTI → EGGVPTLPMQFESH in isoform E1B-93R. CuratedVSP_033961Add
BLAST
Alternative sequencei80 – 845VAELY → QPPPP in isoform E1B-84R. CuratedVSP_033962
Alternative sequencei85 – 496412Missing in isoform E1B-84R. CuratedVSP_033963Add
BLAST
Alternative sequencei94 – 495402Missing in isoform E1B-93R. CuratedVSP_033964Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02996 Genomic DNA. Translation: CAA26743.1.
X02996 Genomic DNA. Translation: CAB40666.1.
PIRiA03809. Q1AD55.
RefSeqiAP_000199.1. AC_000008.1. [P03243-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02996 Genomic DNA. Translation: CAA26743.1.
X02996 Genomic DNA. Translation: CAB40666.1.
PIRiA03809. Q1AD55.
RefSeqiAP_000199.1. AC_000008.1. [P03243-1]

3D structure databases

ProteinModelPortaliP03243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-569N.
IntActiP03243. 7 interactions.
MINTiMINT-1521034.

Proteomic databases

PRIDEiP03243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR006717. Adeno_E1B_55K_N.
IPR002612. Adeno_E1B_55kDa.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF01696. Adeno_E1B_55K. 1 hit.
PF04623. Adeno_E1B_55K_N. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens starting at different AUG triplets."
    Bos J.L., Polder L.J., Bernards R., Schrier P.I., van den Elsen P.J., van der Eb A.J., van Ormondt H.
    Cell 27:121-131(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of the transforming early region E1 of adenovirus type 5 DNA."
    van Ormondt H., Maat J., van Beveren C.P.
    Gene 11:299-309(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
    Chroboczek J., Bieber F., Jacrot B.
    Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Structure of two spliced mRNAs from the transforming region of human subgroup C adenoviruses."
    Perricaudet M., Akusjaervi G., Virtanen A., Pettersson U.
    Nature 281:694-696(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS E1B-496R; E1B-176R; E1B-156R; E1B-93R AND E1B-84R).
  5. "Characterization of the 55K adenovirus type 5 E1B product and related proteins."
    Takayesu D., Teodoro J.G., Whalen S.G., Branton P.E.
    J. Gen. Virol. 75:789-798(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS E1B-496R; E1B-176R; E1B-156R; E1B-93R AND E1B-84R).
  6. "The adenovirus type 5 E1b 55K and E4 Orf3 proteins associate in infected cells and affect ND10 components."
    Leppard K.N., Everett R.D.
    J. Gen. Virol. 80:997-1008(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH E4-ORF3 PROTEIN.
  7. "Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by DAXX."
    Zhao L.Y., Colosimo A.L., Liu Y., Wan Y., Liao D.
    J. Virol. 77:11809-11821(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST DAXX.
  8. "SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML."
    Wimmer P., Schreiner S., Everett R.D., Sirma H., Groitl P., Dobner T.
    Oncogene 29:5511-5522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST PML-4, INTERACTION WITH HOST PML-5.
  9. "Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies."
    Pennella M.A., Liu Y., Woo J.L., Kim C.A., Berk A.J.
    J. Virol. 84:12210-12225(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells."
    Schreiner S., Wimmer P., Sirma H., Everett R.D., Blanchette P., Groitl P., Dobner T.
    J. Virol. 84:7029-7038(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "PML isoforms IV and V contribute to adenovirus-mediated oncogenic transformation by functionally inhibiting the tumor-suppressor p53."
    Wimmer P., Berscheminski J., Blanchette P., Groitl P., Branton P.E., Hay R.T., Dobner T., Schreiner S.
    Oncogene 35:69-82(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST TP53, INTERACTION WITH HOST PML-4, INTERACTION WITH HOST PML-5.

Entry informationi

Entry nameiE1B55_ADE05
AccessioniPrimary (citable) accession number: P03243
Secondary accession number(s): Q64827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.