CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Early E1A 29.5 kDa protein 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12) 
NCBI Taxa ID
 28282 
Lysine Modification
Position
Peptide
Type
References
261VPVDLSVKRPRCN**acetylation[1]
Reference
 [1] Acetylation at a lysine residue adjacent to the CtBP binding motif within adenovirus 12 E1A causes structural disruption and limited reduction of CtBP binding.
 Molloy D, Mapp KL, Webster R, Gallimore PH, Grand RJ.
 Virology. 2006 Nov 25;355(2):115-26. [PMID: 16919702
Functional Description
 E1A protein has both transforming and trans-activating activities. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Disrupts the function of host retinoblastoma protein RB1/pRb and isoform early E1A 26 kDa protein stabilizes TP53, which are key regulators of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1- regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP- CtIP complex through the CtBP binding motif (By similarity). 
Sequence Annotation
 ZN_FING 159 179 Potential.
 REGION 39 47 Interaction with RB1 in competition with
 REGION 75 145 Interaction with UBE2I.
 MOTIF 98 102 PXLXP motif, interaction with host
 MOTIF 107 111 LXCXE motif, interaction with host RB1
 MOTIF 255 259 PXDLS motif, CTBP-binding (By
 MOTIF 261 265 Nuclear localization signal (Potential).  
Keyword
 Activator; Alternative splicing; Complete proteome; Early protein; G1/S host cell cycle checkpoint dysregulation by virus; Host nucleus; Host-virus interaction; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway by virus; Inhibition of host NF-kappa-B by virus; Inhibition of host STAT1 by virus; Metal-binding; Modulation of host cell cycle by virus; Modulation of host E3 ubiquitin ligases by virus; Modulation of host ubiquitin pathway by virus; Oncogene; Transcription; Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 266 AA 
Protein Sequence
MRTEMTPLVL SYQEADDILE HLVDNFFNEV PSDDDLYVPS LYELYDLDVE SAGEDNNEQA 60
VNEFFPESLI LAASEGLFLP EPPVLSPVCE PIGGECMPQL HPEDMDLLCY EMGFPCSDSE 120
DEQDENGMAH VSASAAAAAA DREREEFQLD HPELPGHNCK SCEHHRNSTG NTDLMCSLCY 180
LRAYNMFIYS PVSDNEPEPN STLDGDERPS PPKLGSAVPE GVIKPVPQRV TGRRRCAVES 240
ILDLIQEEER EQTVPVDLSV KRPRCN 266 
Gene Ontology
 GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
 GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
 GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
 GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR014410; Aden_E1A.
 IPR003853; Adeno_E1A. 
Pfam
 PF02703; Adeno_E1A 
SMART
  
PROSITE
  
PRINTS