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Transcription factor E4F1
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| http://www.biopax.org/relea... |
E4F1_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
6.3.2.-,
E4F transcription factor 1,
Putative E3 ubiquitin-protein ligase E4F1,
Transcription factor E4F,
p120E4F,
p50E4F
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| http://www.biopax.org/relea... |
FUNCTION: May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription. FUNCTION: Identified as a cellular target of the adenoviral oncoprotein E1A, it is required for both transcriptional activation and repression of viral genes. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Homodimer; binds DNA as a dimer. Forms a complex with CDKN2A and TP53. Interactions with TP53, RB1, ANP32A, BMI1 and FHL2 regulate E4F1 activity. Interacts with HDAC1, HMGA2 and RASSF1. Interacts with HBV protein X. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=A small fraction is detected in the cytoplasm. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis (By similarity). TISSUE SPECIFICITY: Ubiquitously expressed. DEVELOPMENTAL STAGE: Expressed in a variety of fetal tissues. INDUCTION: Up-regulated by estrogen. PTM: Proteolytic cleavage produces a 50 kDa N-terminal peptide (p50E4F) which has a DNA-binding activity and activates transcription in presence of the adenoviral E1A protein. The major full length protein (p120E4F) functions as a repressor of transcription. PTM: Phosphorylated; p120E4F and p50E4F are both phosphorylated. Phosphorylation is cell cycle-dependent and differentially regulates DNA-binding activity and function of both forms. PTM: May be sumoylated by UBE2I upon interaction with CDKN2A. SIMILARITY: Contains 9 C2H2-type zinc fingers. GENE SYNONYMS: E4F. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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