Q7TNS8 · EPOP_MOUSE
- ProteinElongin BC and Polycomb repressive complex 2-associated protein
- GeneEpop
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Scaffold protein that serves as a bridging partner between the PRC2/EZH2 complex and the elongin BC complex: required to fine-tune the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells (ESCs) (PubMed:27863225, PubMed:27863226).
Plays a key role in genomic regions that display both active and repressive chromatin properties in pluripotent stem cells by sustaining low level expression at PcG target genes: acts by recruiting the elongin BC complex, thereby restricting excessive activity of the PRC2/EZH2 complex (PubMed:27863225, PubMed:27863226).
Interaction with USP7 promotes deubiquitination of H2B at promoter sites (PubMed:27863226).
Acts as a regulator of neuronal differentiation (PubMed:23180766).
Plays a key role in genomic regions that display both active and repressive chromatin properties in pluripotent stem cells by sustaining low level expression at PcG target genes: acts by recruiting the elongin BC complex, thereby restricting excessive activity of the PRC2/EZH2 complex (PubMed:27863225, PubMed:27863226).
Interaction with USP7 promotes deubiquitination of H2B at promoter sites (PubMed:27863226).
Acts as a regulator of neuronal differentiation (PubMed:23180766).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | protein-containing complex binding | |
Biological Process | neuron fate commitment | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | stem cell differentiation | |
Biological Process | transcription elongation-coupled chromatin remodeling |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameElongin BC and Polycomb repressive complex 2-associated protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TNS8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at both PRC2/EZH2 sites (H3K27me3) and broad H3K4me3 sites on chromatin of embryonic stem cells (ESCs) (PubMed:27863226).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 40 | Abolishes interaction with the elongin BC complex. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000332155 | 1-369 | Elongin BC and Polycomb repressive complex 2-associated protein | |||
Sequence: METLCPPPRLAVPASPRGSPCSPTPLKPRRGTPEFSPLCLRALAFCALAKPRPSSLGLGPGELAPRTPVLLGPPASPCTGGWAADGLKHLGGQAGRPSDVSSPAREDADVAVCPGGGEEEEGGGGFPHFGAGSCAPPGRCPAPLRPQDSPTNPAWSPPRPARGLDAASSPPLEPGSPPPSPPAGLSPEPAPSEQPVPASEAPGGGDPAPTAPEAPALSPSTADAAPDPPRDLRQEHFNRLIRRSKLWCYAKGFALDTPSLRRGPERPAAKARGAAKKRRRPAPPPPSVQPRRPVPTLPTSSTFSLLDCFPCPPALVVEENGDLGPASSLRLQGDAKPPPAHPLWKWQMGGPAVPEPPGLKSWWVNLEEL | ||||||
Modified residue | 15 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 19 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 52 | Asymmetric dimethylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Associates with the PRC2 complex, which consists of the core components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:21732481, PubMed:27462409, PubMed:27863225, PubMed:27863226).
Within the complex, interacts with SUZ12 (via C2H2 zinc finger domain); competes with JARID2 for SUZ12 binding (By similarity).
Associates with the elongin BC complex (PubMed:27863225, PubMed:27863226).
Interacts with USP7 (PubMed:27863226).
Within the complex, interacts with SUZ12 (via C2H2 zinc finger domain); competes with JARID2 for SUZ12 binding (By similarity).
Associates with the elongin BC complex (PubMed:27863225, PubMed:27863226).
Interacts with USP7 (PubMed:27863226).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7TNS8 | Eed Q921E6 | 2 | EBI-16024836, EBI-904301 | |
BINARY | Q7TNS8 | Gtf2e2 Q9D902 | 2 | EBI-16024836, EBI-309435 | |
BINARY | Q7TNS8 | Suz12 Q80U70 | 2 | EBI-16024836, EBI-2526494 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: METLCPPPRLAVPASPRGSPCSPTPLKPRRGTP | ||||||
Compositional bias | 9-27 | Pro residues | ||||
Sequence: RLAVPASPRGSPCSPTPLK | ||||||
Region | 39-48 | BC-box | ||||
Sequence: CLRALAFCAL | ||||||
Region | 89-237 | Disordered | ||||
Sequence: HLGGQAGRPSDVSSPAREDADVAVCPGGGEEEEGGGGFPHFGAGSCAPPGRCPAPLRPQDSPTNPAWSPPRPARGLDAASSPPLEPGSPPPSPPAGLSPEPAPSEQPVPASEAPGGGDPAPTAPEAPALSPSTADAAPDPPRDLRQEHF | ||||||
Compositional bias | 139-157 | Pro residues | ||||
Sequence: RCPAPLRPQDSPTNPAWSP | ||||||
Compositional bias | 171-196 | Pro residues | ||||
Sequence: PLEPGSPPPSPPAGLSPEPAPSEQPV | ||||||
Region | 256-299 | Disordered | ||||
Sequence: DTPSLRRGPERPAAKARGAAKKRRRPAPPPPSVQPRRPVPTLPT | ||||||
Region | 301-349 | Interaction with SUZ12 | ||||
Sequence: STFSLLDCFPCPPALVVEENGDLGPASSLRLQGDAKPPPAHPLWKWQMG |
Domain
The BC-box, which mediates binding to the elongin BC complex.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)38,095
- Last updated2003-10-01 v1
- ChecksumC93AC0213E4E97BF
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-27 | Pro residues | ||||
Sequence: RLAVPASPRGSPCSPTPLK | ||||||
Sequence conflict | 129 | in Ref. 1; BAC39864 | ||||
Sequence: F → S | ||||||
Sequence conflict | 135 | in Ref. 3; AAH06054 | ||||
Sequence: A → S | ||||||
Compositional bias | 139-157 | Pro residues | ||||
Sequence: RCPAPLRPQDSPTNPAWSP | ||||||
Compositional bias | 171-196 | Pro residues | ||||
Sequence: PLEPGSPPPSPPAGLSPEPAPSEQPV | ||||||
Sequence conflict | 286 | in Ref. 1; BAC39864 | ||||
Sequence: P → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK087411 EMBL· GenBank· DDBJ | BAC39864.1 EMBL· GenBank· DDBJ | mRNA | ||
AL596123 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC006054 EMBL· GenBank· DDBJ | AAH06054.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC055770 EMBL· GenBank· DDBJ | AAH55770.1 EMBL· GenBank· DDBJ | mRNA |