Q6ZN18 · AEBP2_HUMAN
- ProteinZinc finger protein AEBP2
- GeneAEBP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an accessory subunit for the core Polycomb repressive complex 2 (PRC2), which mediates histone H3K27 (H3K27me3) trimethylation on chromatin leading to transcriptional repression of the affected target gene (PubMed:15225548, PubMed:29499137, PubMed:31959557).
Plays a role in nucleosome localization of the PRC2 complex (PubMed:29499137).
Plays a role in nucleosome localization of the PRC2 complex (PubMed:29499137).
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 | chromatin | |
Cellular Component | ESC/E(Z) complex | |
Cellular Component | nucleoplasm | |
Molecular Function | DNA binding | |
Molecular Function | metal ion binding | |
Molecular Function | transcription coregulator activity | |
Biological Process | chromatin organization | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein AEBP2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6ZN18
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to chromatin as part of the PRC2 complex.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 474 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000341590 | 2-517 | UniProt | Zinc finger protein AEBP2 | |||
Sequence: AAAITDMADLEELSRLSPLPPGSPGSAARGRAEPPEEEEEEEEEEEEAEAEAVAALLLNGGSGGGGGGGGGGVGGGEAETMSEPSPESASQAGEDEDEEEDDEEEEDESSSSGGGEEESSAESLVGSSGGSSSDETRSLSPGAASSSSGDGDGKEGLEEPKGPRGSQGGGGGGSSSSSVVSSGGDEGYGTGGGGSSATSGGRRGSLEMSSDGEPLSRMDSEDSISSTIMDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRTMPQKRLKRTLIRKVFNLYLSKQ | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 18 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 24 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 139 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 141 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 206 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 210 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 211 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Self-associates (PubMed:15225548).
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:12351676, PubMed:15225548, PubMed:29499137, PubMed:31959557).
Found in a monomeric PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 (PubMed:29499137).
Within the PRC2 complex, interacts directly with SUZ12; competes with PHF19 for SUZ12 binding (PubMed:12351676, PubMed:29499137).
Interacts with EED, EZH2, and RBBP4 (PubMed:12351676, PubMed:15225548).
May also interact with RBBP7 (PubMed:12351676).
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:12351676, PubMed:15225548, PubMed:29499137, PubMed:31959557).
Found in a monomeric PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 (PubMed:29499137).
Within the PRC2 complex, interacts directly with SUZ12; competes with PHF19 for SUZ12 binding (PubMed:12351676, PubMed:29499137).
Interacts with EED, EZH2, and RBBP4 (PubMed:12351676, PubMed:15225548).
May also interact with RBBP7 (PubMed:12351676).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6ZN18-2 | HMBOX1 Q6NT76 | 6 | EBI-10255023, EBI-2549423 | |
BINARY | Q6ZN18-2 | KRTAP10-8 P60410 | 3 | EBI-10255023, EBI-10171774 | |
BINARY | Q6ZN18-2 | LDOC1 O95751 | 3 | EBI-10255023, EBI-740738 | |
BINARY | Q6ZN18-2 | MDFI Q99750 | 3 | EBI-10255023, EBI-724076 | |
BINARY | Q6ZN18-2 | PICK1 Q9NRD5 | 3 | EBI-10255023, EBI-79165 | |
BINARY | Q6ZN18-2 | TSPYL2 Q9H2G4 | 3 | EBI-10255023, EBI-947459 | |
BINARY | Q6ZN18-2 | ZNF408 Q9H9D4 | 3 | EBI-10255023, EBI-347633 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-229 | Disordered | ||||
Sequence: MAAAITDMADLEELSRLSPLPPGSPGSAARGRAEPPEEEEEEEEEEEEAEAEAVAALLLNGGSGGGGGGGGGGVGGGEAETMSEPSPESASQAGEDEDEEEDDEEEEDESSSSGGGEEESSAESLVGSSGGSSSDETRSLSPGAASSSSGDGDGKEGLEEPKGPRGSQGGGGGGSSSSSVVSSGGDEGYGTGGGGSSATSGGRRGSLEMSSDGEPLSRMDSEDSISSTI | ||||||
Compositional bias | 36-52 | Acidic residues | ||||
Sequence: PEEEEEEEEEEEEAEAE | ||||||
Compositional bias | 91-114 | Acidic residues | ||||
Sequence: SQAGEDEDEEEDDEEEEDESSSSG | ||||||
Compositional bias | 115-148 | Polar residues | ||||
Sequence: GGEEESSAESLVGSSGGSSSDETRSLSPGAASSS | ||||||
Compositional bias | 170-185 | Polar residues | ||||
Sequence: GGGGGSSSSSVVSSGG | ||||||
Region | 209-294 | Interaction with RBBP4 | ||||
Sequence: MSSDGEPLSRMDSEDSISSTIMDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGV | ||||||
Zinc finger | 261-286 | C2H2-type 1 | ||||
Sequence: YNCCWDQCQACFNSSPDLADHIRSIH | ||||||
Zinc finger | 300-322 | C2H2-type 2; degenerate | ||||
Sequence: KGCKVYNTPSTSQSWLQRHMLTH | ||||||
Zinc finger | 328-352 | C2H2-type 3 | ||||
Sequence: FKCVVGGCNASFASQGGLARHVPTH | ||||||
Compositional bias | 352-369 | Polar residues | ||||
Sequence: HFSQQNSSKVSSQPKAKE | ||||||
Region | 352-394 | Disordered | ||||
Sequence: HFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRP | ||||||
Region | 407-478 | Interaction with SUZ12 | ||||
Sequence: RHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLS | ||||||
Region | 495-517 | Important for nucleosome binding activity of the PRC2 complex | ||||
Sequence: TMPQKRLKRTLIRKVFNLYLSKQ |
Sequence similarities
Belongs to the AEBP2/jing C2H2-type zinc-finger family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6ZN18-1
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.
- Name1
- Length517
- Mass (Da)54,467
- Last updated2008-06-10 v2
- Checksum6C59888ACEE4F9AF
Q6ZN18-2
- Name2
- Differences from canonical
- 504-517: Missing
Q6ZN18-3
- Name3
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YH08 | H0YH08_HUMAN | AEBP2 | 130 | ||
H7BYT4 | H7BYT4_HUMAN | AEBP2 | 140 | ||
G5EA50 | G5EA50_HUMAN | AEBP2 | 274 | ||
F5GZR7 | F5GZR7_HUMAN | AEBP2 | 110 | ||
A0A669KBL4 | A0A669KBL4_HUMAN | AEBP2 | 268 | ||
A0A669KBC9 | A0A669KBC9_HUMAN | AEBP2 | 257 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034357 | 1-216 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 36-52 | Acidic residues | ||||
Sequence: PEEEEEEEEEEEEAEAE | ||||||
Compositional bias | 91-114 | Acidic residues | ||||
Sequence: SQAGEDEDEEEDDEEEEDESSSSG | ||||||
Compositional bias | 115-148 | Polar residues | ||||
Sequence: GGEEESSAESLVGSSGGSSSDETRSLSPGAASSS | ||||||
Compositional bias | 170-185 | Polar residues | ||||
Sequence: GGGGGSSSSSVVSSGG | ||||||
Alternative sequence | VSP_034358 | 217-223 | in isoform 3 | |||
Sequence: SRMDSED → MYTRRYS | ||||||
Compositional bias | 352-369 | Polar residues | ||||
Sequence: HFSQQNSSKVSSQPKAKE | ||||||
Alternative sequence | VSP_034359 | 504-517 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK131361 EMBL· GenBank· DDBJ | BAD18513.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK131410 EMBL· GenBank· DDBJ | BAD18557.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471094 EMBL· GenBank· DDBJ | EAW96400.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
BC015624 EMBL· GenBank· DDBJ | AAH15624.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC022220 EMBL· GenBank· DDBJ | AAH22220.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB209384 EMBL· GenBank· DDBJ | BAD92621.1 EMBL· GenBank· DDBJ | mRNA |