Q6ZN18 · AEBP2_HUMAN

  • Protein
    Zinc finger protein AEBP2
  • Gene
    AEBP2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular ComponentESC/E(Z) complex
Cellular Componentnucleoplasm
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Molecular Functiontranscription coregulator activity
Biological Processchromatin organization
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Zinc finger protein AEBP2
  • Alternative names
    • Adipocyte enhancer-binding protein 2 (AE-binding protein 2)

Gene names

    • Name
      AEBP2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q6ZN18
  • Secondary accessions
    • Q59FS5
    • Q6ZN62
    • Q96BG3

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: Localizes to chromatin as part of the PRC2 complex.

Keywords

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00003415902-517UniProtZinc finger protein AEBP2
Modified residue (large scale data)6PRIDEPhosphothreonine
Modified residue (large scale data)15PRIDEPhosphoserine
Modified residue18UniProtPhosphoserine
Modified residue (large scale data)18PRIDEPhosphoserine
Modified residue24UniProtPhosphoserine
Modified residue (large scale data)24PRIDEPhosphoserine
Modified residue (large scale data)27PRIDEPhosphoserine
Modified residue (large scale data)139PRIDEPhosphoserine
Modified residue141UniProtPhosphoserine
Modified residue (large scale data)141PRIDEPhosphoserine
Modified residue (large scale data)167PRIDEPhosphoserine
Modified residue206UniProtPhosphoserine
Modified residue (large scale data)206PRIDEPhosphoserine
Modified residue210UniProtPhosphoserine
Modified residue (large scale data)210PRIDEPhosphoserine
Modified residue211UniProtPhosphoserine
Modified residue (large scale data)211PRIDEPhosphoserine
Modified residue390UniProtPhosphoserine
Modified residue (large scale data)390PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

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).

Binary interactions

View interactors in UniProtKB
View CPX-2209 in Complex Portal

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Region1-229Disordered
Compositional bias36-52Acidic residues
Compositional bias91-114Acidic residues
Compositional bias115-148Polar residues
Compositional bias170-185Polar residues
Region209-294Interaction with RBBP4
Zinc finger261-286C2H2-type 1
Zinc finger300-322C2H2-type 2; degenerate
Zinc finger328-352C2H2-type 3
Compositional bias352-369Polar residues
Region352-394Disordered
Region407-478Interaction with SUZ12
Region495-517Important for nucleosome binding activity of the PRC2 complex

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

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.

  • Length
    517
  • Mass (Da)
    54,467
  • Last updated
    2008-06-10 v2
  • Checksum
    6C59888ACEE4F9AF
MAAAITDMADLEELSRLSPLPPGSPGSAARGRAEPPEEEEEEEEEEEEAEAEAVAALLLNGGSGGGGGGGGGGVGGGEAETMSEPSPESASQAGEDEDEEEDDEEEEDESSSSGGGEEESSAESLVGSSGGSSSDETRSLSPGAASSSSGDGDGKEGLEEPKGPRGSQGGGGGGSSSSSVVSSGGDEGYGTGGGGSSATSGGRRGSLEMSSDGEPLSRMDSEDSISSTIMDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRTMPQKRLKRTLIRKVFNLYLSKQ

Q6ZN18-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q6ZN18-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YH08H0YH08_HUMANAEBP2130
H7BYT4H7BYT4_HUMANAEBP2140
G5EA50G5EA50_HUMANAEBP2274
F5GZR7F5GZR7_HUMANAEBP2110
A0A669KBL4A0A669KBL4_HUMANAEBP2268
A0A669KBC9A0A669KBC9_HUMANAEBP2257

Sequence caution

The sequence AAH15624.1 differs from that shown. Reason: Erroneous initiation
The sequence AAH22220.1 differs from that shown. Reason: Erroneous initiation
The sequence BAD18513.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.
The sequence EAW96400.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0343571-216in isoform 3
Compositional bias36-52Acidic residues
Compositional bias91-114Acidic residues
Compositional bias115-148Polar residues
Compositional bias170-185Polar residues
Alternative sequenceVSP_034358217-223in isoform 3
Compositional bias352-369Polar residues
Alternative sequenceVSP_034359504-517in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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