AEBP2_BOVIN
ID AEBP2_BOVIN Reviewed; 511 AA.
AC A4FV57;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zinc finger protein AEBP2;
DE AltName: Full=Adipocyte enhancer-binding protein 2;
DE Short=AE-binding protein 2;
GN Name=AEBP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-511.
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an accessory subunit for the core Polycomb repressive
CC complex 2 (PRC2), which mediates histone H3K27 (H3K27me3)
CC trimethylation on chromatin leading to transcriptional repression of
CC the affected target gene. Plays a role in nucleosome localization of
CC the PRC2 complex. {ECO:0000250|UniProtKB:Q6ZN18}.
CC -!- SUBUNIT: Self-associates. Associates with the PRC2 complex, which
CC consists of the core components EED, EZH1 or EZH2, SUZ12, and RBBP4,
CC and various combinations of accessory subunits including AEBP2, JARID2,
CC PHF19, MTF2 and EPOP. Found in a monomeric PRC2.2 (class 2) complex
CC consisting of at least SUZ12, RBBP4, AEBP2 and JARID2. Within the PRC2
CC complex, interacts directly with SUZ12; competes with PHF19 for SUZ12
CC binding. Interacts with EED, EZH2, and RBBP4. May also interact with
CC RBBP7. {ECO:0000250|UniProtKB:Q6ZN18}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6ZN18}.
CC Note=Localizes to chromatin as part of the PRC2 complex.
CC {ECO:0000250|UniProtKB:Q6ZN18}.
CC -!- SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI23768.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFC03004480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03026658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC123767; AAI23768.1; ALT_INIT; mRNA.
DR RefSeq; NP_001076954.2; NM_001083485.2.
DR AlphaFoldDB; A4FV57; -.
DR SMR; A4FV57; -.
DR STRING; 9913.ENSBTAP00000034344; -.
DR PaxDb; A4FV57; -.
DR PRIDE; A4FV57; -.
DR Ensembl; ENSBTAT00000034452; ENSBTAP00000034344; ENSBTAG00000010818.
DR GeneID; 537791; -.
DR KEGG; bta:537791; -.
DR CTD; 121536; -.
DR VEuPathDB; HostDB:ENSBTAG00000010818; -.
DR VGNC; VGNC:25704; AEBP2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00510000048519; -.
DR HOGENOM; CLU_029789_1_0_1; -.
DR InParanoid; A4FV57; -.
DR OMA; LEHATTI; -.
DR OrthoDB; 959457at2759; -.
DR TreeFam; TF328864; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000010818; Expressed in rumen epithelium and 105 other tissues.
DR ExpressionAtlas; A4FV57; baseline and differential.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT CHAIN 2..511
FT /note="Zinc finger protein AEBP2"
FT /id="PRO_0000341589"
FT ZN_FING 255..280
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..346
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..288
FT /note="Interaction with RBBP4"
FT /evidence="ECO:0000250"
FT REGION 346..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..472
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT REGION 489..511
FT /note="Important for nucleosome binding activity of the
FT PRC2 complex"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT COMPBIAS 36..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
SQ SEQUENCE 511 AA; 54049 MW; DD20C9A5678B946A CRC64;
MAAALTDMAD LEELSRLSPL PPGSPGPAAR GRAEPPEEEE EEDEEEEAEA EAVAALLLNG
GGGGGGVGGG EAETMSEPSP ESASQAGEDD DEEEDDDEEE EDESSSGGGE EESSAESLVG
SSSGGSSSDE TRSLSPGAAS SSSGDGDGKE GLEEPKGPRG SQGGGGGGSS SSSVVSSGGD
EGYGTGGGGS SATSGGRRGS LEMSSDGEPL SRMDSEDSIS STIMDVDSTI SSGRSTPAMM
NGQGSTTSSS KNIAYNCCWD QCQACFTSSP DLADHIRSIH VDGQRGGVFV CLWKGCKVYN
TPSTSQSWLQ RHMLTHSGDK PFKCVVGGCN ASFASQGGLA RHVPTHFSQQ NSSKVSSQPK
AKEESPSKAG MNKRRKLKNK RRRSLPRPHD FFDAQTLDAI RHRAICFNLS AHIESLGKGH
SVVFHSTVIA KRKEDSGKIK LLLHWMPEDI LPDVWVNESE RHQLKTKVVH LSKLPKDTAL
LLDPNIYRTM PQKRLKRTLI RKVFNLYLSK Q
