AEBP2_HUMAN
ID AEBP2_HUMAN Reviewed; 517 AA.
AC Q6ZN18; Q59FS5; Q6ZN62; Q96BG3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Teratocarcinoma, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-517 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH EED; EZH2; RBBP4;
RP RBBP7 AND SUZ12.
RX PubMed=12351676; DOI=10.1126/science.1076997;
RA Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
RA Jones R.S., Zhang Y.;
RT "Role of histone H3 lysine 27 methylation in Polycomb-group silencing.";
RL Science 298:1039-1043(2002).
RN [6]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH EED; EZH2; RBBP4 AND
RP SUZ12.
RX PubMed=15225548; DOI=10.1016/j.molcel.2004.06.020;
RA Cao R., Zhang Y.;
RT "SUZ12 is required for both the histone methyltransferase activity and the
RT silencing function of the EED-EZH2 complex.";
RL Mol. Cell 15:57-67(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-210 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-18; SER-24 AND SER-390, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16] {ECO:0000305}
RP FUNCTION, AND ASSOCIATION WITH THE PRC2 COMPLEX.
RX PubMed=31959557; DOI=10.1016/j.molcel.2019.12.019;
RA Chen S., Jiao L., Liu X., Yang X., Liu X.;
RT "A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island
RT Chromatin.";
RL Mol. Cell 77:1265-1278.e7(2020).
RN [17] {ECO:0007744|PDB:5WAI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 407-503 IN COMPLEX WITH SUZ12;
RP RBBP4 AND JARID2, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, INTERACTION
RP WITH SUZ12, AND SUBCELLULAR LOCATION.
RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039;
RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.;
RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for
RT Chromatin Binding.";
RL Mol. Cell 69:840-852.e5(2018).
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 (PubMed:15225548, PubMed:31959557,
CC PubMed:29499137). Plays a role in nucleosome localization of the PRC2
CC complex (PubMed:29499137). {ECO:0000269|PubMed:15225548,
CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}.
CC -!- SUBUNIT: Self-associates (PubMed:15225548). Associates with the PRC2
CC complex, which consists of the core components EED, EZH1 or EZH2,
CC SUZ12, and RBBP4, and various combinations of accessory subunits
CC including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:12351676,
CC PubMed:15225548, PubMed:31959557, PubMed:29499137). Found in a
CC monomeric PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4,
CC AEBP2 and JARID2 (PubMed:29499137). Within the PRC2 complex, interacts
CC directly with SUZ12; competes with PHF19 for SUZ12 binding
CC (PubMed:12351676, PubMed:29499137). Interacts with EED, EZH2, and RBBP4
CC (PubMed:12351676, PubMed:15225548). May also interact with RBBP7
CC (PubMed:12351676). {ECO:0000269|PubMed:12351676,
CC ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:29499137,
CC ECO:0000269|PubMed:31959557}.
CC -!- INTERACTION:
CC Q6ZN18-2; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-10255023, EBI-2549423;
CC Q6ZN18-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10255023, EBI-10171774;
CC Q6ZN18-2; O95751: LDOC1; NbExp=3; IntAct=EBI-10255023, EBI-740738;
CC Q6ZN18-2; Q99750: MDFI; NbExp=3; IntAct=EBI-10255023, EBI-724076;
CC Q6ZN18-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10255023, EBI-79165;
CC Q6ZN18-2; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-10255023, EBI-947459;
CC Q6ZN18-2; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-10255023, EBI-347633;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29499137}.
CC Note=Localizes to chromatin as part of the PRC2 complex.
CC {ECO:0000269|PubMed:29499137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZN18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN18-2; Sequence=VSP_034359;
CC Name=3;
CC IsoId=Q6ZN18-3; Sequence=VSP_034357, VSP_034358;
CC -!- SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH22220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD18513.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW96400.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK131361; BAD18513.1; ALT_SEQ; mRNA.
DR EMBL; AK131410; BAD18557.1; -; mRNA.
DR EMBL; CH471094; EAW96400.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC015624; AAH15624.1; ALT_INIT; mRNA.
DR EMBL; BC022220; AAH22220.1; ALT_INIT; mRNA.
DR EMBL; AB209384; BAD92621.1; -; mRNA.
DR CCDS; CCDS44841.1; -. [Q6ZN18-1]
DR CCDS; CCDS44842.1; -. [Q6ZN18-2]
DR CCDS; CCDS58215.1; -. [Q6ZN18-3]
DR RefSeq; NP_001107648.1; NM_001114176.1. [Q6ZN18-1]
DR RefSeq; NP_001253972.1; NM_001267043.1. [Q6ZN18-3]
DR RefSeq; NP_694939.2; NM_153207.4. [Q6ZN18-2]
DR PDB; 5WAI; X-ray; 2.90 A; C/G=407-503.
DR PDB; 5Y0U; NMR; -; A=258-357.
DR PDB; 5Y1U; X-ray; 2.14 A; C/D=379-390.
DR PDB; 6C23; EM; 3.90 A; P=209-503.
DR PDB; 6C24; EM; 3.50 A; P=209-503.
DR PDB; 6WKR; EM; 3.50 A; P=209-503.
DR PDB; 7KSO; EM; 3.90 A; E=209-503.
DR PDBsum; 5WAI; -.
DR PDBsum; 5Y0U; -.
DR PDBsum; 5Y1U; -.
DR PDBsum; 6C23; -.
DR PDBsum; 6C24; -.
DR PDBsum; 6WKR; -.
DR PDBsum; 7KSO; -.
DR AlphaFoldDB; Q6ZN18; -.
DR SMR; Q6ZN18; -.
DR BioGRID; 125736; 49.
DR CORUM; Q6ZN18; -.
DR DIP; DIP-58581N; -.
DR IntAct; Q6ZN18; 31.
DR MINT; Q6ZN18; -.
DR STRING; 9606.ENSP00000381840; -.
DR BindingDB; Q6ZN18; -.
DR ChEMBL; CHEMBL3137287; -.
DR iPTMnet; Q6ZN18; -.
DR PhosphoSitePlus; Q6ZN18; -.
DR BioMuta; AEBP2; -.
DR DMDM; 190358163; -.
DR EPD; Q6ZN18; -.
DR jPOST; Q6ZN18; -.
DR MassIVE; Q6ZN18; -.
DR MaxQB; Q6ZN18; -.
DR PaxDb; Q6ZN18; -.
DR PeptideAtlas; Q6ZN18; -.
DR PRIDE; Q6ZN18; -.
DR ProteomicsDB; 67961; -. [Q6ZN18-1]
DR ProteomicsDB; 67962; -. [Q6ZN18-2]
DR ProteomicsDB; 67963; -. [Q6ZN18-3]
DR Antibodypedia; 23931; 229 antibodies from 26 providers.
DR DNASU; 121536; -.
DR Ensembl; ENST00000266508.14; ENSP00000266508.9; ENSG00000139154.16. [Q6ZN18-2]
DR Ensembl; ENST00000360995.8; ENSP00000354267.4; ENSG00000139154.16. [Q6ZN18-3]
DR Ensembl; ENST00000398864.7; ENSP00000381840.3; ENSG00000139154.16. [Q6ZN18-1]
DR GeneID; 121536; -.
DR KEGG; hsa:121536; -.
DR MANE-Select; ENST00000266508.14; ENSP00000266508.9; NM_153207.5; NP_694939.2. [Q6ZN18-2]
DR UCSC; uc001ree.3; human. [Q6ZN18-1]
DR CTD; 121536; -.
DR DisGeNET; 121536; -.
DR GeneCards; AEBP2; -.
DR HGNC; HGNC:24051; AEBP2.
DR HPA; ENSG00000139154; Low tissue specificity.
DR MIM; 617934; gene.
DR neXtProt; NX_Q6ZN18; -.
DR OpenTargets; ENSG00000139154; -.
DR PharmGKB; PA134875401; -.
DR VEuPathDB; HostDB:ENSG00000139154; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00510000048519; -.
DR HOGENOM; CLU_029789_1_0_1; -.
DR InParanoid; Q6ZN18; -.
DR OMA; LEHATTI; -.
DR OrthoDB; 959457at2759; -.
DR PhylomeDB; Q6ZN18; -.
DR TreeFam; TF328864; -.
DR PathwayCommons; Q6ZN18; -.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q6ZN18; -.
DR SIGNOR; Q6ZN18; -.
DR BioGRID-ORCS; 121536; 22 hits in 1086 CRISPR screens.
DR ChiTaRS; AEBP2; human.
DR GenomeRNAi; 121536; -.
DR Pharos; Q6ZN18; Tbio.
DR PRO; PR:Q6ZN18; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6ZN18; protein.
DR Bgee; ENSG00000139154; Expressed in calcaneal tendon and 186 other tissues.
DR ExpressionAtlas; Q6ZN18; baseline and differential.
DR Genevisible; Q6ZN18; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT CHAIN 2..517
FT /note="Zinc finger protein AEBP2"
FT /id="PRO_0000341590"
FT ZN_FING 261..286
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..352
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..294
FT /note="Interaction with RBBP4"
FT REGION 352..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..478
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000269|PubMed:29499137"
FT REGION 495..517
FT /note="Important for nucleosome binding activity of the
FT PRC2 complex"
FT /evidence="ECO:0000269|PubMed:29499137"
FT COMPBIAS 36..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034357"
FT VAR_SEQ 217..223
FT /note="SRMDSED -> MYTRRYS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034358"
FT VAR_SEQ 504..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034359"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6WKR"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:6WKR"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:5Y0U"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:5Y0U"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:5Y0U"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:5WAI"
FT TURN 421..426
FT /evidence="ECO:0007829|PDB:5WAI"
FT STRAND 427..443
FT /evidence="ECO:0007829|PDB:5WAI"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:5WAI"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5WAI"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:5WAI"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:5WAI"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:5WAI"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:5WAI"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:5WAI"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:5WAI"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6WKR"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:5WAI"
SQ SEQUENCE 517 AA; 54467 MW; 6C59888ACEE4F9AF CRC64;
MAAAITDMAD LEELSRLSPL PPGSPGSAAR GRAEPPEEEE EEEEEEEEAE AEAVAALLLN
GGSGGGGGGG GGGVGGGEAE TMSEPSPESA SQAGEDEDEE EDDEEEEDES SSSGGGEEES
SAESLVGSSG GSSSDETRSL SPGAASSSSG DGDGKEGLEE PKGPRGSQGG GGGGSSSSSV
VSSGGDEGYG TGGGGSSATS GGRRGSLEMS SDGEPLSRMD SEDSISSTIM DVDSTISSGR
STPAMMNGQG STTSSSKNIA YNCCWDQCQA CFNSSPDLAD HIRSIHVDGQ RGGVFVCLWK
GCKVYNTPST SQSWLQRHML THSGDKPFKC VVGGCNASFA SQGGLARHVP THFSQQNSSK
VSSQPKAKEE SPSKAGMNKR RKLKNKRRRS LPRPHDFFDA QTLDAIRHRA ICFNLSAHIE
SLGKGHSVVF HSTVIAKRKE DSGKIKLLLH WMPEDILPDV WVNESERHQL KTKVVHLSKL
PKDTALLLDP NIYRTMPQKR LKRTLIRKVF NLYLSKQ
