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 27-MAR-2024, entry version 164. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8FYH; EM; 3.40 A; F/L=1-517. DR PDBsum; 5WAI; -. DR PDBsum; 5Y0U; -. DR PDBsum; 5Y1U; -. DR PDBsum; 6C23; -. DR PDBsum; 6C24; -. DR PDBsum; 6WKR; -. DR PDBsum; 7KSO; -. DR PDBsum; 8FYH; -. DR AlphaFoldDB; Q6ZN18; -. DR EMDB; EMD-21707; -. DR EMDB; EMD-23021; -. DR EMDB; EMD-23022; -. DR EMDB; EMD-23103; -. DR EMDB; EMD-29578; -. DR EMDB; EMD-29647; -. DR EMDB; EMD-29656; -. DR EMDB; EMD-7334; -. DR EMDB; EMD-7335; -. DR SMR; Q6ZN18; -. DR BioGRID; 125736; 49. DR ComplexPortal; CPX-2209; Polycomb repressive complex 2.2, EZH2-RBBP4 variant. DR ComplexPortal; CPX-2212; Polycomb repressive complex 2.2, EZH1-RBBP7 variant. DR ComplexPortal; CPX-2213; Polycomb repressive complex 2.2, EZH2-RBBP7 variant. DR ComplexPortal; CPX-2330; Polycomb repressive complex 2.2, EZH1-RBBP4 variant. 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; 9606-ENSP00000381840; -. DR PeptideAtlas; Q6ZN18; -. DR ProteomicsDB; 67961; -. [Q6ZN18-1] DR ProteomicsDB; 67962; -. [Q6ZN18-2] DR ProteomicsDB; 67963; -. [Q6ZN18-3] DR Pumba; Q6ZN18; -. DR Antibodypedia; 23931; 255 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 AGR; HGNC:24051; -. 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; FAENICL; -. DR OrthoDB; 2918982at2759; -. 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; 28 hits in 1168 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 188 other cell types or tissues. DR ExpressionAtlas; Q6ZN18; baseline and differential. 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR46541; ZINC FINGER PROTEIN AEBP2; 1. DR PANTHER; PTHR46541:SF1; ZINC FINGER PROTEIN AEBP2; 1. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. DR Genevisible; Q6ZN18; HS. 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 //