AEBP2_MOUSE
ID AEBP2_MOUSE Reviewed; 504 AA.
AC Q9Z248; Q6PF91; Q78HB0; Q8BGV1; Q8CE51;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 164-503 (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Dendritic cell, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 50-504 (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 178-504 (ISOFORM 1), FUNCTION, DNA-BINDING,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF 315-HIS-SER-316.
RC STRAIN=Swiss albino;
RX PubMed=10329662; DOI=10.1074/jbc.274.21.14678;
RA He G.-P., Kim S., Ro H.-S.;
RT "Cloning and characterization of a novel zinc finger transcriptional
RT repressor. A direct role of the zinc finger motif in repression.";
RL J. Biol. Chem. 274:14678-14684(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION IN THE PRC2/EZH1 COMPLEX.
RX PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA Orkin S.H.;
RT "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in
RT maintaining stem cell identity and executing pluripotency.";
RL Mol. Cell 32:491-502(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-199 AND
RP SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE PRC2 COMPLEX.
RX PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA Krogan N.J., Reiter J.F., Stanford W.L.;
RT "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT networks during mouse embryonic stem cell self-renewal and
RT differentiation.";
RL Cell Stem Cell 6:153-166(2010).
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:0000269|PubMed:20144788,
CC ECO:0000305|PubMed:10329662}.
CC -!- SUBUNIT: Self-associates (By similarity). 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:19026780,
CC PubMed:20144788). Found in a monomeric PRC2.2 (class 2) complex
CC consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 (By similarity).
CC Within the PRC2 complex, interacts directly with SUZ12; competes with
CC PHF19 for SUZ12 binding (By similarity). Interacts with EED, EZH2, and
CC RBBP4 (By similarity). May also interact with RBBP7 (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZN18, ECO:0000269|PubMed:19026780,
CC ECO:0000269|PubMed:20144788}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Z248-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z248-2; Sequence=VSP_034362;
CC Name=3;
CC IsoId=Q9Z248-3; Sequence=VSP_034360, VSP_034363;
CC Name=4;
CC IsoId=Q9Z248-4; Sequence=VSP_034360, VSP_034362;
CC Name=5;
CC IsoId=Q9Z248-5; Sequence=VSP_034361, VSP_034362;
CC -!- TISSUE SPECIFICITY: Expressed in brain, brown adipose tissue, white
CC adipose tissue, heart, kidney, lung, skeletal muscle, small intestine
CC and spleen. Expressed at low levels in liver.
CC {ECO:0000269|PubMed:10329662}.
CC -!- SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD02854.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC32508.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC32562.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK029011; BAC26241.1; -; mRNA.
DR EMBL; AK045838; BAC32508.1; ALT_SEQ; mRNA.
DR EMBL; AK045987; BAC32562.1; ALT_SEQ; mRNA.
DR EMBL; AK155272; BAE33156.1; -; mRNA.
DR EMBL; BC031376; AAH31376.1; -; mRNA.
DR EMBL; BC057681; AAH57681.1; -; mRNA.
DR EMBL; AF090326; AAD02854.1; ALT_FRAME; mRNA.
DR CCDS; CCDS20673.1; -. [Q9Z248-2]
DR CCDS; CCDS20674.1; -. [Q9Z248-4]
DR CCDS; CCDS39689.2; -. [Q9Z248-1]
DR CCDS; CCDS80631.1; -. [Q9Z248-3]
DR RefSeq; NP_001005605.1; NM_001005605.2. [Q9Z248-2]
DR RefSeq; NP_001296365.1; NM_001309436.1. [Q9Z248-3]
DR RefSeq; NP_001296366.1; NM_001309437.1. [Q9Z248-3]
DR RefSeq; NP_033767.2; NM_009637.4. [Q9Z248-1]
DR RefSeq; NP_848918.1; NM_178803.2. [Q9Z248-4]
DR RefSeq; XP_006506969.1; XM_006506906.1. [Q9Z248-2]
DR RefSeq; XP_006506972.1; XM_006506909.3. [Q9Z248-3]
DR AlphaFoldDB; Q9Z248; -.
DR SMR; Q9Z248; -.
DR BioGRID; 198014; 6.
DR IntAct; Q9Z248; 5.
DR MINT; Q9Z248; -.
DR STRING; 10090.ENSMUSP00000084896; -.
DR iPTMnet; Q9Z248; -.
DR PhosphoSitePlus; Q9Z248; -.
DR EPD; Q9Z248; -.
DR jPOST; Q9Z248; -.
DR MaxQB; Q9Z248; -.
DR PaxDb; Q9Z248; -.
DR PeptideAtlas; Q9Z248; -.
DR PRIDE; Q9Z248; -.
DR ProteomicsDB; 285729; -. [Q9Z248-1]
DR ProteomicsDB; 285730; -. [Q9Z248-2]
DR ProteomicsDB; 285731; -. [Q9Z248-3]
DR ProteomicsDB; 285732; -. [Q9Z248-4]
DR ProteomicsDB; 285733; -. [Q9Z248-5]
DR Antibodypedia; 23931; 229 antibodies from 26 providers.
DR DNASU; 11569; -.
DR Ensembl; ENSMUST00000032359; ENSMUSP00000032359; ENSMUSG00000030232. [Q9Z248-4]
DR Ensembl; ENSMUST00000087614; ENSMUSP00000084896; ENSMUSG00000030232. [Q9Z248-2]
DR Ensembl; ENSMUST00000095350; ENSMUSP00000092993; ENSMUSG00000030232. [Q9Z248-1]
DR Ensembl; ENSMUST00000160836; ENSMUSP00000124148; ENSMUSG00000030232. [Q9Z248-3]
DR Ensembl; ENSMUST00000161335; ENSMUSP00000125479; ENSMUSG00000030232. [Q9Z248-3]
DR GeneID; 11569; -.
DR KEGG; mmu:11569; -.
DR UCSC; uc009eoi.1; mouse. [Q9Z248-1]
DR UCSC; uc009eol.1; mouse. [Q9Z248-3]
DR CTD; 121536; -.
DR MGI; MGI:1338038; Aebp2.
DR VEuPathDB; HostDB:ENSMUSG00000030232; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00510000048519; -.
DR HOGENOM; CLU_029789_0_0_1; -.
DR InParanoid; Q9Z248; -.
DR OMA; LEHATTI; -.
DR OrthoDB; 959457at2759; -.
DR PhylomeDB; Q9Z248; -.
DR TreeFam; TF328864; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 11569; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Aebp2; mouse.
DR PRO; PR:Q9Z248; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z248; protein.
DR Bgee; ENSMUSG00000030232; Expressed in metanephric cortical collecting duct and 251 other tissues.
DR ExpressionAtlas; Q9Z248; baseline and differential.
DR Genevisible; Q9Z248; MM.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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 Acetylation; Alternative splicing; Chromatin regulator; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT CHAIN 2..504
FT /note="Zinc finger protein AEBP2"
FT /id="PRO_0000341591"
FT ZN_FING 254..279
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..345
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..287
FT /note="Interaction with RBBP4"
FT /evidence="ECO:0000250"
FT REGION 345..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..471
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT REGION 488..504
FT /note="Important for nucleosome binding activity of the
FT PRC2 complex"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
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 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN18"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 203
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 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034360"
FT VAR_SEQ 116..197
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034361"
FT VAR_SEQ 497..504
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034362"
FT VAR_SEQ 497..504
FT /note="FDILNFPR -> TLIRKMFNLYLSKQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034363"
FT MUTAGEN 315..316
FT /note="HS->R: Abrogates transcriptional repression but does
FT not affect DNA-binding."
FT /evidence="ECO:0000269|PubMed:10329662"
FT CONFLICT 95
FT /note="D -> E (in Ref. 2; AAH31376)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> T (in Ref. 3; AAD02854)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="D -> Y (in Ref. 1; BAC26241)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="S -> F (in Ref. 1; BAC26241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 52963 MW; B08BF191E9C4A289 CRC64;
MAAALADMAD LEELSRLSPL SPGSPGPAAR GRAEPPEEEE EEDDEEAEAE AVAALLLNGG
AGGGAGGGEA ETMSEPSPES ASQAGGDEDE DEEDDEDEGS SSGGAEEESS AESLVGSSSG
GCSGDETRSL SPGAASSSSG DGDGKEGLEE PKGPRGGPGG PGSSGGGSSS SSVVSSGGDE
GYGTGGGGSS ATSGGRRGSL EMSSDGEPLS RMDSEDSISS TLMDIDSTIS SGRSTPAMMN
GQGSTTASSK HIAYNCCWDQ CQACFNSSPD LADHIRSIHV DGQRGGVFVC LWKGCKVYNT
PSTSQSWLQR HMLTHSGDKP FKCVVGGCNA SFASQGGLAR HVPTHFSQQN SSKVSSQPKA
KEESPSKAGM NKRRKLKNKR RRSLPRPHDF FDAQTLDAIR HRAICFNLSA HIESLGKGHS
VVFHSTVIAK RKEESGKIKL LLHWMPEDIL PDVWVNESER HQLKTKVVHL SKLPKDTALL
LDPNIYRTMP QKRLKRFDIL NFPR
