ID MTF2_HUMAN Reviewed; 593 AA. AC Q9Y483; A6NGQ9; A8K2Q3; B1AKT5; B1AKT6; Q96G26; Q9UES9; Q9UP40; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-NOV-2024, entry version 188. DE RecName: Full=Metal-response element-binding transcription factor 2; DE AltName: Full=Metal regulatory transcription factor 2; DE AltName: Full=Metal-response element DNA-binding protein M96; DE AltName: Full=Polycomb-like protein 2; DE Short=hPCl2; GN Name=MTF2; Synonyms=PCL2; 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 [MRNA] (ISOFORMS 2 AND 3). RA Tao B., Wang J., Yuan J., Qiang B.; RT "Isolation and cloning of a novel human M96 cDNA, spliced isoforms."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Holen T., Aasland R.; RT "The polycomblike protein family."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Tongue; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Pre-B cell; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY RP 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 [7] RP FUNCTION, AND H3K36ME3-BINDING. RX PubMed=23142980; DOI=10.1038/nsmb.2435; RA Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E., RA Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A., RA Yasui A., Cote J., Kutateladze T.G.; RT "Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1."; RL Nat. Struct. Mol. Biol. 19:1266-1272(2012). RN [8] RP FUNCTION, AND H3K36ME3-BINDING. RX PubMed=23228662; DOI=10.1016/j.bbrc.2012.11.116; RA Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.; RT "Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to RT histone H3K36me3."; RL Biochem. Biophys. Res. Commun. 430:547-553(2013). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-360 AND LYS-522, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [11] {ECO:0000305} RP FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF 338-LYS-LYS-339 AND 544-GLN--GLY-557. 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). CC -!- FUNCTION: Polycomb group (PcG) protein that specifically binds histone CC H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, CC thus enhancing PRC2 H3K27me3 methylation activity (PubMed:23142980, CC PubMed:23228662, PubMed:31959557). Regulates the transcriptional CC networks during embryonic stem cell self-renewal and differentiation CC (By similarity). Promotes recruitment of the PRC2 complex to the CC inactive X chromosome in differentiating XX ES cells and PRC2 CC recruitment to target genes in undifferentiated ES cells (By CC similarity). Required to repress Hox genes by enhancing H3K27me3 CC methylation of the PRC2 complex (By similarity). In some conditions may CC act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene CC and promote cellular senescence by suppressing the catalytic activity CC of the PRC2 complex locally (By similarity). Binds to the metal- CC regulating-element (MRE) of MT1A gene promoter (By similarity). CC {ECO:0000250|UniProtKB:Q02395, ECO:0000269|PubMed:23142980, CC ECO:0000269|PubMed:23228662, ECO:0000269|PubMed:31959557}. CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2 CC and EPOP (PubMed:31959557). Forms a dimeric PRC2.1 (class 1, PRC-PCL) CC complex consisting of at least SUZ12, RBBP4, and PHF19 or MTF2; PHF19 CC and MTF2 stabilize the dimeric structure which enhances PRC2 CC interaction with chromatin (PubMed:31959557). CC {ECO:0000269|PubMed:31959557}. CC -!- INTERACTION: CC Q9Y483-4; P54252: ATXN3; NbExp=3; IntAct=EBI-10698053, EBI-946046; CC Q9Y483-4; P55273: CDKN2D; NbExp=3; IntAct=EBI-10698053, EBI-745859; CC Q9Y483-4; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-10698053, EBI-715104; CC Q9Y483-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10698053, EBI-10976677; CC Q9Y483-4; P14136: GFAP; NbExp=3; IntAct=EBI-10698053, EBI-744302; CC Q9Y483-4; Q53GS7: GLE1; NbExp=3; IntAct=EBI-10698053, EBI-1955541; CC Q9Y483-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-10698053, EBI-1055254; CC Q9Y483-4; O60260-5: PRKN; NbExp=3; IntAct=EBI-10698053, EBI-21251460; CC Q9Y483-4; P37840: SNCA; NbExp=3; IntAct=EBI-10698053, EBI-985879; CC Q9Y483-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10698053, EBI-5235340; CC Q9Y483-4; Q13148: TARDBP; NbExp=3; IntAct=EBI-10698053, EBI-372899; CC Q9Y483-4; Q96BH6; NbExp=3; IntAct=EBI-10698053, EBI-25872486; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31959557}. CC Note=Localizes to chromatin as part of the PRC2 complex. CC {ECO:0000269|PubMed:31959557}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9Y483-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y483-2; Sequence=VSP_004696; CC Name=3; CC IsoId=Q9Y483-3; Sequence=VSP_040329; CC Name=4; CC IsoId=Q9Y483-4; Sequence=VSP_053348; CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3 CC (PubMed:23142980, PubMed:23228662). {ECO:0000269|PubMed:23142980, CC ECO:0000269|PubMed:23228662}. CC -!- SIMILARITY: Belongs to the Polycomblike family. {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; AF072814; AAC27618.1; -; mRNA. DR EMBL; AF073293; AAC27080.1; -; mRNA. DR EMBL; AJ010014; CAA08970.1; -; mRNA. DR EMBL; AK290318; BAF83007.1; -; mRNA. DR EMBL; AC093577; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117354; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459519; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010013; AAH10013.1; -; mRNA. DR CCDS; CCDS53340.1; -. [Q9Y483-4] DR CCDS; CCDS53341.1; -. [Q9Y483-3] DR CCDS; CCDS742.1; -. [Q9Y483-1] DR RefSeq; NP_001157863.1; NM_001164391.1. [Q9Y483-3] DR RefSeq; NP_001157864.1; NM_001164392.1. [Q9Y483-4] DR RefSeq; NP_001157865.1; NM_001164393.1. [Q9Y483-3] DR RefSeq; NP_031384.1; NM_007358.3. [Q9Y483-1] DR RefSeq; XP_011539318.1; XM_011541016.1. DR RefSeq; XP_016856165.1; XM_017000676.1. DR PDB; 5XFR; X-ray; 2.25 A; A/B=43-358. DR PDBsum; 5XFR; -. DR AlphaFoldDB; Q9Y483; -. DR SMR; Q9Y483; -. DR BioGRID; 116499; 124. DR ComplexPortal; CPX-2309; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL2-PALI1 variant. DR ComplexPortal; CPX-2310; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL2-PALI1 variant. DR ComplexPortal; CPX-2312; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL2-PALI1 variant. DR ComplexPortal; CPX-2314; Polycomb repressive complex 2.1,EZH2-RBBP7-PCL2-PALI1 variant. DR ComplexPortal; CPX-2318; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL2-EPOP variant. DR ComplexPortal; CPX-2320; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL2-EPOP variant. DR ComplexPortal; CPX-2326; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL2-EPOP variant. DR ComplexPortal; CPX-2327; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL2-EPOP variant. DR IntAct; Q9Y483; 50. DR MINT; Q9Y483; -. DR STRING; 9606.ENSP00000359321; -. DR iPTMnet; Q9Y483; -. DR PhosphoSitePlus; Q9Y483; -. DR SwissPalm; Q9Y483; -. DR BioMuta; MTF2; -. DR DMDM; 317373393; -. DR jPOST; Q9Y483; -. DR MassIVE; Q9Y483; -. DR PaxDb; 9606-ENSP00000359321; -. DR PeptideAtlas; Q9Y483; -. DR ProteomicsDB; 3108; -. DR ProteomicsDB; 86123; -. [Q9Y483-1] DR ProteomicsDB; 86124; -. [Q9Y483-2] DR ProteomicsDB; 86125; -. [Q9Y483-3] DR Pumba; Q9Y483; -. DR ABCD; Q9Y483; 1 sequenced antibody. DR Antibodypedia; 19938; 179 antibodies from 28 providers. DR DNASU; 22823; -. DR Ensembl; ENST00000370298.9; ENSP00000359321.4; ENSG00000143033.18. [Q9Y483-1] DR Ensembl; ENST00000370303.4; ENSP00000359326.4; ENSG00000143033.18. [Q9Y483-4] DR Ensembl; ENST00000540243.5; ENSP00000443295.1; ENSG00000143033.18. [Q9Y483-3] DR Ensembl; ENST00000545708.5; ENSP00000444962.1; ENSG00000143033.18. [Q9Y483-3] DR GeneID; 22823; -. DR KEGG; hsa:22823; -. DR MANE-Select; ENST00000370298.9; ENSP00000359321.4; NM_007358.4; NP_031384.1. DR UCSC; uc009wdj.4; human. [Q9Y483-1] DR UCSC; uc009wdk.4; human. DR AGR; HGNC:29535; -. DR CTD; 22823; -. DR DisGeNET; 22823; -. DR GeneCards; MTF2; -. DR HGNC; HGNC:29535; MTF2. DR HPA; ENSG00000143033; Low tissue specificity. DR MIM; 609882; gene. DR neXtProt; NX_Q9Y483; -. DR OpenTargets; ENSG00000143033; -. DR PharmGKB; PA128394586; -. DR VEuPathDB; HostDB:ENSG00000143033; -. DR eggNOG; KOG4323; Eukaryota. DR GeneTree; ENSGT00950000183180; -. DR InParanoid; Q9Y483; -. DR OMA; QWFHEDC; -. DR OrthoDB; 5483634at2759; -. DR PhylomeDB; Q9Y483; -. DR TreeFam; TF106420; -. DR PathwayCommons; Q9Y483; -. DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA. DR SignaLink; Q9Y483; -. DR BioGRID-ORCS; 22823; 19 hits in 1170 CRISPR screens. DR ChiTaRS; MTF2; human. DR GenomeRNAi; 22823; -. DR Pharos; Q9Y483; Tbio. DR PRO; PR:Q9Y483; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y483; protein. DR Bgee; ENSG00000143033; Expressed in secondary oocyte and 214 other cell types or tissues. DR ExpressionAtlas; Q9Y483; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0040029; P:epigenetic regulation of gene expression; ISS:UniProtKB. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IBA:GO_Central. DR GO; GO:0007379; P:segment specification; ISS:UniProtKB. DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB. DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB. DR CDD; cd15578; PHD1_MTF2; 1. DR CDD; cd15580; PHD2_MTF2; 1. DR CDD; cd20450; Tudor_MTF2; 1. DR FunFam; 2.30.30.140:FF:000014; Metal-response element-binding transcription factor 2; 1. DR FunFam; 3.30.40.10:FF:000126; metal-response element-binding transcription factor 2 isoform X1; 1. DR FunFam; 3.90.980.20:FF:000001; metal-response element-binding transcription factor 2 isoform X1; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.90.980.20; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR040477; KDM4-like_Tudor. DR InterPro; IPR025894; Mtf2_C_dom. DR InterPro; IPR042014; MTF2_PHD1. DR InterPro; IPR042015; MTF2_PHD2. DR InterPro; IPR002999; Tudor. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12628:SF12; METAL-RESPONSE ELEMENT-BINDING TRANSCRIPTION FACTOR 2; 1. DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1. DR Pfam; PF14061; Mtf2_C; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF18104; Tudor_2; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Ubl conjugation; KW Zinc; Zinc-finger. FT CHAIN 1..593 FT /note="Metal-response element-binding transcription factor FT 2" FT /id="PRO_0000059317" FT DOMAIN 44..101 FT /note="Tudor" FT ZN_FING 102..157 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 201..255 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 360..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..401 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..474 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 360 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 522 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..331 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_004696" FT VAR_SEQ 1..102 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_040329" FT VAR_SEQ 331..387 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_053348" FT VARIANT 140 FT /note="S -> C (in dbSNP:rs2815427)" FT /id="VAR_054765" FT MUTAGEN 338..339 FT /note="KK->AA: Abolishes chromatin binding activity of the FT PRC2.1 complex." FT /evidence="ECO:0000269|PubMed:31959557" FT MUTAGEN 544..557 FT /note="Missing: Reduced chromatin binding activity of the FT PRC2.1 complex, probably due to loss of dimer stability." FT /evidence="ECO:0000269|PubMed:31959557" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 61..70 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 71..74 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 140..144 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 170..178 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 204..207 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 266..281 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 288..291 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 292..298 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 307..310 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 313..326 FT /evidence="ECO:0007829|PDB:5XFR" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:5XFR" FT HELIX 334..337 FT /evidence="ECO:0007829|PDB:5XFR" FT STRAND 343..348 FT /evidence="ECO:0007829|PDB:5XFR" SQ SEQUENCE 593 AA; 67090 MW; 4517B5DD61BB1AF4 CRC64; MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKAK KPACKFEEGQ DVLARWSDGL FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEP LLDKESISEN PTLDLPCSIG RTEGTAHSSN TSDVDFTGAS SAKETTSSSI SRHYGLSDSR KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS //