MTF2_HUMAN
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 03-AUG-2022, entry version 176.
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}.
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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; 115.
DR IntAct; Q9Y483; 44.
DR MINT; Q9Y483; -.
DR STRING; 9606.ENSP00000359321; -.
DR iPTMnet; Q9Y483; -.
DR PhosphoSitePlus; Q9Y483; -.
DR BioMuta; MTF2; -.
DR DMDM; 317373393; -.
DR EPD; Q9Y483; -.
DR jPOST; Q9Y483; -.
DR MassIVE; Q9Y483; -.
DR MaxQB; Q9Y483; -.
DR PaxDb; Q9Y483; -.
DR PeptideAtlas; Q9Y483; -.
DR PRIDE; Q9Y483; -.
DR ProteomicsDB; 3108; -.
DR ProteomicsDB; 86123; -. [Q9Y483-1]
DR ProteomicsDB; 86124; -. [Q9Y483-2]
DR ProteomicsDB; 86125; -. [Q9Y483-3]
DR ABCD; Q9Y483; 1 sequenced antibody.
DR Antibodypedia; 19938; 186 antibodies from 29 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 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; IDRDKHR; -.
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; 17 hits in 1091 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 tissues.
DR ExpressionAtlas; Q9Y483; baseline and differential.
DR Genevisible; Q9Y483; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
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:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; cd04508; TUDOR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040477; KDM4_Tudor_2.
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 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; SSF57903; 2.
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 Reference proteome; Repeat; Ubl conjugation; 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
