ASHH2_ARATH
ID ASHH2_ARATH Reviewed; 1759 AA.
AC Q2LAE1; A9QA57; O80663; Q56WW4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histone-lysine N-methyltransferase ASHH2;
DE EC=2.1.1.-;
DE AltName: Full=ASH1 homolog 2 {ECO:0000303|PubMed:19915673};
DE AltName: Full=H3-K4-HMTase;
DE AltName: Full=Histone H3-K36 methyltransferase 8;
DE Short=H3-K36-HMTase 8;
DE AltName: Full=Protein EARLY FLOWERING IN SHORT DAYS;
DE AltName: Full=Protein LAZARUS 2 {ECO:0000303|PubMed:20949080};
DE AltName: Full=Protein SET DOMAIN GROUP 8;
GN Name=ASHH2 {ECO:0000303|PubMed:19915673};
GN Synonyms=EFS, LAZ2 {ECO:0000303|PubMed:20949080}, SDG8, SET8;
GN OrderedLocusNames=At1g77300; ORFNames=T14N5.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16299497; DOI=10.1038/ncb1329;
RA Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H.;
RT "Prevention of early flowering by expression of FLOWERING LOCUS C requires
RT methylation of histone H3 K36.";
RL Nat. Cell Biol. 7:1256-1260(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1299-1759 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [6]
RP FUNCTION.
RX PubMed=10518493; DOI=10.1242/dev.126.21.4763;
RA Soppe W.J.J., Bentsink L., Koornneef M.;
RT "The early-flowering mutant efs is involved in the autonomous promotion
RT pathway of Arabidopsis thaliana.";
RL Development 126:4763-4770(1999).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16258034; DOI=10.1105/tpc.105.034645;
RA Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R.;
RT "Establishment of the vernalization-responsive, winter-annual habit in
RT Arabidopsis requires a putative histone H3 methyl transferase.";
RL Plant Cell 17:3301-3310(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18070919; DOI=10.1128/mcb.01607-07;
RA Xu L., Zhao Z., Dong A., Soubigou-Taconnat L., Renou J.P., Steinmetz A.,
RA Shen W.H.;
RT "Di- and tri- but not monomethylation on histone H3 lysine 36 marks active
RT transcription of genes involved in flowering time regulation and other
RT processes in Arabidopsis thaliana.";
RL Mol. Cell. Biol. 28:1348-1360(2008).
RN [9]
RP INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
RX PubMed=19121105; DOI=10.1111/j.1365-313x.2008.03776.x;
RA Choi J., Hyun Y., Kang M.J., In Yun H., Yun J.Y., Lister C., Dean C.,
RA Amasino R.M., Noh B., Noh Y.S., Choi Y.;
RT "Resetting and regulation of Flowering Locus C expression during
RT Arabidopsis reproductive development.";
RL Plant J. 57:918-931(2009).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19915673; DOI=10.1371/journal.pone.0007817;
RA Grini P.E., Thorstensen T., Alm V., Vizcay-Barrena G., Windju S.S.,
RA Jorstad T.S., Wilson Z.A., Aalen R.B.;
RT "The ASH1 HOMOLOG 2 (ASHH2) histone H3 methyltransferase is required for
RT ovule and anther development in Arabidopsis.";
RL PLoS ONE 4:E7817-E7817(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH FRI AND SUF4.
RX PubMed=20711170; DOI=10.1038/emboj.2010.198;
RA Ko J.H., Mitina I., Tamada Y., Hyun Y., Choi Y., Amasino R.M., Noh B.,
RA Noh Y.S.;
RT "Growth habit determination by the balance of histone methylation
RT activities in Arabidopsis.";
RL EMBO J. 29:3208-3215(2010).
RN [12]
RP FUNCTION.
RX PubMed=20949080; DOI=10.1371/journal.ppat.1001137;
RA Palma K., Thorgrimsen S., Malinovsky F.G., Fiil B.K., Nielsen H.B.,
RA Brodersen P., Hofius D., Petersen M., Mundy J.;
RT "Autoimmunity in Arabidopsis acd11 is mediated by epigenetic regulation of
RT an immune receptor.";
RL PLoS Pathog. 6:E1001137-E1001137(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE FRI-C COMPLEX
RP AND SWC6.
RX PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL Plant Cell 23:289-303(2011).
RN [14]
RP FUNCTION, INTERACTION WITH BZR2/BES1 AND IWS1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24838002; DOI=10.1093/mp/ssu056;
RA Wang X., Chen J., Xie Z., Liu S., Nolan T., Ye H., Zhang M., Guo H.,
RA Schnable P.S., Li Z., Yin Y.;
RT "Histone lysine methyltransferase SDG8 is involved in brassinosteroid-
RT regulated gene expression in Arabidopsis thaliana.";
RL Mol. Plant 7:1303-1315(2014).
RN [15]
RP STRUCTURE BY NMR OF 849-937 IN COMPLEX WITH ZINC AND METHYLATED H3K4
RP PEPTIDE, AND MUTAGENESIS OF TRP-865; TRP-874; TRP-891; GLN-908 AND GLU-909.
RX PubMed=21522130; DOI=10.1038/emboj.2011.108;
RA Hoppmann V., Thorstensen T., Kristiansen P.E., Veiseth S.V., Rahman M.A.,
RA Finne K., Aalen R.B., Aasland R.;
RT "The CW domain, a new histone recognition module in chromatin proteins.";
RL EMBO J. 30:1939-1952(2011).
CC -!- FUNCTION: Histone methyltransferase involved in di and tri-methylation
CC of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3). Binds to H3 already
CC mono- or di-methylated on 'Lys-4'(H3K4me1 or H3K4me2), but not to
CC H3K4me3. H3K4me and H3K36me represent specific tags for epigenetic
CC transcriptional activation. Regulates positively FLC transcription to
CC prevent early flowering transition. Required for flowering transition
CC in response to vernalization and for the maintenance of FLC expression
CC in late embryos, but dispensable for the initial reactivation in early
CC embryos during reprogramming. Seems also to modulate several traits
CC including floral organ size, root size and dormancy. Promotes apical
CC dominance (PubMed:16299497, PubMed:10518493, PubMed:16258034,
CC PubMed:18070919, PubMed:19915673, PubMed:20711170). Directly involved
CC in the tri-methylation of 'Lys-36' of histone H3 (H3K36me3) at LAZ5
CC chromatin to maintain a transcriptionally active state of LAZ5, a TIR-
CC NB-LRR protein involved in innate immunity (PubMed:20949080). Required
CC for brassinosteroid (BR)-induced gene expression and histone H3
CC trimethylation on 'Lys-36' (H3K36me3) in BR-regulated genes
CC (PubMed:24838002). {ECO:0000269|PubMed:10518493,
CC ECO:0000269|PubMed:16258034, ECO:0000269|PubMed:16299497,
CC ECO:0000269|PubMed:18070919, ECO:0000269|PubMed:19915673,
CC ECO:0000269|PubMed:20711170, ECO:0000269|PubMed:20949080,
CC ECO:0000269|PubMed:24838002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(36)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60316, Rhea:RHEA-COMP:9786, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60320, Rhea:RHEA-
CC COMP:9787, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976;
CC -!- SUBUNIT: Interacts with FRI and SUF4, two components of the
CC transcription activator complex FRI-C, and with SWC6, a component of
CC the SWR1 chromatin-remodeling complex (PubMed:20711170,
CC PubMed:21282526, PubMed:21522130). Interacts with BZR2/BES1 and IWS1
CC (PubMed:24838002). {ECO:0000269|PubMed:20711170,
CC ECO:0000269|PubMed:21282526, ECO:0000269|PubMed:21522130,
CC ECO:0000269|PubMed:24838002}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18070919,
CC ECO:0000269|PubMed:24838002}. Chromosome, centromere
CC {ECO:0000305|PubMed:18070919}. Note=Associates with centromeric
CC constitutive heterochromatin. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2LAE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2LAE1-2; Sequence=VSP_018133;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in young tissues,
CC including shoot and root apex. Expressed in ovules, tapetum layer and
CC microspores. {ECO:0000269|PubMed:16258034, ECO:0000269|PubMed:16299497,
CC ECO:0000269|PubMed:19121105, ECO:0000269|PubMed:19915673}.
CC -!- INDUCTION: Not regulated by vernalization.
CC {ECO:0000269|PubMed:19121105}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. Pleiotropic developmental
CC effects including dwarf and bushy phenotype, reduced seed setting and
CC defects in ovule and embryo sac development (PubMed:18070919,
CC PubMed:19915673, PubMed:24838002). Altered responses to brassinosteroid
CC (BR) (PubMed:24838002). {ECO:0000269|PubMed:18070919,
CC ECO:0000269|PubMed:19915673, ECO:0000269|PubMed:24838002}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94318.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ340869; ABC69038.1; -; mRNA.
DR EMBL; EU014690; ABV68921.1; -; mRNA.
DR EMBL; AC004260; AAC34358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35960.1; -; Genomic_DNA.
DR EMBL; AK221916; BAD94318.1; ALT_INIT; mRNA.
DR PIR; T00458; T00458.
DR RefSeq; NP_177854.6; NM_106379.9. [Q2LAE1-2]
DR PDB; 2L7P; NMR; -; A=849-937.
DR PDB; 5YVX; X-ray; 1.59 A; A=862-921.
DR PDB; 6QXZ; NMR; -; A=861-928.
DR PDBsum; 2L7P; -.
DR PDBsum; 5YVX; -.
DR PDBsum; 6QXZ; -.
DR AlphaFoldDB; Q2LAE1; -.
DR BMRB; Q2LAE1; -.
DR SMR; Q2LAE1; -.
DR BioGRID; 29285; 15.
DR IntAct; Q2LAE1; 2.
DR MINT; Q2LAE1; -.
DR STRING; 3702.AT1G77300.1; -.
DR iPTMnet; Q2LAE1; -.
DR PaxDb; Q2LAE1; -.
DR PeptideAtlas; Q2LAE1; -.
DR PRIDE; Q2LAE1; -.
DR ProteomicsDB; 246681; -. [Q2LAE1-1]
DR EnsemblPlants; AT1G77300.1; AT1G77300.1; AT1G77300. [Q2LAE1-2]
DR GeneID; 844066; -.
DR Gramene; AT1G77300.1; AT1G77300.1; AT1G77300. [Q2LAE1-2]
DR KEGG; ath:AT1G77300; -.
DR Araport; AT1G77300; -.
DR TAIR; locus:2196000; AT1G77300.
DR eggNOG; KOG4442; Eukaryota.
DR InParanoid; Q2LAE1; -.
DR OMA; HQFGSPG; -.
DR OrthoDB; 45878at2759; -.
DR PhylomeDB; Q2LAE1; -.
DR BRENDA; 2.1.1.359; 399.
DR PRO; PR:Q2LAE1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2LAE1; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:TAIR.
DR GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048653; P:anther development; IMP:TAIR.
DR GO; GO:0016116; P:carotenoid metabolic process; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0010452; P:histone H3-K36 methylation; IDA:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0031062; P:positive regulation of histone methylation; IDA:TAIR.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR GO; GO:0010363; P:regulation of plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0043067; P:regulation of programmed cell death; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0090548; P:response to nitrate starvation; IMP:TAIR.
DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR CDD; cd19172; SET_SETD2; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Centromere; Chromatin regulator;
KW Chromosome; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1759
FT /note="Histone-lysine N-methyltransferase ASHH2"
FT /id="PRO_0000233371"
FT DOMAIN 974..1024
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1026..1143
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1151..1167
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 859..912
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 154..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:21522130"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:21522130"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:21522130"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:21522130"
FT BINDING 1142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT VAR_SEQ 1447
FT /note="G -> GLQMLHNIMKQYRGDFKRIPIIRKLLKVLEYLATRKILALEHIIRRP
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_018133"
FT MUTAGEN 865
FT /note="W->A: Loss of histone tail binding."
FT /evidence="ECO:0000269|PubMed:21522130"
FT MUTAGEN 874
FT /note="W->A: Loss of histone tail binding."
FT /evidence="ECO:0000269|PubMed:21522130"
FT MUTAGEN 891
FT /note="W->A: Loss of histone tail binding."
FT /evidence="ECO:0000269|PubMed:21522130"
FT MUTAGEN 908
FT /note="Q->A: Loss of histone tail binding."
FT /evidence="ECO:0000269|PubMed:21522130"
FT MUTAGEN 909
FT /note="E->A: Loss of histone tail binding."
FT /evidence="ECO:0000269|PubMed:21522130"
FT CONFLICT 1426
FT /note="I -> T (in Ref. 4; BAD94318)"
FT /evidence="ECO:0000305"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:5YVX"
FT TURN 869..871
FT /evidence="ECO:0007829|PDB:5YVX"
FT STRAND 874..878
FT /evidence="ECO:0007829|PDB:5YVX"
FT HELIX 879..882
FT /evidence="ECO:0007829|PDB:5YVX"
FT HELIX 893..895
FT /evidence="ECO:0007829|PDB:5YVX"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:2L7P"
FT HELIX 912..919
FT /evidence="ECO:0007829|PDB:5YVX"
FT TURN 923..926
FT /evidence="ECO:0007829|PDB:6QXZ"
SQ SEQUENCE 1759 AA; 193228 MW; 5616BE25ECEF2155 CRC64;
MDCKENGVGD ASGCNIDANS LASNLAMNTN EDFYEKLSSR GQNLDSVSSL EIPQTASSVN
HTIEGQRKCF TEIEQMGYGN SNSQEDAGNT DDDLYVCYNA DDTQEQGVVS GELEQSQELI
CDTDLLVNCN KLDDGKESQD TNVSLVSIFS GSMQEKEAPQ AKEDEGYGGT TLPIGGSGID
TESTFVNDAP EQFESLETTK HIKPDEVESD GISYRFDDGG KEGRNGPSSD LDTGSSDDIS
LSQSFSFPDS LLDSSVFGCS ATESYLEDAI DIEGNGTIVV SPSLAITEML NNDDGGLCSH
DLNKITVTET INPDLKLVRE DRLDTDLSVM NEKMLKNHVG DSSSESAVAA LSMNNGMAAD
LRAENFSQSS PIDEKTLDME ANSPITDSSL IWNFPLNFGS GGIEVCNPEN AVEPLRIVDD
NGRIGGEVAS ASGSDFCEAG MSSSRRKARD GKQCKVVQTK TSARHLRKSS RKKQSERDIE
SIFKCSKQKR SSLLKTSRSS EWGLPSKTTE IFLQSNNIPY DGPPHHEPQR SQGNLNNGEH
NRSSHNGNVE GSNRNIQASS GSCLRLKVKF GKSGGQNPLN ITVSKVSGNS LPGNGIVKAG
TCLELPGSAH FGEDKMQTVE TKEDLVEKSN PVEKVSYLQS SDSMRDKKYN QDAGGLCRKV
GGDVLDDDPH LSSIRMVEEC ERATGTQSLD AETSPDSEVI NSVPDSIVNI EHKEGLHHGF
FSTPEDVVKK NRVLEKEDEL RASKSPSENG SHLIPNAKKA KHPKSKSNGT KKGKSKFSES
AKDGRKNESH EGVEQRKSLN TSMGRDDSDY PEVGRIESHK TTGALLDADI GKTSATYGTI
SSDVTHGEMV VDVTIEDSYS TESAWVRCDD CFKWRRIPAS VVGSIDESSR WICMNNSDKR
FADCSKSQEM SNEEINEELG IGQDEADAYD CDAAKRGKEK EQKSKRLTGK QKACFKAIKT
NQFLHRNRKS QTIDEIMVCH CKPSPDGRLG CGEECLNRML NIECLQGTCP AGDLCSNQQF
QKRKYVKFER FQSGKKGYGL RLLEDVREGQ FLIEYVGEVL DMQSYETRQK EYAFKGQKHF
YFMTLNGNEV IDAGAKGNLG RFINHSCEPN CRTEKWMVNG EICVGIFSMQ DLKKGQELTF
DYNYVRVFGA AAKKCYCGSS HCRGYIGGDP LNGDVIIQSD SDEEYPELVI LDDDESGEGI
LGATSRTFTD DADEQMPQSF EKVNGYKDLA PDNTQTQSSV SVKLPEREIP PPLLQPTEVL
KELSSGISIT AVQQEVPAEK KTKSTSPTSS SLSRMSPGGT NSDKTTKHGS GEDKKILPRP
RPRMKTSRSS ESSKRDKGGI YPGVNKAQVI PVNKLQQQPI KSKGSEKVSP SIETFEGKLN
ELLDAVGGIS KRRDSAKGYL KLLLLTAASR GTDEEGIYSN RDLSMILDAL LKTKSKSVLV
DIINKNGPFA GMESFKDSVL SFTEHDDYTV HNIARSFRDR WIPKHFRKPW RINREERSES
MRSPINRRFR ASQEPRYDHQ SPRPAEPAAS VTSSKAATPE TASVSEGYSE PNSGLPETNG
RKRKSRWDQP SKTKEQRIMT ILSQQTDETN GNQDVQDDLP PGFSSPCTDV PDAITAQPQQ
KFLSRLPVSY GIPLSIVHQF GSPGKEDPTT WSVAPGMPFY PFPPLPPVSH GEFFAKRNVR
ACSSSMGNLT YSNEILPATP VTDSTAPTRK RELFSSDIGT TYFRQQKQSV PPWLRNNGGE
KTANSPIPGN LTLEKKLNS
