KMT2D_MOUSE
ID KMT2D_MOUSE Reviewed; 5588 AA.
AC Q6PDK2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Histone-lysine N-methyltransferase 2D;
DE Short=Lysine N-methyltransferase 2D;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:O14686};
DE AltName: Full=ALL1-related protein;
DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 2;
GN Name=Kmt2d; Synonyms=Mll2, Mll4;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4339-5588.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4789, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; THR-1223; SER-1226;
RP SER-1627; THR-1822; SER-2266; SER-2299; SER-2597; SER-4410 AND SER-4789,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 [6]
RP IDENTIFICATION IN THE MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30;
RP KMT2A; RRBP5 AND WDR5.
RX PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
RA Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
RT "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
RT methylation within bivalent domains.";
RL Cell 144:513-525(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3071, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2492; ARG-2829; ARG-3725 AND
RP ARG-4255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Histone methyltransferase that catalyzes methyl group
CC transfer from S-adenosyl-L-methionine to the epsilon-amino group of
CC 'Lys-4' of histone H3 (H3K4). Part of chromatin remodeling machinery
CC predominantly forms H3K4me1 methylation marks at active chromatin sites
CC where transcription and DNA repair take place. Acts as a coactivator
CC for estrogen receptor by being recruited by ESR1, thereby activating
CC transcription. {ECO:0000250|UniProtKB:O14686}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000250|UniProtKB:O14686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000250|UniProtKB:O14686};
CC -!- SUBUNIT: Component of the MLL2 complex (also named ASCOM complex), at
CC least composed of catalytic subunit KMT2D/MLL2, ASH2L, RBBP5, WDR5,
CC NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin
CC (PubMed:21335234). Forms a core complex with the evolutionary conserved
CC subcomplex WRAD composed of WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits;
CC WRAD differentially stimulates the methyltransferase activity.
CC Interacts with ESR1; interaction is direct. Interacts (via WIN motif)
CC with WDR5 (By similarity). {ECO:0000250|UniProtKB:O14686,
CC ECO:0000269|PubMed:21335234}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14686}.
CC -!- DOMAIN: LXXLL motifs 5 and 6 are essential for the association with
CC ESR1 nuclear receptor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: Human protein KMT2B/MLL4 was first named MLL2 (see AC Q9UMN6).
CC Thus, also mouse Mll4 is often referred to as Mll2 and vice versa in
CC the literature. {ECO:0000305}.
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DR EMBL; AC161165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058659; AAH58659.1; -; mRNA.
DR CCDS; CCDS49725.2; -.
DR SMR; Q6PDK2; -.
DR IntAct; Q6PDK2; 3.
DR STRING; 10090.ENSMUSP00000023741; -.
DR iPTMnet; Q6PDK2; -.
DR PhosphoSitePlus; Q6PDK2; -.
DR EPD; Q6PDK2; -.
DR jPOST; Q6PDK2; -.
DR MaxQB; Q6PDK2; -.
DR PaxDb; Q6PDK2; -.
DR PeptideAtlas; Q6PDK2; -.
DR PRIDE; Q6PDK2; -.
DR ProteomicsDB; 264856; -.
DR Antibodypedia; 25797; 143 antibodies from 32 providers.
DR Ensembl; ENSMUST00000178486; ENSMUSP00000135941; ENSMUSG00000048154.
DR MGI; MGI:2682319; Kmt2d.
DR VEuPathDB; HostDB:ENSMUSG00000048154; -.
DR eggNOG; KOG4443; Eukaryota.
DR GeneTree; ENSGT00940000156707; -.
DR InParanoid; Q6PDK2; -.
DR OMA; MPLPHEG; -.
DR PhylomeDB; Q6PDK2; -.
DR BRENDA; 2.1.1.354; 3474.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR ChiTaRS; Kmt2d; mouse.
DR PRO; PR:Q6PDK2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6PDK2; protein.
DR Bgee; ENSMUSG00000048154; Expressed in animal zygote and 94 other tissues.
DR ExpressionAtlas; Q6PDK2; baseline and differential.
DR Genevisible; Q6PDK2; MM.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:CACAO.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR CDD; cd15695; ePHD1_KMT2D; 1.
DR CDD; cd15698; ePHD2_KMT2D; 1.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 7.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037890; KMT2D.
DR InterPro; IPR041961; KMT2D_ePHD1.
DR InterPro; IPR041964; KMT2D_ePHD2.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45888:SF2; PTHR45888:SF2; 4.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00249; PHD; 7.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00184; RING; 6.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF57903; SSF57903; 5.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51805; EPHD; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 5.
DR PROSITE; PS50016; ZF_PHD_2; 4.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Coiled coil; Isopeptide bond;
KW Metal-binding; Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..5588
FT /note="Histone-lysine N-methyltransferase 2D"
FT /id="PRO_0000401938"
FT REPEAT 442..446
FT /note="1"
FT REPEAT 460..464
FT /note="2"
FT REPEAT 469..473
FT /note="4"
FT REPEAT 477..481
FT /note="5"
FT REPEAT 520..524
FT /note="7"
FT REPEAT 529..533
FT /note="8"
FT REPEAT 538..542
FT /note="9"
FT REPEAT 547..551
FT /note="10"
FT REPEAT 574..578
FT /note="11"
FT REPEAT 583..587
FT /note="12"
FT REPEAT 592..596
FT /note="13"
FT REPEAT 610..614
FT /note="14"
FT REPEAT 637..641
FT /note="15"
FT DOMAIN 5226..5286
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 5287..5372
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 5448..5564
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 5572..5588
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 104..149
FT /note="C2HC pre-PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 170..218
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 226..276
FT /note="PHD-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 229..274
FT /note="RING-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 270..323
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 276..321
FT /note="RING-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 1071..1124
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1121..1171
FT /note="PHD-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1198..1253
FT /note="PHD-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1201..1251
FT /note="RING-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 4829..4874
FT /note="RING-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 5080..5120
FT /note="C2HC pre-PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 5141..5188
FT /note="PHD-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..642
FT /note="15 X 5 AA repeats of S/P-P-P-E/P-E/A"
FT REGION 922..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2095..2641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2655..2806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3069..3104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3129..3193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3271..3326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3460..3496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3593..3617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3633..3661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3678..3704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3760..3780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3808..3827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4053..4249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4290..4452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4553..4596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4664..4716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4729..4778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4877..4908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4956..5031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2627..2665
FT /evidence="ECO:0000255"
FT COILED 2768..2813
FT /evidence="ECO:0000255"
FT COILED 3559..3613
FT /evidence="ECO:0000255"
FT COILED 3712..3747
FT /evidence="ECO:0000255"
FT COILED 3854..3883
FT /evidence="ECO:0000255"
FT COILED 3912..4052
FT /evidence="ECO:0000255"
FT MOTIF 2644..2648
FT /note="LXXLL motif 1"
FT MOTIF 3030..3034
FT /note="LXXLL motif 2"
FT MOTIF 4279..4293
FT /note="LXXLL motif 3"
FT MOTIF 4310..4314
FT /note="LXXLL motif 4"
FT MOTIF 4514..4518
FT /note="LXXLL motif 5"
FT MOTIF 5041..5045
FT /note="LXXLL motif 6"
FT MOTIF 5388..5393
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2144..2164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2165..2184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2399..2434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2471..2490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2527..2554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2606..2635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2687..2707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2739..2806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3271..3290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3460..3475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4066..4097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4127..4150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4158..4187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4199..4234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4290..4313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4320..4334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4360..4378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4388..4404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4435..4452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4565..4596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4671..4685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4878..4892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4960..4981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4993..5007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5013..5031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5502
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 5525..5526
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 5528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 1223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 1822
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 2299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2492
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2829
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 3071
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 3122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 3193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 3430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 3725
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4255
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 4410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT MOD_RES 4789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 4827
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT CROSSLNK 4807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14686"
FT CROSSLNK 4931
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14686"
SQ SEQUENCE 5588 AA; 600245 MW; 37A0E5D319A5F1A6 CRC64;
MDSQKPPAED KDSDPAADGL AAPEKPGATE PDLPILCIGE VSVPGSGGSR PQKPPHDCSR
GPARRCALCN CGEPGLHGQR ELQRFELPSD WPGFPVVPSG GNSGPCEAVL PKEDASQIGF
PEGLTPAHLG EPGGHCWAHH WCAAWSAGVW GQEGPELCGV DKAIFSGISQ RCSHCARFGA
SVPCRSPGCS RLYHFPCATA SGSFLSMKTL QLLCPEHSDG AAHLEEARCA VCEGPGQLCD
LLFCTSCGHH YHGACLDTAL TARKRASWQC PECKVCQSCR KPGNDSKMLV CETCDKGYHT
FCLKPPMEDL PAHSWKCKTC RLCRACGAGS AELNPNSEWF ENYSLCHRCH KAQGSQPVTS
VAEQHPAVCS RLSPPEPGEI PIDAPDALYV ACQGQPKGGH VTSMQPKELA PLQCEAKPLG
RAGTQLEAQL EAPLHEEMPL LPPPEESPLS PPPEESPTSP PPEASRLSPP TEESPLSPPP
ESSPFSPLEG CPPSPALDTP LSPPPEASPL SPPFEESPLS PPPEELPSSP PPEASRLSPP
PEESPMSPPP EESPMSPPPE ASRLFPPFEE SPLSPPPEDS PLSPPPEASR LSPPPEDSPM
SPPPEDSPMS PPPEVSRFLP LPVLSHLSPL PEVSRLSPPP EESPLSPPPE DSPASPPPEA
SRLSPPPEDS PASPPPEASR LSRPREDSPA SPPPEDSLVS LPMEESPLSP LPEELRLCPQ
PEEPYLSPQP EEPRLCPQPE ELPLSPQSEE PCLSPVLVEP GPSSQPEEPH LSPVPQEPHL
SPQPEEPHLS PQPQQLHLSP HSEEPCLSPM PEEPCLSPQP EELNGPPQPA EPPEEPSQSS
APKELSLFSP SGEPPLPPML GEPALSEPGE PPLSPLPEEL PLSLSGEPVL SPQLMPPDPL
PPPLSPIIPA AAPPALSPLG ELEYPFGAKG DSDPESPLAA PILETPISPP PEANCTDPEP
VPPMILPPSP GSPLGPASPI LMERLPPPCS PLLPHSLPPP TPPPSHCSPP ALPLSVPSPL
SPVQKAVDVS DEAELHEMET DKGPEPECPA LEPRATSPLP SPLGDLSCPA PSPAPALDDF
SGLGEDTAPL DGTGQMSGSL AGELKGSPVL LDPEELTPVT PMEVYGPECK QAGQGSPCEE
QEEPGAPMAP MPPTLIKSDI VNEISNLSQG DASASFPGSE PLLGSPDPEG GGSLSMELGV
STDVSPARDE GSLRLCTDSL PETDDSLLCD TGTATSGGKA EGDKGRRRSS PARSRIKQGR
SSSFPGRRRP RGGAAHGGRG RGRARLKSTT SSVETLVADI DSSPSKEEEE EDDDTMQNTV
VLFSNTDKFV LMQDMCVVCG SFGRGAEGHL LACSQCSQCY HPYCVNSKIT KVMLLKGWRC
VECIVCEVCG QASDPSRLLL CDDCDISYHT YCLDPPLLTV PKGGWKCKWC VSCMQCGAAS
PGFHCEWQNS YTHCGPCASL VTCPVCHAPY VEEDLLIQCR HCERWMHAGC ESLFTEDEVE
QAADEGFDCV SCQPYVVKPV VPVAPPELVP VKVKEPEPQF FRFEGVWLTE TGMAVLRNLT
MSPLHKRRQR RGRLGLPGEA GLEGSEPSDA LGPDDKKDGD LDTDDLLKGE GGVEQMECEI
KLEGPASPDV ELGKEETEES KKRKRKPYRP GIGGFMVRQR KSHTRVKRGP AAQAEVLSGD
GQPDEVMPAD LPAEGSVEQS LAEGDEKKKQ QRRARKKSKL EDMFPAYLQA AFFGKDLLDL
SRKALFAVGV GRPGFGLGAS KPRADGGSDR KELMTAMHKG DDGPDVADEE SHGPEGTADL
PGLEDGGVKA SPVPSDPEKP GTPGEGVLSS DLDRIPTEEL PKMESKDLQQ LFKDVLGSER
EQHLGCGTPG LEGGRTSLQR PFLQGGLALG SLPSSSPMDS YPGLCQSPFL DSRERGGFFS
PEPGEPDSPW TGSGGTTPST PTTPTTEGEG DGLSYNQRSL QRWEKDEELG QLSTISPVLY
ANINFPNLKQ DYPDWSSRCK QIMKLWRKVP AADKAPYLQK AKDNRAAHRI SKVQKQAESQ
ISKQAKMGDI ARKTDRPALH LRIPSQPGAL GSPPPAAAPT IFLGSPTTPA GLSTSADGFL
KPPAGTVPGP DSPGELFLKL PPQVPAQVPS QDPFGLAPAY APEPRFSAAP PTYPPYPSPT
GAPAQPPMLG TTTRPGTGQP GEFHTTPPGT PRHQPSTPDP FLKPRCPSLD NLAVPESPGV
AGGKASEPLL SPPPFGESRK SLEVKKEELG ASSPGYGPPN LGCVDSPSAG PHLGGLELKA
PDVFKAPLTP RASQVEPQSP GLGLRAQEPP PAQALAPSPP SHPDVFRSGP YPDPYAQPPL
TPRPQPPPPE SCCAPPPRSL PSDPFSRVPA SPQSQSSSQS PLTPRPLSAE AFCPSPVTPR
FQSPDPYSRP PSRPQSRDPF APLHKPPRPQ PPEVAFKAGP LAHTPLGAGG FPAALPSGPA
GELHAKVPSG QPTNFARSPG TGTFVGTPSP MRFTFPQGVG EPSLKPPVPQ PGLPSPHGIN
SHFGPGPTLG KPQSTNYAVA TGNFHPSGSP LGPNSGPTGE GYGLSPLRPA SVLPPPAPDG
SLPYLTHGAS QRVGITSPVE KREDPGATMS SSSLATPELS SAQDAGISSL SQTELEKQRQ
RQRLRELLIR QQIQRNTLRQ EKETAAAAAG AVGPPGNWGA EPSSPAFEQL SRGQTPFTGS
QDRSSIVGLP ASKLGGPTLG PGAFSSDDRL ARPLPPATPS SMDMNSRQLV GGSQAFYQRT
PYPGSLPLQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLWQ QQQQQQQQQQ QQAAAAAAAT
SMRLAMSARF PSTPGPELGR QALGSPLAGI PTRLPGPAEP VPGPAGPAQF IELRHNVQKG
LGPGVSPFPG QGPPQRPRFY PVSEELHRLA PEGLRGLAVP GLPSQKPSAL PAPELNNSLH
QTPHAKGPAL ASGLELVSRP PSNTELSRPP LALEAGKLPC EDPELDDDFD AHKALEDDEE
LAHLGLGVDV AKGDDELGTL ENLETNDPHL DDLLNGDEFD LLAYTDPELD TGDKKDIFNE
HLRLVESANE KAEREALLRG VEPVSLGPEE RPPPAPDNSE PRLTSVLPEV KPKVEEGGRH
PSPCQFTINT PKVEPAPPAT SLSLGLKPGQ TVMGTRDTRG GVGTGSFPSS GHTAEKGPFG
ATGGTPAHLL NPSSLSGPAA SSLLEKFELE SGALTLPSGH AAAGDELDKM ESSLVASELP
LLIEDLLEHE KKELQKKQQL SAQTVLPAQQ QQQQQQQQQQ QQQQHTLLPT PGPAQALPLP
HEPGPPQQLA LGIGSTRQPG LGQSMVPIQP PAHALQQRLA PSVAMVSNQG HMLSGQQAGQ
TGLVPQQSSQ PVLAQKPMSA MPASMCMKPQ QLAMQQQQLA NSFFPDTDLD KFAAEDIIDP
IAKAKMVALK GIKKVMAQGS IGVAPGMNRQ QVSLLAQRLS GGSGSDLQNH VAPGSGQERN
AGDPAQPRPN PPTFAQGVIN EADQRQYEEW LFHTQQLLQM QLKVLEEQIG VHRKSRKALC
AKQRTAKKAG REFPEADAEK LKLVTEQQSK IQKQLDQVRK QQKEHTNLMA EYRNKQQQQQ
QQQQQQQQQQ HSAVLAVSPS QNPRVLTKLP GQLLPAHGLQ PPQAPPGGQA GGLRLPPGGM
VLPGQSGGPF LNTTLAQQQQ QQHSGVAGSL TGPPGSFFPG NLALRSLGPD SRLLQERQLQ
LQQQRMQLAQ KLQQQQQQQQ QQQQQQHLLG QVAIQQQQGP GVQNQALGPK PQGLLPPSNH
QGLLVQQLSP QQSQGSQGLL GPAQVTVLQQ QQQQQQHSGA LGPQGPHRQV LMTQSRVLSS
PQLAQQGHSL MGHRLLTAQQ QQQQQQQQQQ QQQQQQQQQQ QQQGSMTGLS QLQQGMMSHG
GQPKMSAQAL GSLQQQQQQL QQQQMLQQQQ LQQQQQQLQQ QQQQQQLQQQ QQQQLQLQQQ
QQQQQQHLQH QQQQQQQLQQ QQQLQQQQQQ QLHLQQQLHQ QQQLQLQQQQ MGLLNQNRTL
LSPQQQQQQQ QQQQQQQQQQ QQQQQQQQQV TLGPGLPVKP LQHFSSSGAL GPTLLLTGKE
QNNAETALPS EVTEGPSTHQ GGPPAVGTAP EPMSVEPGEV KPSISGDSQL LLVQSQAQSQ
ATSVQLQPPL RLPGQPQPQV NLLHTAGGGS HGQQLGSGSS SESPAVPHLL AQPSVSLGEQ
PGPMAQNLLG SQQPLGLDRP IQNNTGSQPP KSGPAPQSGQ GPPGAGVMPT VGQLRAQLQG
VLAKNPQLRH LSPQQQQQLQ ALLMQRQLQQ SQAVRQTPPF QEPGTQPSPL QGLLGCQPQP
GGFSVSQTGP LQELGAGSRP QGPPRLPVPQ GALSTGPVLG PAHPTPPPSS PQEPKRPSQL
PSPSAQLTPT HPGTPKPQGP ALELPPGRVS PAAAQLADTF FGKGLGPWDP SDNLTEAQKP
EQSSLVPGHL DQVNGQVVHE PSQLSIKQEP REEPCALGAQ TVKREANGEP AGAPGTSNHL
LLAGSRSEAG HLLLQKLLRA KNVQLGAGRG PEGLRAEING HIDSKLSGLE QKLQGTSSNK
EDAATRKPLP AKPKRVQKTS DRLPSSRKKL RKEDGVRANE ALLKQLKQEL SQLPLTEPTI
TANFSLFAPF GSGCLVSGQS QLRGAFGSGA LHTGPDYYSQ LLTKNNLSNP PTPPSSLPPT
PPPSVQQKMV NGVTPSDELG ERPKDTASAQ DSEGALRDAA EVKSLDLLAA LPTPPHNQTE
DVRMESDEDS DSPDSIVPAS SPESILGEEA PRFPQLGSGR WEQDNRALSP VIPIIPRTGI
PVFPDTKPYG VLDLEVPGKL PATAWEKGKG SEVSVMLTVS AAAAKNLNGV MVAVAELLSM
KIPNSYEVLF PDGPARAGLE PKKGEAEGPG GKEKGLSGKG PDTGPDWLKQ FDAVLPGYTL
KSQLDILSLL KQESPAPEPS IQHSYTYNVS NLDVRQLSAP PPEEPSPPPS PLAPSPASPP
AEPMVELQAE RPAEPPIPSP LPLASSPESA RPKPRARPPE ESEDSRPPRL KKWKGVRWKR
LRLLLTIQKG SGHQEDEREV AEFMEQFGTA LRPSKVPRDN RRCCFCHEEG DGATDGPARL
LNLDLDLWVH LNCALWSTEV YETQGGALMN VEVALHRGLL TKCSLCQRTG ATSSCNRMRC
PNVYHFACAI RAKCMFFKDK TMLCPVHKIK GPCEQELSSF AVFRRVYIER DEVKQIASII
QRGERLHMFR VGGLVFHAIG QLLPHQMADF HSATALYPVG YEATRIYWSL RTNNRRCCYR
CSISENNGRP EFVIKVIEQG LEDLVFTDAS PQAVWNRIIE PVAAMRKEAD MLRLFPEYLK
GEELFGLTVH AVLRIAESLP GVESCQNYLF RYGRHPLMEL PLMINPTGCA RSEPKILTHY
KRPHTLNSTS MSKAYQSTFT GETNTPYSKQ FVHSKSSQYR RLRTEWKNNV YLARSRIQGL
GLYAAKDLEK HTMVIEYIGT IIRNEVANRR EKIYEEQNRG IYMFRINNEH VIDATLTGGP
ARYINHSCAP NCVAEVVTFD KEDKIIIISS RRIPKGEELT YDYQFDFEDD QHKIPCHCGA
WNCRKWMN
