KMT2B_MOUSE
ID KMT2B_MOUSE Reviewed; 2713 AA.
AC O08550; E9QKF4; Q5NU09;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone-lysine N-methyltransferase 2B;
DE Short=Lysine N-methyltransferase 2B;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:Q9UMN6};
DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog;
DE AltName: Full=Trithorax homolog 2;
DE AltName: Full=WW domain-binding protein 7;
DE Short=WBP-7;
GN Name=Kmt2b; Synonyms=Mll2, Trx2, Wbp7;
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 [MRNA].
RA Yoshida K.;
RT "Murine MLL2 gene and its expression.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 379-657.
RX PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA Bedford M.T., Chan D.C., Leder P.;
RT "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT rich ligands.";
RL EMBO J. 16:2376-2383(1997).
RN [4]
RP IDENTIFICATION BY 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-113; SER-114; SER-118;
RP SER-1037; SER-1040; SER-1098; SER-1101; THR-2064 AND SER-2346, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20808952; DOI=10.1371/journal.pbio.1000453;
RA Andreu-Vieyra C.V., Chen R., Agno J.E., Glaser S., Anastassiadis K.,
RA Stewart A.F., Matzuk M.M.;
RT "MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and
RT transcriptional silencing.";
RL PLoS Biol. 8:1657-1680(2010).
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) via a non-processive mechanism. Part of
CC chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2
CC methylation marks at active chromatin sites where transcription and DNA
CC repair take place (By similarity). Likely plays a redundant role with
CC KMT2C in enriching H3K4me1 marks on primed and active enhancer elements
CC (By similarity). Plays a central role in beta-globin locus
CC transcription regulation by being recruited by NFE2 (By similarity).
CC Plays an important role in controlling bulk H3K4me during oocyte growth
CC and preimplantation development (PubMed:20808952). Required during the
CC transcriptionally active period of oocyte growth for the establishment
CC and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global
CC transcriptional silencing that preceeds resumption of meiosis, oocyte
CC survival and normal zygotic genome activation (PubMed:20808952).
CC {ECO:0000250|UniProtKB:Q9UMN6, ECO:0000269|PubMed:20808952}.
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:Q9UMN6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000250|UniProtKB:Q9UMN6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q9UMN6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269;
CC Evidence={ECO:0000250|UniProtKB:Q9UMN6};
CC -!- SUBUNIT: Component of the menin-associated histone methyltransferase
CC complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, DPY30,
CC MEN1; the complex interacts with POLR2A and POLR2B via MEN1 (By
CC similarity). Interacts with NFE2 (By similarity). Interacts with KDM6B
CC (By similarity). Interacts (via WIN motif) with WDR5 (By similarity).
CC Interacts (via MBM motif) with MEN1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UMN6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMN6}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to DNA containing
CC unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
CC {ECO:0000250|UniProtKB:Q9UMN6}.
CC -!- DISRUPTION PHENOTYPE: Females are infertile due to anovulation and
CC follicle loss. Oocytes show reduced H3K4me3 but not H3K4me1, abnormal
CC expression of pro-apoptotic genes and Iap elements (which may
CC contribute to oocyte death and, ultimately, follicle loss) and fail to
CC establish transcriptional repression. {ECO:0000269|PubMed:20808952}.
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: The human ortholog, KMT2B/MLL4, was first named MLL2 (see AC
CC Q9UMN6). Thus, mouse Kmt2b/Mll4 is also often referred to as Mll2 and
CC vice versa in the literature. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53192.1; Type=Miscellaneous discrepancy; Note=Possible contaminating sequence. The N-terminal 3 residues and C-terminal 8 residues do not match the underlying genomic sequence.; Evidence={ECO:0000305};
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DR EMBL; AB182318; BAD81031.1; -; mRNA.
DR EMBL; AC167970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U92455; AAC53192.1; ALT_SEQ; mRNA.
DR CCDS; CCDS21101.1; -.
DR RefSeq; NP_083550.2; NM_029274.2.
DR SMR; O08550; -.
DR BioGRID; 217461; 19.
DR CORUM; O08550; -.
DR IntAct; O08550; 1.
DR MINT; O08550; -.
DR STRING; 10090.ENSMUSP00000103789; -.
DR iPTMnet; O08550; -.
DR PhosphoSitePlus; O08550; -.
DR EPD; O08550; -.
DR jPOST; O08550; -.
DR MaxQB; O08550; -.
DR PaxDb; O08550; -.
DR PRIDE; O08550; -.
DR ProteomicsDB; 264786; -.
DR Antibodypedia; 70148; 191 antibodies from 32 providers.
DR DNASU; 75410; -.
DR Ensembl; ENSMUST00000108154; ENSMUSP00000103789; ENSMUSG00000006307.
DR GeneID; 75410; -.
DR KEGG; mmu:75410; -.
DR UCSC; uc009gfg.1; mouse.
DR CTD; 9757; -.
DR MGI; MGI:109565; Kmt2b.
DR VEuPathDB; HostDB:ENSMUSG00000006307; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000161496; -.
DR InParanoid; O08550; -.
DR TreeFam; TF319820; -.
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 BioGRID-ORCS; 75410; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Kmt2b; mouse.
DR PRO; PR:O08550; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O08550; protein.
DR Bgee; ENSMUSG00000006307; Expressed in secondary oocyte and 225 other tissues.
DR ExpressionAtlas; O08550; baseline and differential.
DR Genevisible; O08550; MM.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IMP:MGI.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
DR GO; GO:0034968; P:histone lysine methylation; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0009994; P:oocyte differentiation; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0030728; P:ovulation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
DR CDD; cd15694; ePHD_KMT2B; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR041959; KMT2B_ePHD.
DR InterPro; IPR016569; MeTrfase_trithorax.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; DNA-binding; Isopeptide bond;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT CHAIN 2..2713
FT /note="Histone-lysine N-methyltransferase 2B"
FT /id="PRO_0000124882"
FT DOMAIN 1733..1789
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 2409..2490
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 2573..2689
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 2697..2713
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DNA_BIND 37..44
FT /note="A.T hook 1"
FT DNA_BIND 110..117
FT /note="A.T hook 2"
FT DNA_BIND 357..365
FT /note="A.T hook 3"
FT ZN_FING 964..1011
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 1207..1258
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1255..1309
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1341..1402
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1584..1624
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1645..1692
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2056..2104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2279..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2382..2408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 17..36
FT /note="Menin-binding motif (MBM)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOTIF 2506..2511
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT COMPBIAS 145..159
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2393..2408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 983
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 986
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 989
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1005
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1010
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 2583
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 2585
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 2627
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 2650..2651
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 2653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 2701
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 2702
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 2703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 2708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1926
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 1932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 2064
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2079
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 2286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT MOD_RES 2346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT CROSSLNK 1142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UMN6"
FT CONFLICT 18
FT /note="G -> V (in Ref. 1; BAD81031)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..27
FT /note="RGS -> LGC (in Ref. 1; BAD81031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2713 AA; 294821 MW; 2AD4343C5C081933 CRC64;
MAAAAGGGSC PGPGSARGRF PGRPRGSGGG GGRGGRGNGA ERVRVALRRG GGAAGPGGAE
PGEDTALLRL LGLRRGLRRL RRLWAGARVQ RGRGRGRGRG WGPNRGCMPE EESSDGESEE
EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPRLADVTP VPPKAPTRKR
GEEGTERMVQ ALTELLRRSQ APQPPRSRAR AREPSTPRRS RGRPPGRPAG PCRKKQQAVV
LAEAAVTIPK PEPPPPVVPV KNKAGSWKCK EGPGPGPGTP KRGGQPGRGG RGGRGRGRGG
LPLMIKFVSK AKKVKMGQLS QELESGQGHG QRGESWQDAP QRKDGDEPER GSCRKKQEQK
LEEEEEEEEK EGEEKEEKDD NEDNNKQEEE EETERAVAEE EAMLAKEKEE AKLPSPPLTP
PVPSPPPPLP PPSTSPPPPA SPLPPPVSPP PPLSPPPYPA PEKQEESPPL VPATCSRKRG
RPPLTPSQRA EREAARSGPE GTLSPTPNPS TTTGSPLEDS PTVVPKSTTF LKNIRQFIMP
VVSARSSRVI KTPRRFMDED PPKPPKVEAS IVRPPVATSP PAPQEPVPVS SPPRVPTPPS
TPVPLPEKRR SILREPTFRW TSLTRELPPP PPAPPPAPSP PPAPATPSRR PLLLRAPQFT
PSEAHLKIYE SVLTPPPLGA LETPEPELPP ADDSPAEPEP RAVGRTNHLS LPRFVPVVTS
PVKVEVPPHG APALSEGQQL QLQQPPQALQ TQLLPQALPP QQPQAQPPPS PQHTPPLEKA
RVASLGSLPL SGVEEKMFSL LKRAKVQLFK IDQQQQQKVA ASMPLSPAVQ TEEAVGTVKQ
TPDRGCVRSE DESMEAKRDR ASGPESPLQG PRIKHVCRHA AVALGQARAM VPEDVPRLSA
LPLRDRQDLA TEDTSSASET ESVPSRSQRE KVESAGPGGD SEPTGSTGAL AHTPRRSLPS
HHGKKMRMAR CGHCRGCLRV QDCGSCVNCL DKPKFGGPNT KKQCCVYRKC DKIEARKMER
LAKKGRTIVK TLLPWDSDES PEASPGPPGP RRGAGAGGSR EEVGATPGPE EQDSLLLQRK
SARRCVKQRP SYDVFEDSDD SEPGGPPAPR RRTPREHELP VLEPEEQSRP RKPTLQPVLQ
LKARRRLDKD ALAPGPFASF PNGWTGKQKS PDGVHRVRVD FKEDCDLENV WLMGGLSVLT
SVPGGPPMVC LLCASKGLHE LVFCQVCCDP FHPFCLEEAE RPSPQHRDTW CCRRCKFCHV
CGRKGRGSKH LLECERCRHA YHPACLGPSY PTRATRRRRH WICSACVRCK SCGATPGKNW
DVEWSGDYSL CPRCTELYEK GNYCPICTRC YEDNDYESKM MQCAQCDHWV HAKCEGLSDE
DYEILSGLPD SVLYTCGPCA GATQPRWREA LSGALQGGLR QVLQGLLSSK VAGPLLLCTQ
CGQDGKQLHP GPCDLQAVGK RFEEGLYKSV HSFMEDVVAI LMRHSEEGET PERRAGSQMK
GLLLKLLESA FCWFDAHDPK YWRRSTRLPN GVLPNAVLPP SLDHVYAQWR QQESETPESG
QPPGDPSAAF QSKDPAAFSH LDDPRQCALC LKYGDADSKE AGRLLYIGQN EWTHVNCAIW
SAEVFEENDG SLKNVHAAVA RGRQMRCELC LKPGATVGCC LSSCLSNFHF MCARASYCIF
QDDKKVFCQK HTDLLDGKEI VTPDGFDVLR RVYVDFEGIN FKRKFLTGLE PDVINVLIGS
IRINSLGTLS DLSDCEGRLF PIGYQCSRLY WSTVDARRRC WYRCRILEYR PWGPREEPVH
LEAAEENQTI VHSPTPSSDT DSLIPGDPVH HSPIQNLDPP LRTDSSNGPP PTPRSFSGAR
IKVPNYSPSR RPLGGVSFGP LPSPGSPSSL THHIPTVGDS DFPAPPRRSR RPSPLATRPP
PSRRTSSPLR TSPQLRVPLS TSVTALTPTS GELAPPDLAP SPLPPSEDLG PDFEDMEVVS
GLSAADLDFA ASLLGTEPFQ EEIVAAGAVG SSQGGPGDSS EEEASPTTHY VHFPVTVVSG
PALAPSSLAG APRIEQLDGV DDGTDSEAEA VQQPRGQGTP PSGPGVGRGG VLGAAGDRAQ
PPEDLPSEIV DFVLKNLGGP GEGAAGPRED SLPSAPPLAN GSQPPQSLST SPADPTRTFA
WLPGAPGVRV LSLGPAPEPP KPATSKIILV NKLGQVFVKM AGEGEPVAPP VKQPPLPPII
PPTAPTSWTL PPGPLLSVLP VVGVGVVRPA PPPPPPPLTL VFSSGPPSPP RQAIRVKRVS
TFSGRSPPVP PPNKTPRLDE DGESLEDAHH VPGISGSGFS RVRMKTPTVR GVLDLNNPGE
QPEEESPGRP QDRCPLLPLA EAPSQALDGS SDLLFESQWH HYSAGEASSS EEEPPSPEDK
ENQVPKRVGP HLRFEISSDD GFSVEAESLE VAWRTLIEKV QEARGHARLR HLSFSGMSGA
RLLGIHHDAV IFLAEQLPGA QRCQHYKFRY HQQGEGQEEP PLNPHGAARA EVYLRKCTFD
MFNFLASQHR VLPEGATCDE EEDEVQLRST RRATSLELPM AMRFRHLKKT SKEAVGVYRS
AIHGRGLFCK RNIDAGEMVI EYSGIVIRSV LTDKREKFYD GKGIGCYMFR MDDFDVVDAT
MHGNAARFIN HSCEPNCFSR VIHVEGQKHI VIFALRRILR GEELTYDYKF PIEDASNKLP
CNCGAKRCRR FLN
