ID   KMT2A_MOUSE             Reviewed;        3966 AA.
AC   P55200; E9QNE7; Q3UEU1; Q3USE7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   02-SEP-2026, entry version 211.
DE   RecName: Full=Histone-lysine N-methyltransferase 2A;
DE            Short=Lysine N-methyltransferase 2A;
DE            EC=2.1.1.364 {ECO:0000250|UniProtKB:Q03164};
DE   AltName: Full=ALL-1;
DE   AltName: Full=Cysteine methyltransferase KMT2A {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q03164};
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 1;
DE   AltName: Full=Zinc finger protein HRX;
DE   Contains:
DE     RecName: Full=MLL cleavage product N320;
DE     AltName: Full=N-terminal cleavage product of 320 kDa;
DE              Short=p320;
DE   Contains:
DE     RecName: Full=MLL cleavage product C180;
DE     AltName: Full=C-terminal cleavage product of 180 kDa;
DE              Short=p180;
GN   Name=Kmt2a; Synonyms=All1, Hrx, Mll, Mll1;
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 [MRNA] OF 101-3966 (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6 X CBA, and C57BL/6J; TISSUE=Lung, and Spleen;
RX   PubMed=8327517; DOI=10.1073/pnas.90.13.6350;
RA   Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T.,
RA   Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M.;
RT   "Analysis of the murine All-1 gene reveals conserved domains with human
RT   ALL-1 and identifies a motif shared with DNA methyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-1053; SER-1839;
RP   THR-1847; SER-2100 AND SER-2560, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [5]
RP   FUNCTION, AND INTERACTION WITH CLOCK AND BMAL1.
RX   PubMed=21113167; DOI=10.1038/nsmb.1961;
RA   Katada S., Sassone-Corsi P.;
RT   "The histone methyltransferase MLL1 permits the oscillation of circadian
RT   gene expression.";
RL   Nat. Struct. Mol. Biol. 17:1414-1421(2010).
RN   [6]
RP   IDENTIFICATION IN MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30; KMT2D;
RP   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-237; LYS-371; LYS-2954 AND
RP   LYS-3459, AND IDENTIFICATION BY MASS 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).
CC   -!- FUNCTION: Histone methyltransferase that plays an essential role in
CC       early development and hematopoiesis (By similarity). Catalytic subunit
CC       of the MLL1/MLL complex, a multiprotein complex that mediates both
CC       methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation
CC       of 'Lys-16' of histone H4 (H4K16ac) (By similarity). Catalyzes methyl
CC       group transfer from S-adenosyl-L-methionine to the epsilon-amino group
CC       of '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). Has weak methyltransferase activity
CC       by itself, and requires other component of the MLL1/MLL complex to
CC       obtain full methyltransferase activity (By similarity). Has no activity
CC       toward histone H3 phosphorylated on 'Thr-3', less activity toward H3
CC       dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward
CC       H3 acetylated on 'Lys-9' (By similarity). Binds to unmethylated CpG
CC       elements in the promoter of target genes and helps maintain them in the
CC       nonmethylated state (By similarity). Required for transcriptional
CC       activation of HOXA9 (By similarity). Promotes PPP1R15A-induced
CC       apoptosis (By similarity). Plays a critical role in the control of
CC       circadian gene expression and is essential for the transcriptional
CC       activation mediated by the CLOCK-BMAL1 heterodimer (PubMed:21113167).
CC       Establishes a permissive chromatin state for circadian transcription by
CC       mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and
CC       this histone modification directs the circadian acetylation at H3K9 and
CC       H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin
CC       (PubMed:21113167). Also has auto-methylation activity on Cys-3879 in
CC       absence of histone H3 substrate (By similarity).
CC       {ECO:0000250|UniProtKB:Q03164, ECO:0000269|PubMed:21113167}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6)-
CC         methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+);
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:Q03164};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC         Evidence={ECO:0000250|UniProtKB:Q03164};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine + H(+); Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540,
CC         Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000250|UniProtKB:Q03164};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269;
CC         Evidence={ECO:0000250|UniProtKB:Q03164};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = S-methyl-L-
CC         cysteinyl-[protein] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:82612;
CC         Evidence={ECO:0000250|UniProtKB:Q03164};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545;
CC         Evidence={ECO:0000250|UniProtKB:Q03164};
CC   -!- SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL cleavage
CC       product C180 (via SET and FYRC domains). Component of some MLL1/MLL
CC       complex, at least composed of the core components KMT2A/MLL1, ASH2L,
CC       HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative
CC       components BACC1, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC       MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A,
CC       RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts
CC       (via WIN motif) with WDR5; the interaction is direct. Interaction with
CC       WDR5 is required for stable interaction with ASH2L and RBBP5, and
CC       thereby also for optimal histone methyltransferase activity. Interacts
CC       with KAT8/MOF; the interaction is direct. Interacts with SBF1 and
CC       PPP1R15A. Interacts with ZNF335 (By similarity). Interacts with CLOCK
CC       and BMAL1 in a circadian manner (PubMed:21113167). Interacts with PPIE;
CC       this results in decreased histone H3 methyltransferase activity.
CC       Interacts with CREBBP (By similarity). Interacts with the WRAD complex
CC       composed of WDR5, RBBP5, ASH2L and DPY30 (By similarity). Interacts
CC       (via MBM motif) with MEN1 (By similarity). Interacts (via IBM motifs)
CC       with PSIP1 (via IBD domain) with moderate affinity whereas the KMT2A-
CC       MEN1 complex interacts with a greater affinity; MEN1 enhances
CC       interaction of KMT2A with PSIP1 (By similarity). Phosphorylation
CC       increases its affinity for PSIP1 (By similarity). Forms a complex with
CC       CREBBP and CREB1 (By similarity). {ECO:0000250|UniProtKB:Q03164,
CC       ECO:0000269|PubMed:21113167, ECO:0000269|PubMed:21335234}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03164}.
CC   -!- SUBCELLULAR LOCATION: [MLL cleavage product N320]: Nucleus
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- SUBCELLULAR LOCATION: [MLL cleavage product C180]: Nucleus
CC       {ECO:0000250|UniProtKB:Q03164}. Note=Localizes to a diffuse nuclear
CC       pattern when not associated with MLL cleavage product N320.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P55200-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55200-2; Sequence=VSP_006667;
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- DOMAIN: The SET domain structure is atypical and is not in an optimal
CC       position to have methyltransferase activity. It requires other
CC       components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order
CC       the active site and obtain optimal histone methyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- DOMAIN: The CXXC-type zinc finger binds to DNA sequence elements
CC       containing unmethylated CpG dinucleotides.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- DOMAIN: The third PHD-type zinc-finger binds both trimethylated histone
CC       H3K4me3 and PPIE; histone and PPIE bind to distinct surfaces.
CC       Nevertheless, PPIE binding and histone binding are mutually inhibitory.
CC       Isomerization of a peptidylproline bond in the linker between the third
CC       PHD-type zinc-finger and the bromo domain disrupts the interaction
CC       between the bromo domain and the third PHD-type zinc-finger, and
CC       thereby facilitates interaction with PPIE.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- PTM: Proteolytic cleavage by TASP1 generates MLL cleavage 3product N320
CC       and MLL cleavage product C180, which reassemble through a non-covalent
CC       association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage
CC       site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is
CC       the major site. {ECO:0000250|UniProtKB:Q03164}.
CC   -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC       {ECO:0000250|UniProtKB:Q03164}.
CC   -!- PTM: Auto-methylated at Cys-3879: auto-methylation is inhibited by the
CC       WRAD complex and unmodified histone H3. {ECO:0000250|UniProtKB:Q03164}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE24386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC061963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC142113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L17069; AAA62593.1; -; mRNA.
DR   EMBL; AK140439; BAE24386.1; ALT_INIT; mRNA.
DR   EMBL; AK149341; BAE28820.1; -; mRNA.
DR   BMRB; P55200; -.
DR   SMR; P55200; -.
DR   BioGRID; 229502; 34.
DR   DIP; DIP-58597N; -.
DR   FunCoup; P55200; 4428.
DR   IntAct; P55200; 3.
DR   STRING; 10090.ENSMUSP00000002095; -.
DR   GlyGen; P55200; 9 sites, 2 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P55200; -.
DR   PhosphoSitePlus; P55200; -.
DR   jPOST; P55200; -.
DR   PaxDb; 10090-ENSMUSP00000002095; -.
DR   PeptideAtlas; P55200; -.
DR   ProteomicsDB; 263666; -. [P55200-1]
DR   ProteomicsDB; 263667; -. [P55200-2]
DR   Pumba; P55200; -.
DR   Ensembl; ENSMUST00000002095.11; ENSMUSP00000002095.4; ENSMUSG00000002028.14. [P55200-2]
DR   Ensembl; ENSMUST00000114689.8; ENSMUSP00000110337.2; ENSMUSG00000002028.14. [P55200-1]
DR   UCSC; uc009pep.1; mouse. [P55200-2]
DR   UCSC; uc009peq.1; mouse. [P55200-1]
DR   AGR; MGI:96995; -.
DR   MGI; MGI:96995; Kmt2a.
DR   VEuPathDB; HostDB:ENSMUSG00000002028; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   GeneTree; ENSGT00940000160099; -.
DR   HOGENOM; CLU_000208_2_0_1; -.
DR   InParanoid; P55200; -.
DR   OMA; VVRSQQW; -.
DR   OrthoDB; 308383at2759; -.
DR   PhylomeDB; P55200; -.
DR   BRENDA; 2.1.1.364; 3474.
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   Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   BioGRID-ORCS; 214162; 15 hits in 81 CRISPR screens.
DR   PRO; PR:P55200; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P55200; protein.
DR   Bgee; ENSMUSG00000002028; Expressed in embryonic post-anal tail and 252 other cell types or tissues.
DR   ExpressionAtlas; P55200; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:GO_Central.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IDA:CACAO.
DR   GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0106363; F:protein-cysteine methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:GO_Central.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:MGI.
DR   GO; GO:0060216; P:definitive hemopoiesis; IMP:CACAO.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:MGI.
DR   GO; GO:0035640; P:exploration behavior; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin formation; ISO:GO_Central.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CACAO.
DR   GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR   GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR   GO; GO:0048536; P:spleen development; IGI:MGI.
DR   GO; GO:0045064; P:T-helper 2 cell differentiation; ISO:GO_Central.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   CDD; cd05493; Bromo_ALL-1; 1.
DR   CDD; cd15693; ePHD_KMT2A; 1.
DR   CDD; cd15588; PHD1_KMT2A; 1.
DR   CDD; cd15590; PHD2_KMT2A; 1.
DR   CDD; cd15592; PHD3_KMT2A; 1.
DR   CDD; cd19170; SET_KMT2A_2B; 1.
DR   FunFam; 3.30.160.360:FF:000002; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 3.30.160.360:FF:000003; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 3.30.40.10:FF:000002; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 3.30.40.10:FF:000071; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 3.30.40.10:FF:000089; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 2.170.270.10:FF:000149; Myeloid/lymphoid or mixed-lineage leukemia; 1.
DR   Gene3D; 3.30.160.360; -; 2.
DR   Gene3D; 6.10.250.2390; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR047219; KMT2A_2B_SET.
DR   InterPro; IPR041958; KMT2A_ePHD.
DR   InterPro; IPR042023; KMT2A_PHD1.
DR   InterPro; IPR042025; KMT2A_PHD2.
DR   InterPro; IPR044133; KMT2A_PHD3.
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   PANTHER; PTHR45838:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2A; 1.
DR   PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR   SMART; SM00297; BROMO; 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; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 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; Alternative splicing; Biological rhythms; Bromodomain;
KW   Chromatin regulator; DNA-binding; Isopeptide bond; Metal-binding;
KW   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..3966
FT                   /note="Histone-lysine N-methyltransferase 2A"
FT                   /id="PRO_0000124877"
FT   CHAIN           1..2714
FT                   /note="MLL cleavage product N320"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT                   /id="PRO_0000390951"
FT   CHAIN           2715..3966
FT                   /note="MLL cleavage product C180"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT                   /id="PRO_0000390952"
FT   DOMAIN          1637..1767
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          2020..2076
FT                   /note="FYR N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT   DOMAIN          3663..3744
FT                   /note="FYR C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT   DOMAIN          3826..3942
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          3950..3966
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DNA_BIND        167..178
FT                   /note="A.T hook 1"
FT   DNA_BIND        215..225
FT                   /note="A.T hook 2"
FT   DNA_BIND        299..307
FT                   /note="A.T hook 3"
FT   ZN_FING         1144..1192
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   ZN_FING         1430..1481
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1478..1532
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1565..1629
FT                   /note="PHD-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1872..1912
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         1933..1980
FT                   /note="PHD-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1196..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1599
FT                   /note="Interaction with histone H3K4me3"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   REGION          1665..1714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1807..1870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2147..2174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2214..2339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2371..2619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2639..2673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2709..2759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2958..3060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3164..3239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3462..3640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3782..3805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           6..25
FT                   /note="Menin-binding motif (MBM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOTIF           121..132
FT                   /note="Integrase domain-binding motif 1 (IBM1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOTIF           145..150
FT                   /note="Integrase domain-binding motif 2 (IBM2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOTIF           2843..2851
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOTIF           3759..3764
FT                   /note="WDR5 interaction motif (WIN)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   COMPBIAS        15..29
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..102
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..489
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..557
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..571
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..730
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..790
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..887
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1003
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1059
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1241
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1245..1270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1828..1849
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2218..2230
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2250..2284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2308..2320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2411..2422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2430..2440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2498..2509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2528..2537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2569..2588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2609..2618
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2663..2673
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2722..2737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2740..2759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3012..3025
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3035..3060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3167..3178
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3196..3212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3214..3229
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3475..3487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3501..3528
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3558..3570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         1191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   BINDING         3836
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         3838
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         3880
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         3903..3904
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   BINDING         3906
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   BINDING         3954
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   BINDING         3955
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         3956
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   BINDING         3961
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   SITE            2662..2663
FT                   /note="Cleavage; by TASP1, site 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   SITE            2714..2715
FT                   /note="Cleavage; by TASP1, site 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   SITE            3762
FT                   /note="Important for WDR5-recognition and binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         134
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         140
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         237
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         371
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         516
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         634
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         837
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         923
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         1053
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1127
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         1232
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         1839
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1847
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2148
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2792
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2951
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         2954
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         3032
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         3369
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         3459
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         3510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         3523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   MOD_RES         3879
FT                   /note="S-methylcysteine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   CROSSLNK        2524
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q03164"
FT   VAR_SEQ         1603..1605
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8327517"
FT                   /id="VSP_006667"
FT   VARIANT         1597
FT                   /note="K -> T"
FT   CONFLICT        372
FT                   /note="Q -> E (in Ref. 3; BAE28820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="Q -> K (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        564
FT                   /note="L -> F (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        797
FT                   /note="P -> S (in Ref. 3; BAE28820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        806
FT                   /note="E -> D (in Ref. 2; AAA62593 and 3; BAE28820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        821
FT                   /note="L -> P (in Ref. 2; AAA62593 and 3; BAE28820)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1069
FT                   /note="C -> Y (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1230
FT                   /note="A -> S (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1349
FT                   /note="R -> L (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1437
FT                   /note="A -> S (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1440
FT                   /note="G -> E (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1632
FT                   /note="A -> P (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2292
FT                   /note="S -> L (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3481
FT                   /note="N -> I (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3493
FT                   /note="R -> S (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3548
FT                   /note="G -> V (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3769
FT                   /note="Q -> K (in Ref. 2; AAA62593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3966 AA;  429649 MW;  EA9CB2A467AB3545 CRC64;
     MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV
     AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI
     GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG
     SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA
     ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR
     RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP
     SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII
     KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP
     SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA
     TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA
     PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG
     FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT
     SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI
     PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS
     QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS
     ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK
     KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV
     ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR
     AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE
     PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK
     ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP
     RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK
     AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN
     PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG
     HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC
     RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK
     LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA
     YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE
     SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI
     NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL
     DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS
     PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL
     KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR
     DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS
     DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS
     PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC
     RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY
     SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG
     SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE
     LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL
     KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP
     EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV
     TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ
     SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED
     IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR
     EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK
     EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY
     NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD
     SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ
     NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI
     SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV
     QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP
     MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL
     LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA
     PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP
     QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT
     LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA
     SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS
     NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ
     LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE
     CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER
     KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL
     HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS
     KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL
     FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR
     FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK
     CRKFLN
//