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Database: UniProt
Entry: Q03164
LinkDB: Q03164
Original site: Q03164 
ID   KMT2A_HUMAN             Reviewed;        3969 AA.
AC   Q03164; E9PQG7; Q13743; Q13744; Q14845; Q16364; Q59FF2; Q6UBD1;
AC   Q9HBJ3; Q9UD94; Q9UMA3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 5.
DT   13-FEB-2019, entry version 230.
DE   RecName: Full=Histone-lysine N-methyltransferase 2A;
DE            Short=Lysine N-methyltransferase 2A;
DE            EC=2.1.1.43 {ECO:0000269|PubMed:12453419, ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:26886794};
DE   AltName: Full=ALL-1 {ECO:0000303|PubMed:12453419};
DE   AltName: Full=CXXC-type zinc finger protein 7;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 1;
DE   AltName: Full=Trithorax-like protein;
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, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1423624; DOI=10.1016/0092-8674(92)90602-9;
RA   Tkachuk D.C., Kohler S., Cleary M.L.;
RT   "Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal
RT   translocations in acute leukemias.";
RL   Cell 71:691-700(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANT GLY-30.
RX   PubMed=8703835; DOI=10.1046/j.1365-2141.1996.d01-1748.x;
RA   Nilson I., Loechner K., Siegler G., Greil J., Beck J.D., Fey G.H.,
RA   Marschalek R.;
RT   "Exon/intron structure of the human ALL-1 (MLL) gene involved in
RT   translocations to chromosomal region 11q23 and acute leukaemias.";
RL   Br. J. Haematol. 93:966-972(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-53; LYS-502;
RP   THR-2319; ARG-2354; ARG-2387; ILE-3714 AND ALA-3773.
RG   NIEHS SNPs program;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1909.
RX   PubMed=8378076;
RA   Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S.,
RA   Kodera Y., Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R.;
RT   "Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19)
RT   leukemia.";
RL   Oncogene 8:2617-2625(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-3969 (ISOFORM 3), AND CHROMOSOMAL
RP   TRANSLOCATION WITH AFF1/MLLT2.
RX   PubMed=1423625; DOI=10.1016/0092-8674(92)90603-A;
RA   Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G.,
RA   Croce C.M., Canaani E.;
RT   "The t(4;11) chromosome translocation of human acute leukemias fuses
RT   the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene.";
RL   Cell 71:701-708(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 812-3969.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1112-1140 AND 1552-162, AND
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1317-2328.
RC   TISSUE=Brain;
RX   PubMed=1303259; DOI=10.1038/ng1092-113;
RA   Djabali M., Selleri L., Parry P., Bower M., Young B.D., Evans G.A.;
RT   "A trithorax-like gene is interrupted by chromosome 11q23
RT   translocations in acute leukaemias.";
RL   Nat. Genet. 2:113-118(1992).
RN   [9]
RP   ERRATUM.
RX   PubMed=8401594;
RA   Djabali M., Selleri L., Parry P., Bower M., Young B., Evans G.A.;
RL   Nat. Genet. 4:431-431(1993).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1212-1603 (ISOFORM 3).
RX   PubMed=7794749; DOI=10.1111/j.1365-2141.1995.tb05151.x;
RA   Marschalek R., Greil J., Lochner K., Nilson I., Siegler G.,
RA   Zweckbronner I., Beck J.D., Fey G.H.;
RT   "Molecular analysis of the chromosomal breakpoint and fusion
RT   transcripts in the acute lymphoblastic SEM cell line with chromosomal
RT   translocation t(4;11).";
RL   Br. J. Haematol. 90:308-320(1995).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1654 (ISOFORM 2).
RX   PubMed=7598802; DOI=10.1089/dna.1995.14.475;
RA   Mbangkollo D., Burnett R., McCabe N., Thirman M., Gill H., Yu H.,
RA   Rowley J.D., Diaz M.O.;
RT   "The human MLL gene: nucleotide sequence, homology to the Drosophila
RT   trx zinc-finger domain, and alternative splicing.";
RL   DNA Cell Biol. 14:475-483(1995).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1538.
RX   PubMed=8162575;
RA   Gu Y., Alder H., Nakamura T., Schichman S.A., Prasad R., Canaani O.,
RA   Saito H., Croce C.M., Canaani E.;
RT   "Sequence analysis of the breakpoint cluster region in the ALL-1 gene
RT   involved in acute leukemia.";
RL   Cancer Res. 54:2327-2330(1994).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1687 (ISOFORM 3), AND CHROMOSOMAL
RP   TRANSLOCATION WITH GAS7.
RX   PubMed=10706619; DOI=10.1073/pnas.050397097;
RA   Megonigal M.D., Cheung N.-K.V., Rappaport E.F., Nowell P.C.,
RA   Wilson R.B., Jones D.H., Addya K., Leonard D.G.B., Kushner B.H.,
RA   Williams T.M., Lange B.J., Felix C.A.;
RT   "Detection of leukemia-associated MLL-GAS7 translocation early during
RT   chemotherapy with DNA topoisomerase II inhibitors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:2814-2819(2000).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1421-1540.
RX   PubMed=8414518;
RA   Forster A., Rabbitts T.H.;
RT   "A method for identifying genes within yeast artificial chromosomes:
RT   application to isolation of MLL fusion cDNAs from acute leukaemia
RT   translocations.";
RL   Oncogene 8:3157-3160(1993).
RN   [15]
RP   PROTEIN SEQUENCE OF 2719-2730, CLEAVAGE, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF 2718-ASP--VAL-2720.
RX   PubMed=12482972; DOI=10.1128/MCB.23.1.186-194.2003;
RA   Hsieh J.J.-D., Ernst P., Erdjument-Bromage H., Tempst P.,
RA   Korsmeyer S.J.;
RT   "Proteolytic cleavage of MLL generates a complex of N- and C-terminal
RT   fragments that confers protein stability and subnuclear
RT   localization.";
RL   Mol. Cell. Biol. 23:186-194(2003).
RN   [16]
RP   CHROMOSOMAL TRANSLOCATION WITH CENPK.
RX   PubMed=8950979;
RA   Taki T., Hayashi Y., Taniwaki M., Seto M., Ueda R., Hanada R.,
RA   Suzukawa K., Yokota J., Morishita K.;
RT   "Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha,
RT   by a complex translocation involving chromosomes 5, 6, 8 and 11 in
RT   infant leukemia.";
RL   Oncogene 13:2121-2130(1996).
RN   [17]
RP   CHROMOSOMAL TRANSLOCATION WITH ABI1.
RX   PubMed=9694699;
RA   Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F.,
RA   Yanagisawa M., Hayashi Y.;
RT   "ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene
RT   in acute myeloid leukemia with t(10;11)(p11.2;q23).";
RL   Blood 92:1125-1130(1998).
RN   [18]
RP   INTERACTION WITH SBF1.
RX   PubMed=9537414; DOI=10.1038/ng0498-331;
RA   Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.;
RT   "Association of SET domain and myotubularin-related proteins modulates
RT   growth control.";
RL   Nat. Genet. 18:331-337(1998).
RN   [19]
RP   INTERACTION WITH PPP1R15A, DISEASE, AND FUNCTION.
RX   PubMed=10490642; DOI=10.1128/MCB.19.10.7050;
RA   Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M.,
RA   Fornace A.J. Jr., Tkachuk D.C.;
RT   "Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and
RT   associate with the GADD34 and hSNF5/INI1 proteins.";
RL   Mol. Cell. Biol. 19:7050-7060(1999).
RN   [20]
RP   CHROMOSOMAL TRANSLOCATION WITH AFF4.
RC   TISSUE=Placenta;
RX   PubMed=10588740; DOI=10.1073/pnas.96.25.14535;
RA   Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y.;
RT   "AF5q31, a newly identified AF4-related gene, is fused to MLL in
RT   infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23).";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999).
RN   [21]
RP   CHROMOSOMAL TRANSLOCATION WITH NCKIPSD/AF3P21.
RX   PubMed=10648423;
RA   Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H.;
RT   "Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed
RT   lineage leukemia protein in a therapy-related leukemia with
RT   t(3;11)(p21;q23).";
RL   Blood 95:1066-1068(2000).
RN   [22]
RP   CHROMOSOMAL TRANSLOCATION WITH GMPS.
RX   PubMed=11110714;
RA   Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D.,
RA   Rappaport E.F., Felix C.A.;
RT   "t(3;11) translocation in treatment-related acute myeloid leukemia
RT   fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase)
RT   gene.";
RL   Blood 96:4360-4362(2000).
RN   [23]
RP   CHROMOSOMAL TRANSLOCATION WITH LPP.
RX   PubMed=11433529; DOI=10.1002/gcc.1157;
RA   Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L.,
RA   Guilhot F., Larsen C.J., Brizard A., Roche J.;
RT   "Human LPP gene is fused to MLL in a secondary acute leukemia with a
RT   t(3;11) (q28;q23).";
RL   Genes Chromosomes Cancer 31:382-389(2001).
RN   [24]
RP   CHROMOSOMAL TRANSLOCATION WITH TET1.
RX   PubMed=12124344;
RA   Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y.;
RT   "LCX, leukemia-associated protein with a CXXC domain, is fused to MLL
RT   in acute myeloid leukemia with trilineage dysplasia having
RT   t(10;11)(q22;q23).";
RL   Cancer Res. 62:4075-4080(2002).
RN   [25]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12453419; DOI=10.1016/S1097-2765(02)00740-2;
RA   Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T.,
RA   Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E.;
RT   "ALL-1 is a histone methyltransferase that assembles a supercomplex of
RT   proteins involved in transcriptional regulation.";
RL   Mol. Cell 10:1119-1128(2002).
RN   [26]
RP   CLEAVAGE, INTERACTION WITH TASP1, AND MUTAGENESIS OF 2666-ASP-GLY-2667
RP   AND 2718-ASP--VAL-2720.
RX   PubMed=14636557; DOI=10.1016/S0092-8674(03)00816-X;
RA   Hsieh J.J.-D., Cheng E.H.-Y., Korsmeyer S.J.;
RT   "Taspase1: a threonine aspartase required for cleavage of MLL and
RT   proper HOX gene expression.";
RL   Cell 115:293-303(2003).
RN   [27]
RP   CHROMOSOMAL TRANSLOCATION WITH ZFYVE19 AND KNL1.
RX   PubMed=12618766; DOI=10.1038/sj.onc.1206273;
RA   Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J.,
RA   Rowley J.D.;
RT   "A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene
RT   MPFYVE on chromosome 15.";
RL   Oncogene 22:1400-1410(2003).
RN   [28]
RP   CHROMOSOMAL TRANSLOCATION WITH KNL1.
RX   PubMed=12618768; DOI=10.1038/sj.onc.1206272;
RA   Kuefer M.U., Chinwalla V., Zeleznik-Le N.J., Behm F.G., Naeve C.W.,
RA   Rakestraw K.M., Mukatira S.T., Raimondi S.C., Morris S.W.;
RT   "Characterization of the MLL partner gene AF15q14 involved in
RT   t(11;15)(q23;q14).";
RL   Oncogene 22:1418-1424(2003).
RN   [29]
RP   CHROMOSOMAL TRANSLOCATION WITH DAB2IP.
RX   PubMed=14978793; DOI=10.1002/gcc.20004;
RA   von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S.,
RA   Falkenburg J.H.F., Kluin P.M., Schuuring E.;
RT   "Identification of a novel RAS GTPase-activating protein (RASGAP) gene
RT   at 9q34 as an MLL fusion partner in a patient with de novo acute
RT   myeloid leukemia.";
RL   Genes Chromosomes Cancer 39:324-334(2004).
RN   [30]
RP   CHROMOSOMAL TRANSLOCATION WITH SEPT11.
RX   PubMed=14999297; DOI=10.1038/sj.leu.2403334;
RA   Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y.,
RA   Fujii N., Tanimoto M., Fujita S.;
RT   "FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell
RT   line CNLBC1 derived from chronic neutrophilic leukemia in
RT   transformation with t(4;11)(q21;q23).";
RL   Leukemia 18:998-1005(2004).
RN   [31]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
RA   Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
RA   Kitabayashi I., Herr W., Cleary M.L.;
RT   "Leukemia proto-oncoprotein MLL forms a SET1-like histone
RT   methyltransferase complex with menin to regulate Hox gene
RT   expression.";
RL   Mol. Cell. Biol. 24:5639-5649(2004).
RN   [32]
RP   CHROMOSOMAL TRANSLOCATION WITH FRYL.
RX   PubMed=16061630; DOI=10.1158/0008-5472.CAN-05-1325;
RA   Hayette S., Cornillet-Lefebvre P., Tigaud I., Struski S.,
RA   Forissier S., Berchet A., Doll D., Gillot L., Brahim W., Delabesse E.,
RA   Magaud J.-P., Rimokh R.;
RT   "AF4p12, a human homologue to the furry gene of Drosophila, as a novel
RT   MLL fusion partner.";
RL   Cancer Res. 65:6521-6525(2005).
RN   [33]
RP   FUNCTION, IDENTIFICATION IN THE MLL1/MLL COMPLEX, AND INTERACTION WITH
RP   KAT8.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [34]
RP   DOMAIN 9AATAD.
RX   PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA   Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
RA   Piskacek M.;
RT   "Nine-amino-acid transactivation domain: establishment and prediction
RT   utilities.";
RL   Genomics 89:756-768(2007).
RN   [35]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=17500065; DOI=10.1074/jbc.M701574200;
RA   Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA   Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT   "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT   methyltransferase complex.";
RL   J. Biol. Chem. 282:20395-20406(2007).
RN   [36]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-518;
RP   SER-680; THR-840; SER-1056; THR-1845; SER-2098; THR-2147; SER-2151;
RP   THR-2525; SER-2955; SER-3036; THR-3372 AND SER-3511, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [38]
RP   FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH
RP   WDR5, AND MUTAGENESIS OF ASN-3906 AND TYR-3942.
RX   PubMed=19556245; DOI=10.1074/jbc.M109.014498;
RA   Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
RT   "On the mechanism of multiple lysine methylation by the human mixed
RT   lineage leukemia protein-1 (MLL1) core complex.";
RL   J. Biol. Chem. 284:24242-24256(2009).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-2098 AND
RP   SER-3515, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [41]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-1130 AND LYS-1235,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-926;
RP   SER-2955 AND THR-3372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [43]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2201, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [44]
RP   INVOLVEMENT IN WDSTS.
RX   PubMed=22795537; DOI=10.1016/j.ajhg.2012.06.008;
RA   Jones W.D., Dafou D., McEntagart M., Woollard W.J., Elmslie F.V.,
RA   Holder-Espinasse M., Irving M., Saggar A.K., Smithson S.,
RA   Trembath R.C., Deshpande C., Simpson M.A.;
RT   "De novo mutations in MLL cause Wiedemann-Steiner syndrome.";
RL   Am. J. Hum. Genet. 91:358-364(2012).
RN   [45]
RP   INTERACTION WITH ZNF335.
RX   PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA   Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA   Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA   Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
RA   Mahajnah M., Shenhav R., Walsh C.A.;
RT   "Microcephaly gene links trithorax and REST/NRSF to control neural
RT   stem cell proliferation and differentiation.";
RL   Cell 151:1097-1112(2012).
RN   [46]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858; SER-2098;
RP   THR-2525; SER-2611; SER-2796; SER-2955; SER-3036; SER-3511 AND
RP   SER-3527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [47]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1837, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [48]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2528, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [49]
RP   STRUCTURE BY NMR OF 1146-1214 IN COMPLEX WITH ZINC, DOMAIN CXXC-TYPE
RP   ZINC-FINGER, DNA-BINDING, AND MUTAGENESIS OF ARG-1151; ARG-1153;
RP   ARG-1154; CYS-1155; CYS-1158; CYS-1161; GLN-1162; ASP-1166; CYS-1167;
RP   CYS-1170; ASN-1172; CYS-1173; ASP-1175; LYS-1176; 1178-LYS--GLY-1181;
RP   LYS-1178; PHE-1179; ASN-1183; LYS-1185; LYS-1186; GLN-1187; CYS-1188;
RP   CYS-1189; ARG-1192; LYS-1193; CYS-1194; GLN-1195 AND ASN-1196.
RX   PubMed=16990798; DOI=10.1038/sj.emboj.7601340;
RA   Allen M.D., Grummitt C.G., Hilcenko C., Min S.Y., Tonkin L.M.,
RA   Johnson C.M., Freund S.M., Bycroft M., Warren A.J.;
RT   "Solution structure of the nonmethyl-CpG-binding CXXC domain of the
RT   leukaemia-associated MLL histone methyltransferase.";
RL   EMBO J. 25:4503-4512(2006).
RN   [50]
RP   STRUCTURE BY NMR OF 2842-2869 IN COMPLEX WITH CREBBP.
RX   PubMed=16253272; DOI=10.1016/j.jmb.2005.09.059;
RA   De Guzman R.N., Goto N.K., Dyson H.J., Wright P.E.;
RT   "Structural basis for cooperative transcription factor binding to the
RT   CBP coactivator.";
RL   J. Mol. Biol. 355:1005-1013(2006).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 3764-3776 IN COMPLEX WITH
RP   WDR5.
RX   PubMed=18829459; DOI=10.1074/jbc.C800164200;
RA   Patel A., Dharmarajan V., Cosgrove M.S.;
RT   "Structure of WDR5 bound to mixed lineage leukemia protein-1
RT   peptide.";
RL   J. Biol. Chem. 283:32158-32161(2008).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3785-3969 IN COMPLEX WITH
RP   ZINC; S-ADENOSYL-L-HOMOCYSTEINE AND HISTONE H3 PEPTIDE, FUNCTION,
RP   CATALYTIC ACTIVITY, DOMAIN SET, INTERACTION WITH ASH2L AND RBBP5, AND
RP   MUTAGENESIS OF TYR-3858; GLN-3867; ASP-3869; ARG-3871; GLU-3872;
RP   TYR-3874; LYS-3878 AND TYR-3942.
RX   PubMed=19187761; DOI=10.1016/j.molcel.2008.12.029;
RA   Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R.;
RT   "Structural basis for the requirement of additional factors for MLL1
RT   SET domain activity and recognition of epigenetic marks.";
RL   Mol. Cell 33:181-191(2009).
RN   [53] {ECO:0000244|PDB:2KYU}
RP   STRUCTURE BY NMR OF 1564-1628 IN COMPLEX WITH ZINC, FUNCTION, DOMAIN,
RP   MUTAGENESIS OF TRP-1594; VAL-1617 AND TYR-1619, AND INTERACTION WITH
RP   PPIE.
RX   PubMed=20677832; DOI=10.1021/bi1009387;
RA   Park S., Osmers U., Raman G., Schwantes R.H., Diaz M.O.,
RA   Bushweller J.H.;
RT   "The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-
RT   mediated activation and repression.";
RL   Biochemistry 49:6576-6586(2010).
RN   [54] {ECO:0000244|PDB:2KU7, ECO:0000244|PDB:3LQH, ECO:0000244|PDB:3LQI, ECO:0000244|PDB:3LQJ}
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1566-1784 IN COMPLEX WITH
RP   ZINC AND METHYLATED HISTONE H3, INTERACTION WITH PPIE, DOMAIN, AND
RP   MUTAGENESIS OF TYR-1581; GLN-1587 AND TRP-1594.
RX   PubMed=20541251; DOI=10.1016/j.cell.2010.05.016;
RA   Wang Z., Song J., Milne T.A., Wang G.G., Li H., Allis C.D.,
RA   Patel D.J.;
RT   "Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout
RT   to CyP33 and HDAC-mediated repression.";
RL   Cell 141:1183-1194(2010).
RN   [55] {ECO:0000244|PDB:2KKF}
RP   STRUCTURE BY NMR OF 1147-1203 IN COMPLEX WITH ZINC AND TARGET DNA,
RP   FUNCTION, DOMAIN, AND MUTAGENESIS OF ARG-1150; ARG-1154; LYS-1185;
RP   GLN-1187; CYS-1188; LYS-1193; LEU-1197 AND MET-1200.
RX   PubMed=20010842; DOI=10.1038/nsmb.1714;
RA   Cierpicki T., Risner L.E., Grembecka J., Lukasik S.M., Popovic R.,
RA   Omonkowska M., Shultis D.D., Zeleznik-Le N.J., Bushweller J.H.;
RT   "Structure of the MLL CXXC domain-DNA complex and its functional role
RT   in MLL-AF9 leukemia.";
RL   Nat. Struct. Mol. Biol. 17:62-68(2010).
RN   [56] {ECO:0000244|PDB:5F5E, ECO:0000244|PDB:5F6L}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3813-3969 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND ZINC, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASN-3861; ARG-3864 AND GLN-3867.
RX   PubMed=26886794; DOI=10.1038/nature16952;
RA   Li Y., Han J., Zhang Y., Cao F., Liu Z., Li S., Wu J., Hu C., Wang Y.,
RA   Shuai J., Chen J., Cao L., Li D., Shi P., Tian C., Zhang J., Dou Y.,
RA   Li G., Chen Y., Lei M.;
RT   "Structural basis for activity regulation of MLL family
RT   methyltransferases.";
RL   Nature 530:447-452(2016).
CC   -!- FUNCTION: Histone methyltransferase that plays an essential role
CC       in early development and hematopoiesis. Catalytic subunit of the
CC       MLL1/MLL complex, a multiprotein complex that mediates both
CC       methylation of 'Lys-4' of histone H3 (H3K4me) complex and
CC       acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL
CC       complex, it specifically mediates H3K4me, a specific tag for
CC       epigenetic transcriptional activation (PubMed:12453419,
CC       PubMed:20677832, PubMed:26886794). Has weak methyltransferase
CC       activity by itself, and requires other component of the MLL1/MLL
CC       complex to obtain full methyltransferase activity
CC       (PubMed:19187761, PubMed:26886794). Has no activity toward histone
CC       H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated
CC       on 'Arg-8' or 'Lys-9', while it has higher activity toward H3
CC       acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the
CC       promoter of target genes and helps maintain them in the
CC       nonmethylated state (PubMed:20010842). Required for
CC       transcriptional activation of HOXA9 (PubMed:12453419,
CC       PubMed:20677832, PubMed:20010842). Promotes PPP1R15A-induced
CC       apoptosis. Plays a critical role in the control of circadian gene
CC       expression and is essential for the transcriptional activation
CC       mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a
CC       permissive chromatin state for circadian transcription by
CC       mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me)
CC       and this histone modification directs the circadian acetylation at
CC       H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to
CC       chromatin (By similarity). {ECO:0000250|UniProtKB:P55200,
CC       ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12453419,
CC       ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:19187761,
CC       ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20010842,
CC       ECO:0000269|PubMed:26886794, ECO:0000305|PubMed:20677832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:12453419,
CC         ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:26886794};
CC   -!- SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL
CC       cleavage product C180 (via SET and FYRC domains). Component of
CC       some MLL1/MLL complex, at least composed of the core components
CC       KMT2A/MLL1, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as
CC       well as the facultative components BAP18, CHD8, E2F6, HSP70,
CC       INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1,
CC       PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1,
CC       TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15199122,
CC       PubMed:15960975, PubMed:17500065, PubMed:19556245,
CC       PubMed:19187761, PubMed:26886794). Interacts with WDR5; the
CC       interaction is direct (PubMed:19556245, PubMed:18829459).
CC       Interaction with WDR5 is required for stable interaction with
CC       ASH2L and RBBP5, and thereby also for optimal histone
CC       methyltransferase activity (PubMed:26886794). Interacts with
CC       KAT8/MOF; the interaction is direct (PubMed:15960975). Interacts
CC       with SBF1 and PPP1R15A (PubMed:9537414, PubMed:10490642).
CC       Interacts with ZNF335 (PubMed:23178126). Interacts with CLOCK and
CC       ARNTL/BMAL1 in a circadian manner (By similarity). Interacts with
CC       PPIE; this results in decreased histone H3 methyltransferase
CC       activity (PubMed:20677832, PubMed:20541251). Interacts with CREBBP
CC       (PubMed:16253272). {ECO:0000250|UniProtKB:P55200,
CC       ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12482972,
CC       ECO:0000269|PubMed:14636557, ECO:0000269|PubMed:15199122,
CC       ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16253272,
CC       ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:17500065,
CC       ECO:0000269|PubMed:18829459, ECO:0000269|PubMed:19187761,
CC       ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20541251,
CC       ECO:0000269|PubMed:20677832, ECO:0000269|PubMed:23178126,
CC       ECO:0000269|PubMed:26886794, ECO:0000269|PubMed:9537414}.
CC   -!- INTERACTION:
CC       Self; NbExp=5; IntAct=EBI-591370, EBI-591370;
CC       P10275:AR; NbExp=2; IntAct=EBI-591370, EBI-608057;
CC       Q9WTL8:Arntl (xeno); NbExp=3; IntAct=EBI-591370, EBI-644534;
CC       Q9UBL3-3:ASH2L; NbExp=4; IntAct=EBI-591370, EBI-16130425;
CC       Q6P1J9:CDC73; NbExp=4; IntAct=EBI-591370, EBI-930143;
CC       O08785:Clock (xeno); NbExp=3; IntAct=EBI-591370, EBI-79859;
CC       P45481:Crebbp (xeno); NbExp=7; IntAct=EBI-591370, EBI-296306;
CC       Q6PD62:CTR9; NbExp=5; IntAct=EBI-591370, EBI-1019583;
CC       P68431:HIST1H3D; NbExp=11; IntAct=EBI-591370, EBI-79722;
CC       Q92794:KAT6A; NbExp=10; IntAct=EBI-2638616, EBI-948013;
CC       Q9H7Z6:KAT8; NbExp=3; IntAct=EBI-591370, EBI-896414;
CC       O00255-2:MEN1; NbExp=12; IntAct=EBI-591370, EBI-9869387;
CC       Q8N7H5:PAF1; NbExp=4; IntAct=EBI-591370, EBI-2607770;
CC       Q02548:PAX5; NbExp=2; IntAct=EBI-2610266, EBI-296331;
CC       Q9UNP9:PPIE; NbExp=4; IntAct=EBI-591370, EBI-591818;
CC       Q15291:RBBP5; NbExp=9; IntAct=EBI-591370, EBI-592823;
CC       Q96EB6:SIRT1; NbExp=5; IntAct=EBI-591370, EBI-1802965;
CC       Q13309-1:SKP2; NbExp=2; IntAct=EBI-591370, EBI-15490084;
CC       P61964:WDR5; NbExp=13; IntAct=EBI-591370, EBI-540834;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482972}.
CC   -!- SUBCELLULAR LOCATION: MLL cleavage product N320: Nucleus.
CC   -!- SUBCELLULAR LOCATION: MLL cleavage product C180: Nucleus.
CC       Note=Localizes to a diffuse nuclear pattern when not associated
CC       with MLL cleavage product N320.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q03164-1; Sequence=Displayed;
CC       Name=2; Synonyms=14P-18B;
CC         IsoId=Q03164-2; Sequence=VSP_006666;
CC       Name=3;
CC         IsoId=Q03164-3; Sequence=VSP_046879;
CC   -!- TISSUE SPECIFICITY: Heart, lung, brain and T- and B-lymphocytes.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a
CC       large number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:17467953}.
CC   -!- DOMAIN: The SET domain structure is atypical and is not in an
CC       optimal position to have methyltransferase activity. It requires
CC       other components of the MLL1/MLL complex, such as ASH2L or RBBP5,
CC       to order the active site and obtain optimal histone
CC       methyltransferase activity. {ECO:0000269|PubMed:19187761,
CC       ECO:0000269|PubMed:26886794}.
CC   -!- DOMAIN: The CXXC-type zinc finger binds to DNA sequence elements
CC       containing nonmethylated CpG dinucleotides.
CC       {ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842}.
CC   -!- DOMAIN: The third PHD-type zinc-finger binds both trimethylated
CC       histone H3K4me3 and PPIE; histone and PPIE bind to distinct
CC       surfaces (PubMed:20677832, PubMed:20541251). Nevertheless, PPIE
CC       binding and histone binding are mutually inhibitory
CC       (PubMed:20677832). Isomerization of a peptidylproline bond in the
CC       linker between the third PHD-type zinc-finger and the bromo domain
CC       disrupts the interaction between the bromo domain and the third
CC       PHD-type zinc-finger, and thereby facilitates interaction with
CC       PPIE (PubMed:20541251). {ECO:0000269|PubMed:20541251,
CC       ECO:0000269|PubMed:20677832}.
CC   -!- PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product
CC       N320 and MLL cleavage product C180, which reassemble through a
CC       non-covalent association. 2 cleavage sites exist, cleavage site 1
CC       (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products
CC       N320 and C180. CS2 is the major site.
CC       {ECO:0000269|PubMed:12482972, ECO:0000269|PubMed:14636557}.
CC   -!- DISEASE: Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A
CC       syndrome characterized by hairy elbows (hypertrichosis cubiti),
CC       intellectual disability, a distinctive facial appearance, and
CC       short stature. Facial characteristics include long eyelashes,
CC       thick or arched eyebrows with a lateral flare, and downslanting
CC       and vertically narrow palpebral fissures.
CC       {ECO:0000269|PubMed:22795537}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=Chromosomal aberrations involving KMT2A are a cause
CC       of acute leukemias. Translocation t(1;11)(q21;q23) with
CC       MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21;
CC       translocation t(3,11)(q25,q23) with GMPS; translocation
CC       t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion
CC       ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation
CC       t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation
CC       t(6;11)(q27;q23) with AFDN; translocation t(9;11)(p22;q23) with
CC       MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1;
CC       translocation t(10;11)(p12;q23) with MLLT10/AF10;
CC       t(11;15)(q23;q14) with KNL1 and ZFYVE19; translocation
CC       t(11;17)(q23;q21) with MLLT6/AF17; translocation
CC       t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3)
CC       with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7;
CC       translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation
CC       t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with
CC       TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation
CC       t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A-
CC       MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to
CC       unfused KMT2A, inhibit PPP1R15A-induced apoptosis.
CC       {ECO:0000269|PubMed:10490642}.
CC   -!- DISEASE: Note=A chromosomal aberration involving KMT2A may be a
CC       cause of chronic neutrophilic leukemia. Translocation
CC       t(4;11)(q21;q23) with SEPT11. {ECO:0000269|PubMed:10490642}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58669.1; Type=Frameshift; Positions=317, 380; Evidence={ECO:0000305};
CC       Sequence=AAG26332.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAD92745.1; Type=Frameshift; Positions=1098; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MLLID13.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/mll/";
DR   EMBL; L04284; AAA58669.1; ALT_FRAME; mRNA.
DR   EMBL; Z69744; CAA93625.1; -; Genomic_DNA.
DR   EMBL; Z69745; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69746; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69747; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69748; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69749; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69750; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69751; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69752; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69753; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69754; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69755; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69756; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69757; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69758; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69759; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69760; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69761; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69762; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69763; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69764; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69765; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69766; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69767; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69768; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69769; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69770; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69772; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69773; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69774; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69775; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69776; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69777; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69778; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69779; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; Z69780; CAA93625.1; JOINED; Genomic_DNA.
DR   EMBL; AY373585; AAQ63624.1; -; Genomic_DNA.
DR   EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D14540; BAA03407.1; -; mRNA.
DR   EMBL; AB209508; BAD92745.1; ALT_FRAME; mRNA.
DR   EMBL; L04731; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L01986; AAA92511.1; -; mRNA.
DR   EMBL; X83604; CAA58584.1; -; Genomic_DNA.
DR   EMBL; S78570; AAB34770.1; -; mRNA.
DR   EMBL; U04737; AAA18644.1; -; Genomic_DNA.
DR   EMBL; S66432; AAB28545.1; -; mRNA.
DR   EMBL; AF232001; AAG26335.2; -; mRNA.
DR   EMBL; AF231998; AAG26332.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS31686.1; -. [Q03164-1]
DR   CCDS; CCDS55791.1; -. [Q03164-3]
DR   PIR; A44265; A44265.
DR   PIR; I52578; I52578.
DR   PIR; I53035; I53035.
DR   RefSeq; NP_001184033.1; NM_001197104.1. [Q03164-3]
DR   RefSeq; NP_005924.2; NM_005933.3. [Q03164-1]
DR   UniGene; Hs.258855; -.
DR   PDB; 2AGH; NMR; -; C=2840-2869.
DR   PDB; 2J2S; NMR; -; A=1143-1214.
DR   PDB; 2JYI; NMR; -; A=1147-1203.
DR   PDB; 2KKF; NMR; -; A=1147-1203.
DR   PDB; 2KU7; NMR; -; A=1585-1628.
DR   PDB; 2KYU; NMR; -; A=1564-1628.
DR   PDB; 2LXS; NMR; -; B=2840-2858.
DR   PDB; 2LXT; NMR; -; B=2840-2858.
DR   PDB; 2MSR; NMR; -; A=140-160.
DR   PDB; 2MTN; NMR; -; A=110-160.
DR   PDB; 2W5Y; X-ray; 2.00 A; A=3785-3969.
DR   PDB; 2W5Z; X-ray; 2.20 A; A=3785-3969.
DR   PDB; 3EG6; X-ray; 1.72 A; C=3762-3773.
DR   PDB; 3EMH; X-ray; 1.37 A; B=3764-3776.
DR   PDB; 3LQH; X-ray; 1.72 A; A=1566-1784.
DR   PDB; 3LQI; X-ray; 1.92 A; A/B/C=1566-1784.
DR   PDB; 3LQJ; X-ray; 1.90 A; A/B=1566-1784.
DR   PDB; 3P4F; X-ray; 2.35 A; C=3761-3770.
DR   PDB; 3U85; X-ray; 3.00 A; B=6-25.
DR   PDB; 3U88; X-ray; 3.00 A; M/N=103-153.
DR   PDB; 4ESG; X-ray; 1.70 A; C/D=3755-3771.
DR   PDB; 4GQ6; X-ray; 1.55 A; B=6-15.
DR   PDB; 4NW3; X-ray; 2.82 A; A=1147-1204.
DR   PDB; 5F5E; X-ray; 1.80 A; A=3813-3969.
DR   PDB; 5F6L; X-ray; 1.90 A; A=3813-3969.
DR   PDB; 5SVH; X-ray; 2.05 A; B=2839-2869.
DR   PDB; 6EMQ; NMR; -; A=111-160.
DR   PDBsum; 2AGH; -.
DR   PDBsum; 2J2S; -.
DR   PDBsum; 2JYI; -.
DR   PDBsum; 2KKF; -.
DR   PDBsum; 2KU7; -.
DR   PDBsum; 2KYU; -.
DR   PDBsum; 2LXS; -.
DR   PDBsum; 2LXT; -.
DR   PDBsum; 2MSR; -.
DR   PDBsum; 2MTN; -.
DR   PDBsum; 2W5Y; -.
DR   PDBsum; 2W5Z; -.
DR   PDBsum; 3EG6; -.
DR   PDBsum; 3EMH; -.
DR   PDBsum; 3LQH; -.
DR   PDBsum; 3LQI; -.
DR   PDBsum; 3LQJ; -.
DR   PDBsum; 3P4F; -.
DR   PDBsum; 3U85; -.
DR   PDBsum; 3U88; -.
DR   PDBsum; 4ESG; -.
DR   PDBsum; 4GQ6; -.
DR   PDBsum; 4NW3; -.
DR   PDBsum; 5F5E; -.
DR   PDBsum; 5F6L; -.
DR   PDBsum; 5SVH; -.
DR   PDBsum; 6EMQ; -.
DR   ProteinModelPortal; Q03164; -.
DR   SMR; Q03164; -.
DR   BioGrid; 110443; 110.
DR   CORUM; Q03164; -.
DR   DIP; DIP-29221N; -.
DR   ELM; Q03164; -.
DR   IntAct; Q03164; 56.
DR   MINT; Q03164; -.
DR   STRING; 9606.ENSP00000436786; -.
DR   BindingDB; Q03164; -.
DR   ChEMBL; CHEMBL1293299; -.
DR   CarbonylDB; Q03164; -.
DR   iPTMnet; Q03164; -.
DR   PhosphoSitePlus; Q03164; -.
DR   BioMuta; KMT2A; -.
DR   DMDM; 146345435; -.
DR   EPD; Q03164; -.
DR   jPOST; Q03164; -.
DR   MaxQB; Q03164; -.
DR   PaxDb; Q03164; -.
DR   PeptideAtlas; Q03164; -.
DR   PRIDE; Q03164; -.
DR   ProteomicsDB; 58195; -.
DR   ProteomicsDB; 58196; -. [Q03164-2]
DR   Ensembl; ENST00000389506; ENSP00000374157; ENSG00000118058. [Q03164-1]
DR   Ensembl; ENST00000534358; ENSP00000436786; ENSG00000118058. [Q03164-3]
DR   Ensembl; ENST00000649699; ENSP00000496927; ENSG00000118058. [Q03164-2]
DR   GeneID; 4297; -.
DR   KEGG; hsa:4297; -.
DR   UCSC; uc001pta.4; human. [Q03164-1]
DR   CTD; 4297; -.
DR   DisGeNET; 4297; -.
DR   EuPathDB; HostDB:ENSG00000118058.20; -.
DR   GeneCards; KMT2A; -.
DR   HGNC; HGNC:7132; KMT2A.
DR   HPA; CAB017794; -.
DR   HPA; CAB024270; -.
DR   HPA; HPA044910; -.
DR   MalaCards; KMT2A; -.
DR   MIM; 159555; gene+phenotype.
DR   MIM; 605130; phenotype.
DR   neXtProt; NX_Q03164; -.
DR   OpenTargets; ENSG00000118058; -.
DR   Orphanet; 98837; Acute biphenotypic leukemia.
DR   Orphanet; 98831; Acute myeloid leukemia with 11q23 abnormalities.
DR   Orphanet; 402017; Acute myeloid leukemia with t(9;11)(p22;q23).
DR   Orphanet; 98835; Acute undifferentiated leukemia.
DR   Orphanet; 98836; Bilineal acute leukemia.
DR   Orphanet; 199; Cornelia de Lange syndrome.
DR   Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR   Orphanet; 319182; Wiedemann-Steiner syndrome.
DR   PharmGKB; PA241; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000160099; -.
DR   HOVERGEN; HBG051927; -.
DR   InParanoid; Q03164; -.
DR   KO; K09186; -.
DR   OMA; GVMYFEQ; -.
DR   OrthoDB; 738155at2759; -.
DR   PhylomeDB; Q03164; -.
DR   TreeFam; TF319820; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   SIGNOR; Q03164; -.
DR   ChiTaRS; KMT2A; human.
DR   EvolutionaryTrace; Q03164; -.
DR   GeneWiki; MLL_(gene); -.
DR   GenomeRNAi; 4297; -.
DR   PRO; PR:Q03164; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000118058; Expressed in 244 organ(s), highest expression level in forebrain.
DR   ExpressionAtlas; Q03164; baseline and differential.
DR   Genevisible; Q03164; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003680; F:AT DNA binding; NAS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0035162; P:embryonic hemopoiesis; TAS:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:BHF-UCL.
DR   GO; GO:0043984; P:histone H4-K16 acetylation; IMP:UniProtKB.
DR   GO; GO:1905642; P:negative regulation of DNA methylation; IMP:UniProtKB.
DR   GO; GO:2001040; P:positive regulation of cellular response to drug; IMP:BHF-UCL.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0032411; P:positive regulation of transporter activity; IMP:BHF-UCL.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:0071440; P:regulation of histone H3-K14 acetylation; ISS:UniProtKB.
DR   GO; GO:2000615; P:regulation of histone H3-K9 acetylation; ISS:UniProtKB.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   Gene3D; 3.30.40.10; -; 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; IPR037927; KMT2A.
DR   InterPro; IPR016569; MeTrfase_trithorax.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
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; PTHR22884:SF387; PTHR22884:SF387; 1.
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; 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; SSF47370; 1.
DR   SUPFAM; SSF57903; SSF57903; 2.
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   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   Biological rhythms; Bromodomain; Chromatin regulator;
KW   Chromosomal rearrangement; Complete proteome;
KW   Direct protein sequencing; DNA-binding; Isopeptide bond;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   3969       Histone-lysine N-methyltransferase 2A.
FT                                /FTId=PRO_0000124876.
FT   CHAIN         1   2718       MLL cleavage product N320.
FT                                /FTId=PRO_0000390949.
FT   CHAIN      2719   3969       MLL cleavage product C180.
FT                                /FTId=PRO_0000390950.
FT   DOMAIN     1703   1748       Bromo; divergent. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   DOMAIN     2018   2074       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     3666   3747       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     3829   3945       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     3953   3969       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    169    180       A.T hook 1.
FT   DNA_BIND    217    227       A.T hook 2.
FT   DNA_BIND    301    309       A.T hook 3.
FT   ZN_FING    1147   1195       CXXC-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00509}.
FT   ZN_FING    1431   1482       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1479   1533       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1566   1627       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1870   1910       C2HC pre-PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING    1931   1978       PHD-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION     1584   1600       Interaction with histone H3K4me3.
FT                                {ECO:0000269|PubMed:20677832}.
FT   REGION     3764   3771       Interaction with WDR5.
FT                                {ECO:0000269|PubMed:18829459}.
FT   REGION     3906   3907       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:26886794}.
FT   MOTIF      2847   2855       9aaTAD. {ECO:0000269|PubMed:17467953}.
FT   COMPBIAS     17    102       Ala/Gly/Ser-rich.
FT   COMPBIAS    137    143       Poly-Gly.
FT   COMPBIAS    561    564       Poly-Pro.
FT   COMPBIAS    568    571       Poly-Pro.
FT   METAL      3909   3909       Zinc. {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:2W5Z,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:19187761}.
FT   METAL      3957   3957       Zinc. {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:2W5Z,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:19187761}.
FT   METAL      3959   3959       Zinc. {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:2W5Z,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:19187761}.
FT   METAL      3964   3964       Zinc. {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:2W5Z,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:19187761}.
FT   BINDING    3839   3839       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:26886794}.
FT   BINDING    3841   3841       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:26886794}.
FT   BINDING    3883   3883       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:2W5Z,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:26886794}.
FT   BINDING    3958   3958       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:2W5Y,
FT                                ECO:0000244|PDB:5F5E,
FT                                ECO:0000244|PDB:5F6L,
FT                                ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:26886794}.
FT   SITE       1334   1335       Breakpoint for translocation to form
FT                                KMT2A-ZFYVE19 oncogene.
FT   SITE       1362   1363       Breakpoint for translocation to form
FT                                KMT2A-AF3P21 and KMT2A-KNL1 oncogenes.
FT   SITE       1362   1363       Breakpoint for translocation to form
FT                                KMT2A-CENPK oncogene.
FT   SITE       1362   1362       Breakpoint for translocation to form
FT                                KMT2A-FRYL fusion protein.
FT   SITE       1406   1407       Breakpoint for translocation to form
FT                                KMT2A-AFF4 fusion protein.
FT   SITE       1444   1445       Breakpoint for translocation to form
FT                                KMT2A-GAS7 oncogene.
FT   SITE       1444   1445       Breakpoint for translocation to form
FT                                KMT2A-LPP.
FT   SITE       2666   2667       Cleavage; by TASP1, site 1.
FT                                {ECO:0000269|PubMed:14636557}.
FT   SITE       2718   2719       Cleavage; by TASP1, site 2.
FT                                {ECO:0000269|PubMed:14636557}.
FT   SITE       3765   3765       Important for WDR5-recognition and
FT                                binding. {ECO:0000269|PubMed:19556245}.
FT   MOD_RES     153    153       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     197    197       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     239    239       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P55200}.
FT   MOD_RES     373    373       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P55200}.
FT   MOD_RES     518    518       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     636    636       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     680    680       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     840    840       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     926    926       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1056   1056       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1130   1130       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    1235   1235       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    1837   1837       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1845   1845       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1858   1858       Phosphoserine.
FT                                {ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2098   2098       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2147   2147       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    2151   2151       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    2201   2201       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES    2525   2525       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2611   2611       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2796   2796       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2955   2955       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2958   2958       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P55200}.
FT   MOD_RES    3036   3036       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    3372   3372       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES    3462   3462       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P55200}.
FT   MOD_RES    3511   3511       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    3515   3515       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES    3527   3527       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK   2528   2528       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ    1407   1444       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7598802}.
FT                                /FTId=VSP_006666.
FT   VAR_SEQ    1603   1603       S -> SGTE (in isoform 3).
FT                                {ECO:0000303|PubMed:10706619,
FT                                ECO:0000303|PubMed:1423625}.
FT                                /FTId=VSP_046879.
FT   VARIANT      30     30       A -> G (in dbSNP:rs9332745).
FT                                {ECO:0000269|PubMed:8703835}.
FT                                /FTId=VAR_021317.
FT   VARIANT      53     53       A -> V (in dbSNP:rs9332747).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021318.
FT   VARIANT     502    502       E -> K (in dbSNP:rs9332772).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021319.
FT   VARIANT    1975   1975       Q -> P (in dbSNP:rs693598).
FT                                /FTId=VAR_052652.
FT   VARIANT    2319   2319       S -> T (in dbSNP:rs9332837).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021320.
FT   VARIANT    2354   2354       P -> R (in dbSNP:rs9332838).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021321.
FT   VARIANT    2387   2387       Q -> R (in dbSNP:rs9332839).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021322.
FT   VARIANT    3714   3714       V -> I (in dbSNP:rs9332859).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021323.
FT   VARIANT    3773   3773       S -> A (in dbSNP:rs9332861).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_021324.
FT   MUTAGEN    1150   1150       R->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1151   1151       R->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1153   1153       R->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1154   1154       R->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1155   1155       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1158   1158       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1161   1161       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1162   1162       Q->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1166   1166       D->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1167   1167       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1170   1170       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1172   1172       N->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1173   1173       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1175   1175       D->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1176   1176       K->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1178   1181       KFGG->AAAA: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1178   1178       K->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1179   1179       F->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1183   1183       N->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1185   1185       K->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1186   1186       K->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1187   1187       Q->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1188   1188       C->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1188   1188       C->D: Abolishes DNA-binding and increases
FT                                CpG methylation of the HOXA9 promoter
FT                                region. Does not lead to the development
FT                                of leukemia when overexpressed in mice as
FT                                gene fusion with MLLT3.
FT                                {ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1189   1189       C->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1192   1192       R->A: Abolishes zinc-binding and
FT                                stability of the CXXC-type zinc finger
FT                                and causes loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1193   1193       K->A: Impairs DNA-binding.
FT                                {ECO:0000269|PubMed:16990798,
FT                                ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1194   1194       C->A: Impairs zinc-binding and stability
FT                                of the CXXC-type zinc finger and causes
FT                                loss of DNA-binding.
FT                                {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1195   1195       Q->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1196   1196       N->A: No effect on stability or DNA-
FT                                binding. {ECO:0000269|PubMed:16990798}.
FT   MUTAGEN    1197   1197       L->A: Mildly decreases DNA-binding.
FT                                {ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1200   1200       M->A: No effect on DNA-binding.
FT                                {ECO:0000269|PubMed:20010842}.
FT   MUTAGEN    1581   1581       Y->A: Decreases affinity for histone
FT                                H3K4me3. {ECO:0000269|PubMed:20541251}.
FT   MUTAGEN    1587   1587       Q->A: Decreases affinity for histone
FT                                H3K4me3. {ECO:0000269|PubMed:20541251}.
FT   MUTAGEN    1594   1594       W->A: Abolishes interaction with histone
FT                                H3K4me3. {ECO:0000269|PubMed:20677832}.
FT   MUTAGEN    1594   1594       W->E: Decreases affinity for histone
FT                                H3K4me3. {ECO:0000269|PubMed:20541251}.
FT   MUTAGEN    1617   1617       V->A: Decreases binding affinity for
FT                                PPIE. {ECO:0000269|PubMed:20677832}.
FT   MUTAGEN    1619   1619       Y->A: May perturb protein folding and
FT                                thereby decrease binding affinity for
FT                                PPIE. {ECO:0000269|PubMed:20677832}.
FT   MUTAGEN    2666   2667       DG->AA: Reduces cleavage without
FT                                abolishing it. Abolishes cleavage by
FT                                TASP1; when associated with 2718-A--A-
FT                                2720. {ECO:0000269|PubMed:14636557}.
FT   MUTAGEN    2718   2720       DGV->AAA: Abolishes cleavage by TASP1;
FT                                when associated with 2666-A-A-2667.
FT                                {ECO:0000269|PubMed:12482972,
FT                                ECO:0000269|PubMed:14636557}.
FT   MUTAGEN    3858   3858       Y->A: Impairs methyltransferase activity
FT                                toward unmodified or monomethylated
FT                                H3K4me. {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3858   3858       Y->F: Slightly affects methyltransferase
FT                                activity toward unmodified or
FT                                monomethylated H3K4me.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3861   3861       N->I: Leads to stable interaction with
FT                                ASH2L and RBBP5 in the absence of WDR5;
FT                                when associated with L-3867.
FT                                {ECO:0000269|PubMed:26886794}.
FT   MUTAGEN    3861   3861       N->T: Leads to stable interaction with
FT                                ASH2L and RBBP5 in the absence of WDR5;
FT                                when associated with V-3867.
FT                                {ECO:0000269|PubMed:26886794}.
FT   MUTAGEN    3864   3864       R->A: Disrupts interaction with ASH2L and
FT                                RBBP5 and nearly abolishes histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:26886794}.
FT   MUTAGEN    3867   3867       Q->A: Slightly affects methyltransferase
FT                                activity of the enzyme alone, while it
FT                                impairs methyltransferase activity in
FT                                complex; when associated with A-3871.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3867   3867       Q->L: Leads to stable interaction with
FT                                ASH2L and RBBP5 in the absence of WDR5;
FT                                when associated with I-3861.
FT                                {ECO:0000269|PubMed:26886794}.
FT   MUTAGEN    3867   3867       Q->V: Leads to stable interaction with
FT                                ASH2L and RBBP5 in the absence of WDR5;
FT                                when associated with T-3861.
FT                                {ECO:0000269|PubMed:26886794}.
FT   MUTAGEN    3869   3869       D->A: Does not affect methyltransferase
FT                                activity of the enzyme alone or in
FT                                complex; when associated with A-3872.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3871   3871       R->A: Slightly affects methyltransferase
FT                                activity of the enzyme alone, while it
FT                                impairs methyltransferase activity in
FT                                complex; when associated with A-3867.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3872   3872       E->A: Does not affect methyltransferase
FT                                activity of the enzyme alone or in
FT                                complex; when associated with A-3869.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3874   3874       Y->A: Affects methyltransferase activity
FT                                of the enzyme alone, while it does not
FT                                affect methyltransferase activity in
FT                                complex; when associated with A-3878.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3878   3878       K->A: Affects methyltransferase activity
FT                                of the enzyme alone, while it does not
FT                                affect methyltransferase activity in
FT                                complex; when associated with A-3874.
FT                                {ECO:0000269|PubMed:19187761}.
FT   MUTAGEN    3906   3906       N->A: Loss of the histone H3
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:19556245}.
FT   MUTAGEN    3942   3942       Y->A,F: Impairs methyltransferase
FT                                activity toward unmodified or
FT                                monomethylated H3K4me.
FT                                {ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:19556245}.
FT   MUTAGEN    3942   3942       Y->F: Shifts from a specific
FT                                monomethyltransferase to a di- and
FT                                trimethyltransferase activity.
FT                                {ECO:0000269|PubMed:19187761,
FT                                ECO:0000269|PubMed:19556245}.
FT   CONFLICT    144    144       E -> ELTTQIPCSWRTKGHIHDKKTEPFRLLAWSWCLN
FT                                (in Ref. 2; CAA93625). {ECO:0000305}.
FT   CONFLICT    556    556       Q -> E (in Ref. 2; CAA93625 and 6;
FT                                L04731). {ECO:0000305}.
FT   CONFLICT   1347   1347       V -> A (in Ref. 13; AAG26335).
FT                                {ECO:0000305}.
FT   CONFLICT   1487   1487       R -> G (in Ref. 12; AAA18644).
FT                                {ECO:0000305}.
FT   CONFLICT   1490   1490       Q -> R (in Ref. 13; AAG26335).
FT                                {ECO:0000305}.
FT   CONFLICT   1507   1507       P -> L (in Ref. 13; AAG26335).
FT                                {ECO:0000305}.
FT   CONFLICT   1513   1513       N -> T (in Ref. 13; AAG26335).
FT                                {ECO:0000305}.
FT   CONFLICT   1600   1600       E -> G (in Ref. 13; AAG26335).
FT                                {ECO:0000305}.
FT   CONFLICT   1616   1616       S -> C (in Ref. 11; AAB34770).
FT                                {ECO:0000305}.
FT   CONFLICT   1937   1937       Q -> H (in Ref. 8; AAA92511).
FT                                {ECO:0000305}.
FT   CONFLICT   2181   2181       P -> S (in Ref. 8; AAA92511).
FT                                {ECO:0000305}.
FT   CONFLICT   3556   3556       K -> N (in Ref. 6; L04731).
FT                                {ECO:0000305}.
FT   CONFLICT   3718   3718       R -> G (in Ref. 2; CAA93625).
FT                                {ECO:0000305}.
FT   CONFLICT   3759   3759       N -> D (in Ref. 2; CAA93625).
FT                                {ECO:0000305}.
FT   CONFLICT   3813   3813       D -> G (in Ref. 2; CAA93625).
FT                                {ECO:0000305}.
FT   CONFLICT   3901   3901       A -> R (in Ref. 1; AAA58669).
FT                                {ECO:0000305}.
FT   HELIX       114    133       {ECO:0000244|PDB:3U88}.
FT   STRAND      135    138       {ECO:0000244|PDB:2MTN}.
FT   STRAND      140    145       {ECO:0000244|PDB:6EMQ}.
FT   STRAND      150    152       {ECO:0000244|PDB:2MSR}.
FT   STRAND     1151   1154       {ECO:0000244|PDB:2J2S}.
FT   STRAND     1156   1158       {ECO:0000244|PDB:4NW3}.
FT   HELIX      1159   1162       {ECO:0000244|PDB:4NW3}.
FT   STRAND     1168   1170       {ECO:0000244|PDB:4NW3}.
FT   HELIX      1171   1175       {ECO:0000244|PDB:4NW3}.
FT   HELIX      1177   1179       {ECO:0000244|PDB:4NW3}.
FT   STRAND     1183   1185       {ECO:0000244|PDB:2J2S}.
FT   TURN       1190   1192       {ECO:0000244|PDB:4NW3}.
FT   STRAND     1197   1200       {ECO:0000244|PDB:2J2S}.
FT   TURN       1204   1206       {ECO:0000244|PDB:2J2S}.
FT   STRAND     1566   1568       {ECO:0000244|PDB:3LQI}.
FT   TURN       1570   1572       {ECO:0000244|PDB:3LQH}.
FT   STRAND     1575   1577       {ECO:0000244|PDB:3LQI}.
FT   TURN       1578   1582       {ECO:0000244|PDB:2KYU}.
FT   STRAND     1585   1587       {ECO:0000244|PDB:3LQH}.
FT   TURN       1589   1591       {ECO:0000244|PDB:3LQH}.
FT   STRAND     1594   1596       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1597   1599       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1604   1612       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1614   1617       {ECO:0000244|PDB:3LQH}.
FT   TURN       1622   1624       {ECO:0000244|PDB:3LQH}.
FT   STRAND     1627   1629       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1631   1652       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1655   1661       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1708   1716       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1723   1740       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1745   1765       {ECO:0000244|PDB:3LQH}.
FT   HELIX      1771   1773       {ECO:0000244|PDB:3LQH}.
FT   HELIX      2847   2855       {ECO:0000244|PDB:5SVH}.
FT   HELIX      3764   3766       {ECO:0000244|PDB:4ESG}.
FT   HELIX      3796   3799       {ECO:0000244|PDB:2W5Y}.
FT   HELIX      3809   3811       {ECO:0000244|PDB:2W5Y}.
FT   HELIX      3816   3820       {ECO:0000244|PDB:5F5E}.
FT   HELIX      3823   3830       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3831   3835       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3837   3847       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3854   3857       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3860   3864       {ECO:0000244|PDB:5F5E}.
FT   HELIX      3865   3867       {ECO:0000244|PDB:5F5E}.
FT   HELIX      3868   3877       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3884   3886       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3888   3894       {ECO:0000244|PDB:5F5E}.
FT   TURN       3896   3898       {ECO:0000244|PDB:5F5E}.
FT   HELIX      3901   3904       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3912   3920       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3923   3932       {ECO:0000244|PDB:5F5E}.
FT   STRAND     3939   3942       {ECO:0000244|PDB:5F5E}.
SQ   SEQUENCE   3969 AA;  431764 MW;  1150F37EAB1430D3 CRC64;
     MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV
     AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA
     AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR
     SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD
     ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV
     RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI
     IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR
     IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS
     SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS
     RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS
     TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED
     VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN
     RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL
     SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT
     PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ
     SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI
     LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD
     KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG
     RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA
     PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM
     PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE
     PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP
     KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL
     STLSNGNSSK QKIPADGVHR IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS
     GHVEFVYCQV CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK
     CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS HDFSLCHDCA
     KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE NLSDEMYEIL SNLPESVAYT
     CVNCTERHPA EWRLALEKEL QISLKQVLTA LLNSRTTSHL LRYRQAAKPP DLNPETEESI
     PSRSSPEGPD PPVLTEVSKQ DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS
     DGGQPEIKKA NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH
     NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS TDRSREDSPE
     LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH VNCALWSAEV FEDDDGSLKN
     VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL
     IKGEVVPENG FEVFRRVFVD FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC
     EDKLFPIGYQ CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT
     SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY SPTQRSPGCR
     PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL SPQRSKLRIM SPMRTGNTYS
     RNNVSSVSTT GTATDLESSA KVVDHVLGPL NSSTSLGQNT STSSNLQRTV VTVGNKNSHL
     DGSSSSEMKQ SSASDLVSKS SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS
     RELNVSKIGS FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK
     TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG QVTTGEEGNL
     KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA PPMQVEGSAK ELQAPRKRTV
     KVTLTPLKME NESQSKNALK ESSPASPLQI ESTSPTEPIS ASENPGDGPV AQPSPNNTSC
     QDSQSNNYQN LPVQDRNLML PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY
     GEEDIPFYSS STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH
     NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT ENLKIDRPED
     AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ LSSLESSRRV HTSTPSDKNL
     LDTYNTELLK SDSDNNNSDD CGNILPSDIM DFVLKNTPSM QALGESPESS SSELLNLGEG
     LGLDSNREKD MGLFEVFSQQ LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT
     VPSQNPSRLA VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD
     ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS TDSPGPSQIS
     NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ KIQLTSSVSS TPSVMETNTS
     VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP
     PSGLLIGVQP PPDPQLLVSE SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP
     SNIAPSDVVS NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP
     LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT TPTSSASVPG
     HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP PSSGMFPQLG TSQTPSTAAI
     TAASSICVLP STQTTGITAA SPSGEADEHY QLQHVNQLLA SKTGIHSSQR DLDSASGPQV
     SNFTQTVDAP NSMGLEQNKA LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT
     KRFQLPLDKG NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS
     QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL QQEQKRKESI
     TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA RSNARLKQLS FAGVNGLRML
     GILHDAVVFL IEQLSGAKHC RNYKFRFHKP EEANEPPLNP HGSARAEVHL RKSAFDMFNF
     LASKHRQPPE YNPNDEEEEE VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG
     RGLFCKRNID AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN
     AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED ASNKLPCNCG
     AKKCRKFLN
//
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