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Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]

 KMT2A_HUMAN             Reviewed;        3969 AA.
Q03164; E9PQG7; Q13743; Q13744; Q14845; Q16364; Q59FF2; Q6UBD1;
Q9HBJ3; Q9UD94; Q9UMA3;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 5.
22-NOV-2017, entry version 217.
RecName: Full=Histone-lysine N-methyltransferase 2A;
Short=Lysine N-methyltransferase 2A;
EC=2.1.1.43;
AltName: Full=ALL-1;
AltName: Full=CXXC-type zinc finger protein 7;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 1;
AltName: Full=Trithorax-like protein;
AltName: Full=Zinc finger protein HRX;
Contains:
RecName: Full=MLL cleavage product N320;
AltName: Full=N-terminal cleavage product of 320 kDa;
Short=p320;
Contains:
RecName: Full=MLL cleavage product C180;
AltName: Full=C-terminal cleavage product of 180 kDa;
Short=p180;
Name=KMT2A; Synonyms=ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1423624; DOI=10.1016/0092-8674(92)90602-9;
Tkachuk D.C., Kohler S., Cleary M.L.;
"Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal
translocations in acute leukemias.";
Cell 71:691-700(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANT GLY-30.
PubMed=8703835; DOI=10.1046/j.1365-2141.1996.d01-1748.x;
Nilson I., Loechner K., Siegler G., Greil J., Beck J.D., Fey G.H.,
Marschalek R.;
"Exon/intron structure of the human ALL-1 (MLL) gene involved in
translocations to chromosomal region 11q23 and acute leukaemias.";
Br. J. Haematol. 93:966-972(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-53; LYS-502;
THR-2319; ARG-2354; ARG-2387; ILE-3714 AND ALA-3773.
NIEHS SNPs program;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1909.
PubMed=8378076;
Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S.,
Kodera Y., Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R.;
"Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19)
leukemia.";
Oncogene 8:2617-2625(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 63-3969 (ISOFORM 3), AND CHROMOSOMAL
TRANSLOCATION WITH AFF1/MLLT2.
PubMed=1423625; DOI=10.1016/0092-8674(92)90603-A;
Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G.,
Croce C.M., Canaani E.;
"The t(4;11) chromosome translocation of human acute leukemias fuses
the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene.";
Cell 71:701-708(1992).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 812-3969.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1112-1140 AND 1552-162, AND
NUCLEOTIDE SEQUENCE [MRNA] OF 1317-2328.
TISSUE=Brain;
PubMed=1303259; DOI=10.1038/ng1092-113;
Djabali M., Selleri L., Parry P., Bower M., Young B.D., Evans G.A.;
"A trithorax-like gene is interrupted by chromosome 11q23
translocations in acute leukaemias.";
Nat. Genet. 2:113-118(1992).
[9]
ERRATUM.
PubMed=8401594;
Djabali M., Selleri L., Parry P., Bower M., Young B., Evans G.A.;
Nat. Genet. 4:431-431(1993).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1212-1603 (ISOFORM 3).
PubMed=7794749; DOI=10.1111/j.1365-2141.1995.tb05151.x;
Marschalek R., Greil J., Lochner K., Nilson I., Siegler G.,
Zweckbronner I., Beck J.D., Fey G.H.;
"Molecular analysis of the chromosomal breakpoint and fusion
transcripts in the acute lymphoblastic SEM cell line with chromosomal
translocation t(4;11).";
Br. J. Haematol. 90:308-320(1995).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1654 (ISOFORM 2).
PubMed=7598802; DOI=10.1089/dna.1995.14.475;
Mbangkollo D., Burnett R., McCabe N., Thirman M., Gill H., Yu H.,
Rowley J.D., Diaz M.O.;
"The human MLL gene: nucleotide sequence, homology to the Drosophila
trx zinc-finger domain, and alternative splicing.";
DNA Cell Biol. 14:475-483(1995).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1538.
PubMed=8162575;
Gu Y., Alder H., Nakamura T., Schichman S.A., Prasad R., Canaani O.,
Saito H., Croce C.M., Canaani E.;
"Sequence analysis of the breakpoint cluster region in the ALL-1 gene
involved in acute leukemia.";
Cancer Res. 54:2327-2330(1994).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1687 (ISOFORM 3), AND CHROMOSOMAL
TRANSLOCATION WITH GAS7.
PubMed=10706619; DOI=10.1073/pnas.050397097;
Megonigal M.D., Cheung N.-K.V., Rappaport E.F., Nowell P.C.,
Wilson R.B., Jones D.H., Addya K., Leonard D.G.B., Kushner B.H.,
Williams T.M., Lange B.J., Felix C.A.;
"Detection of leukemia-associated MLL-GAS7 translocation early during
chemotherapy with DNA topoisomerase II inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 97:2814-2819(2000).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1421-1540.
PubMed=8414518;
Forster A., Rabbitts T.H.;
"A method for identifying genes within yeast artificial chromosomes:
application to isolation of MLL fusion cDNAs from acute leukaemia
translocations.";
Oncogene 8:3157-3160(1993).
[15]
PROTEIN SEQUENCE OF 2719-2730, CLEAVAGE, SUBUNIT, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 2718-ASP--VAL-2720.
PubMed=12482972; DOI=10.1128/MCB.23.1.186-194.2003;
Hsieh J.J.-D., Ernst P., Erdjument-Bromage H., Tempst P.,
Korsmeyer S.J.;
"Proteolytic cleavage of MLL generates a complex of N- and C-terminal
fragments that confers protein stability and subnuclear
localization.";
Mol. Cell. Biol. 23:186-194(2003).
[16]
CHROMOSOMAL TRANSLOCATION WITH CENPK.
PubMed=8950979;
Taki T., Hayashi Y., Taniwaki M., Seto M., Ueda R., Hanada R.,
Suzukawa K., Yokota J., Morishita K.;
"Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha,
by a complex translocation involving chromosomes 5, 6, 8 and 11 in
infant leukemia.";
Oncogene 13:2121-2130(1996).
[17]
CHROMOSOMAL TRANSLOCATION WITH ABI1.
PubMed=9694699;
Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F.,
Yanagisawa M., Hayashi Y.;
"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene
in acute myeloid leukemia with t(10;11)(p11.2;q23).";
Blood 92:1125-1130(1998).
[18]
INTERACTION WITH SBF1.
PubMed=9537414; DOI=10.1038/ng0498-331;
Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.;
"Association of SET domain and myotubularin-related proteins modulates
growth control.";
Nat. Genet. 18:331-337(1998).
[19]
INTERACTION WITH PPP1R15A, DISEASE, AND FUNCTION.
PubMed=10490642; DOI=10.1128/MCB.19.10.7050;
Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M.,
Fornace A.J. Jr., Tkachuk D.C.;
"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and
associate with the GADD34 and hSNF5/INI1 proteins.";
Mol. Cell. Biol. 19:7050-7060(1999).
[20]
CHROMOSOMAL TRANSLOCATION WITH AFF4.
TISSUE=Placenta;
PubMed=10588740; DOI=10.1073/pnas.96.25.14535;
Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y.;
"AF5q31, a newly identified AF4-related gene, is fused to MLL in
infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23).";
Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999).
[21]
CHROMOSOMAL TRANSLOCATION WITH NCKIPSD/AF3P21.
PubMed=10648423;
Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H.;
"Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed
lineage leukemia protein in a therapy-related leukemia with
t(3;11)(p21;q23).";
Blood 95:1066-1068(2000).
[22]
CHROMOSOMAL TRANSLOCATION WITH GMPS.
PubMed=11110714;
Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D.,
Rappaport E.F., Felix C.A.;
"t(3;11) translocation in treatment-related acute myeloid leukemia
fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase)
gene.";
Blood 96:4360-4362(2000).
[23]
CHROMOSOMAL TRANSLOCATION WITH LPP.
PubMed=11433529; DOI=10.1002/gcc.1157;
Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L.,
Guilhot F., Larsen C.J., Brizard A., Roche J.;
"Human LPP gene is fused to MLL in a secondary acute leukemia with a
t(3;11) (q28;q23).";
Genes Chromosomes Cancer 31:382-389(2001).
[24]
CHROMOSOMAL TRANSLOCATION WITH TET1.
PubMed=12124344;
Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y.;
"LCX, leukemia-associated protein with a CXXC domain, is fused to MLL
in acute myeloid leukemia with trilineage dysplasia having
t(10;11)(q22;q23).";
Cancer Res. 62:4075-4080(2002).
[25]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12453419; DOI=10.1016/S1097-2765(02)00740-2;
Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T.,
Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E.;
"ALL-1 is a histone methyltransferase that assembles a supercomplex of
proteins involved in transcriptional regulation.";
Mol. Cell 10:1119-1128(2002).
[26]
CLEAVAGE, INTERACTION WITH TASP1, AND MUTAGENESIS OF 2666-ASP-GLY-2667
AND 2718-ASP--VAL-2720.
PubMed=14636557; DOI=10.1016/S0092-8674(03)00816-X;
Hsieh J.J.-D., Cheng E.H.-Y., Korsmeyer S.J.;
"Taspase1: a threonine aspartase required for cleavage of MLL and
proper HOX gene expression.";
Cell 115:293-303(2003).
[27]
CHROMOSOMAL TRANSLOCATION WITH ZFYVE19 AND KNL1.
PubMed=12618766; DOI=10.1038/sj.onc.1206273;
Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J.,
Rowley J.D.;
"A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene
MPFYVE on chromosome 15.";
Oncogene 22:1400-1410(2003).
[28]
CHROMOSOMAL TRANSLOCATION WITH KNL1.
PubMed=12618768; DOI=10.1038/sj.onc.1206272;
Kuefer M.U., Chinwalla V., Zeleznik-Le N.J., Behm F.G., Naeve C.W.,
Rakestraw K.M., Mukatira S.T., Raimondi S.C., Morris S.W.;
"Characterization of the MLL partner gene AF15q14 involved in
t(11;15)(q23;q14).";
Oncogene 22:1418-1424(2003).
[29]
CHROMOSOMAL TRANSLOCATION WITH DAB2IP.
PubMed=14978793; DOI=10.1002/gcc.20004;
von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S.,
Falkenburg J.H.F., Kluin P.M., Schuuring E.;
"Identification of a novel RAS GTPase-activating protein (RASGAP) gene
at 9q34 as an MLL fusion partner in a patient with de novo acute
myeloid leukemia.";
Genes Chromosomes Cancer 39:324-334(2004).
[30]
CHROMOSOMAL TRANSLOCATION WITH SEPT11.
PubMed=14999297; DOI=10.1038/sj.leu.2403334;
Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y.,
Fujii N., Tanimoto M., Fujita S.;
"FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell
line CNLBC1 derived from chronic neutrophilic leukemia in
transformation with t(4;11)(q21;q23).";
Leukemia 18:998-1005(2004).
[31]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
Kitabayashi I., Herr W., Cleary M.L.;
"Leukemia proto-oncoprotein MLL forms a SET1-like histone
methyltransferase complex with menin to regulate Hox gene
expression.";
Mol. Cell. Biol. 24:5639-5649(2004).
[32]
CHROMOSOMAL TRANSLOCATION WITH FRYL.
PubMed=16061630; DOI=10.1158/0008-5472.CAN-05-1325;
Hayette S., Cornillet-Lefebvre P., Tigaud I., Struski S.,
Forissier S., Berchet A., Doll D., Gillot L., Brahim W., Delabesse E.,
Magaud J.-P., Rimokh R.;
"AF4p12, a human homologue to the furry gene of Drosophila, as a novel
MLL fusion partner.";
Cancer Res. 65:6521-6525(2005).
[33]
FUNCTION, IDENTIFICATION IN THE MLL1/MLL COMPLEX, AND INTERACTION WITH
KAT8.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[34]
DOMAIN 9AATAD.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[35]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=17500065; DOI=10.1074/jbc.M701574200;
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
methyltransferase complex.";
J. Biol. Chem. 282:20395-20406(2007).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-518;
SER-680; THR-840; SER-1056; THR-1845; SER-2098; THR-2147; SER-2151;
THR-2525; SER-2955; SER-3036; THR-3372 AND SER-3511, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[38]
FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH
WDR5, AND MUTAGENESIS OF ASN-3906 AND TYR-3942.
PubMed=19556245; DOI=10.1074/jbc.M109.014498;
Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
"On the mechanism of multiple lysine methylation by the human mixed
lineage leukemia protein-1 (MLL1) core complex.";
J. Biol. Chem. 284:24242-24256(2009).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-2098 AND
SER-3515, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-1130 AND LYS-1235,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-926;
SER-2955 AND THR-3372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2201, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[44]
INVOLVEMENT IN WDSTS.
PubMed=22795537; DOI=10.1016/j.ajhg.2012.06.008;
Jones W.D., Dafou D., McEntagart M., Woollard W.J., Elmslie F.V.,
Holder-Espinasse M., Irving M., Saggar A.K., Smithson S.,
Trembath R.C., Deshpande C., Simpson M.A.;
"De novo mutations in MLL cause Wiedemann-Steiner syndrome.";
Am. J. Hum. Genet. 91:358-364(2012).
[45]
INTERACTION WITH ZNF335.
PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
Mahajnah M., Shenhav R., Walsh C.A.;
"Microcephaly gene links trithorax and REST/NRSF to control neural
stem cell proliferation and differentiation.";
Cell 151:1097-1112(2012).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858; SER-2098;
THR-2525; SER-2611; SER-2796; SER-2955; SER-3036; SER-3511 AND
SER-3527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1837, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2528, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[49]
STRUCTURE BY NMR OF 1146-1214 IN COMPLEX WITH ZINC, DOMAIN CXXC-TYPE
ZINC-FINGER, DNA-BINDING, AND MUTAGENESIS OF ARG-1151; ARG-1153;
ARG-1154; CYS-1155; CYS-1158; CYS-1161; GLN-1162; ASP-1166; CYS-1167;
CYS-1170; ASN-1172; CYS-1173; ASP-1175; LYS-1176; 1178-LYS--GLY-1181;
LYS-1178; PHE-1179; ASN-1183; LYS-1185; LYS-1186; GLN-1187; CYS-1188;
CYS-1189; ARG-1192; LYS-1193; CYS-1194; GLN-1195 AND ASN-1196.
PubMed=16990798; DOI=10.1038/sj.emboj.7601340;
Allen M.D., Grummitt C.G., Hilcenko C., Min S.Y., Tonkin L.M.,
Johnson C.M., Freund S.M., Bycroft M., Warren A.J.;
"Solution structure of the nonmethyl-CpG-binding CXXC domain of the
leukaemia-associated MLL histone methyltransferase.";
EMBO J. 25:4503-4512(2006).
[50]
STRUCTURE BY NMR OF 2842-2869 IN COMPLEX WITH CREBBP.
PubMed=16253272; DOI=10.1016/j.jmb.2005.09.059;
De Guzman R.N., Goto N.K., Dyson H.J., Wright P.E.;
"Structural basis for cooperative transcription factor binding to the
CBP coactivator.";
J. Mol. Biol. 355:1005-1013(2006).
[51]
X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 3764-3776 IN COMPLEX WITH
WDR5.
PubMed=18829459; DOI=10.1074/jbc.C800164200;
Patel A., Dharmarajan V., Cosgrove M.S.;
"Structure of WDR5 bound to mixed lineage leukemia protein-1
peptide.";
J. Biol. Chem. 283:32158-32161(2008).
[52]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3785-3969 IN COMPLEX WITH
ZINC; S-ADENOSYL-L-HOMOCYSTEINE AND HISTONE H3 PEPTIDE, CATALYTIC
ACTIVITY, DOMAIN SET, INTERACTION WITH ASH2L AND RBBP5, AND
MUTAGENESIS OF TYR-3858; GLN-3867; ASP-3869; ARG-3871; GLU-3872;
TYR-3874; LYS-3878 AND TYR-3942.
PubMed=19187761; DOI=10.1016/j.molcel.2008.12.029;
Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R.;
"Structural basis for the requirement of additional factors for MLL1
SET domain activity and recognition of epigenetic marks.";
Mol. Cell 33:181-191(2009).
-!- FUNCTION: Histone methyltransferase that plays an essential role
in early development and hematopoiesis. Catalytic subunit of the
MLL1/MLL complex, a multiprotein complex that mediates both
methylation of 'Lys-4' of histone H3 (H3K4me) complex and
acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL
complex, it specifically mediates H3K4me, a specific tag for
epigenetic transcriptional activation. Has weak methyltransferase
activity by itself, and requires other component of the MLL1/MLL
complex to obtain full methyltransferase activity. Has no activity
toward histone H3 phosphorylated on 'Thr-3', less activity toward
H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher
activity toward H3 acetylated on 'Lys-9'. Required for
transcriptional activation of HOXA9. Promotes PPP1R15A-induced
apoptosis. Plays a critical role in the control of circadian gene
expression and is essential for the transcriptional activation
mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a
permissive chromatin state for circadian transcription by
mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me)
and this histone modification directs the circadian acetylation at
H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to
chromatin (By similarity). {ECO:0000250|UniProtKB:P55200,
ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12453419,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:19556245}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:12453419, ECO:0000269|PubMed:19187761}.
-!- SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL
cleavage product C180 (via SET and FYRC domains). Component of
some MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as
well as the facultative components BAP18, CHD8, E2F6, HSP70,
INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1,
PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1,
TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with WDR5; the
interaction is direct. Interacts with KAT8/MOF; the interaction is
direct. Interacts with SBF1 and PPP1R15A. Interacts with ZNF335.
Interacts with CLOCK and ARNTL/BMAL1 in a circadian manner (By
similarity). {ECO:0000250|UniProtKB:P55200,
ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12482972,
ECO:0000269|PubMed:14636557, ECO:0000269|PubMed:15199122,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16253272,
ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:17500065,
ECO:0000269|PubMed:18829459, ECO:0000269|PubMed:19187761,
ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:23178126,
ECO:0000269|PubMed:9537414}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-591370, EBI-591370;
P10275:AR; NbExp=2; IntAct=EBI-591370, EBI-608057;
Q9WTL8:Arntl (xeno); NbExp=3; IntAct=EBI-591370, EBI-644534;
Q9UBL3-3:ASH2L; NbExp=4; IntAct=EBI-591370, EBI-16130425;
Q6P1J9:CDC73; NbExp=4; IntAct=EBI-591370, EBI-930143;
O08785:Clock (xeno); NbExp=3; IntAct=EBI-591370, EBI-79859;
P45481:Crebbp (xeno); NbExp=7; IntAct=EBI-591370, EBI-296306;
Q6PD62:CTR9; NbExp=5; IntAct=EBI-591370, EBI-1019583;
P68431:HIST1H3D; NbExp=11; IntAct=EBI-591370, EBI-79722;
Q92794:KAT6A; NbExp=10; IntAct=EBI-2638616, EBI-948013;
Q9H7Z6:KAT8; NbExp=3; IntAct=EBI-591370, EBI-896414;
O00255-2:MEN1; NbExp=12; IntAct=EBI-591370, EBI-9869387;
Q8N7H5:PAF1; NbExp=4; IntAct=EBI-591370, EBI-2607770;
Q02548:PAX5; NbExp=2; IntAct=EBI-2610266, EBI-296331;
Q9UNP9:PPIE; NbExp=4; IntAct=EBI-591370, EBI-591818;
Q15291:RBBP5; NbExp=9; IntAct=EBI-591370, EBI-592823;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-591370, EBI-1802965;
Q13309-1:SKP2; NbExp=2; IntAct=EBI-591370, EBI-15490084;
P61964:WDR5; NbExp=13; IntAct=EBI-591370, EBI-540834;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482972}.
-!- SUBCELLULAR LOCATION: MLL cleavage product N320: Nucleus.
-!- SUBCELLULAR LOCATION: MLL cleavage product C180: Nucleus.
Note=Localizes to a diffuse nuclear pattern when not associated
with MLL cleavage product N320.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q03164-1; Sequence=Displayed;
Name=2; Synonyms=14P-18B;
IsoId=Q03164-2; Sequence=VSP_006666;
Name=3;
IsoId=Q03164-3; Sequence=VSP_046879;
-!- TISSUE SPECIFICITY: Heart, lung, brain and T- and B-lymphocytes.
-!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- DOMAIN: The SET domain structure is atypical and is not in an
optimal position to have methyltransferase activity. It requires
other components of the MLL1/MLL complex, such as ASH2L or RBBP5,
to order the active site and obtain optimal histone
methyltransferase activity. {ECO:0000269|PubMed:19187761}.
-!- DOMAIN: The CXXC-type zinc finger binds bind to nonmethyl-CpG
dinucleotides. {ECO:0000269|PubMed:16990798}.
-!- PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product
N320 and MLL cleavage product C180, which reassemble through a
non-covalent association. 2 cleavage sites exist, cleavage site 1
(CS1) and cleavage site 2 (CS2), to generate MLL cleavage products
N320 and C180. CS2 is the major site.
{ECO:0000269|PubMed:12482972, ECO:0000269|PubMed:14636557}.
-!- DISEASE: Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A
syndrome characterized by hairy elbows (hypertrichosis cubiti),
intellectual disability, a distinctive facial appearance, and
short stature. Facial characteristics include long eyelashes,
thick or arched eyebrows with a lateral flare, and downslanting
and vertically narrow palpebral fissures.
{ECO:0000269|PubMed:22795537}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Chromosomal aberrations involving KMT2A are a cause
of acute leukemias. Translocation t(1;11)(q21;q23) with
MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21;
translocation t(3,11)(q25,q23) with GMPS; translocation
t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion
ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation
t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation
t(6;11)(q27;q23) with AFDN; translocation t(9;11)(p22;q23) with
MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1;
translocation t(10;11)(p12;q23) with MLLT10/AF10;
t(11;15)(q23;q14) with KNL1 and ZFYVE19; translocation
t(11;17)(q23;q21) with MLLT6/AF17; translocation
t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3)
with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7;
translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation
t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with
TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation
t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A-
MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to
unfused KMT2A, inhibit PPP1R15A-induced apoptosis.
{ECO:0000269|PubMed:10490642}.
-!- DISEASE: Note=A chromosomal aberration involving KMT2A may be a
cause of chronic neutrophilic leukemia. Translocation
t(4;11)(q21;q23) with SEPT11. {ECO:0000269|PubMed:10490642}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAA58669.1; Type=Frameshift; Positions=317, 380; Evidence={ECO:0000305};
Sequence=AAG26332.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAD92745.1; Type=Frameshift; Positions=1098; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MLLID13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mll/";
-----------------------------------------------------------------------
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EMBL; L04284; AAA58669.1; ALT_FRAME; mRNA.
EMBL; Z69744; CAA93625.1; -; Genomic_DNA.
EMBL; Z69745; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69746; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69747; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69748; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69749; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69750; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69751; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69752; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69753; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69754; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69755; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69756; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69757; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69758; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69759; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69760; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69761; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69762; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69763; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69764; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69765; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69766; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69767; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69768; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69769; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69770; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69772; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69773; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69774; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69775; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69776; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69777; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69778; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69779; CAA93625.1; JOINED; Genomic_DNA.
EMBL; Z69780; CAA93625.1; JOINED; Genomic_DNA.
EMBL; AY373585; AAQ63624.1; -; Genomic_DNA.
EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D14540; BAA03407.1; -; mRNA.
EMBL; AB209508; BAD92745.1; ALT_FRAME; mRNA.
EMBL; L04731; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L01986; AAA92511.1; -; mRNA.
EMBL; X83604; CAA58584.1; -; Genomic_DNA.
EMBL; S78570; AAB34770.1; -; mRNA.
EMBL; U04737; AAA18644.1; -; Genomic_DNA.
EMBL; S66432; AAB28545.1; -; mRNA.
EMBL; AF232001; AAG26335.2; -; mRNA.
EMBL; AF231998; AAG26332.2; ALT_SEQ; mRNA.
CCDS; CCDS31686.1; -. [Q03164-1]
CCDS; CCDS55791.1; -. [Q03164-3]
PIR; A44265; A44265.
PIR; I52578; I52578.
PIR; I53035; I53035.
RefSeq; NP_001184033.1; NM_001197104.1. [Q03164-3]
RefSeq; NP_005924.2; NM_005933.3. [Q03164-1]
UniGene; Hs.258855; -.
PDB; 2AGH; NMR; -; C=2840-2869.
PDB; 2J2S; NMR; -; A=1143-1214.
PDB; 2JYI; NMR; -; A=1147-1203.
PDB; 2KKF; NMR; -; A=1147-1203.
PDB; 2KU7; NMR; -; A=1585-1628.
PDB; 2KYU; NMR; -; A=1564-1628.
PDB; 2LXS; NMR; -; B=2840-2858.
PDB; 2LXT; NMR; -; B=2840-2858.
PDB; 2MSR; NMR; -; A=140-160.
PDB; 2MTN; NMR; -; A=110-160.
PDB; 2W5Y; X-ray; 2.00 A; A=3785-3969.
PDB; 2W5Z; X-ray; 2.20 A; A=3785-3969.
PDB; 3EG6; X-ray; 1.72 A; C=3762-3773.
PDB; 3EMH; X-ray; 1.37 A; B=3764-3776.
PDB; 3LQH; X-ray; 1.72 A; A=1566-1784.
PDB; 3LQI; X-ray; 1.92 A; A/B/C=1566-1784.
PDB; 3LQJ; X-ray; 1.90 A; A/B=1566-1784.
PDB; 3P4F; X-ray; 2.35 A; C=3761-3770.
PDB; 3U85; X-ray; 3.00 A; B=6-25.
PDB; 3U88; X-ray; 3.00 A; M/N=103-153.
PDB; 4ESG; X-ray; 1.70 A; C/D=3755-3771.
PDB; 4GQ6; X-ray; 1.55 A; B=6-15.
PDB; 4NW3; X-ray; 2.82 A; A=1147-1204.
PDB; 5F5E; X-ray; 1.80 A; A=3813-3969.
PDB; 5F6L; X-ray; 1.90 A; A=3813-3969.
PDBsum; 2AGH; -.
PDBsum; 2J2S; -.
PDBsum; 2JYI; -.
PDBsum; 2KKF; -.
PDBsum; 2KU7; -.
PDBsum; 2KYU; -.
PDBsum; 2LXS; -.
PDBsum; 2LXT; -.
PDBsum; 2MSR; -.
PDBsum; 2MTN; -.
PDBsum; 2W5Y; -.
PDBsum; 2W5Z; -.
PDBsum; 3EG6; -.
PDBsum; 3EMH; -.
PDBsum; 3LQH; -.
PDBsum; 3LQI; -.
PDBsum; 3LQJ; -.
PDBsum; 3P4F; -.
PDBsum; 3U85; -.
PDBsum; 3U88; -.
PDBsum; 4ESG; -.
PDBsum; 4GQ6; -.
PDBsum; 4NW3; -.
PDBsum; 5F5E; -.
PDBsum; 5F6L; -.
ProteinModelPortal; Q03164; -.
SMR; Q03164; -.
BioGrid; 110443; 100.
CORUM; Q03164; -.
DIP; DIP-29221N; -.
ELM; Q03164; -.
IntAct; Q03164; 50.
MINT; MINT-4532017; -.
STRING; 9606.ENSP00000436786; -.
BindingDB; Q03164; -.
ChEMBL; CHEMBL1293299; -.
iPTMnet; Q03164; -.
PhosphoSitePlus; Q03164; -.
BioMuta; KMT2A; -.
DMDM; 146345435; -.
EPD; Q03164; -.
MaxQB; Q03164; -.
PaxDb; Q03164; -.
PeptideAtlas; Q03164; -.
PRIDE; Q03164; -.
Ensembl; ENST00000389506; ENSP00000374157; ENSG00000118058. [Q03164-1]
Ensembl; ENST00000534358; ENSP00000436786; ENSG00000118058. [Q03164-3]
GeneID; 4297; -.
KEGG; hsa:4297; -.
UCSC; uc001pta.4; human. [Q03164-1]
CTD; 4297; -.
DisGeNET; 4297; -.
EuPathDB; HostDB:ENSG00000118058.20; -.
GeneCards; KMT2A; -.
HGNC; HGNC:7132; KMT2A.
HPA; CAB017794; -.
HPA; CAB024270; -.
HPA; HPA044910; -.
MalaCards; KMT2A; -.
MIM; 159555; gene+phenotype.
MIM; 605130; phenotype.
neXtProt; NX_Q03164; -.
OpenTargets; ENSG00000118058; -.
Orphanet; 402017; 'Acute myeloid leukemia with t(9;11)(p22;q23)'.
Orphanet; 98837; Acute biphenotypic leukemia.
Orphanet; 98831; Acute myeloid leukemia with 11q23 abnormalities.
Orphanet; 98835; Acute undifferentiated leukemia.
Orphanet; 98836; Bilineal acute leukemia.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 319182; Wiedemann-Steiner syndrome.
PharmGKB; PA241; -.
eggNOG; KOG1084; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOVERGEN; HBG051927; -.
InParanoid; Q03164; -.
KO; K09186; -.
OMA; RIMSPMR; -.
OrthoDB; EOG091G001P; -.
PhylomeDB; Q03164; -.
TreeFam; TF319820; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
SIGNOR; Q03164; -.
ChiTaRS; KMT2A; human.
EvolutionaryTrace; Q03164; -.
GeneWiki; MLL_(gene); -.
GenomeRNAi; 4297; -.
PRO; PR:Q03164; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000118058; -.
CleanEx; HS_MLL; -.
ExpressionAtlas; Q03164; baseline and differential.
Genevisible; Q03164; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003680; F:AT DNA binding; NAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; TAS:UniProtKB.
GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
GO; GO:0044648; P:histone H3-K4 dimethylation; IEA:Ensembl.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:BHF-UCL.
GO; GO:0043984; P:histone H4-K16 acetylation; IMP:UniProtKB.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IEA:Ensembl.
GO; GO:2001040; P:positive regulation of cellular response to drug; IMP:BHF-UCL.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032411; P:positive regulation of transporter activity; IMP:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0071440; P:regulation of histone H3-K14 acetylation; ISS:UniProtKB.
GO; GO:1901674; P:regulation of histone H3-K27 acetylation; IEA:Ensembl.
GO; GO:2000615; P:regulation of histone H3-K9 acetylation; ISS:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR034732; EPHD.
InterPro; IPR003889; FYrich_C.
InterPro; IPR003888; FYrich_N.
InterPro; IPR016569; MeTrfase_trithorax.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR002857; Znf_CXXC.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 2.
Pfam; PF00856; SET; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
SMART; SM00297; BROMO; 1.
SMART; SM00542; FYRC; 1.
SMART; SM00541; FYRN; 1.
SMART; SM00249; PHD; 4.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51805; EPHD; 1.
PROSITE; PS51543; FYRC; 1.
PROSITE; PS51542; FYRN; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS51058; ZF_CXXC; 1.
PROSITE; PS01359; ZF_PHD_1; 3.
PROSITE; PS50016; ZF_PHD_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Biological rhythms; Bromodomain; Chromatin regulator;
Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 3969 Histone-lysine N-methyltransferase 2A.
/FTId=PRO_0000124876.
CHAIN 1 2718 MLL cleavage product N320.
/FTId=PRO_0000390949.
CHAIN 2719 3969 MLL cleavage product C180.
/FTId=PRO_0000390950.
DOMAIN 1703 1748 Bromo; divergent. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 2018 2074 FYR N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00875}.
DOMAIN 3666 3747 FYR C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00876}.
DOMAIN 3829 3945 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 3953 3969 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 169 180 A.T hook 1.
DNA_BIND 217 227 A.T hook 2.
DNA_BIND 301 309 A.T hook 3.
ZN_FING 1147 1195 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 1431 1482 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1479 1533 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1566 1627 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1870 1910 C2HC pre-PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 1931 1978 PHD-type 4. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 3906 3907 S-adenosyl-L-methionine binding.
MOTIF 2847 2855 9aaTAD. {ECO:0000269|PubMed:17467953}.
COMPBIAS 17 102 Ala/Gly/Ser-rich.
COMPBIAS 137 143 Poly-Gly.
COMPBIAS 561 564 Poly-Pro.
COMPBIAS 568 571 Poly-Pro.
METAL 3909 3909 Zinc. {ECO:0000269|PubMed:16990798,
ECO:0000269|PubMed:19187761}.
METAL 3957 3957 Zinc. {ECO:0000269|PubMed:16990798,
ECO:0000269|PubMed:19187761}.
METAL 3959 3959 Zinc. {ECO:0000269|PubMed:16990798,
ECO:0000269|PubMed:19187761}.
METAL 3964 3964 Zinc. {ECO:0000269|PubMed:16990798,
ECO:0000269|PubMed:19187761}.
BINDING 3839 3839 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3841 3841 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3883 3883 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3958 3958 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
SITE 1334 1335 Breakpoint for translocation to form
KMT2A-ZFYVE19 oncogene.
SITE 1362 1363 Breakpoint for translocation to form
KMT2A-AF3P21 and KMT2A-KNL1 oncogenes.
SITE 1362 1363 Breakpoint for translocation to form
KMT2A-CENPK oncogene.
SITE 1362 1362 Breakpoint for translocation to form
KMT2A-FRYL fusion protein.
SITE 1406 1407 Breakpoint for translocation to form
KMT2A-AFF4 fusion protein.
SITE 1444 1445 Breakpoint for translocation to form
KMT2A-GAS7 oncogene.
SITE 1444 1445 Breakpoint for translocation to form
KMT2A-LPP.
SITE 2666 2667 Cleavage; by TASP1, site 1.
{ECO:0000269|PubMed:14636557}.
SITE 2718 2719 Cleavage; by TASP1, site 2.
{ECO:0000269|PubMed:14636557}.
SITE 3765 3765 Important for WDR5-recognition and
binding. {ECO:0000269|PubMed:19556245}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 239 239 N6-acetyllysine.
{ECO:0000250|UniProtKB:P55200}.
MOD_RES 373 373 N6-acetyllysine.
{ECO:0000250|UniProtKB:P55200}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 840 840 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 926 926 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1056 1056 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1130 1130 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1235 1235 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1837 1837 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1845 1845 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1858 1858 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 2098 2098 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2147 2147 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2151 2151 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2201 2201 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 2525 2525 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2611 2611 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2796 2796 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2955 2955 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2958 2958 N6-acetyllysine.
{ECO:0000250|UniProtKB:P55200}.
MOD_RES 3036 3036 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 3372 3372 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 3462 3462 N6-acetyllysine.
{ECO:0000250|UniProtKB:P55200}.
MOD_RES 3511 3511 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 3515 3515 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 3527 3527 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 2528 2528 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1407 1444 Missing (in isoform 2).
{ECO:0000303|PubMed:7598802}.
/FTId=VSP_006666.
VAR_SEQ 1603 1603 S -> SGTE (in isoform 3).
{ECO:0000303|PubMed:10706619,
ECO:0000303|PubMed:1423625}.
/FTId=VSP_046879.
VARIANT 30 30 A -> G (in dbSNP:rs9332745).
{ECO:0000269|PubMed:8703835}.
/FTId=VAR_021317.
VARIANT 53 53 A -> V (in dbSNP:rs9332747).
{ECO:0000269|Ref.3}.
/FTId=VAR_021318.
VARIANT 502 502 E -> K (in dbSNP:rs9332772).
{ECO:0000269|Ref.3}.
/FTId=VAR_021319.
VARIANT 1975 1975 Q -> P (in dbSNP:rs693598).
/FTId=VAR_052652.
VARIANT 2319 2319 S -> T (in dbSNP:rs9332837).
{ECO:0000269|Ref.3}.
/FTId=VAR_021320.
VARIANT 2354 2354 P -> R (in dbSNP:rs9332838).
{ECO:0000269|Ref.3}.
/FTId=VAR_021321.
VARIANT 2387 2387 Q -> R (in dbSNP:rs9332839).
{ECO:0000269|Ref.3}.
/FTId=VAR_021322.
VARIANT 3714 3714 V -> I (in dbSNP:rs9332859).
{ECO:0000269|Ref.3}.
/FTId=VAR_021323.
VARIANT 3773 3773 S -> A (in dbSNP:rs9332861).
{ECO:0000269|Ref.3}.
/FTId=VAR_021324.
MUTAGEN 1151 1151 R->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1153 1153 R->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 1154 1154 R->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1155 1155 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1158 1158 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1161 1161 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1162 1162 Q->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 1166 1166 D->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1167 1167 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1170 1170 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1172 1172 N->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 1173 1173 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1175 1175 D->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1176 1176 K->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1178 1181 KFGG->AAAA: Abolishes zinc-binding,
leading to unfold the CXXC-type zinc
finger and abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1178 1178 K->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1179 1179 F->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1183 1183 N->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1185 1185 K->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1186 1186 K->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1187 1187 Q->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1188 1188 C->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 1189 1189 C->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1192 1192 R->A: Abolishes zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1193 1193 K->A: Impairs DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1194 1194 C->A: Impair zinc-binding, leading to
unfold the CXXC-type zinc finger and
abolish DNA-binding.
{ECO:0000269|PubMed:16990798}.
MUTAGEN 1195 1195 Q->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 1196 1196 N->A: No effect on stability or DNA-
binding. {ECO:0000269|PubMed:16990798}.
MUTAGEN 2666 2667 DG->AA: Reduces cleavage without
abolishing it. Abolishes cleavage by
TASP1; when associated with 2718-A--A-
2720. {ECO:0000269|PubMed:14636557}.
MUTAGEN 2718 2720 DGV->AAA: Abolishes cleavage by TASP1;
when associated with 2666-A-A-2667.
{ECO:0000269|PubMed:12482972,
ECO:0000269|PubMed:14636557}.
MUTAGEN 3858 3858 Y->A: Impairs methyltransferase activity
toward unmodified or monomethylated
H3K4me. {ECO:0000269|PubMed:19187761}.
MUTAGEN 3858 3858 Y->F: Slightly affects methyltransferase
activity toward unmodified or
monomethylated H3K4me.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3867 3867 Q->A: Slightly affects methyltransferase
activity of the enzyme alone, while it
impairs methyltransferase activity in
complex; when associated with A-3871.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3869 3869 D->A: Does not affect methyltransferase
activity of the enzyme alone or in
complex; when associated with A-3872.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3871 3871 R->A: Slightly affects methyltransferase
activity of the enzyme alone, while it
impairs methyltransferase activity in
complex; when associated with A-3867.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3872 3872 E->A: Does not affect methyltransferase
activity of the enzyme alone or in
complex; when associated with A-3869.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3874 3874 Y->A: Affects methyltransferase activity
of the enzyme alone, while it does not
affect methyltransferase activity in
complex; when associated with A-3878.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3878 3878 K->A: Affects methyltransferase activity
of the enzyme alone, while it does not
affect methyltransferase activity in
complex; when associated with A-3874.
{ECO:0000269|PubMed:19187761}.
MUTAGEN 3906 3906 N->A: Loss of the histone H3
methyltransferase activity.
{ECO:0000269|PubMed:19556245}.
MUTAGEN 3942 3942 Y->A,F: Impairs methyltransferase
activity toward unmodified or
monomethylated H3K4me.
{ECO:0000269|PubMed:19187761,
ECO:0000269|PubMed:19556245}.
MUTAGEN 3942 3942 Y->F: Shifts from a specific
monomethyltransferase to a di- and
trimethyltransferase activity.
{ECO:0000269|PubMed:19187761,
ECO:0000269|PubMed:19556245}.
CONFLICT 144 144 E -> ELTTQIPCSWRTKGHIHDKKTEPFRLLAWSWCLN
(in Ref. 2; CAA93625). {ECO:0000305}.
CONFLICT 556 556 Q -> E (in Ref. 2; CAA93625 and 6;
L04731). {ECO:0000305}.
CONFLICT 1347 1347 V -> A (in Ref. 13; AAG26335).
{ECO:0000305}.
CONFLICT 1487 1487 R -> G (in Ref. 12; AAA18644).
{ECO:0000305}.
CONFLICT 1490 1490 Q -> R (in Ref. 13; AAG26335).
{ECO:0000305}.
CONFLICT 1507 1507 P -> L (in Ref. 13; AAG26335).
{ECO:0000305}.
CONFLICT 1513 1513 N -> T (in Ref. 13; AAG26335).
{ECO:0000305}.
CONFLICT 1600 1600 E -> G (in Ref. 13; AAG26335).
{ECO:0000305}.
CONFLICT 1616 1616 S -> C (in Ref. 11; AAB34770).
{ECO:0000305}.
CONFLICT 1937 1937 Q -> H (in Ref. 8; AAA92511).
{ECO:0000305}.
CONFLICT 2181 2181 P -> S (in Ref. 8; AAA92511).
{ECO:0000305}.
CONFLICT 3556 3556 K -> N (in Ref. 6; L04731).
{ECO:0000305}.
CONFLICT 3718 3718 R -> G (in Ref. 2; CAA93625).
{ECO:0000305}.
CONFLICT 3759 3759 N -> D (in Ref. 2; CAA93625).
{ECO:0000305}.
CONFLICT 3813 3813 D -> G (in Ref. 2; CAA93625).
{ECO:0000305}.
CONFLICT 3901 3901 A -> R (in Ref. 1; AAA58669).
{ECO:0000305}.
HELIX 114 133 {ECO:0000244|PDB:3U88}.
STRAND 135 138 {ECO:0000244|PDB:2MTN}.
STRAND 150 152 {ECO:0000244|PDB:2MSR}.
STRAND 1151 1154 {ECO:0000244|PDB:2J2S}.
STRAND 1156 1158 {ECO:0000244|PDB:4NW3}.
HELIX 1159 1162 {ECO:0000244|PDB:4NW3}.
STRAND 1168 1170 {ECO:0000244|PDB:4NW3}.
HELIX 1171 1175 {ECO:0000244|PDB:4NW3}.
HELIX 1177 1179 {ECO:0000244|PDB:4NW3}.
STRAND 1183 1185 {ECO:0000244|PDB:2J2S}.
TURN 1190 1192 {ECO:0000244|PDB:4NW3}.
STRAND 1197 1200 {ECO:0000244|PDB:2J2S}.
TURN 1204 1206 {ECO:0000244|PDB:2J2S}.
STRAND 1574 1576 {ECO:0000244|PDB:2KYU}.
TURN 1578 1582 {ECO:0000244|PDB:2KYU}.
STRAND 1585 1587 {ECO:0000244|PDB:2KYU}.
STRAND 1589 1591 {ECO:0000244|PDB:2KYU}.
HELIX 1595 1599 {ECO:0000244|PDB:2KU7}.
HELIX 1604 1611 {ECO:0000244|PDB:2KU7}.
TURN 1615 1618 {ECO:0000244|PDB:2KU7}.
TURN 1625 1627 {ECO:0000244|PDB:2KU7}.
HELIX 2847 2856 {ECO:0000244|PDB:2AGH}.
HELIX 3764 3766 {ECO:0000244|PDB:4ESG}.
HELIX 3796 3799 {ECO:0000244|PDB:2W5Y}.
HELIX 3809 3811 {ECO:0000244|PDB:2W5Y}.
HELIX 3816 3820 {ECO:0000244|PDB:5F5E}.
HELIX 3823 3830 {ECO:0000244|PDB:5F5E}.
STRAND 3831 3835 {ECO:0000244|PDB:5F5E}.
STRAND 3837 3847 {ECO:0000244|PDB:5F5E}.
STRAND 3854 3857 {ECO:0000244|PDB:5F5E}.
STRAND 3860 3864 {ECO:0000244|PDB:5F5E}.
HELIX 3865 3867 {ECO:0000244|PDB:5F5E}.
HELIX 3868 3877 {ECO:0000244|PDB:5F5E}.
STRAND 3884 3886 {ECO:0000244|PDB:5F5E}.
STRAND 3888 3894 {ECO:0000244|PDB:5F5E}.
TURN 3896 3898 {ECO:0000244|PDB:5F5E}.
HELIX 3901 3904 {ECO:0000244|PDB:5F5E}.
STRAND 3912 3920 {ECO:0000244|PDB:5F5E}.
STRAND 3923 3932 {ECO:0000244|PDB:5F5E}.
STRAND 3939 3942 {ECO:0000244|PDB:5F5E}.
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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