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Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.43) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2)

 KMT2D_HUMAN             Reviewed;        5537 AA.
O14686; O14687;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
11-DEC-2019, entry version 189.
RecName: Full=Histone-lysine N-methyltransferase 2D;
Short=Lysine N-methyltransferase 2D;
EC=2.1.1.354 {ECO:0000269|PubMed:17500065, ECO:0000305|PubMed:16603732};
AltName: Full=ALL1-related protein;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 2;
Name=KMT2D; Synonyms=ALR, MLL2, MLL4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
PubMed=9247308; DOI=10.1038/sj.onc.1201211;
Prasad R., Zhadanov A.B., Sedkov Y., Bullrich F., Druck T., Rallapalli R.,
Yano T., Alder H., Croce C.M., Huebner K., Mazo A., Canaani E.;
"Structure and expression pattern of human ALR, a novel gene with strong
homology to ALL-1 involved in acute leukemia and to Drosophila trithorax.";
Oncogene 15:549-560(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
IDENTIFICATION IN THE MLL2/3 COMPLEX.
TISSUE=Cervix carcinoma;
PubMed=12482968; DOI=10.1128/mcb.23.1.140-149.2003;
Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J.,
Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O.,
Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.;
"Activating signal cointegrator 2 belongs to a novel steady-state complex
that contains a subset of trithorax group proteins.";
Mol. Cell. Biol. 23:140-149(2003).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3130, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[5]
FUNCTION, ENZYME ACTIVITY, IDENTIFICATION IN THE MLL2 COMPLEX, LXXLL
MOTIFS, AND INTERACTION WITH ESR1.
PubMed=16603732; DOI=10.1074/jbc.m513245200;
Mo R., Rao S.M., Zhu Y.-J.;
"Identification of the MLL2 complex as a coactivator for estrogen receptor
alpha.";
J. Biol. Chem. 281:15714-15720(2006).
[6]
IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
PubMed=17021013; DOI=10.1073/pnas.0607313103;
Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K.,
Roeder R.G., Lee J.W.;
"Coactivator as a target gene specificity determinant for histone H3 lysine
4 methyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
IDENTIFICATION IN THE MLL2/3 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).
[8]
FUNCTION, AND IDENTIFICATION IN THE MLL2/3 COMPLEX.
PubMed=17851529; DOI=10.1038/nature06192;
Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S.,
Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M., Chang H.Y.,
Shi Y.;
"A histone H3 lysine 27 demethylase regulates animal posterior
development.";
Nature 449:689-694(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
IDENTIFICATION IN THE MLL2/3 COMPLEX.
PubMed=17761849; DOI=10.1126/science.1149042;
Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D.,
Di Croce L., Shiekhattar R.;
"Demethylation of H3K27 regulates polycomb recruitment and H2A
ubiquitination.";
Science 318:447-450(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4738, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-2274; SER-2309;
SER-2311; THR-3197 AND SER-4822, 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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274; THR-3197;
SER-4359 AND SER-4822, 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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2246; LYS-3079; LYS-3433;
LYS-4465 AND LYS-4776, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; THR-3197; SER-3199;
SER-4215; SER-4359 AND SER-4738, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274 AND SER-4738,
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; SER-1671; SER-1820;
SER-1834; THR-1843; THR-2240; SER-2260; SER-2274; SER-2640; SER-3130;
SER-3199; SER-4359; SER-4738; SER-4822 AND SER-4849, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1151; THR-1195; SER-1249;
SER-2239 AND SER-4738, 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).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-3727, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4756, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4756 AND LYS-4880, 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).
[23] {ECO:0000244|PDB:4ERQ}
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 5333-5346 IN COMPLEX WITH WDR5,
INTERACTION WITH WDR5, AND MOTIF WIN.
PubMed=22665483; DOI=10.1074/jbc.M112.364125;
Dharmarajan V., Lee J.H., Patel A., Skalnik D.G., Cosgrove M.S.;
"Structural basis for WDR5 interaction (Win) motif recognition in human
SET1 family histone methyltransferases.";
J. Biol. Chem. 287:27275-27289(2012).
[24] {ECO:0000244|PDB:3UVK}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 5337-5347 IN COMPLEX WITH WDR5,
INTERACTION WITH WDR5, AND MOTIF WIN.
PubMed=22266653; DOI=10.1093/nar/gkr1235;
Zhang P., Lee H., Brunzelle J.S., Couture J.F.;
"The plasticity of WDR5 peptide-binding cleft enables the binding of the
SET1 family of histone methyltransferases.";
Nucleic Acids Res. 40:4237-4246(2012).
[25]
VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464, AND
INVOLVEMENT IN KABUK1.
PubMed=20711175; DOI=10.1038/ng.646;
Ng S.B., Bigham A.W., Buckingham K.J., Hannibal M.C., McMillin M.J.,
Gildersleeve H.I., Beck A.E., Tabor H.K., Cooper G.M., Mefford H.C.,
Lee C., Turner E.H., Smith J.D., Rieder M.J., Yoshiura K., Matsumoto N.,
Ohta T., Niikawa N., Nickerson D.A., Bamshad M.J., Shendure J.;
"Exome sequencing identifies MLL2 mutations as a cause of Kabuki
syndrome.";
Nat. Genet. 42:790-793(2010).
[26]
VARIANTS KABUK1 LEU-1388; ARG-1430; TYR-1471; CYS-5048; PHE-5109; HIS-5179;
CYS-5214; HIS-5214; LEU-5340; MET-5464 AND THR-5471.
PubMed=21671394; DOI=10.1002/ajmg.a.34074;
Hannibal M.C., Buckingham K.J., Ng S.B., Ming J.E., Beck A.E.,
McMillin M.J., Gildersleeve H.I., Bigham A.W., Tabor H.K., Mefford H.C.,
Cook J., Yoshiura K., Matsumoto T., Matsumoto N., Miyake N., Tonoki H.,
Naritomi K., Kaname T., Nagai T., Ohashi H., Kurosawa K., Hou J.W.,
Ohta T., Liang D., Sudo A., Morris C.A., Banka S., Black G.C.,
Clayton-Smith J., Nickerson D.A., Zackai E.H., Shaikh T.H., Donnai D.,
Niikawa N., Shendure J., Bamshad M.J.;
"Spectrum of MLL2 (ALR) mutations in 110 cases of Kabuki syndrome.";
Am. J. Med. Genet. A 155A:1511-1516(2011).
[27]
VARIANTS KABUK1 LEU-543; GLN-647; MET-1192; ARG-1453; VAL-1718; GLN-5154
AND PHE-5498.
PubMed=21607748; DOI=10.1007/s00439-011-1004-y;
Li Y., Boegershausen N., Alanay Y., Simsek Kiper P.O., Plume N., Keupp K.,
Pohl E., Pawlik B., Rachwalski M., Milz E., Thoenes M., Albrecht B.,
Prott E.C., Lehmkuehler M., Demuth S., Utine G.E., Boduroglu K.,
Frankenbusch K., Borck G., Gillessen-Kaesbach G., Yigit G., Wieczorek D.,
Wollnik B.;
"A mutation screen in patients with Kabuki syndrome.";
Hum. Genet. 130:715-724(2011).
[28]
VARIANTS KABUK1 CYS-5210 AND ASP-5428, AND VARIANTS THR-692; LEU-813;
SER-2382; CYS-2460; LEU-2557; VAL-3398; GLY-3419 AND SER-4357.
PubMed=21280141; DOI=10.1002/humu.21416;
Paulussen A.D., Stegmann A.P., Blok M.J., Tserpelis D., Posma-Velter C.,
Detisch Y., Smeets E.E., Wagemans A., Schrander J.J.,
van den Boogaard M.J., van der Smagt J., van Haeringen A.,
Stolte-Dijkstra I., Kerstjens-Frederikse W.S., Mancini G.M., Wessels M.W.,
Hennekam R.C., Vreeburg M., Geraedts J., de Ravel T., Fryns J.P.,
Smeets H.J., Devriendt K., Schrander-Stumpel C.T.;
"MLL2 mutation spectrum in 45 patients with Kabuki syndrome.";
Hum. Mutat. 32:E2018-E2025(2011).
[29]
VARIANTS KABUK1 GLN-1258; VAL-1417; MET-1418; ARG-1522; THR-2841; GLU-5028;
VAL-5034; PRO-5059 AND GLN-5340.
PubMed=21658225; DOI=10.1186/1750-1172-6-38;
Micale L., Augello B., Fusco C., Selicorni A., Loviglio M.N., Silengo M.C.,
Reymond A., Gumiero B., Zucchetti F., D'Addetta E.V., Belligni E.,
Calcagni A., Digilio M.C., Dallapiccola B., Faravelli F., Forzano F.,
Accadia M., Bonfante A., Clementi M., Daolio C., Douzgou S., Ferrari P.,
Fischetto R., Garavelli L., Lapi E., Mattina T., Melis D., Patricelli M.G.,
Priolo M., Prontera P., Renieri A., Mencarelli M.A., Scarano G.,
della Monica M., Toschi B., Turolla L., Vancini A., Zatterale A.,
Gabrielli O., Zelante L., Merla G.;
"Mutation spectrum of MLL2 in a cohort of Kabuki syndrome patients.";
Orphanet J. Rare Dis. 6:38-38(2011).
[30]
VARIANTS KABUK1 LEU-337; LEU-4353; VAL-5047; CYS-5048; CYS-5214; THR-5471
AND TYR-5481.
PubMed=22126750; DOI=10.1038/ejhg.2011.220;
Banka S., Veeramachaneni R., Reardon W., Howa rd E., Bunstone S., Ragge N.,
Parker M.J., Crow Y.J., Kerr B., Kingston H., Metcalfe K., Chandler K.,
Magee A., Stewart F., McConnell V.P., Donnelly D.E., Berland S., Houge G.,
Morton J.E., Oley C., Revencu N., Park S.M., Davies S.J., Fry A.E.,
Lynch S.A., Gill H., Schweiger S., Lam W.W., Tolmie J., Mohammed S.N.,
Hobson E., Smith A., Blyth M., Bennett C., Vasudevan P.C.,
Garcia-Minaur S., Henderson A., Goodship J., Wright M.J., Fisher R.,
Gibbons R., Price S.M., C de Silva D., Temple I.K., Collins A.L.,
Lachlan K., Elmslie F., McEntagart M., Castle B., Clayton-Smith J.,
Black G.C., Donnai D.;
"How genetically heterogeneous is Kabuki syndrome?: MLL2 testing in 116
patients, review and analyses of mutation and phenotypic spectrum.";
Eur. J. Hum. Genet. 20:381-388(2012).
[31]
VARIANTS KABUK1 ARG-1376; CYS-1423; GLY-1445; PHE-1526; CYS-5030; GLY-5040;
CYS-5048; HIS-5048; GLN-5154; HIS-5179; ARG-5189 AND GLN-5351.
PubMed=23913813; DOI=10.1002/ajmg.a.36072;
Miyake N., Koshimizu E., Okamoto N., Mizuno S., Ogata T., Nagai T.,
Kosho T., Ohashi H., Kato M., Sasaki G., Mabe H., Watanabe Y., Yoshino M.,
Matsuishi T., Takanashi J., Shotelersuk V., Tekin M., Ochi N., Kubota M.,
Ito N., Ihara K., Hara T., Tonoki H., Ohta T., Saito K., Matsuo M.,
Urano M., Enokizono T., Sato A., Tanaka H., Ogawa A., Fujita T., Hiraki Y.,
Kitanaka S., Matsubara Y., Makita T., Taguri M., Nakashima M.,
Tsurusaki Y., Saitsu H., Yoshiura K., Matsumoto N., Niikawa N.;
"MLL2 and KDM6A mutations in patients with Kabuki syndrome.";
Am. J. Med. Genet. A 161A:2234-2243(2013).
[32]
VARIANTS KABUK1 PHE-1424 AND GLN-4420.
PubMed=24739679; DOI=10.1038/jhg.2014.25;
Cheon C.K., Sohn Y.B., Ko J.M., Lee Y.J., Song J.S., Moon J.W., Yang B.K.,
Ha I.S., Bae E.J., Jin H.S., Jeong S.Y.;
"Identification of KMT2D and KDM6A mutations by exome sequencing in Korean
patients with Kabuki syndrome.";
J. Hum. Genet. 59:321-325(2014).
[33]
VARIANTS KABUK1 HIS-170; LEU-170; GLN-647; ARG-1380; ARG-1471; ARG-3876;
SER-3897; CYS-5030; CYS-5048; HIS-5048; CYS-5214; TRP-5432 AND PHE-5498,
AND VARIANTS LEU-2557; LEU-2652 AND PRO-4010.
PubMed=23320472; DOI=10.1111/cge.12081;
Makrythanasis P., van Bon B.W., Steehouwer M., Rodriguez-Santiago B.,
Simpson M., Dias P., Anderlid B.M., Arts P., Bhat M., Augello B.,
Biamino E., Bongers E.M., Del Campo M., Cordeiro I., Cueto-Gonzalez A.M.,
Cusco I., Deshpande C., Frysira E., Izatt L., Flores R., Galan E.,
Gener B., Gilissen C., Granneman S.M., Hoyer J., Yntema H.G., Kets C.M.,
Koolen D.A., Marcelis C.L., Medeira A., Micale L., Mohammed S.,
de Munnik S.A., Nordgren A., Psoni S., Reardon W., Revencu N., Roscioli T.,
Ruiterkamp-Versteeg M., Santos H.G., Schoumans J.,
Schuurs-Hoeijmakers J.H., Silengo M.C., Toledo L., Vendrell T.,
van der Burgt I., van Lier B., Zweier C., Reymond A., Trembath R.C.,
Perez-Jurado L., Dupont J., de Vries B.B., Brunner H.G., Veltman J.A.,
Merla G., Antonarakis S.E., Hoischen A.;
"MLL2 mutation detection in 86 patients with Kabuki syndrome: a genotype-
phenotype study.";
Clin. Genet. 84:539-545(2013).
-!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3
(H3K4me). H3K4me represents a specific tag for epigenetic
transcriptional activation. Acts as a coactivator for estrogen receptor
by being recruited by ESR1, thereby activating transcription.
{ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17500065,
ECO:0000269|PubMed:17851529}.
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
Evidence={ECO:0000269|PubMed:17500065, ECO:0000305|PubMed:16603732};
-!- SUBUNIT: Component of the MLL2/3 complex (also named ASCOM complex), at
least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6,
DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts
with ESR1; interaction is direct. Interacts (via WIN motif) with WDR5
(PubMed:22665483, PubMed:22266653). {ECO:0000269|PubMed:12482968,
ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17021013,
ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17761849,
ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:22266653,
ECO:0000269|PubMed:22665483}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-996065, EBI-608057;
Q9UBL3-3:ASH2L; NbExp=2; IntAct=EBI-996065, EBI-16130425;
P03372:ESR1; NbExp=3; IntAct=EBI-996065, EBI-78473;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14686-1; Sequence=Displayed;
Name=3;
IsoId=O14686-3; Sequence=VSP_008560;
-!- TISSUE SPECIFICITY: Expressed in most adult tissues, including a
variety of hematoipoietic cells, with the exception of the liver.
-!- DOMAIN: LXXLL motifs 5 and 6 are essential for the association with
ESR1 nuclear receptor.
-!- DISEASE: Kabuki syndrome 1 (KABUK1) [MIM:147920]: A congenital mental
retardation syndrome with additional features, including postnatal
dwarfism, a peculiar facies characterized by long palpebral fissures
with eversion of the lateral third of the lower eyelids, a broad and
depressed nasal tip, large prominent earlobes, a cleft or high-arched
palate, scoliosis, short fifth finger, persistence of fingerpads,
radiographic abnormalities of the vertebrae, hands, and hip joints, and
recurrent otitis media in infancy. {ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21280141, ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:21658225, ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813, ECO:0000269|PubMed:24739679}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- MISCELLANEOUS: This gene mapped to a chromosomal region involved in
duplications and translocations associated with cancer.
-!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
superfamily. Histone-lysine methyltransferase family. TRX/MLL
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- CAUTION: Another protein KMT2B/MLL4, located on chromosome 19, was
first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often referred to
as MLL2 and vice versa in the literature. {ECO:0000305}.
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EMBL; AF010403; AAC51734.1; -; mRNA.
EMBL; AF010404; AAC51735.1; -; mRNA.
EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS44873.1; -. [O14686-1]
PIR; T03454; T03454.
PIR; T03455; T03455.
RefSeq; NP_003473.3; NM_003482.3. [O14686-1]
RefSeq; XP_005269219.1; XM_005269162.4. [O14686-1]
RefSeq; XP_006719677.1; XM_006719614.3. [O14686-3]
PDB; 3UVK; X-ray; 1.40 A; B=5337-5347.
PDB; 4ERQ; X-ray; 1.91 A; D/E/F=5333-5346.
PDB; 4Z4P; X-ray; 2.20 A; A=5382-5536.
PDB; 6O7G; NMR; -; B=1503-1562.
PDBsum; 3UVK; -.
PDBsum; 4ERQ; -.
PDBsum; 4Z4P; -.
PDBsum; 6O7G; -.
SMR; O14686; -.
BioGrid; 113758; 45.
CORUM; O14686; -.
DIP; DIP-37875N; -.
ELM; O14686; -.
IntAct; O14686; 29.
MINT; O14686; -.
STRING; 9606.ENSP00000301067; -.
BindingDB; O14686; -.
ChEMBL; CHEMBL2189114; -.
iPTMnet; O14686; -.
PhosphoSitePlus; O14686; -.
BioMuta; KMT2D; -.
CPTAC; CPTAC-978; -.
EPD; O14686; -.
jPOST; O14686; -.
MassIVE; O14686; -.
MaxQB; O14686; -.
PaxDb; O14686; -.
PeptideAtlas; O14686; -.
PRIDE; O14686; -.
ProteomicsDB; 48168; -. [O14686-1]
ProteomicsDB; 48169; -. [O14686-3]
Ensembl; ENST00000301067; ENSP00000301067; ENSG00000167548. [O14686-1]
GeneID; 8085; -.
KEGG; hsa:8085; -.
UCSC; uc001rta.4; human. [O14686-1]
CTD; 8085; -.
DisGeNET; 8085; -.
EuPathDB; HostDB:ENSG00000167548.14; -.
GeneCards; KMT2D; -.
GeneReviews; KMT2D; -.
HGNC; HGNC:7133; KMT2D.
HPA; HPA035977; -.
MalaCards; KMT2D; -.
MIM; 147920; phenotype.
MIM; 602113; gene.
neXtProt; NX_O14686; -.
OpenTargets; ENSG00000167548; -.
Orphanet; 2322; Kabuki syndrome.
PharmGKB; PA30846; -.
eggNOG; KOG4443; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00940000156707; -.
InParanoid; O14686; -.
KO; K09187; -.
OMA; LPGVGVM; -.
OrthoDB; 236292at2759; -.
PhylomeDB; O14686; -.
TreeFam; TF354317; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SIGNOR; O14686; -.
ChiTaRS; KMT2D; human.
GeneWiki; MLL2; -.
GenomeRNAi; 8085; -.
Pharos; O14686; Tbio.
PRO; PR:O14686; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; O14686; protein.
Bgee; ENSG00000167548; Expressed in 100 organ(s), highest expression level in left lobe of thyroid gland.
ExpressionAtlas; O14686; baseline and differential.
Genevisible; O14686; HS.
GO; GO:0035097; C:histone methyltransferase complex; IPI:MGI.
GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0006342; P:chromatin silencing; ISS:UniProtKB.
GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
GO; GO:0001555; P:oocyte growth; ISS:UniProtKB.
GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
CDD; cd15695; ePHD1_KMT2D; 1.
CDD; cd15698; ePHD2_KMT2D; 1.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 3.30.40.10; -; 6.
InterPro; IPR034732; EPHD.
InterPro; IPR003889; FYrich_C.
InterPro; IPR003888; FYrich_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR037890; KMT2D.
InterPro; IPR041961; KMT2D_ePHD1.
InterPro; IPR041964; KMT2D_ePHD2.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR45888:SF2; PTHR45888:SF2; 2.
Pfam; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 3.
Pfam; PF00856; SET; 1.
SMART; SM00542; FYRC; 1.
SMART; SM00541; FYRN; 1.
SMART; SM00398; HMG; 1.
SMART; SM00249; PHD; 7.
SMART; SM00508; PostSET; 1.
SMART; SM00184; RING; 6.
SMART; SM00317; SET; 1.
SUPFAM; SSF47095; SSF47095; 1.
SUPFAM; SSF57903; SSF57903; 5.
PROSITE; PS51805; EPHD; 2.
PROSITE; PS51543; FYRC; 1.
PROSITE; PS51542; FYRN; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 5.
PROSITE; PS50016; ZF_PHD_2; 5.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Coiled coil; Disease mutation; Isopeptide bond; Mental retardation;
Metal-binding; Methylation; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1..5537
/note="Histone-lysine N-methyltransferase 2D"
/id="PRO_0000124878"
REPEAT 442..446
/note="1"
REPEAT 460..464
/note="2"
REPEAT 469..473
/note="3"
REPEAT 496..500
/note="4"
REPEAT 504..508
/note="5"
REPEAT 521..525
/note="6"
REPEAT 555..559
/note="7"
REPEAT 564..568
/note="8"
REPEAT 573..577
/note="9"
REPEAT 582..586
/note="10"
REPEAT 609..613
/note="11"
REPEAT 618..622
/note="12"
REPEAT 627..631
/note="13"
REPEAT 645..649
/note="14"
REPEAT 663..667
/note="15"
DOMAIN 5175..5235
/note="FYR N-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
DOMAIN 5236..5321
/note="FYR C-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
DOMAIN 5397..5513
/note="SET"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
DOMAIN 5521..5537
/note="Post-SET"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
ZN_FING 104..149
/note="C2HC pre-PHD-type 1; degenerate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
ZN_FING 170..218
/note="PHD-type 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
ZN_FING 226..276
/note="PHD-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
ZN_FING 229..274
/note="RING-type 1; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 273..323
/note="PHD-type 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
ZN_FING 276..321
/note="RING-type 2; degenerate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 1377..1430
/note="PHD-type 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
ZN_FING 1427..1477
/note="PHD-type 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
ZN_FING 1504..1559
/note="PHD-type 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
ZN_FING 1507..1557
/note="RING-type 3; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 5029..5069
/note="C2HC pre-PHD-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
ZN_FING 5090..5137
/note="PHD-type 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
REGION 439..668
/note="15 X 5 AA repeats of S/P-P-P-E/P-E/A"
REGION 5474..5475
/note="S-adenosyl-L-methionine binding"
/evidence="ECO:0000250"
COILED 2669..2707
/evidence="ECO:0000255"
COILED 3249..3282
/evidence="ECO:0000255"
COILED 3562..3614
/evidence="ECO:0000255"
COILED 3714..3750
/evidence="ECO:0000255"
COILED 3897..3975
/evidence="ECO:0000255"
MOTIF 2686..2690
/note="LXXLL motif 1"
MOTIF 3038..3042
/note="LXXLL motif 2"
MOTIF 4222..4236
/note="LXXLL motif 3"
MOTIF 4253..4257
/note="LXXLL motif 4"
MOTIF 4463..4467
/note="LXXLL motif 5"
MOTIF 4990..4994
/note="LXXLL motif 6"
MOTIF 5337..5342
/note="WDR5 interaction motif (WIN)"
/evidence="ECO:0000269|PubMed:22266653,
ECO:0000269|PubMed:22665483"
COMPBIAS 229..326
/note="Cys-rich"
COMPBIAS 374..1197
/note="Pro-rich"
COMPBIAS 1290..1328
/note="Arg-rich"
COMPBIAS 1351..1355
/note="Poly-Glu"
COMPBIAS 1397..1510
/note="Cys-rich"
COMPBIAS 2107..2626
/note="Pro-rich"
COMPBIAS 2385..2392
/note="Poly-Pro"
COMPBIAS 2707..2713
/note="Poly-Ala"
COMPBIAS 2811..2822
/note="Gln-rich"
COMPBIAS 2862..2978
/note="Pro-rich"
COMPBIAS 3261..4275
/note="Gln-rich"
COMPBIAS 4241..4360
/note="Pro-rich"
COMPBIAS 4909..4977
/note="Pro-rich"
COMPBIAS 5494..5497
/note="Poly-Ile"
METAL 5477
/note="Zinc"
/evidence="ECO:0000250"
METAL 5525
/note="Zinc"
/evidence="ECO:0000250"
METAL 5527
/note="Zinc"
/evidence="ECO:0000250"
METAL 5532
/note="Zinc"
/evidence="ECO:0000250"
BINDING 5451
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
MOD_RES 27
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 744
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 1151
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 1195
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 1249
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 1267
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 1270
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 1606
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
MOD_RES 1671
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
MOD_RES 1820
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1834
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1843
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1865
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 2239
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 2240
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 2246
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 2260
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 2274
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 2309
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 2311
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 2342
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 2535
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 2640
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 2836
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 3079
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 3130
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163"
MOD_RES 3197
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231"
MOD_RES 3199
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
MOD_RES 3433
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 3727
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 4198
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q6PDK2"
MOD_RES 4215
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 4359
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 4465
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 4738
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
MOD_RES 4776
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 4822
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163"
MOD_RES 4849
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 4756
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 4880
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 1729
/note="E -> EGET (in isoform 3)"
/evidence="ECO:0000303|PubMed:9247308"
/id="VSP_008560"
VARIANT 170
/note="Q -> H (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074216"
VARIANT 170
/note="Q -> L (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074217"
VARIANT 337
/note="S -> L (in KABUK1; unknown pathological
significance; dbSNP:rs200245957)"
/evidence="ECO:0000269|PubMed:22126750"
/id="VAR_074218"
VARIANT 476
/note="A -> T (in dbSNP:rs1064210)"
/id="VAR_057359"
VARIANT 543
/note="S -> L (in KABUK1; unknown pathological
significance; dbSNP:rs776242478)"
/evidence="ECO:0000269|PubMed:21607748"
/id="VAR_074219"
VARIANT 647
/note="P -> Q (in KABUK1; dbSNP:rs200088180)"
/evidence="ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23320472"
/id="VAR_074220"
VARIANT 692
/note="P -> T (in dbSNP:rs202076833)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064370"
VARIANT 813
/note="P -> L (in dbSNP:rs75226229)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064371"
VARIANT 1192
/note="V -> M (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21607748"
/id="VAR_074221"
VARIANT 1258
/note="R -> Q (in KABUK1; unknown pathological
significance; dbSNP:rs1341612248)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074222"
VARIANT 1376
/note="M -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074223"
VARIANT 1380
/note="C -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074224"
VARIANT 1388
/note="R -> L (in KABUK1; unknown pathological
significance; dbSNP:rs202217665)"
/evidence="ECO:0000269|PubMed:21671394"
/id="VAR_074225"
VARIANT 1417
/note="M -> V (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074226"
VARIANT 1418
/note="L -> M (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074227"
VARIANT 1423
/note="R -> C (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074228"
VARIANT 1424
/note="C -> F (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:24739679"
/id="VAR_074229"
VARIANT 1430
/note="C -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21671394"
/id="VAR_074230"
VARIANT 1445
/note="C -> G (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074231"
VARIANT 1453
/note="H -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21607748"
/id="VAR_074232"
VARIANT 1471
/note="C -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074233"
VARIANT 1471
/note="C -> Y (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21671394"
/id="VAR_074234"
VARIANT 1522
/note="Q -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074235"
VARIANT 1526
/note="C -> F (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074236"
VARIANT 1718
/note="A -> V (in KABUK1; unknown pathological
significance; dbSNP:rs111266743)"
/evidence="ECO:0000269|PubMed:21607748"
/id="VAR_074237"
VARIANT 2382
/note="P -> S (in dbSNP:rs3741626)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064372"
VARIANT 2460
/note="R -> C (in dbSNP:rs570260017)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064373"
VARIANT 2557
/note="P -> L (in dbSNP:rs189888707)"
/evidence="ECO:0000269|PubMed:21280141,
ECO:0000269|PubMed:23320472"
/id="VAR_064374"
VARIANT 2652
/note="M -> L (in dbSNP:rs147706410)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074238"
VARIANT 2841
/note="P -> T (in KABUK1; unknown pathological
significance; dbSNP:rs763347763)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074239"
VARIANT 3398
/note="M -> V (in dbSNP:rs75937132)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064375"
VARIANT 3419
/note="D -> G (in dbSNP:rs146044282)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064376"
VARIANT 3876
/note="L -> R (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074240"
VARIANT 3897
/note="L -> S (in KABUK1; unknown pathological
significance; dbSNP:rs1342235871)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074241"
VARIANT 4010
/note="S -> P (in dbSNP:rs80132640)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074242"
VARIANT 4353
/note="P -> L (in KABUK1; unknown pathological
significance; dbSNP:rs778418522)"
/evidence="ECO:0000269|PubMed:22126750"
/id="VAR_074243"
VARIANT 4357
/note="R -> S (in dbSNP:rs533214351)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064377"
VARIANT 4420
/note="R -> Q (in KABUK1; unknown pathological
significance; dbSNP:rs375999143)"
/evidence="ECO:0000269|PubMed:24739679"
/id="VAR_074244"
VARIANT 5028
/note="D -> E (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074245"
VARIANT 5030
/note="R -> C (in KABUK1; dbSNP:rs1555185875)"
/evidence="ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813"
/id="VAR_074246"
VARIANT 5034
/note="F -> V (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074247"
VARIANT 5040
/note="D -> G (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074248"
VARIANT 5047
/note="A -> V (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:22126750"
/id="VAR_074249"
VARIANT 5048
/note="R -> C (in KABUK1; dbSNP:rs398123724)"
/evidence="ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813"
/id="VAR_074250"
VARIANT 5048
/note="R -> H (in KABUK1; dbSNP:rs886041404)"
/evidence="ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813"
/id="VAR_074251"
VARIANT 5059
/note="H -> P (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074252"
VARIANT 5109
/note="C -> F (in KABUK1)"
/evidence="ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394"
/id="VAR_063830"
VARIANT 5154
/note="R -> Q (in KABUK1; dbSNP:rs886043497)"
/evidence="ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23913813"
/id="VAR_074253"
VARIANT 5179
/note="R -> H (in KABUK1; dbSNP:rs267607237)"
/evidence="ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394, ECO:0000269|PubMed:23913813"
/id="VAR_063831"
VARIANT 5189
/note="G -> R (in KABUK1; unknown pathological
significance; dbSNP:rs1555185701)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074254"
VARIANT 5210
/note="Y -> C (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064378"
VARIANT 5214
/note="R -> C (in KABUK1)"
/evidence="ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472"
/id="VAR_074255"
VARIANT 5214
/note="R -> H (in KABUK1; dbSNP:rs398123729)"
/evidence="ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394"
/id="VAR_063832"
VARIANT 5224
/note="R -> H (in dbSNP:rs3782356)"
/id="VAR_017115"
VARIANT 5340
/note="R -> L (in KABUK1)"
/evidence="ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394"
/id="VAR_063833"
VARIANT 5340
/note="R -> Q (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21658225"
/id="VAR_074256"
VARIANT 5351
/note="R -> Q (in KABUK1; unknown pathological
significance; dbSNP:rs1555185217)"
/evidence="ECO:0000269|PubMed:23913813"
/id="VAR_074257"
VARIANT 5428
/note="G -> D (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:21280141"
/id="VAR_064379"
VARIANT 5432
/note="R -> W (in KABUK1; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:23320472"
/id="VAR_074258"
VARIANT 5464
/note="T -> M (in KABUK1; dbSNP:rs267607238)"
/evidence="ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394"
/id="VAR_063834"
VARIANT 5471
/note="R -> T (in KABUK1)"
/evidence="ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750"
/id="VAR_074259"
VARIANT 5481
/note="C -> Y (in KABUK1; unknown pathological
significance; dbSNP:rs1388523736)"
/evidence="ECO:0000269|PubMed:22126750"
/id="VAR_074260"
VARIANT 5498
/note="S -> F (in KABUK1)"
/evidence="ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23320472"
/id="VAR_074261"
CONFLICT 5
/note="K -> N (in Ref. 1; AAC51734)"
/evidence="ECO:0000305"
CONFLICT 14
/note="E -> Q (in Ref. 1; AAC51734)"
/evidence="ECO:0000305"
CONFLICT 75
/note="S -> A (in Ref. 1; AAC51734)"
/evidence="ECO:0000305"
CONFLICT 156
/note="E -> Q (in Ref. 1; AAC51734)"
/evidence="ECO:0000305"
CONFLICT 674..948
/note="Missing (in Ref. 1; AAC51734)"
/evidence="ECO:0000305"
CONFLICT 1178
/note="Q -> R (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 1544..1547
/note="EQAA -> DHAP (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 1761
/note="K -> R (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 1766
/note="D -> G (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 2171
/note="V -> A (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 2413
/note="A -> V (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 3079
/note="K -> E (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 3287
/note="S -> P (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 3319
/note="G -> V (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 3422
/note="D -> G (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4478
/note="R -> Q (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4747
/note="A -> D (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4793
/note="A -> D (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4826
/note="A -> G (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4865
/note="P -> A (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4871
/note="S -> R (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4893
/note="S -> R (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 4974
/note="S -> T (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 5116
/note="A -> G (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
CONFLICT 5522
/note="K -> E (in Ref. 1; AAC51734/AAC51735)"
/evidence="ECO:0000305"
TURN 1508..1511
/evidence="ECO:0000244|PDB:6O7G"
STRAND 1516..1518
/evidence="ECO:0000244|PDB:6O7G"
STRAND 1520..1522
/evidence="ECO:0000244|PDB:6O7G"
TURN 1524..1526
/evidence="ECO:0000244|PDB:6O7G"
STRAND 1529..1532
/evidence="ECO:0000244|PDB:6O7G"
HELIX 1533..1535
/evidence="ECO:0000244|PDB:6O7G"
HELIX 1540..1548
/evidence="ECO:0000244|PDB:6O7G"
HELIX 1556..1560
/evidence="ECO:0000244|PDB:6O7G"
HELIX 5339..5341
/evidence="ECO:0000244|PDB:3UVK"
HELIX 5384..5398
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5399..5403
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5405..5415
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5422..5425
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5428..5432
/evidence="ECO:0000244|PDB:4Z4P"
HELIX 5433..5444
/evidence="ECO:0000244|PDB:4Z4P"
TURN 5445..5447
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5452..5454
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5456..5462
/evidence="ECO:0000244|PDB:4Z4P"
TURN 5464..5466
/evidence="ECO:0000244|PDB:4Z4P"
HELIX 5469..5472
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5480..5488
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5491..5500
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5516..5520
/evidence="ECO:0000244|PDB:4Z4P"
STRAND 5534..5536
/evidence="ECO:0000244|PDB:4Z4P"
SEQUENCE 5537 AA; 593389 MW; 31C6DAB0A754F72A CRC64;
MDSQKLAGED KDSEPAADGP AASEDPSATE SDLPNPHVGE VSVLSSGSPR LQETPQDCSG
GPVRRCALCN CGEPSLHGQR ELRRFELPFD WPRCPVVSPG GSPGPNEAVL PSEDLSQIGF
PEGLTPAHLG EPGGSCWAHH WCAAWSAGVW GQEGPELCGV DKAIFSGISQ RCSHCTRLGA
SIPCRSPGCP RLYHFPCATA SGSFLSMKTL QLLCPEHSEG AAYLEEARCA VCEGPGELCD
LFFCTSCGHH YHGACLDTAL TARKRAGWQC PECKVCQACR KPGNDSKMLV CETCDKGYHT
FCLKPPMEEL PAHSWKCKAC RVCRACGAGS AELNPNSEWF ENYSLCHRCH KAQGGQTIRS
VAEQHTPVCS RFSPPEPGDT PTDEPDALYV ACQGQPKGGH VTSMQPKEPG PLQCEAKPLG
KAGVQLEPQL EAPLNEEMPL LPPPEESPLS PPPEESPTSP PPEASRLSPP PEELPASPLP
EALHLSRPLE ESPLSPPPEE SPLSPPPESS PFSPLEESPL SPPEESPPSP ALETPLSPPP
EASPLSPPFE ESPLSPPPEE LPTSPPPEAS RLSPPPEESP MSPPPEESPM SPPPEASRLF
PPFEESPLSP PPEESPLSPP PEASRLSPPP EDSPMSPPPE ESPMSPPPEV SRLSPLPVVS
RLSPPPEESP LSPPPEESPT SPPPEASRLS PPPEDSPTSP PPEDSPASPP PEDSLMSLPL
EESPLLPLPE EPQLCPRSEG PHLSPRPEEP HLSPRPEEPH LSPQAEEPHL SPQPEEPCLC
AVPEEPHLSP QAEGPHLSPQ PEELHLSPQT EEPHLSPVPE EPCLSPQPEE SHLSPQSEEP
CLSPRPEESH LSPELEKPPL SPRPEKPPEE PGQCPAPEEL PLFPPPGEPS LSPLLGEPAL
SEPGEPPLSP LPEELPLSPS GEPSLSPQLM PPDPLPPPLS PIITAAAPPA LSPLGELEYP
FGAKGDSDPE SPLAAPILET PISPPPEANC TDPEPVPPMI LPPSPGSPVG PASPILMEPL
PPQCSPLLQH SLVPQNSPPS QCSPPALPLS VPSPLSPIGK VVGVSDEAEL HEMETEKVSE
PECPALEPSA TSPLPSPMGD LSCPAPSPAP ALDDFSGLGE DTAPLDGIDA PGSQPEPGQT
PGSLASELKG SPVLLDPEEL APVTPMEVYP ECKQTAGQGS PCEEQEEPRA PVAPTPPTLI
KSDIVNEISN LSQGDASASF PGSEPLLGSP DPEGGGSLSM ELGVSTDVSP ARDEGSLRLC
TDSLPETDDS LLCDAGTAIS GGKAEGEKGR RRSSPARSRI KQGRSSSFPG RRRPRGGAHG
GRGRGRARLK STASSIETLV VADIDSSPSK EEEEEDDDTM QNTVVLFSNT DKFVLMQDMC
VVCGSFGRGA EGHLLACSQC SQCYHPYCVN SKITKVMLLK GWRCVECIVC EVCGQASDPS
RLLLCDDCDI SYHTYCLDPP LLTVPKGGWK CKWCVSCMQC GAASPGFHCE WQNSYTHCGP
CASLVTCPIC HAPYVEEDLL IQCRHCERWM HAGCESLFTE DDVEQAADEG FDCVSCQPYV
VKPVAPVAPP ELVPMKVKEP EPQYFRFEGV WLTETGMALL RNLTMSPLHK RRQRRGRLGL
PGEAGLEGSE PSDALGPDDK KDGDLDTDEL LKGEGGVEHM ECEIKLEGPV SPDVEPGKEE
TEESKKRKRK PYRPGIGGFM VRQRKSHTRT KKGPAAQAEV LSGDGQPDEV IPADLPAEGA
VEQSLAEGDE KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFG
LGTPKAKGDG GSERKELPTS QKGDDGPDIA DEESRGLEGK ADTPGPEDGG VKASPVPSDP
EKPGTPGEGM LSSDLDRIST EELPKMESKD LQQLFKDVLG SEREQHLGCG TPGLEGSRTP
LQRPFLQGGL PLGNLPSSSP MDSYPGLCQS PFLDSRERGG FFSPEPGEPD SPWTGSGGTT
PSTPTTPTTE GEGDGLSYNQ RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS
RCKQIMKLWR KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDIARKTDRP
ALHLRIPPQP GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGSV PGPDSPGELF
LKLPPQVPAQ VPSQDPFGLA PAYPLEPRFP TAPPTYPPYP SPTGAPAQPP MLGASSRPGA
GQPGEFHTTP PGTPRHQPST PDPFLKPRCP SLDNLAVPES PGVGGGKASE PLLSPPPFGE
SRKALEVKKE ELGASSPSYG PPNLGFVDSP SSGTHLGGLE LKTPDVFKAP LTPRASQVEP
QSPGLGLRPQ EPPPAQALAP SPPSHPDIFR PGSYTDPYAQ PPLTPRPQPP PPESCCALPP
RSLPSDPFSR VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY SRPPSRPQSR
DPFAPLHKPP RPQPPEVAFK AGSLAHTSLG AGGFPAALPA GPAGELHAKV PSGQPPNFVR
SPGTGAFVGT PSPMRFTFPQ AVGEPSLKPP VPQPGLPPPH GINSHFGPGP TLGKPQSTNY
TVATGNFHPS GSPLGPSSGS TGESYGLSPL RPPSVLPPPA PDGSLPYLSH GASQRSGITS
PVEKREDPGT GMGSSLATAE LPGTQDPGMS GLSQTELEKQ RQRQRLRELL IRQQIQRNTL
RQEKETAAAA AGAVGPPGSW GAEPSSPAFE QLSRGQTPFA GTQDKSSLVG LPPSKLSGPI
LGPGSFPSDD RLSRPPPPAT PSSMDVNSRQ LVGGSQAFYQ RAPYPGSLPL QQQQQQLWQQ
QQATAATSMR FAMSARFPST PGPELGRQAL GSPLAGISTR LPGPGEPVPG PAGPAQFIEL
RHNVQKGLGP GGTPFPGQGP PQRPRFYPVS EDPHRLAPEG LRGLAVSGLP PQKPSAPPAP
ELNNSLHPTP HTKGPTLPTG LELVNRPPSS TELGRPNPLA LEAGKLPCED PELDDDFDAH
KALEDDEELA HLGLGVDVAK GDDELGTLEN LETNDPHLDD LLNGDEFDLL AYTDPELDTG
DKKDIFNEHL RLVESANEKA EREALLRGVE PGPLGPEERP PPAADASEPR LASVLPEVKP
KVEEGGRHPS PCQFTIATPK VEPAPAANSL GLGLKPGQSM MGSRDTRMGT GPFSSSGHTA
EKASFGATGG PPAHLLTPSP LSGPGGSSLL EKFELESGAL TLPGGPAASG DELDKMESSL
VASELPLLIE DLLEHEKKEL QKKQQLSAQL QPAQQQQQQQ QQHSLLSAPG PAQAMSLPHE
GSSPSLAGSQ QQLSLGLAGA RQPGLPQPLM PTQPPAHALQ QRLAPSMAMV SNQGHMLSGQ
HGGQAGLVPQ QSSQPVLSQK PMGTMPPSMC MKPQQLAMQQ QLANSFFPDT DLDKFAAEDI
IDPIAKAKMV ALKGIKKVMA QGSIGVAPGM NRQQVSLLAQ RLSGGPSSDL QNHVAAGSGQ
ERSAGDPSQP RPNPPTFAQG VINEADQRQY EEWLFHTQQL LQMQLKVLEE QIGVHRKSRK
ALCAKQRTAK KAGREFPEAD AEKLKLVTEQ QSKIQKQLDQ VRKQQKEHTN LMAEYRNKQQ
QQQQQQQQQQ QQHSAVLALS PSQSPRLLTK LPGQLLPGHG LQPPQGPPGG QAGGLRLTPG
GMALPGQPGG PFLNTALAQQ QQQQHSGGAG SLAGPSGGFF PGNLALRSLG PDSRLLQERQ
LQLQQQRMQL AQKLQQQQQQ QQQQQHLLGQ VAIQQQQQQG PGVQTNQALG PKPQGLMPPS
SHQGLLVQQL SPQPPQGPQG MLGPAQVAVL QQQHPGALGP QGPHRQVLMT QSRVLSSPQL
AQQGQGLMGH RLVTAQQQQQ QQQHQQQGSM AGLSHLQQSL MSHSGQPKLS AQPMGSLQQL
QQQQQLQQQQ QLQQQQQQQL QQQQQLQQQQ LQQQQQQQQL QQQQQQQLQQ QQQQLQQQQQ
QQQQQFQQQQ QQQQMGLLNQ SRTLLSPQQQ QQQQVALGPG MPAKPLQHFS SPGALGPTLL
LTGKEQNTVD PAVSSEATEG PSTHQGGPLA IGTTPESMAT EPGEVKPSLS GDSQLLLVQP
QPQPQPSSLQ LQPPLRLPGQ QQQQVSLLHT AGGGSHGQLG SGSSSEASSV PHLLAQPSVS
LGDQPGSMTQ NLLGPQQPML ERPMQNNTGP QPPKPGPVLQ SGQGLPGVGI MPTVGQLRAQ
LQGVLAKNPQ LRHLSPQQQQ QLQALLMQRQ LQQSQAVRQT PPYQEPGTQT SPLQGLLGCQ
PQLGGFPGPQ TGPLQELGAG PRPQGPPRLP APPGALSTGP VLGPVHPTPP PSSPQEPKRP
SQLPSPSSQL PTEAQLPPTH PGTPKPQGPT LEPPPGRVSP AAAQLADTLF SKGLGPWDPP
DNLAETQKPE QSSLVPGHLD QVNGQVVPEA SQLSIKQEPR EEPCALGAQS VKREANGEPI
GAPGTSNHLL LAGPRSEAGH LLLQKLLRAK NVQLSTGRGS EGLRAEINGH IDSKLAGLEQ
KLQGTPSNKE DAAARKPLTP KPKRVQKASD RLVSSRKKLR KEDGVRASEA LLKQLKQELS
LLPLTEPAIT ANFSLFAPFG SGCPVNGQSQ LRGAFGSGAL PTGPDYYSQL LTKNNLSNPP
TPPSSLPPTP PPSVQQKMVN GVTPSEELGE HPKDAASARD SERALRDTSE VKSLDLLAAL
PTPPHNQTED VRMESDEDSD SPDSIVPASS PESILGEEAP RFPHLGSGRW EQEDRALSPV
IPLIPRASIP VFPDTKPYGA LGLEVPGKLP VTTWEKGKGS EVSVMLTVSA AAAKNLNGVM
VAVAELLSMK IPNSYEVLFP ESPARAGTEP KKGEAEGPGG KEKGLEGKSP DTGPDWLKQF
DAVLPGYTLK SQLDILSLLK QESPAPEPPT QHSYTYNVSN LDVRQLSAPP PEEPSPPPSP
LAPSPASPPT EPLVELPTEP LAEPPVPSPL PLASSPESAR PKPRARPPEE GEDSRPPRLK
KWKGVRWKRL RLLLTIQKGS GRQEDEREVA EFMEQLGTAL RPDKVPRDMR RCCFCHEEGD
GATDGPARLL NLDLDLWVHL NCALWSTEVY ETQGGALMNV EVALHRGLLT KCSLCQRTGA
TSSCNRMRCP NVYHFACAIR AKCMFFKDKT MLCPMHKIKG PCEQELSSFA VFRRVYIERD
EVKQIASIIQ RGERLHMFRV GGLVFHAIGQ LLPHQMADFH SATALYPVGY EATRIYWSLR
TNNRRCCYRC SIGENNGRPE FVIKVIEQGL EDLVFTDASP QAVWNRIIEP VAAMRKEADM
LRLFPEYLKG EELFGLTVHA VLRIAESLPG VESCQNYLFR YGRHPLMELP LMINPTGCAR
SEPKILTHYK RPHTLNSTSM SKAYQSTFTG ETNTPYSKQF VHSKSSQYRR LRTEWKNNVY
LARSRIQGLG LYAAKDLEKH TMVIEYIGTI IRNEVANRRE KIYEEQNRGI YMFRINNEHV
IDATLTGGPA RYINHSCAPN CVAEVVTFDK EDKIIIISSR RIPKGEELTY DYQFDFEDDQ
HKIPCHCGAW NCRKWMN


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