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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.
25-OCT-2017, entry version 169.
RecName: Full=Histone-lysine N-methyltransferase 2D;
Short=Lysine N-methyltransferase 2D;
EC=2.1.1.43;
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, ENZYME 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]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17500065}.
-!- 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. {ECO:0000269|PubMed:12482968, ECO:0000269|PubMed:16603732,
ECO:0000269|PubMed:17021013, ECO:0000269|PubMed:17500065,
ECO:0000269|PubMed:17761849, ECO:0000269|PubMed:17851529}.
-!- 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]
UniGene; Hs.731384; -.
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.
PDBsum; 3UVK; -.
PDBsum; 4ERQ; -.
PDBsum; 4Z4P; -.
ProteinModelPortal; O14686; -.
SMR; O14686; -.
BioGrid; 113758; 37.
CORUM; O14686; -.
DIP; DIP-37875N; -.
ELM; O14686; -.
IntAct; O14686; 24.
MINT; MINT-1192941; -.
STRING; 9606.ENSP00000301067; -.
BindingDB; O14686; -.
ChEMBL; CHEMBL2189114; -.
iPTMnet; O14686; -.
PhosphoSitePlus; O14686; -.
BioMuta; KMT2D; -.
EPD; O14686; -.
MaxQB; O14686; -.
PaxDb; O14686; -.
PeptideAtlas; O14686; -.
PRIDE; O14686; -.
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; ENSGT00760000119228; -.
HOVERGEN; HBG006738; -.
InParanoid; O14686; -.
KO; K09187; -.
OMA; QSTNYAV; -.
OrthoDB; EOG091G000T; -.
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; -.
GeneWiki; MLL2; -.
GenomeRNAi; 8085; -.
PRO; PR:O14686; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167548; -.
CleanEx; HS_MLL2; -.
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:0042800; F:histone methyltransferase activity (H3-K4 specific); TAS:Reactome.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 from RNA polymerase II promoter; 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.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; 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.
Pfam; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 2.
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; Complete proteome; 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 Histone-lysine N-methyltransferase 2D.
/FTId=PRO_0000124878.
REPEAT 442 446 1.
REPEAT 460 464 2.
REPEAT 469 473 3.
REPEAT 496 500 4.
REPEAT 504 508 5.
REPEAT 521 525 6.
REPEAT 555 559 7.
REPEAT 564 568 8.
REPEAT 573 577 9.
REPEAT 582 586 10.
REPEAT 609 613 11.
REPEAT 618 622 12.
REPEAT 627 631 13.
REPEAT 645 649 14.
REPEAT 663 667 15.
DOMAIN 5175 5235 FYR N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00875}.
DOMAIN 5236 5321 FYR C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00876}.
DOMAIN 5397 5513 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 5521 5537 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
ZN_FING 104 149 C2HC pre-PHD-type 1; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU01146}.
ZN_FING 170 218 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 226 276 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 229 274 RING-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 273 323 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 276 321 RING-type 2; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 1377 1430 PHD-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1427 1477 PHD-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1504 1559 PHD-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1507 1557 RING-type 3; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 5029 5069 C2HC pre-PHD-type 2.
{ECO:0000255|PROSITE-ProRule:PRU01146}.
ZN_FING 5090 5137 PHD-type 7. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 439 668 15 X 5 AA repeats of S/P-P-P-E/P-E/A.
REGION 5474 5475 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COILED 2669 2707 {ECO:0000255}.
COILED 3249 3282 {ECO:0000255}.
COILED 3562 3614 {ECO:0000255}.
COILED 3714 3750 {ECO:0000255}.
COILED 3897 3975 {ECO:0000255}.
MOTIF 2686 2690 LXXLL motif 1.
MOTIF 3038 3042 LXXLL motif 2.
MOTIF 4222 4236 LXXLL motif 3.
MOTIF 4253 4257 LXXLL motif 4.
MOTIF 4463 4467 LXXLL motif 5.
MOTIF 4990 4994 LXXLL motif 6.
COMPBIAS 229 326 Cys-rich.
COMPBIAS 374 1197 Pro-rich.
COMPBIAS 1290 1328 Arg-rich.
COMPBIAS 1351 1355 Poly-Glu.
COMPBIAS 1397 1510 Cys-rich.
COMPBIAS 2107 2626 Pro-rich.
COMPBIAS 2385 2392 Poly-Pro.
COMPBIAS 2707 2713 Poly-Ala.
COMPBIAS 2811 2822 Gln-rich.
COMPBIAS 2862 2978 Pro-rich.
COMPBIAS 3261 4275 Gln-rich.
COMPBIAS 4241 4360 Pro-rich.
COMPBIAS 4909 4977 Pro-rich.
COMPBIAS 5494 5497 Poly-Ile.
METAL 5477 5477 Zinc. {ECO:0000250}.
METAL 5525 5525 Zinc. {ECO:0000250}.
METAL 5527 5527 Zinc. {ECO:0000250}.
METAL 5532 5532 Zinc. {ECO:0000250}.
BINDING 5451 5451 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 1151 1151 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1195 1195 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1249 1249 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1267 1267 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 1270 1270 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 1606 1606 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1671 1671 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1820 1820 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1834 1834 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1843 1843 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1865 1865 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 2239 2239 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2240 2240 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2246 2246 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 2260 2260 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2274 2274 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2309 2309 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2311 2311 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2342 2342 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 2535 2535 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 2640 2640 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2836 2836 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 3079 3079 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 3130 3130 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 3197 3197 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 3199 3199 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3433 3433 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 3727 3727 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 4198 4198 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q6PDK2}.
MOD_RES 4215 4215 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 4359 4359 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 4465 4465 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 4738 4738 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 4776 4776 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 4822 4822 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 4849 4849 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 4756 4756 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 4880 4880 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1729 1729 E -> EGET (in isoform 3).
{ECO:0000303|PubMed:9247308}.
/FTId=VSP_008560.
VARIANT 170 170 Q -> H (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074216.
VARIANT 170 170 Q -> L (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074217.
VARIANT 337 337 S -> L (in KABUK1; unknown pathological
significance; dbSNP:rs200245957).
{ECO:0000269|PubMed:22126750}.
/FTId=VAR_074218.
VARIANT 476 476 A -> T (in dbSNP:rs1064210).
/FTId=VAR_057359.
VARIANT 543 543 S -> L (in KABUK1; unknown pathological
significance; dbSNP:rs776242478).
{ECO:0000269|PubMed:21607748}.
/FTId=VAR_074219.
VARIANT 647 647 P -> Q (in KABUK1; dbSNP:rs200088180).
{ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23320472}.
/FTId=VAR_074220.
VARIANT 692 692 P -> T (in dbSNP:rs202076833).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064370.
VARIANT 813 813 P -> L (in dbSNP:rs75226229).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064371.
VARIANT 1192 1192 V -> M (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21607748}.
/FTId=VAR_074221.
VARIANT 1258 1258 R -> Q (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074222.
VARIANT 1376 1376 M -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074223.
VARIANT 1380 1380 C -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074224.
VARIANT 1388 1388 R -> L (in KABUK1; unknown pathological
significance; dbSNP:rs202217665).
{ECO:0000269|PubMed:21671394}.
/FTId=VAR_074225.
VARIANT 1417 1417 M -> V (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074226.
VARIANT 1418 1418 L -> M (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074227.
VARIANT 1423 1423 R -> C (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074228.
VARIANT 1424 1424 C -> F (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:24739679}.
/FTId=VAR_074229.
VARIANT 1430 1430 C -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21671394}.
/FTId=VAR_074230.
VARIANT 1445 1445 C -> G (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074231.
VARIANT 1453 1453 H -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21607748}.
/FTId=VAR_074232.
VARIANT 1471 1471 C -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074233.
VARIANT 1471 1471 C -> Y (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21671394}.
/FTId=VAR_074234.
VARIANT 1522 1522 Q -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074235.
VARIANT 1526 1526 C -> F (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074236.
VARIANT 1718 1718 A -> V (in KABUK1; unknown pathological
significance; dbSNP:rs111266743).
{ECO:0000269|PubMed:21607748}.
/FTId=VAR_074237.
VARIANT 2382 2382 P -> S (in dbSNP:rs3741626).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064372.
VARIANT 2460 2460 R -> C (in dbSNP:rs570260017).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064373.
VARIANT 2557 2557 P -> L (in dbSNP:rs189888707).
{ECO:0000269|PubMed:21280141,
ECO:0000269|PubMed:23320472}.
/FTId=VAR_064374.
VARIANT 2652 2652 M -> L (in dbSNP:rs147706410).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074238.
VARIANT 2841 2841 P -> T (in KABUK1; unknown pathological
significance; dbSNP:rs763347763).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074239.
VARIANT 3398 3398 M -> V (in dbSNP:rs75937132).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064375.
VARIANT 3419 3419 D -> G (in dbSNP:rs146044282).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064376.
VARIANT 3876 3876 L -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074240.
VARIANT 3897 3897 L -> S (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074241.
VARIANT 4010 4010 S -> P (in dbSNP:rs80132640).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074242.
VARIANT 4353 4353 P -> L (in KABUK1; unknown pathological
significance; dbSNP:rs778418522).
{ECO:0000269|PubMed:22126750}.
/FTId=VAR_074243.
VARIANT 4357 4357 R -> S (in dbSNP:rs533214351).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064377.
VARIANT 4420 4420 R -> Q (in KABUK1; unknown pathological
significance; dbSNP:rs375999143).
{ECO:0000269|PubMed:24739679}.
/FTId=VAR_074244.
VARIANT 5028 5028 D -> E (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074245.
VARIANT 5030 5030 R -> C (in KABUK1).
{ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813}.
/FTId=VAR_074246.
VARIANT 5034 5034 F -> V (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074247.
VARIANT 5040 5040 D -> G (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074248.
VARIANT 5047 5047 A -> V (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:22126750}.
/FTId=VAR_074249.
VARIANT 5048 5048 R -> C (in KABUK1; dbSNP:rs398123724).
{ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750,
ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813}.
/FTId=VAR_074250.
VARIANT 5048 5048 R -> H (in KABUK1).
{ECO:0000269|PubMed:23320472,
ECO:0000269|PubMed:23913813}.
/FTId=VAR_074251.
VARIANT 5059 5059 H -> P (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074252.
VARIANT 5109 5109 C -> F (in KABUK1).
{ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394}.
/FTId=VAR_063830.
VARIANT 5154 5154 R -> Q (in KABUK1).
{ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23913813}.
/FTId=VAR_074253.
VARIANT 5179 5179 R -> H (in KABUK1; dbSNP:rs267607237).
{ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:23913813}.
/FTId=VAR_063831.
VARIANT 5189 5189 G -> R (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074254.
VARIANT 5210 5210 Y -> C (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064378.
VARIANT 5214 5214 R -> C (in KABUK1).
{ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750,
ECO:0000269|PubMed:23320472}.
/FTId=VAR_074255.
VARIANT 5214 5214 R -> H (in KABUK1; dbSNP:rs398123729).
{ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394}.
/FTId=VAR_063832.
VARIANT 5224 5224 R -> H (in dbSNP:rs3782356).
/FTId=VAR_017115.
VARIANT 5340 5340 R -> L (in KABUK1).
{ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394}.
/FTId=VAR_063833.
VARIANT 5340 5340 R -> Q (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21658225}.
/FTId=VAR_074256.
VARIANT 5351 5351 R -> Q (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23913813}.
/FTId=VAR_074257.
VARIANT 5428 5428 G -> D (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:21280141}.
/FTId=VAR_064379.
VARIANT 5432 5432 R -> W (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:23320472}.
/FTId=VAR_074258.
VARIANT 5464 5464 T -> M (in KABUK1; dbSNP:rs267607238).
{ECO:0000269|PubMed:20711175,
ECO:0000269|PubMed:21671394}.
/FTId=VAR_063834.
VARIANT 5471 5471 R -> T (in KABUK1).
{ECO:0000269|PubMed:21671394,
ECO:0000269|PubMed:22126750}.
/FTId=VAR_074259.
VARIANT 5481 5481 C -> Y (in KABUK1; unknown pathological
significance).
{ECO:0000269|PubMed:22126750}.
/FTId=VAR_074260.
VARIANT 5498 5498 S -> F (in KABUK1).
{ECO:0000269|PubMed:21607748,
ECO:0000269|PubMed:23320472}.
/FTId=VAR_074261.
CONFLICT 5 5 K -> N (in Ref. 1; AAC51734).
{ECO:0000305}.
CONFLICT 14 14 E -> Q (in Ref. 1; AAC51734).
{ECO:0000305}.
CONFLICT 75 75 S -> A (in Ref. 1; AAC51734).
{ECO:0000305}.
CONFLICT 156 156 E -> Q (in Ref. 1; AAC51734).
{ECO:0000305}.
CONFLICT 674 948 Missing (in Ref. 1; AAC51734).
{ECO:0000305}.
CONFLICT 1178 1178 Q -> R (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 1544 1547 EQAA -> DHAP (in Ref. 1; AAC51734/
AAC51735). {ECO:0000305}.
CONFLICT 1761 1761 K -> R (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 1766 1766 D -> G (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 2171 2171 V -> A (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 2413 2413 A -> V (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 3079 3079 K -> E (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 3287 3287 S -> P (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 3319 3319 G -> V (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 3422 3422 D -> G (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4478 4478 R -> Q (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4747 4747 A -> D (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4793 4793 A -> D (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4826 4826 A -> G (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4865 4865 P -> A (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4871 4871 S -> R (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4893 4893 S -> R (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 4974 4974 S -> T (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 5116 5116 A -> G (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
CONFLICT 5522 5522 K -> E (in Ref. 1; AAC51734/AAC51735).
{ECO:0000305}.
HELIX 5339 5341 {ECO:0000244|PDB:3UVK}.
HELIX 5384 5398 {ECO:0000244|PDB:4Z4P}.
STRAND 5399 5403 {ECO:0000244|PDB:4Z4P}.
STRAND 5405 5415 {ECO:0000244|PDB:4Z4P}.
STRAND 5422 5425 {ECO:0000244|PDB:4Z4P}.
STRAND 5428 5432 {ECO:0000244|PDB:4Z4P}.
HELIX 5433 5444 {ECO:0000244|PDB:4Z4P}.
TURN 5445 5447 {ECO:0000244|PDB:4Z4P}.
STRAND 5452 5454 {ECO:0000244|PDB:4Z4P}.
STRAND 5456 5462 {ECO:0000244|PDB:4Z4P}.
TURN 5464 5466 {ECO:0000244|PDB:4Z4P}.
HELIX 5469 5472 {ECO:0000244|PDB:4Z4P}.
STRAND 5480 5488 {ECO:0000244|PDB:4Z4P}.
STRAND 5491 5500 {ECO:0000244|PDB:4Z4P}.
STRAND 5516 5520 {ECO:0000244|PDB:4Z4P}.
STRAND 5534 5536 {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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EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
EIAAB24937 All1,ALL-1,Histone-lysine N-methyltransferase MLL,Hrx,Mll,Mll1,Mouse,Mus musculus,Zinc finger protein HRX
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
EIAAB12655 BAT8,C6orf30,EHMT2,Euchromatic histone-lysine N-methyltransferase 2,G9A,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Homo sap
EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se


 

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