KMT2D_HUMAN
ID KMT2D_HUMAN Reviewed; 5537 AA.
AC O14686; O14687;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Histone-lysine N-methyltransferase 2D;
DE Short=Lysine N-methyltransferase 2D;
DE EC=2.1.1.364 {ECO:0000269|PubMed:25561738};
DE AltName: Full=ALL1-related protein;
DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 2;
GN Name=KMT2D; Synonyms=ALR, MLL2, MLL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=9247308; DOI=10.1038/sj.onc.1201211;
RA Prasad R., Zhadanov A.B., Sedkov Y., Bullrich F., Druck T., Rallapalli R.,
RA Yano T., Alder H., Croce C.M., Huebner K., Mazo A., Canaani E.;
RT "Structure and expression pattern of human ALR, a novel gene with strong
RT homology to ALL-1 involved in acute leukemia and to Drosophila trithorax.";
RL Oncogene 15:549-560(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP IDENTIFICATION IN THE MLL2/3 COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=12482968; DOI=10.1128/mcb.23.1.140-149.2003;
RA Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J.,
RA Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O.,
RA Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.;
RT "Activating signal cointegrator 2 belongs to a novel steady-state complex
RT that contains a subset of trithorax group proteins.";
RL Mol. Cell. Biol. 23:140-149(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE MLL2 COMPLEX, LXXLL MOTIFS, AND INTERACTION
RP WITH ESR1.
RX PubMed=16603732; DOI=10.1074/jbc.m513245200;
RA Mo R., Rao S.M., Zhu Y.-J.;
RT "Identification of the MLL2 complex as a coactivator for estrogen receptor
RT alpha.";
RL J. Biol. Chem. 281:15714-15720(2006).
RN [6]
RP IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
RX PubMed=17021013; DOI=10.1073/pnas.0607313103;
RA Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K.,
RA Roeder R.G., Lee J.W.;
RT "Coactivator as a target gene specificity determinant for histone H3 lysine
RT 4 methyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP MLL2/3 COMPLEX.
RX PubMed=17500065; DOI=10.1074/jbc.m701574200;
RA Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:20395-20406(2007).
RN [8]
RP IDENTIFICATION IN THE MLL2/3 COMPLEX.
RX PubMed=17851529; DOI=10.1038/nature06192;
RA Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S.,
RA Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M., Chang H.Y.,
RA Shi Y.;
RT "A histone H3 lysine 27 demethylase regulates animal posterior
RT development.";
RL Nature 449:689-694(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION IN THE MLL2/3 COMPLEX.
RX PubMed=17761849; DOI=10.1126/science.1149042;
RA Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D.,
RA Di Croce L., Shiekhattar R.;
RT "Demethylation of H3K27 regulates polycomb recruitment and H2A
RT ubiquitination.";
RL Science 318:447-450(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4738, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-2274; SER-2309;
RP SER-2311; THR-3197 AND SER-4822, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274; THR-3197;
RP SER-4359 AND SER-4822, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2246; LYS-3079; LYS-3433;
RP LYS-4465 AND LYS-4776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; THR-3197; SER-3199;
RP SER-4215; SER-4359 AND SER-4738, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274 AND SER-4738,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; SER-1671; SER-1820;
RP SER-1834; THR-1843; THR-2240; SER-2260; SER-2274; SER-2640; SER-3130;
RP SER-3199; SER-4359; SER-4738; SER-4822 AND SER-4849, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION IN MLL2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=23508102; DOI=10.1128/mcb.01742-12;
RA van Nuland R., Smits A.H., Pallaki P., Jansen P.W., Vermeulen M.,
RA Timmers H.T.;
RT "Quantitative dissection and stoichiometry determination of the human
RT SET1/MLL histone methyltransferase complexes.";
RL Mol. Cell. Biol. 33:2067-2077(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1151; THR-1195; SER-1249;
RP SER-2239 AND SER-4738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-3727, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4756, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4756 AND LYS-4880, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ASN-5474.
RX PubMed=25561738; DOI=10.1074/jbc.m114.627646;
RA Shinsky S.A., Monteith K.E., Viggiano S., Cosgrove M.S.;
RT "Biochemical reconstitution and phylogenetic comparison of human SET1
RT family core complexes involved in histone methylation.";
RL J. Biol. Chem. 290:6361-6375(2015).
RN [25] {ECO:0007744|PDB:4ERQ}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 5333-5346 IN COMPLEX WITH WDR5,
RP INTERACTION WITH WDR5, AND MOTIF WIN.
RX PubMed=22665483; DOI=10.1074/jbc.m112.364125;
RA Dharmarajan V., Lee J.H., Patel A., Skalnik D.G., Cosgrove M.S.;
RT "Structural basis for WDR5 interaction (Win) motif recognition in human
RT SET1 family histone methyltransferases.";
RL J. Biol. Chem. 287:27275-27289(2012).
RN [26] {ECO:0007744|PDB:3UVK}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 5337-5347 IN COMPLEX WITH WDR5,
RP INTERACTION WITH WDR5, AND MOTIF WIN.
RX PubMed=22266653; DOI=10.1093/nar/gkr1235;
RA Zhang P., Lee H., Brunzelle J.S., Couture J.F.;
RT "The plasticity of WDR5 peptide-binding cleft enables the binding of the
RT SET1 family of histone methyltransferases.";
RL Nucleic Acids Res. 40:4237-4246(2012).
RN [27]
RP VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464, AND
RP INVOLVEMENT IN KABUK1.
RX PubMed=20711175; DOI=10.1038/ng.646;
RA Ng S.B., Bigham A.W., Buckingham K.J., Hannibal M.C., McMillin M.J.,
RA Gildersleeve H.I., Beck A.E., Tabor H.K., Cooper G.M., Mefford H.C.,
RA Lee C., Turner E.H., Smith J.D., Rieder M.J., Yoshiura K., Matsumoto N.,
RA Ohta T., Niikawa N., Nickerson D.A., Bamshad M.J., Shendure J.;
RT "Exome sequencing identifies MLL2 mutations as a cause of Kabuki
RT syndrome.";
RL Nat. Genet. 42:790-793(2010).
RN [28]
RP VARIANTS KABUK1 LEU-1388; ARG-1430; TYR-1471; CYS-5048; PHE-5109; HIS-5179;
RP CYS-5214; HIS-5214; LEU-5340; MET-5464 AND THR-5471.
RX PubMed=21671394; DOI=10.1002/ajmg.a.34074;
RA Hannibal M.C., Buckingham K.J., Ng S.B., Ming J.E., Beck A.E.,
RA McMillin M.J., Gildersleeve H.I., Bigham A.W., Tabor H.K., Mefford H.C.,
RA Cook J., Yoshiura K., Matsumoto T., Matsumoto N., Miyake N., Tonoki H.,
RA Naritomi K., Kaname T., Nagai T., Ohashi H., Kurosawa K., Hou J.W.,
RA Ohta T., Liang D., Sudo A., Morris C.A., Banka S., Black G.C.,
RA Clayton-Smith J., Nickerson D.A., Zackai E.H., Shaikh T.H., Donnai D.,
RA Niikawa N., Shendure J., Bamshad M.J.;
RT "Spectrum of MLL2 (ALR) mutations in 110 cases of Kabuki syndrome.";
RL Am. J. Med. Genet. A 155A:1511-1516(2011).
RN [29]
RP VARIANTS KABUK1 LEU-543; GLN-647; MET-1192; ARG-1453; VAL-1718; GLN-5154
RP AND PHE-5498.
RX PubMed=21607748; DOI=10.1007/s00439-011-1004-y;
RA Li Y., Boegershausen N., Alanay Y., Simsek Kiper P.O., Plume N., Keupp K.,
RA Pohl E., Pawlik B., Rachwalski M., Milz E., Thoenes M., Albrecht B.,
RA Prott E.C., Lehmkuehler M., Demuth S., Utine G.E., Boduroglu K.,
RA Frankenbusch K., Borck G., Gillessen-Kaesbach G., Yigit G., Wieczorek D.,
RA Wollnik B.;
RT "A mutation screen in patients with Kabuki syndrome.";
RL Hum. Genet. 130:715-724(2011).
RN [30]
RP VARIANTS KABUK1 CYS-5210 AND ASP-5428, AND VARIANTS THR-692; LEU-813;
RP SER-2382; CYS-2460; LEU-2557; VAL-3398; GLY-3419 AND SER-4357.
RX PubMed=21280141; DOI=10.1002/humu.21416;
RA Paulussen A.D., Stegmann A.P., Blok M.J., Tserpelis D., Posma-Velter C.,
RA Detisch Y., Smeets E.E., Wagemans A., Schrander J.J.,
RA van den Boogaard M.J., van der Smagt J., van Haeringen A.,
RA Stolte-Dijkstra I., Kerstjens-Frederikse W.S., Mancini G.M., Wessels M.W.,
RA Hennekam R.C., Vreeburg M., Geraedts J., de Ravel T., Fryns J.P.,
RA Smeets H.J., Devriendt K., Schrander-Stumpel C.T.;
RT "MLL2 mutation spectrum in 45 patients with Kabuki syndrome.";
RL Hum. Mutat. 32:E2018-E2025(2011).
RN [31]
RP VARIANTS KABUK1 GLN-1258; VAL-1417; MET-1418; ARG-1522; THR-2841; GLU-5028;
RP VAL-5034; PRO-5059 AND GLN-5340.
RX PubMed=21658225; DOI=10.1186/1750-1172-6-38;
RA Micale L., Augello B., Fusco C., Selicorni A., Loviglio M.N., Silengo M.C.,
RA Reymond A., Gumiero B., Zucchetti F., D'Addetta E.V., Belligni E.,
RA Calcagni A., Digilio M.C., Dallapiccola B., Faravelli F., Forzano F.,
RA Accadia M., Bonfante A., Clementi M., Daolio C., Douzgou S., Ferrari P.,
RA Fischetto R., Garavelli L., Lapi E., Mattina T., Melis D., Patricelli M.G.,
RA Priolo M., Prontera P., Renieri A., Mencarelli M.A., Scarano G.,
RA della Monica M., Toschi B., Turolla L., Vancini A., Zatterale A.,
RA Gabrielli O., Zelante L., Merla G.;
RT "Mutation spectrum of MLL2 in a cohort of Kabuki syndrome patients.";
RL Orphanet J. Rare Dis. 6:38-38(2011).
RN [32]
RP VARIANTS KABUK1 LEU-337; LEU-4353; VAL-5047; CYS-5048; CYS-5214; THR-5471
RP AND TYR-5481.
RX PubMed=22126750; DOI=10.1038/ejhg.2011.220;
RA Banka S., Veeramachaneni R., Reardon W., Howa rd E., Bunstone S., Ragge N.,
RA Parker M.J., Crow Y.J., Kerr B., Kingston H., Metcalfe K., Chandler K.,
RA Magee A., Stewart F., McConnell V.P., Donnelly D.E., Berland S., Houge G.,
RA Morton J.E., Oley C., Revencu N., Park S.M., Davies S.J., Fry A.E.,
RA Lynch S.A., Gill H., Schweiger S., Lam W.W., Tolmie J., Mohammed S.N.,
RA Hobson E., Smith A., Blyth M., Bennett C., Vasudevan P.C.,
RA Garcia-Minaur S., Henderson A., Goodship J., Wright M.J., Fisher R.,
RA Gibbons R., Price S.M., C de Silva D., Temple I.K., Collins A.L.,
RA Lachlan K., Elmslie F., McEntagart M., Castle B., Clayton-Smith J.,
RA Black G.C., Donnai D.;
RT "How genetically heterogeneous is Kabuki syndrome?: MLL2 testing in 116
RT patients, review and analyses of mutation and phenotypic spectrum.";
RL Eur. J. Hum. Genet. 20:381-388(2012).
RN [33]
RP VARIANTS KABUK1 ARG-1376; CYS-1423; GLY-1445; PHE-1526; CYS-5030; GLY-5040;
RP CYS-5048; HIS-5048; GLN-5154; HIS-5179; ARG-5189 AND GLN-5351.
RX PubMed=23913813; DOI=10.1002/ajmg.a.36072;
RA Miyake N., Koshimizu E., Okamoto N., Mizuno S., Ogata T., Nagai T.,
RA Kosho T., Ohashi H., Kato M., Sasaki G., Mabe H., Watanabe Y., Yoshino M.,
RA Matsuishi T., Takanashi J., Shotelersuk V., Tekin M., Ochi N., Kubota M.,
RA Ito N., Ihara K., Hara T., Tonoki H., Ohta T., Saito K., Matsuo M.,
RA Urano M., Enokizono T., Sato A., Tanaka H., Ogawa A., Fujita T., Hiraki Y.,
RA Kitanaka S., Matsubara Y., Makita T., Taguri M., Nakashima M.,
RA Tsurusaki Y., Saitsu H., Yoshiura K., Matsumoto N., Niikawa N.;
RT "MLL2 and KDM6A mutations in patients with Kabuki syndrome.";
RL Am. J. Med. Genet. A 161A:2234-2243(2013).
RN [34]
RP VARIANTS KABUK1 PHE-1424 AND GLN-4420.
RX PubMed=24739679; DOI=10.1038/jhg.2014.25;
RA Cheon C.K., Sohn Y.B., Ko J.M., Lee Y.J., Song J.S., Moon J.W., Yang B.K.,
RA Ha I.S., Bae E.J., Jin H.S., Jeong S.Y.;
RT "Identification of KMT2D and KDM6A mutations by exome sequencing in Korean
RT patients with Kabuki syndrome.";
RL J. Hum. Genet. 59:321-325(2014).
RN [35]
RP VARIANTS KABUK1 HIS-170; LEU-170; GLN-647; ARG-1380; ARG-1471; ARG-3876;
RP SER-3897; CYS-5030; CYS-5048; HIS-5048; CYS-5214; TRP-5432 AND PHE-5498,
RP AND VARIANTS LEU-2557; LEU-2652 AND PRO-4010.
RX PubMed=23320472; DOI=10.1111/cge.12081;
RA Makrythanasis P., van Bon B.W., Steehouwer M., Rodriguez-Santiago B.,
RA Simpson M., Dias P., Anderlid B.M., Arts P., Bhat M., Augello B.,
RA Biamino E., Bongers E.M., Del Campo M., Cordeiro I., Cueto-Gonzalez A.M.,
RA Cusco I., Deshpande C., Frysira E., Izatt L., Flores R., Galan E.,
RA Gener B., Gilissen C., Granneman S.M., Hoyer J., Yntema H.G., Kets C.M.,
RA Koolen D.A., Marcelis C.L., Medeira A., Micale L., Mohammed S.,
RA de Munnik S.A., Nordgren A., Psoni S., Reardon W., Revencu N., Roscioli T.,
RA Ruiterkamp-Versteeg M., Santos H.G., Schoumans J.,
RA Schuurs-Hoeijmakers J.H., Silengo M.C., Toledo L., Vendrell T.,
RA van der Burgt I., van Lier B., Zweier C., Reymond A., Trembath R.C.,
RA Perez-Jurado L., Dupont J., de Vries B.B., Brunner H.G., Veltman J.A.,
RA Merla G., Antonarakis S.E., Hoischen A.;
RT "MLL2 mutation detection in 86 patients with Kabuki syndrome: a genotype-
RT phenotype study.";
RL Clin. Genet. 84:539-545(2013).
CC -!- FUNCTION: Histone methyltransferase that catalyzes methyl group
CC transfer from S-adenosyl-L-methionine to the epsilon-amino group of
CC 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin
CC remodeling machinery predominantly forms H3K4me1 methylation marks at
CC active chromatin sites where transcription and DNA repair take place
CC (PubMed:25561738, PubMed:17500065). Acts as a coactivator for estrogen
CC receptor by being recruited by ESR1, thereby activating transcription
CC (PubMed:16603732). {ECO:0000269|PubMed:16603732,
CC ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:25561738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000269|PubMed:25561738};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000305|PubMed:25561738};
CC -!- SUBUNIT: Component of the MLL2 complex (also named ASCOM complex), at
CC least composed of catalytic subunit KMT2D/MLL2, ASH2L, RBBP5, WDR5,
CC NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin
CC (PubMed:23508102, PubMed:17500065, PubMed:12482968, PubMed:16603732,
CC PubMed:17021013, PubMed:17761849, PubMed:17851529). Forms a core
CC complex with the evolutionary conserved subcomplex WRAD composed of
CC WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits; WRAD differentially
CC stimulates the methyltransferase activity (PubMed:25561738). Interacts
CC with ESR1; interaction is direct (PubMed:16603732). Interacts (via WIN
CC motif) with WDR5 (PubMed:22665483, PubMed:22266653).
CC {ECO:0000269|PubMed:12482968, ECO:0000269|PubMed:16603732,
CC ECO:0000269|PubMed:17021013, ECO:0000269|PubMed:17500065,
CC ECO:0000269|PubMed:17761849, ECO:0000269|PubMed:17851529,
CC ECO:0000269|PubMed:22266653, ECO:0000269|PubMed:22665483,
CC ECO:0000269|PubMed:23508102, ECO:0000269|PubMed:25561738}.
CC -!- INTERACTION:
CC O14686; P10275: AR; NbExp=3; IntAct=EBI-996065, EBI-608057;
CC O14686; Q9UBL3-3: ASH2L; NbExp=2; IntAct=EBI-996065, EBI-16130425;
CC O14686; P03372: ESR1; NbExp=3; IntAct=EBI-996065, EBI-78473;
CC O14686; P61964: WDR5; NbExp=9; IntAct=EBI-996065, EBI-540834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23508102}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14686-1; Sequence=Displayed;
CC Name=3;
CC IsoId=O14686-3; Sequence=VSP_008560;
CC -!- TISSUE SPECIFICITY: Expressed in most adult tissues, including a
CC variety of hematoipoietic cells, with the exception of the liver.
CC -!- DOMAIN: LXXLL motifs 5 and 6 are essential for the association with
CC ESR1 nuclear receptor.
CC -!- DISEASE: Kabuki syndrome 1 (KABUK1) [MIM:147920]: An autosomal
CC dominant, congenital syndrome characterized by intellectual disability
CC and additional features, including postnatal dwarfism, a peculiar
CC facies characterized by long palpebral fissures with eversion of the
CC lateral third of the lower eyelids, a broad and depressed nasal tip,
CC large prominent earlobes, a cleft or high-arched palate, scoliosis,
CC short fifth finger, persistence of fingerpads, radiographic
CC abnormalities of the vertebrae, hands, and hip joints, and recurrent
CC otitis media in infancy. {ECO:0000269|PubMed:20711175,
CC ECO:0000269|PubMed:21280141, ECO:0000269|PubMed:21607748,
CC ECO:0000269|PubMed:21658225, ECO:0000269|PubMed:21671394,
CC ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472,
CC ECO:0000269|PubMed:23913813, ECO:0000269|PubMed:24739679}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: This gene mapped to a chromosomal region involved in
CC duplications and translocations associated with cancer.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: Another protein KMT2B/MLL4, located on chromosome 19, was
CC first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often referred to
CC as MLL2 and vice versa in the literature. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; AF010403; AAC51734.1; -; mRNA.
DR EMBL; AF010404; AAC51735.1; -; mRNA.
DR EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44873.1; -. [O14686-1]
DR PIR; T03454; T03454.
DR PIR; T03455; T03455.
DR RefSeq; NP_003473.3; NM_003482.3. [O14686-1]
DR RefSeq; XP_005269219.1; XM_005269162.4.
DR RefSeq; XP_006719677.1; XM_006719614.3. [O14686-3]
DR PDB; 3UVK; X-ray; 1.40 A; B=5337-5347.
DR PDB; 4ERQ; X-ray; 1.91 A; D/E/F=5333-5346.
DR PDB; 4Z4P; X-ray; 2.20 A; A=5382-5536.
DR PDB; 6O7G; NMR; -; B=1503-1562.
DR PDBsum; 3UVK; -.
DR PDBsum; 4ERQ; -.
DR PDBsum; 4Z4P; -.
DR PDBsum; 6O7G; -.
DR SMR; O14686; -.
DR BioGRID; 113758; 132.
DR ComplexPortal; CPX-7104; Histone-lysine N-methyltransferase complex, KMT2D variant.
DR CORUM; O14686; -.
DR DIP; DIP-37875N; -.
DR ELM; O14686; -.
DR IntAct; O14686; 98.
DR MINT; O14686; -.
DR STRING; 9606.ENSP00000301067; -.
DR BindingDB; O14686; -.
DR ChEMBL; CHEMBL2189114; -.
DR GlyGen; O14686; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O14686; -.
DR PhosphoSitePlus; O14686; -.
DR BioMuta; KMT2D; -.
DR CPTAC; CPTAC-978; -.
DR EPD; O14686; -.
DR jPOST; O14686; -.
DR MassIVE; O14686; -.
DR MaxQB; O14686; -.
DR PaxDb; O14686; -.
DR PeptideAtlas; O14686; -.
DR PRIDE; O14686; -.
DR ProteomicsDB; 48168; -. [O14686-1]
DR ProteomicsDB; 48169; -. [O14686-3]
DR Antibodypedia; 25797; 143 antibodies from 32 providers.
DR DNASU; 8085; -.
DR Ensembl; ENST00000301067.12; ENSP00000301067.7; ENSG00000167548.18. [O14686-1]
DR Ensembl; ENST00000685166.1; ENSP00000509386.1; ENSG00000167548.18. [O14686-3]
DR GeneID; 8085; -.
DR KEGG; hsa:8085; -.
DR MANE-Select; ENST00000301067.12; ENSP00000301067.7; NM_003482.4; NP_003473.3.
DR UCSC; uc001rta.4; human. [O14686-1]
DR CTD; 8085; -.
DR DisGeNET; 8085; -.
DR GeneCards; KMT2D; -.
DR GeneReviews; KMT2D; -.
DR HGNC; HGNC:7133; KMT2D.
DR HPA; ENSG00000167548; Low tissue specificity.
DR MalaCards; KMT2D; -.
DR MIM; 147920; phenotype.
DR MIM; 602113; gene.
DR neXtProt; NX_O14686; -.
DR OpenTargets; ENSG00000167548; -.
DR Orphanet; 589856; Choanal atresia-athelia-hypothyroidism-delayed puberty-short stature syndrome.
DR Orphanet; 2322; Kabuki syndrome.
DR PharmGKB; PA30846; -.
DR VEuPathDB; HostDB:ENSG00000167548; -.
DR eggNOG; KOG4443; Eukaryota.
DR GeneTree; ENSGT00940000156707; -.
DR HOGENOM; CLU_000065_0_0_1; -.
DR InParanoid; O14686; -.
DR OMA; MPLPHEG; -.
DR OrthoDB; 61027at2759; -.
DR PhylomeDB; O14686; -.
DR TreeFam; TF354317; -.
DR BioCyc; MetaCyc:HS09574-MON; -.
DR PathwayCommons; O14686; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR SignaLink; O14686; -.
DR SIGNOR; O14686; -.
DR BioGRID-ORCS; 8085; 239 hits in 1057 CRISPR screens.
DR ChiTaRS; KMT2D; human.
DR GeneWiki; MLL2; -.
DR GenomeRNAi; 8085; -.
DR Pharos; O14686; Tbio.
DR PRO; PR:O14686; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O14686; protein.
DR Bgee; ENSG00000167548; Expressed in buccal mucosa cell and 182 other tissues.
DR ExpressionAtlas; O14686; baseline and differential.
DR Genevisible; O14686; HS.
DR GO; GO:0035097; C:histone methyltransferase complex; IPI:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IDA:CACAO.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IDA:CACAO.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:CACAO.
DR GO; GO:0001555; P:oocyte growth; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR CDD; cd15695; ePHD1_KMT2D; 1.
DR CDD; cd15698; ePHD2_KMT2D; 1.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 6.
DR IDEAL; IID00356; -.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037890; KMT2D.
DR InterPro; IPR041961; KMT2D_ePHD1.
DR InterPro; IPR041964; KMT2D_ePHD2.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45888:SF2; PTHR45888:SF2; 4.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00249; PHD; 7.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00184; RING; 6.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF57903; SSF57903; 5.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51805; EPHD; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 5.
DR PROSITE; PS50016; ZF_PHD_2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Coiled coil; Disease variant; Intellectual disability; Isopeptide bond;
KW Metal-binding; Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..5537
FT /note="Histone-lysine N-methyltransferase 2D"
FT /id="PRO_0000124878"
FT REPEAT 442..446
FT /note="1"
FT REPEAT 460..464
FT /note="2"
FT REPEAT 469..473
FT /note="3"
FT REPEAT 496..500
FT /note="4"
FT REPEAT 504..508
FT /note="5"
FT REPEAT 521..525
FT /note="6"
FT REPEAT 555..559
FT /note="7"
FT REPEAT 564..568
FT /note="8"
FT REPEAT 573..577
FT /note="9"
FT REPEAT 582..586
FT /note="10"
FT REPEAT 609..613
FT /note="11"
FT REPEAT 618..622
FT /note="12"
FT REPEAT 627..631
FT /note="13"
FT REPEAT 645..649
FT /note="14"
FT REPEAT 663..667
FT /note="15"
FT DOMAIN 5175..5235
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 5236..5321
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 5397..5513
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 5521..5537
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 104..149
FT /note="C2HC pre-PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 170..218
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 226..276
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 229..274
FT /note="RING-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 273..323
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 276..321
FT /note="RING-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 1377..1430
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1427..1477
FT /note="PHD-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1504..1559
FT /note="PHD-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1507..1557
FT /note="RING-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 5029..5069
FT /note="C2HC pre-PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 5090..5137
FT /note="PHD-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..668
FT /note="15 X 5 AA repeats of S/P-P-P-E/P-E/A"
FT REGION 1340..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2697..2814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2835..2996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3078..3110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3147..3209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3263..3339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3462..3499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3596..3673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3758..3802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3984..4191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4233..4398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4410..4452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4503..4544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4613..4727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4822..4857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4905..4980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2669..2707
FT /evidence="ECO:0000255"
FT COILED 3249..3282
FT /evidence="ECO:0000255"
FT COILED 3562..3614
FT /evidence="ECO:0000255"
FT COILED 3714..3750
FT /evidence="ECO:0000255"
FT COILED 3897..3975
FT /evidence="ECO:0000255"
FT MOTIF 2686..2690
FT /note="LXXLL motif 1"
FT MOTIF 3038..3042
FT /note="LXXLL motif 2"
FT MOTIF 4222..4236
FT /note="LXXLL motif 3"
FT MOTIF 4253..4257
FT /note="LXXLL motif 4"
FT MOTIF 4463..4467
FT /note="LXXLL motif 5"
FT MOTIF 4990..4994
FT /note="LXXLL motif 6"
FT MOTIF 5337..5342
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000269|PubMed:22266653,
FT ECO:0000269|PubMed:22665483"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..892
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..2002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2186..2207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2346..2367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2409..2428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2545..2564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2570..2607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2657..2677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2729..2750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3163..3182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3264..3289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3298..3317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3462..3487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3596..3629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3781..3796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4021..4050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4092..4167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4233..4257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4303..4321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4322..4336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4337..4356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4514..4544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4620..4634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4647..4670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4827..4849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4909..4956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4962..4980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5451
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 5474..5475
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 5477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 5532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1843
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1865
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 2239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2246
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 2535
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 2640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2836
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 3079
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3197
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 3199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3433
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3727
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4198
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDK2"
FT MOD_RES 4215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4465
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 4738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 4822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 4849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 4756
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 4880
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1729
FT /note="E -> EGET (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9247308"
FT /id="VSP_008560"
FT VARIANT 170
FT /note="Q -> H (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074216"
FT VARIANT 170
FT /note="Q -> L (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074217"
FT VARIANT 337
FT /note="S -> L (in KABUK1; unknown pathological
FT significance; dbSNP:rs200245957)"
FT /evidence="ECO:0000269|PubMed:22126750"
FT /id="VAR_074218"
FT VARIANT 476
FT /note="A -> T (in dbSNP:rs1064210)"
FT /id="VAR_057359"
FT VARIANT 543
FT /note="S -> L (in KABUK1; unknown pathological
FT significance; dbSNP:rs776242478)"
FT /evidence="ECO:0000269|PubMed:21607748"
FT /id="VAR_074219"
FT VARIANT 647
FT /note="P -> Q (in KABUK1; dbSNP:rs200088180)"
FT /evidence="ECO:0000269|PubMed:21607748,
FT ECO:0000269|PubMed:23320472"
FT /id="VAR_074220"
FT VARIANT 692
FT /note="P -> T (in dbSNP:rs202076833)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064370"
FT VARIANT 813
FT /note="P -> L (in dbSNP:rs75226229)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064371"
FT VARIANT 1192
FT /note="V -> M (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21607748"
FT /id="VAR_074221"
FT VARIANT 1258
FT /note="R -> Q (in KABUK1; unknown pathological
FT significance; dbSNP:rs1341612248)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074222"
FT VARIANT 1376
FT /note="M -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074223"
FT VARIANT 1380
FT /note="C -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074224"
FT VARIANT 1388
FT /note="R -> L (in KABUK1; unknown pathological
FT significance; dbSNP:rs202217665)"
FT /evidence="ECO:0000269|PubMed:21671394"
FT /id="VAR_074225"
FT VARIANT 1417
FT /note="M -> V (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074226"
FT VARIANT 1418
FT /note="L -> M (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074227"
FT VARIANT 1423
FT /note="R -> C (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074228"
FT VARIANT 1424
FT /note="C -> F (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24739679"
FT /id="VAR_074229"
FT VARIANT 1430
FT /note="C -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21671394"
FT /id="VAR_074230"
FT VARIANT 1445
FT /note="C -> G (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074231"
FT VARIANT 1453
FT /note="H -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21607748"
FT /id="VAR_074232"
FT VARIANT 1471
FT /note="C -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074233"
FT VARIANT 1471
FT /note="C -> Y (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21671394"
FT /id="VAR_074234"
FT VARIANT 1522
FT /note="Q -> R (in KABUK1; unknown pathological
FT significance; dbSNP:rs1592145879)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074235"
FT VARIANT 1526
FT /note="C -> F (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074236"
FT VARIANT 1718
FT /note="A -> V (in KABUK1; unknown pathological
FT significance; dbSNP:rs111266743)"
FT /evidence="ECO:0000269|PubMed:21607748"
FT /id="VAR_074237"
FT VARIANT 2382
FT /note="P -> S (in dbSNP:rs3741626)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064372"
FT VARIANT 2460
FT /note="R -> C (in dbSNP:rs570260017)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064373"
FT VARIANT 2557
FT /note="P -> L (in dbSNP:rs189888707)"
FT /evidence="ECO:0000269|PubMed:21280141,
FT ECO:0000269|PubMed:23320472"
FT /id="VAR_064374"
FT VARIANT 2652
FT /note="M -> L (in dbSNP:rs147706410)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074238"
FT VARIANT 2841
FT /note="P -> T (in KABUK1; unknown pathological
FT significance; dbSNP:rs763347763)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074239"
FT VARIANT 3398
FT /note="M -> V (in dbSNP:rs75937132)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064375"
FT VARIANT 3419
FT /note="D -> G (in dbSNP:rs146044282)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064376"
FT VARIANT 3876
FT /note="L -> R (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074240"
FT VARIANT 3897
FT /note="L -> S (in KABUK1; unknown pathological
FT significance; dbSNP:rs1342235871)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074241"
FT VARIANT 4010
FT /note="S -> P (in dbSNP:rs80132640)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074242"
FT VARIANT 4353
FT /note="P -> L (in KABUK1; unknown pathological
FT significance; dbSNP:rs778418522)"
FT /evidence="ECO:0000269|PubMed:22126750"
FT /id="VAR_074243"
FT VARIANT 4357
FT /note="R -> S (in dbSNP:rs533214351)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064377"
FT VARIANT 4420
FT /note="R -> Q (in KABUK1; unknown pathological
FT significance; dbSNP:rs375999143)"
FT /evidence="ECO:0000269|PubMed:24739679"
FT /id="VAR_074244"
FT VARIANT 5028
FT /note="D -> E (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074245"
FT VARIANT 5030
FT /note="R -> C (in KABUK1; dbSNP:rs1555185875)"
FT /evidence="ECO:0000269|PubMed:23320472,
FT ECO:0000269|PubMed:23913813"
FT /id="VAR_074246"
FT VARIANT 5034
FT /note="F -> V (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074247"
FT VARIANT 5040
FT /note="D -> G (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074248"
FT VARIANT 5047
FT /note="A -> V (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22126750"
FT /id="VAR_074249"
FT VARIANT 5048
FT /note="R -> C (in KABUK1; dbSNP:rs398123724)"
FT /evidence="ECO:0000269|PubMed:21671394,
FT ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472,
FT ECO:0000269|PubMed:23913813"
FT /id="VAR_074250"
FT VARIANT 5048
FT /note="R -> H (in KABUK1; dbSNP:rs886041404)"
FT /evidence="ECO:0000269|PubMed:23320472,
FT ECO:0000269|PubMed:23913813"
FT /id="VAR_074251"
FT VARIANT 5059
FT /note="H -> P (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074252"
FT VARIANT 5109
FT /note="C -> F (in KABUK1)"
FT /evidence="ECO:0000269|PubMed:20711175,
FT ECO:0000269|PubMed:21671394"
FT /id="VAR_063830"
FT VARIANT 5154
FT /note="R -> Q (in KABUK1; dbSNP:rs886043497)"
FT /evidence="ECO:0000269|PubMed:21607748,
FT ECO:0000269|PubMed:23913813"
FT /id="VAR_074253"
FT VARIANT 5179
FT /note="R -> H (in KABUK1; dbSNP:rs267607237)"
FT /evidence="ECO:0000269|PubMed:20711175,
FT ECO:0000269|PubMed:21671394, ECO:0000269|PubMed:23913813"
FT /id="VAR_063831"
FT VARIANT 5189
FT /note="G -> R (in KABUK1; unknown pathological
FT significance; dbSNP:rs1555185701)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074254"
FT VARIANT 5210
FT /note="Y -> C (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064378"
FT VARIANT 5214
FT /note="R -> C (in KABUK1; dbSNP:rs398123728)"
FT /evidence="ECO:0000269|PubMed:21671394,
FT ECO:0000269|PubMed:22126750, ECO:0000269|PubMed:23320472"
FT /id="VAR_074255"
FT VARIANT 5214
FT /note="R -> H (in KABUK1; dbSNP:rs398123729)"
FT /evidence="ECO:0000269|PubMed:20711175,
FT ECO:0000269|PubMed:21671394"
FT /id="VAR_063832"
FT VARIANT 5224
FT /note="R -> H (in dbSNP:rs3782356)"
FT /id="VAR_017115"
FT VARIANT 5340
FT /note="R -> L (in KABUK1)"
FT /evidence="ECO:0000269|PubMed:20711175,
FT ECO:0000269|PubMed:21671394"
FT /id="VAR_063833"
FT VARIANT 5340
FT /note="R -> Q (in KABUK1; unknown pathological
FT significance; dbSNP:rs1565756106)"
FT /evidence="ECO:0000269|PubMed:21658225"
FT /id="VAR_074256"
FT VARIANT 5351
FT /note="R -> Q (in KABUK1; unknown pathological
FT significance; dbSNP:rs1555185217)"
FT /evidence="ECO:0000269|PubMed:23913813"
FT /id="VAR_074257"
FT VARIANT 5428
FT /note="G -> D (in KABUK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:21280141"
FT /id="VAR_064379"
FT VARIANT 5432
FT /note="R -> W (in KABUK1; unknown pathological
FT significance; dbSNP:rs1565753611)"
FT /evidence="ECO:0000269|PubMed:23320472"
FT /id="VAR_074258"
FT VARIANT 5464
FT /note="T -> M (in KABUK1; dbSNP:rs267607238)"
FT /evidence="ECO:0000269|PubMed:20711175,
FT ECO:0000269|PubMed:21671394"
FT /id="VAR_063834"
FT VARIANT 5471
FT /note="R -> T (in KABUK1)"
FT /evidence="ECO:0000269|PubMed:21671394,
FT ECO:0000269|PubMed:22126750"
FT /id="VAR_074259"
FT VARIANT 5481
FT /note="C -> Y (in KABUK1; unknown pathological
FT significance; dbSNP:rs1388523736)"
FT /evidence="ECO:0000269|PubMed:22126750"
FT /id="VAR_074260"
FT VARIANT 5498
FT /note="S -> F (in KABUK1)"
FT /evidence="ECO:0000269|PubMed:21607748,
FT ECO:0000269|PubMed:23320472"
FT /id="VAR_074261"
FT MUTAGEN 5474
FT /note="N->A: Abolishes interaction with S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25561738"
FT CONFLICT 5
FT /note="K -> N (in Ref. 1; AAC51734)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="E -> Q (in Ref. 1; AAC51734)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> A (in Ref. 1; AAC51734)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="E -> Q (in Ref. 1; AAC51734)"
FT /evidence="ECO:0000305"
FT CONFLICT 674..948
FT /note="Missing (in Ref. 1; AAC51734)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="Q -> R (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1544..1547
FT /note="EQAA -> DHAP (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1761
FT /note="K -> R (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1766
FT /note="D -> G (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 2171
FT /note="V -> A (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 2413
FT /note="A -> V (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 3079
FT /note="K -> E (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 3287
FT /note="S -> P (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 3319
FT /note="G -> V (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 3422
FT /note="D -> G (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4478
FT /note="R -> Q (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4747
FT /note="A -> D (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4793
FT /note="A -> D (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4826
FT /note="A -> G (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4865
FT /note="P -> A (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4871
FT /note="S -> R (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4893
FT /note="S -> R (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 4974
FT /note="S -> T (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 5116
FT /note="A -> G (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT CONFLICT 5522
FT /note="K -> E (in Ref. 1; AAC51734/AAC51735)"
FT /evidence="ECO:0000305"
FT TURN 1508..1511
FT /evidence="ECO:0007829|PDB:6O7G"
FT STRAND 1516..1518
FT /evidence="ECO:0007829|PDB:6O7G"
FT STRAND 1520..1522
FT /evidence="ECO:0007829|PDB:6O7G"
FT TURN 1524..1526
FT /evidence="ECO:0007829|PDB:6O7G"
FT STRAND 1529..1532
FT /evidence="ECO:0007829|PDB:6O7G"
FT HELIX 1533..1535
FT /evidence="ECO:0007829|PDB:6O7G"
FT HELIX 1540..1548
FT /evidence="ECO:0007829|PDB:6O7G"
FT HELIX 1556..1560
FT /evidence="ECO:0007829|PDB:6O7G"
FT HELIX 5339..5341
FT /evidence="ECO:0007829|PDB:3UVK"
FT HELIX 5384..5398
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5399..5403
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5405..5415
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5422..5425
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5428..5432
FT /evidence="ECO:0007829|PDB:4Z4P"
FT HELIX 5433..5444
FT /evidence="ECO:0007829|PDB:4Z4P"
FT TURN 5445..5447
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5452..5454
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5456..5462
FT /evidence="ECO:0007829|PDB:4Z4P"
FT TURN 5464..5466
FT /evidence="ECO:0007829|PDB:4Z4P"
FT HELIX 5469..5472
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5480..5488
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5491..5500
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5516..5520
FT /evidence="ECO:0007829|PDB:4Z4P"
FT STRAND 5534..5536
FT /evidence="ECO:0007829|PDB:4Z4P"
SQ 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
