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Database: UniProt
Entry: O14686
LinkDB: O14686
Original site: O14686 
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   13-FEB-2019, entry version 181.
DE   RecName: Full=Histone-lysine N-methyltransferase 2D;
DE            Short=Lysine N-methyltransferase 2D;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Rallapalli R., Yano T., Alder H., Croce C.M., Huebner K., Mazo A.,
RA   Canaani E.;
RT   "Structure and expression pattern of human ALR, a novel gene with
RT   strong homology to ALL-1 involved in acute leukemia and to Drosophila
RT   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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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.,
RA   Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C.,
RA   Lee J.W.;
RT   "Activating signal cointegrator 2 belongs to a novel steady-state
RT   complex 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
RP   BY 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   FUNCTION, ENZYME ACTIVITY, IDENTIFICATION IN THE MLL2 COMPLEX, LXXLL
RP   MOTIFS, AND INTERACTION 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
RT   receptor 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.,
RA   Lee S.K., Roeder R.G., Lee J.W.;
RT   "Coactivator as a target gene specificity determinant for histone H3
RT   lysine 4 methyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006).
RN   [7]
RP   FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   IDENTIFICATION IN THE 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   FUNCTION, AND 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.,
RA   Chang H.Y., 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,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., 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
RP   BY 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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient 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
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274;
RP   THR-3197; SER-4359 AND SER-4822, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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
RP   SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; THR-3197;
RP   SER-3199; SER-4215; SER-4359 AND SER-4738, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274 AND
RP   SER-4738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; SER-1671;
RP   SER-1820; SER-1834; THR-1843; THR-2240; SER-2260; SER-2274; SER-2640;
RP   SER-3130; SER-3199; SER-4359; SER-4738; SER-4822 AND SER-4849, AND
RP   IDENTIFICATION BY 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1151; THR-1195;
RP   SER-1249; SER-2239 AND SER-4738, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-3727, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4756, AND IDENTIFICATION BY
RP   MASS 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   [22]
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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [23]
RP   VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464,
RP   AND 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.,
RA   Matsumoto N., Ohta T., Niikawa N., Nickerson D.A., Bamshad M.J.,
RA   Shendure J.;
RT   "Exome sequencing identifies MLL2 mutations as a cause of Kabuki
RT   syndrome.";
RL   Nat. Genet. 42:790-793(2010).
RN   [24]
RP   VARIANTS KABUK1 LEU-1388; ARG-1430; TYR-1471; CYS-5048; PHE-5109;
RP   HIS-5179; 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.,
RA   Mefford H.C., Cook J., Yoshiura K., Matsumoto T., Matsumoto N.,
RA   Miyake N., Tonoki H., Naritomi K., Kaname T., Nagai T., Ohashi H.,
RA   Kurosawa K., Hou J.W., Ohta T., Liang D., Sudo A., Morris C.A.,
RA   Banka S., Black G.C., Clayton-Smith J., Nickerson D.A., Zackai E.H.,
RA   Shaikh T.H., Donnai D., 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   [25]
RP   VARIANTS KABUK1 LEU-543; GLN-647; MET-1192; ARG-1453; VAL-1718;
RP   GLN-5154 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.,
RA   Keupp K., Pohl E., Pawlik B., Rachwalski M., Milz E., Thoenes M.,
RA   Albrecht B., Prott E.C., Lehmkuehler M., Demuth S., Utine G.E.,
RA   Boduroglu K., Frankenbusch K., Borck G., Gillessen-Kaesbach G.,
RA   Yigit G., Wieczorek D., Wollnik B.;
RT   "A mutation screen in patients with Kabuki syndrome.";
RL   Hum. Genet. 130:715-724(2011).
RN   [26]
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.,
RA   Posma-Velter C., 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.,
RA   Wessels M.W., Hennekam R.C., Vreeburg M., Geraedts J., de Ravel T.,
RA   Fryns J.P., 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   [27]
RP   VARIANTS KABUK1 GLN-1258; VAL-1417; MET-1418; ARG-1522; THR-2841;
RP   GLU-5028; 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.,
RA   Silengo M.C., Reymond A., Gumiero B., Zucchetti F., D'Addetta E.V.,
RA   Belligni E., Calcagni A., Digilio M.C., Dallapiccola B., Faravelli F.,
RA   Forzano F., Accadia M., Bonfante A., Clementi M., Daolio C.,
RA   Douzgou S., Ferrari P., Fischetto R., Garavelli L., Lapi E.,
RA   Mattina T., Melis D., Patricelli M.G., Priolo M., Prontera P.,
RA   Renieri A., Mencarelli M.A., Scarano G., della Monica M., Toschi B.,
RA   Turolla L., Vancini A., Zatterale A., Gabrielli O., Zelante L.,
RA   Merla G.;
RT   "Mutation spectrum of MLL2 in a cohort of Kabuki syndrome patients.";
RL   Orphanet J. Rare Dis. 6:38-38(2011).
RN   [28]
RP   VARIANTS KABUK1 LEU-337; LEU-4353; VAL-5047; CYS-5048; CYS-5214;
RP   THR-5471 AND TYR-5481.
RX   PubMed=22126750; DOI=10.1038/ejhg.2011.220;
RA   Banka S., Veeramachaneni R., Reardon W., Howa rd E., Bunstone S.,
RA   Ragge N., Parker M.J., Crow Y.J., Kerr B., Kingston H., Metcalfe K.,
RA   Chandler K., Magee A., Stewart F., McConnell V.P., Donnelly D.E.,
RA   Berland S., Houge G., Morton J.E., Oley C., Revencu N., Park S.M.,
RA   Davies S.J., Fry A.E., Lynch S.A., Gill H., Schweiger S., Lam W.W.,
RA   Tolmie J., Mohammed S.N., Hobson E., Smith A., Blyth M., Bennett C.,
RA   Vasudevan P.C., Garcia-Minaur S., Henderson A., Goodship J.,
RA   Wright M.J., Fisher R., Gibbons R., Price S.M., C de Silva D.,
RA   Temple I.K., Collins A.L., Lachlan K., Elmslie F., McEntagart M.,
RA   Castle B., Clayton-Smith J., Black G.C., Donnai D.;
RT   "How genetically heterogeneous is Kabuki syndrome?: MLL2 testing in
RT   116 patients, review and analyses of mutation and phenotypic
RT   spectrum.";
RL   Eur. J. Hum. Genet. 20:381-388(2012).
RN   [29]
RP   VARIANTS KABUK1 ARG-1376; CYS-1423; GLY-1445; PHE-1526; CYS-5030;
RP   GLY-5040; CYS-5048; HIS-5048; GLN-5154; HIS-5179; ARG-5189 AND
RP   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.,
RA   Yoshino M., Matsuishi T., Takanashi J., Shotelersuk V., Tekin M.,
RA   Ochi N., Kubota M., Ito N., Ihara K., Hara T., Tonoki H., Ohta T.,
RA   Saito K., Matsuo M., Urano M., Enokizono T., Sato A., Tanaka H.,
RA   Ogawa A., Fujita T., Hiraki Y., Kitanaka S., Matsubara Y., Makita T.,
RA   Taguri M., Nakashima M., Tsurusaki Y., Saitsu H., Yoshiura K.,
RA   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   [30]
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.,
RA   Yang B.K., Ha I.S., Bae E.J., Jin H.S., Jeong S.Y.;
RT   "Identification of KMT2D and KDM6A mutations by exome sequencing in
RT   Korean patients with Kabuki syndrome.";
RL   J. Hum. Genet. 59:321-325(2014).
RN   [31]
RP   VARIANTS KABUK1 HIS-170; LEU-170; GLN-647; ARG-1380; ARG-1471;
RP   ARG-3876; SER-3897; CYS-5030; CYS-5048; HIS-5048; CYS-5214; TRP-5432
RP   AND PHE-5498, 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.,
RA   Cueto-Gonzalez A.M., Cusco I., Deshpande C., Frysira E., Izatt L.,
RA   Flores R., Galan E., Gener B., Gilissen C., Granneman S.M., Hoyer J.,
RA   Yntema H.G., Kets C.M., Koolen D.A., Marcelis C.L., Medeira A.,
RA   Micale L., Mohammed S., de Munnik S.A., Nordgren A., Psoni S.,
RA   Reardon W., Revencu N., Roscioli T., Ruiterkamp-Versteeg M.,
RA   Santos H.G., Schoumans J., Schuurs-Hoeijmakers J.H., Silengo M.C.,
RA   Toledo L., Vendrell T., van der Burgt I., van Lier B., Zweier C.,
RA   Reymond A., Trembath R.C., Perez-Jurado L., Dupont J., de Vries B.B.,
RA   Brunner H.G., Veltman J.A., Merla G., Antonarakis S.E., Hoischen A.;
RT   "MLL2 mutation detection in 86 patients with Kabuki syndrome: a
RT   genotype-phenotype study.";
RL   Clin. Genet. 84:539-545(2013).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
CC       H3 (H3K4me). H3K4me represents a specific tag for epigenetic
CC       transcriptional activation. Acts as a coactivator for estrogen
CC       receptor by being recruited by ESR1, thereby activating
CC       transcription. {ECO:0000269|PubMed:16603732,
CC       ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17851529}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:16603732,
CC         ECO:0000269|PubMed:17500065};
CC   -!- SUBUNIT: Component of the MLL2/3 complex (also named ASCOM
CC       complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L,
CC       RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and
CC       alpha- and beta-tubulin. Interacts with ESR1; interaction is
CC       direct. {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   -!- INTERACTION:
CC       P10275:AR; NbExp=2; IntAct=EBI-996065, EBI-608057;
CC       Q9UBL3-3:ASH2L; NbExp=2; IntAct=EBI-996065, EBI-16130425;
CC       P03372:ESR1; NbExp=3; IntAct=EBI-996065, EBI-78473;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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
CC       with ESR1 nuclear receptor.
CC   -!- DISEASE: Kabuki syndrome 1 (KABUK1) [MIM:147920]: A congenital
CC       mental retardation syndrome with additional features, including
CC       postnatal dwarfism, a peculiar facies characterized by long
CC       palpebral fissures with eversion of the lateral third of the lower
CC       eyelids, a broad and depressed nasal tip, large prominent
CC       earlobes, a cleft or high-arched palate, scoliosis, short fifth
CC       finger, persistence of fingerpads, radiographic abnormalities of
CC       the vertebrae, hands, and hip joints, and recurrent otitis media
CC       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}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: This gene mapped to a chromosomal region involved
CC       in duplications and translocations associated with cancer.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- CAUTION: Another protein KMT2B/MLL4, located on chromosome 19, was
CC       first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often
CC       referred to as MLL2 and vice versa in the literature.
CC       {ECO:0000305}.
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. [O14686-1]
DR   RefSeq; XP_006719677.1; XM_006719614.3. [O14686-3]
DR   UniGene; Hs.731384; -.
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   PDBsum; 3UVK; -.
DR   PDBsum; 4ERQ; -.
DR   PDBsum; 4Z4P; -.
DR   ProteinModelPortal; O14686; -.
DR   SMR; O14686; -.
DR   BioGrid; 113758; 38.
DR   CORUM; O14686; -.
DR   DIP; DIP-37875N; -.
DR   ELM; O14686; -.
DR   IntAct; O14686; 29.
DR   MINT; O14686; -.
DR   STRING; 9606.ENSP00000301067; -.
DR   BindingDB; O14686; -.
DR   ChEMBL; CHEMBL2189114; -.
DR   iPTMnet; O14686; -.
DR   PhosphoSitePlus; O14686; -.
DR   BioMuta; KMT2D; -.
DR   EPD; O14686; -.
DR   jPOST; O14686; -.
DR   MaxQB; O14686; -.
DR   PaxDb; O14686; -.
DR   PeptideAtlas; O14686; -.
DR   PRIDE; O14686; -.
DR   ProteomicsDB; 48168; -.
DR   ProteomicsDB; 48169; -. [O14686-3]
DR   Ensembl; ENST00000301067; ENSP00000301067; ENSG00000167548. [O14686-1]
DR   GeneID; 8085; -.
DR   KEGG; hsa:8085; -.
DR   UCSC; uc001rta.4; human. [O14686-1]
DR   CTD; 8085; -.
DR   DisGeNET; 8085; -.
DR   EuPathDB; HostDB:ENSG00000167548.14; -.
DR   GeneCards; KMT2D; -.
DR   GeneReviews; KMT2D; -.
DR   HGNC; HGNC:7133; KMT2D.
DR   HPA; HPA035977; -.
DR   MalaCards; KMT2D; -.
DR   MIM; 147920; phenotype.
DR   MIM; 602113; gene.
DR   neXtProt; NX_O14686; -.
DR   OpenTargets; ENSG00000167548; -.
DR   Orphanet; 2322; Kabuki syndrome.
DR   PharmGKB; PA30846; -.
DR   eggNOG; KOG4443; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156707; -.
DR   HOVERGEN; HBG006738; -.
DR   InParanoid; O14686; -.
DR   KO; K09187; -.
DR   OMA; HLRIPPQ; -.
DR   OrthoDB; 236292at2759; -.
DR   PhylomeDB; O14686; -.
DR   TreeFam; TF354317; -.
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   SIGNOR; O14686; -.
DR   ChiTaRS; KMT2D; human.
DR   GeneWiki; MLL2; -.
DR   GenomeRNAi; 8085; -.
DR   PRO; PR:O14686; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000167548; Expressed in 100 organ(s), highest expression level in left lobe of thyroid gland.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
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:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
DR   GO; GO:0006342; P:chromatin silencing; ISS:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
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:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 6.
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; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
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; PTHR22884:SF380; PTHR22884:SF380; 3.
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   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; Complete proteome; Disease mutation; Isopeptide bond;
KW   Mental retardation; Metal-binding; Methylation; Methyltransferase;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   5537       Histone-lysine N-methyltransferase 2D.
FT                                /FTId=PRO_0000124878.
FT   REPEAT      442    446       1.
FT   REPEAT      460    464       2.
FT   REPEAT      469    473       3.
FT   REPEAT      496    500       4.
FT   REPEAT      504    508       5.
FT   REPEAT      521    525       6.
FT   REPEAT      555    559       7.
FT   REPEAT      564    568       8.
FT   REPEAT      573    577       9.
FT   REPEAT      582    586       10.
FT   REPEAT      609    613       11.
FT   REPEAT      618    622       12.
FT   REPEAT      627    631       13.
FT   REPEAT      645    649       14.
FT   REPEAT      663    667       15.
FT   DOMAIN     5175   5235       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     5236   5321       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     5397   5513       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     5521   5537       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     104    149       C2HC pre-PHD-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01146}.
FT   ZN_FING     170    218       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING     226    276       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     229    274       RING-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING     273    323       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     276    321       RING-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING    1377   1430       PHD-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1427   1477       PHD-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1504   1559       PHD-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1507   1557       RING-type 3; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING    5029   5069       C2HC pre-PHD-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01146}.
FT   ZN_FING    5090   5137       PHD-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION      439    668       15 X 5 AA repeats of S/P-P-P-E/P-E/A.
FT   REGION     5474   5475       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED     2669   2707       {ECO:0000255}.
FT   COILED     3249   3282       {ECO:0000255}.
FT   COILED     3562   3614       {ECO:0000255}.
FT   COILED     3714   3750       {ECO:0000255}.
FT   COILED     3897   3975       {ECO:0000255}.
FT   MOTIF      2686   2690       LXXLL motif 1.
FT   MOTIF      3038   3042       LXXLL motif 2.
FT   MOTIF      4222   4236       LXXLL motif 3.
FT   MOTIF      4253   4257       LXXLL motif 4.
FT   MOTIF      4463   4467       LXXLL motif 5.
FT   MOTIF      4990   4994       LXXLL motif 6.
FT   COMPBIAS    229    326       Cys-rich.
FT   COMPBIAS    374   1197       Pro-rich.
FT   COMPBIAS   1290   1328       Arg-rich.
FT   COMPBIAS   1351   1355       Poly-Glu.
FT   COMPBIAS   1397   1510       Cys-rich.
FT   COMPBIAS   2107   2626       Pro-rich.
FT   COMPBIAS   2385   2392       Poly-Pro.
FT   COMPBIAS   2707   2713       Poly-Ala.
FT   COMPBIAS   2811   2822       Gln-rich.
FT   COMPBIAS   2862   2978       Pro-rich.
FT   COMPBIAS   3261   4275       Gln-rich.
FT   COMPBIAS   4241   4360       Pro-rich.
FT   COMPBIAS   4909   4977       Pro-rich.
FT   COMPBIAS   5494   5497       Poly-Ile.
FT   METAL      5477   5477       Zinc. {ECO:0000250}.
FT   METAL      5525   5525       Zinc. {ECO:0000250}.
FT   METAL      5527   5527       Zinc. {ECO:0000250}.
FT   METAL      5532   5532       Zinc. {ECO:0000250}.
FT   BINDING    5451   5451       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES      27     27       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     744    744       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    1151   1151       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1195   1195       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1249   1249       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1267   1267       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    1270   1270       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    1606   1606       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1671   1671       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1820   1820       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1834   1834       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1843   1843       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1865   1865       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    2239   2239       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    2240   2240       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2246   2246       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    2260   2260       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2274   2274       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2309   2309       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    2311   2311       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    2342   2342       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    2535   2535       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    2640   2640       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2836   2836       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    3079   3079       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    3130   3130       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    3197   3197       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES    3199   3199       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    3433   3433       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    3727   3727       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    4198   4198       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:Q6PDK2}.
FT   MOD_RES    4215   4215       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    4359   4359       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    4465   4465       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    4738   4738       Phosphoserine.
FT                                {ECO:0000244|PubMed:18220336,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    4776   4776       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    4822   4822       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    4849   4849       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK   4756   4756       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   4880   4880       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ    1729   1729       E -> EGET (in isoform 3).
FT                                {ECO:0000303|PubMed:9247308}.
FT                                /FTId=VSP_008560.
FT   VARIANT     170    170       Q -> H (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074216.
FT   VARIANT     170    170       Q -> L (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074217.
FT   VARIANT     337    337       S -> L (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs200245957).
FT                                {ECO:0000269|PubMed:22126750}.
FT                                /FTId=VAR_074218.
FT   VARIANT     476    476       A -> T (in dbSNP:rs1064210).
FT                                /FTId=VAR_057359.
FT   VARIANT     543    543       S -> L (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs776242478).
FT                                {ECO:0000269|PubMed:21607748}.
FT                                /FTId=VAR_074219.
FT   VARIANT     647    647       P -> Q (in KABUK1; dbSNP:rs200088180).
FT                                {ECO:0000269|PubMed:21607748,
FT                                ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074220.
FT   VARIANT     692    692       P -> T (in dbSNP:rs202076833).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064370.
FT   VARIANT     813    813       P -> L (in dbSNP:rs75226229).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064371.
FT   VARIANT    1192   1192       V -> M (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21607748}.
FT                                /FTId=VAR_074221.
FT   VARIANT    1258   1258       R -> Q (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs1341612248).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074222.
FT   VARIANT    1376   1376       M -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074223.
FT   VARIANT    1380   1380       C -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074224.
FT   VARIANT    1388   1388       R -> L (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs202217665).
FT                                {ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_074225.
FT   VARIANT    1417   1417       M -> V (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074226.
FT   VARIANT    1418   1418       L -> M (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074227.
FT   VARIANT    1423   1423       R -> C (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074228.
FT   VARIANT    1424   1424       C -> F (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:24739679}.
FT                                /FTId=VAR_074229.
FT   VARIANT    1430   1430       C -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_074230.
FT   VARIANT    1445   1445       C -> G (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074231.
FT   VARIANT    1453   1453       H -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21607748}.
FT                                /FTId=VAR_074232.
FT   VARIANT    1471   1471       C -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074233.
FT   VARIANT    1471   1471       C -> Y (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_074234.
FT   VARIANT    1522   1522       Q -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074235.
FT   VARIANT    1526   1526       C -> F (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074236.
FT   VARIANT    1718   1718       A -> V (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs111266743).
FT                                {ECO:0000269|PubMed:21607748}.
FT                                /FTId=VAR_074237.
FT   VARIANT    2382   2382       P -> S (in dbSNP:rs3741626).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064372.
FT   VARIANT    2460   2460       R -> C (in dbSNP:rs570260017).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064373.
FT   VARIANT    2557   2557       P -> L (in dbSNP:rs189888707).
FT                                {ECO:0000269|PubMed:21280141,
FT                                ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_064374.
FT   VARIANT    2652   2652       M -> L (in dbSNP:rs147706410).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074238.
FT   VARIANT    2841   2841       P -> T (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs763347763).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074239.
FT   VARIANT    3398   3398       M -> V (in dbSNP:rs75937132).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064375.
FT   VARIANT    3419   3419       D -> G (in dbSNP:rs146044282).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064376.
FT   VARIANT    3876   3876       L -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074240.
FT   VARIANT    3897   3897       L -> S (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs1342235871).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074241.
FT   VARIANT    4010   4010       S -> P (in dbSNP:rs80132640).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074242.
FT   VARIANT    4353   4353       P -> L (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs778418522).
FT                                {ECO:0000269|PubMed:22126750}.
FT                                /FTId=VAR_074243.
FT   VARIANT    4357   4357       R -> S (in dbSNP:rs533214351).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064377.
FT   VARIANT    4420   4420       R -> Q (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs375999143).
FT                                {ECO:0000269|PubMed:24739679}.
FT                                /FTId=VAR_074244.
FT   VARIANT    5028   5028       D -> E (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074245.
FT   VARIANT    5030   5030       R -> C (in KABUK1).
FT                                {ECO:0000269|PubMed:23320472,
FT                                ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074246.
FT   VARIANT    5034   5034       F -> V (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074247.
FT   VARIANT    5040   5040       D -> G (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074248.
FT   VARIANT    5047   5047       A -> V (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22126750}.
FT                                /FTId=VAR_074249.
FT   VARIANT    5048   5048       R -> C (in KABUK1; dbSNP:rs398123724).
FT                                {ECO:0000269|PubMed:21671394,
FT                                ECO:0000269|PubMed:22126750,
FT                                ECO:0000269|PubMed:23320472,
FT                                ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074250.
FT   VARIANT    5048   5048       R -> H (in KABUK1; dbSNP:rs886041404).
FT                                {ECO:0000269|PubMed:23320472,
FT                                ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074251.
FT   VARIANT    5059   5059       H -> P (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074252.
FT   VARIANT    5109   5109       C -> F (in KABUK1).
FT                                {ECO:0000269|PubMed:20711175,
FT                                ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_063830.
FT   VARIANT    5154   5154       R -> Q (in KABUK1; dbSNP:rs886043497).
FT                                {ECO:0000269|PubMed:21607748,
FT                                ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074253.
FT   VARIANT    5179   5179       R -> H (in KABUK1; dbSNP:rs267607237).
FT                                {ECO:0000269|PubMed:20711175,
FT                                ECO:0000269|PubMed:21671394,
FT                                ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_063831.
FT   VARIANT    5189   5189       G -> R (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074254.
FT   VARIANT    5210   5210       Y -> C (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064378.
FT   VARIANT    5214   5214       R -> C (in KABUK1).
FT                                {ECO:0000269|PubMed:21671394,
FT                                ECO:0000269|PubMed:22126750,
FT                                ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074255.
FT   VARIANT    5214   5214       R -> H (in KABUK1; dbSNP:rs398123729).
FT                                {ECO:0000269|PubMed:20711175,
FT                                ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_063832.
FT   VARIANT    5224   5224       R -> H (in dbSNP:rs3782356).
FT                                /FTId=VAR_017115.
FT   VARIANT    5340   5340       R -> L (in KABUK1).
FT                                {ECO:0000269|PubMed:20711175,
FT                                ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_063833.
FT   VARIANT    5340   5340       R -> Q (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21658225}.
FT                                /FTId=VAR_074256.
FT   VARIANT    5351   5351       R -> Q (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23913813}.
FT                                /FTId=VAR_074257.
FT   VARIANT    5428   5428       G -> D (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:21280141}.
FT                                /FTId=VAR_064379.
FT   VARIANT    5432   5432       R -> W (in KABUK1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074258.
FT   VARIANT    5464   5464       T -> M (in KABUK1; dbSNP:rs267607238).
FT                                {ECO:0000269|PubMed:20711175,
FT                                ECO:0000269|PubMed:21671394}.
FT                                /FTId=VAR_063834.
FT   VARIANT    5471   5471       R -> T (in KABUK1).
FT                                {ECO:0000269|PubMed:21671394,
FT                                ECO:0000269|PubMed:22126750}.
FT                                /FTId=VAR_074259.
FT   VARIANT    5481   5481       C -> Y (in KABUK1; unknown pathological
FT                                significance; dbSNP:rs1388523736).
FT                                {ECO:0000269|PubMed:22126750}.
FT                                /FTId=VAR_074260.
FT   VARIANT    5498   5498       S -> F (in KABUK1).
FT                                {ECO:0000269|PubMed:21607748,
FT                                ECO:0000269|PubMed:23320472}.
FT                                /FTId=VAR_074261.
FT   CONFLICT      5      5       K -> N (in Ref. 1; AAC51734).
FT                                {ECO:0000305}.
FT   CONFLICT     14     14       E -> Q (in Ref. 1; AAC51734).
FT                                {ECO:0000305}.
FT   CONFLICT     75     75       S -> A (in Ref. 1; AAC51734).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       E -> Q (in Ref. 1; AAC51734).
FT                                {ECO:0000305}.
FT   CONFLICT    674    948       Missing (in Ref. 1; AAC51734).
FT                                {ECO:0000305}.
FT   CONFLICT   1178   1178       Q -> R (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   1544   1547       EQAA -> DHAP (in Ref. 1; AAC51734/
FT                                AAC51735). {ECO:0000305}.
FT   CONFLICT   1761   1761       K -> R (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   1766   1766       D -> G (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   2171   2171       V -> A (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   2413   2413       A -> V (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   3079   3079       K -> E (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   3287   3287       S -> P (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   3319   3319       G -> V (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   3422   3422       D -> G (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4478   4478       R -> Q (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4747   4747       A -> D (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4793   4793       A -> D (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4826   4826       A -> G (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4865   4865       P -> A (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4871   4871       S -> R (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4893   4893       S -> R (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   4974   4974       S -> T (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   5116   5116       A -> G (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   CONFLICT   5522   5522       K -> E (in Ref. 1; AAC51734/AAC51735).
FT                                {ECO:0000305}.
FT   HELIX      5339   5341       {ECO:0000244|PDB:3UVK}.
FT   HELIX      5384   5398       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5399   5403       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5405   5415       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5422   5425       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5428   5432       {ECO:0000244|PDB:4Z4P}.
FT   HELIX      5433   5444       {ECO:0000244|PDB:4Z4P}.
FT   TURN       5445   5447       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5452   5454       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5456   5462       {ECO:0000244|PDB:4Z4P}.
FT   TURN       5464   5466       {ECO:0000244|PDB:4Z4P}.
FT   HELIX      5469   5472       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5480   5488       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5491   5500       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5516   5520       {ECO:0000244|PDB:4Z4P}.
FT   STRAND     5534   5536       {ECO:0000244|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
//
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