KMT2C_MOUSE
ID KMT2C_MOUSE Reviewed; 4903 AA.
AC Q8BRH4; Q5YLV9; Q8BK12; Q8C6M3; Q923H5; Q923H6;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Histone-lysine N-methyltransferase 2C;
DE Short=Lysine N-methyltransferase 2C;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:Q8NEZ4};
DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog;
GN Name=Kmt2c; Synonyms=Mll3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=16459028; DOI=10.1016/j.gene.2005.11.013;
RA Brun M.-E., Gasca S., Girard C., Bouton K., De Massy B., De Sario A.;
RT "Characterization and expression analysis during embryo development of the
RT mouse ortholog of MLL3.";
RL Gene 371:25-33(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-814 AND 4803-4903.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 957-1376 AND 4214-4894.
RC TISSUE=Myeloma;
RX PubMed=11718452;
RA Tan Y.C., Chow V.T.;
RT "Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to
RT ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with
RT leukemia and developmental defects.";
RL Cancer Detect. Prev. 25:454-469(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2824, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1761; LYS-2005; LYS-2796 AND
RP LYS-2862, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2447; ARG-2563 AND ARG-4132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
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). Part of chromatin remodeling machinery
CC predominantly forms H3K4me1 methylation marks at active chromatin sites
CC where transcription and DNA repair take place. Likely plays a redundant
CC role with KMT2D in enriching H3K4me1 mark on primed and active enhancer
CC elements. {ECO:0000250|UniProtKB:Q8NEZ4}.
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:0000250|UniProtKB:Q8NEZ4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000250|UniProtKB:Q8NEZ4};
CC -!- SUBUNIT: Component of the MLL3 complex (also named ASCOM complex), at
CC least composed of catalytic subunit KMT2C/MLL3, ASH2L, RBBP5, WDR5,
CC NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin.
CC Forms a core complex with the evolutionary conserved subcomplex WRAD
CC composed of WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits; WRAD
CC differentially stimulates the methyltransferase activity. Interacts
CC (via WIN motif) with WDR5. {ECO:0000250|UniProtKB:Q8NEZ4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NEZ4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BRH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRH4-2; Sequence=VSP_020568, VSP_020569, VSP_020570,
CC VSP_020571, VSP_020572;
CC -!- TISSUE SPECIFICITY: In adult, detected in testis, kidney, spleen and
CC lung, weakly expressed in brain and absent in heart and liver. First
CC detected throughout the embryo at 8 dpc when expression is strong in
CC forebrain neuroepithelium and absent in heart. Expressed in the eye
CC lens between 10 and 14.5 dpc. By 13 dpc, expressed strongly in spinal
CC cord, hand/foot plates and gonads. {ECO:0000269|PubMed:16459028}.
CC -!- DOMAIN: The SET domain interacts with histone H3 but not H2A, H2B and
CC H4, and may have a H3 lysine specific methylation activity.
CC {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAN11291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY138582; AAN11291.1; ALT_INIT; mRNA.
DR EMBL; AC116469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK044828; BAC32109.1; -; mRNA.
DR EMBL; AK054270; BAC35712.2; -; mRNA.
DR EMBL; AK077567; BAC36867.1; -; mRNA.
DR EMBL; AY036886; AAK70213.1; -; mRNA.
DR EMBL; AY036887; AAK70214.1; -; mRNA.
DR SMR; Q8BRH4; -.
DR DIP; DIP-61282N; -.
DR IntAct; Q8BRH4; 6.
DR MINT; Q8BRH4; -.
DR STRING; 10090.ENSMUSP00000043874; -.
DR iPTMnet; Q8BRH4; -.
DR PhosphoSitePlus; Q8BRH4; -.
DR EPD; Q8BRH4; -.
DR jPOST; Q8BRH4; -.
DR MaxQB; Q8BRH4; -.
DR PaxDb; Q8BRH4; -.
DR PRIDE; Q8BRH4; -.
DR ProteomicsDB; 263638; -. [Q8BRH4-1]
DR ProteomicsDB; 263639; -. [Q8BRH4-2]
DR MGI; MGI:2444959; Kmt2c.
DR eggNOG; KOG4443; Eukaryota.
DR InParanoid; Q8BRH4; -.
DR PhylomeDB; Q8BRH4; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR ChiTaRS; Kmt2c; mouse.
DR PRO; PR:Q8BRH4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BRH4; protein.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISO:MGI.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR CDD; cd15696; ePHD1_KMT2C; 1.
DR CDD; cd15697; ePHD2_KMT2C; 1.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 7.
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; IPR000637; HMGI/Y_DNA-bd_CS.
DR InterPro; IPR037877; KMT2C.
DR InterPro; IPR041967; KMT2C_ePHD1.
DR InterPro; IPR041968; KMT2C_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:SF1; PTHR45888:SF1; 2.
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; 8.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00184; RING; 4.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF57903; SSF57903; 6.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS51805; EPHD; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS00354; HMGI_Y; 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; 6.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Alternative splicing;
KW Chromatin regulator; Coiled coil; DNA-binding; Lipoprotein; Metal-binding;
KW Methylation; Methyltransferase; Nucleus; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..4903
FT /note="Histone-lysine N-methyltransferase 2C"
FT /id="PRO_0000124880"
FT DOMAIN 435..488
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT DOMAIN 4537..4597
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 4598..4683
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 4763..4879
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 4887..4903
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DNA_BIND 34..46
FT /note="A.T hook"
FT ZN_FING 226..261
FT /note="C2HC pre-PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 282..330
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 340..390
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 343..388
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 387..437
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 463..519
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 950..1003
FT /note="PHD-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1000..1050
FT /note="PHD-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1077..1132
FT /note="PHD-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 4391..4431
FT /note="C2HC pre-PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 4452..4499
FT /note="PHD-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1791..2375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2561..2668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2702..2736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2786..2844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2920..2953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3198..3223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3329..3407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3444..3910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4159..4184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1330..1352
FT /evidence="ECO:0000255"
FT COILED 1743..1790
FT /evidence="ECO:0000255"
FT COILED 3047..3074
FT /evidence="ECO:0000255"
FT COILED 3166..3193
FT /evidence="ECO:0000255"
FT COILED 3224..3270
FT /evidence="ECO:0000255"
FT COILED 3387..3432
FT /evidence="ECO:0000255"
FT MOTIF 4699..4704
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT COMPBIAS 12..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2152..2178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2255..2269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2601..2632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2649..2668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2786..2810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2829..2843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2929..2950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3353..3374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3387..3407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3462..3523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3554..3588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3629..3652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3668..3699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3704..3737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3750..3764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3777..3791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3820..3835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3836..3871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3872..3890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3891..3905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4159..4174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4817
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 4840..4841
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 4843
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 4891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 4893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 4898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 751
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 1497
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 1761
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 2005
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2447
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2563
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2796
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 2822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 2824
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2826
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 2862
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 3709
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 4027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT MOD_RES 4132
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ4"
FT VAR_SEQ 839..878
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16459028"
FT /id="VSP_020568"
FT VAR_SEQ 1414..1448
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16459028"
FT /id="VSP_020569"
FT VAR_SEQ 1791..3080
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16459028"
FT /id="VSP_020570"
FT VAR_SEQ 3814..3884
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16459028"
FT /id="VSP_020571"
FT VAR_SEQ 4714..4717
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16459028"
FT /id="VSP_020572"
FT CONFLICT 28..36
FT /note="SPAAADKRP -> RSFVCGCGA (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> A (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..440
FT /note="NCRICIEC -> VSDFLICF (in Ref. 3; BAC32109)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="E -> G (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="D -> DA (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="S -> C (in Ref. 3; BAC35712)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="K -> E (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="F -> L (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="H -> Y (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324..1325
FT /note="VD -> LH (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 1737
FT /note="E -> V (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 1776
FT /note="Q -> R (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 3236
FT /note="M -> MM (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 3423..3424
FT /note="QR -> P (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 3657
FT /note="E -> G (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 3668
FT /note="A -> V (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 4283
FT /note="C -> Y (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 4306
FT /note="E -> D (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 4520
FT /note="Q -> R (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 4531
FT /note="V -> G (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
FT CONFLICT 4649
FT /note="Y -> H (in Ref. 1; AAN11291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4903 AA; 540187 MW; 0B896490B081BA6C CRC64;
MSSEEDRSAE QQQPPPAPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR ARKKPRSRGK
STVEDEDSMD GLETTETENI VETEIKEQSV EEDAETEVDS SKQPVSALQR SVSEESANSL
VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL KQFRVTPGLT LPWKDQPSNK DIDDNSSGTC
EKIQNYAPRK QRGQRKERPP QQSAVSCVSV STQTACEDQA GKLWDELSLV GLPDAIDVQA
LFDSTGTCWA HHRCVEWSLG ICQMEEPLLV NVDKAVVSGS TERCAFCKHL GATIKCCEEK
CTQMYHYPCA AGAGTFQDFS HFFLLCPEHI DQAPERSKED ANCAVCDSPG DLLDQFFCTT
CGQHYHGMCL DIAVTPLKRA GWQCPECKVC QNCKQSGEDS KMLVCDTCDK GYHTFCLQPV
MKSVPTNGWK CKNCRICIEC GTRSSTQWHH NCLICDTCYQ QQDNLCPFCG KCYHPELQKD
MLHCNMCKRW VHLECDKPTD QELDSQLKED YICMYCKHLG AEIDPLHPGN EVEMPELPTD
YASGMEIEGT EDEVVFLEQT VNKDVSDHQC RPGIVPDVQV YTEEPQKSNP LESPDTVGLI
TSESSDNKMN PDLANEIAHE VDTEKTEMLS KGRHVCEEDQ NEDRMEVTEN IEVLPHQTIV
PQEDLLLSED SEVASKELSP PKSAPETAAP EALLSPHSER SLSCKEPLLT ERVQEEMEQK
ENSEFSTGCV DFEMTLAVDS CDKDSSCQGD KYVELPAEEE STFSSATDLN KADVSSSSTL
CSDLPSCDML HGYPPAFNSA AGSIMPTTYI SVTPKIGMGK PAITKRKFSP GRPRSKQGAW
SNHNTVSPPS WAPDTSEGRE IFKPRQLSGS AIWSIKVGRG SGFPGKRRPR GAGLSGRGGR
GRSKLKSGIG AVVLPGVSAA DISSNKDEEE NSMHNTVVLF SSSDKFTLQQ DMCVVCGSFG
QGAEGRLLAC SQCGQCYHPY CVSIKITKVV LSKGWRCLEC TVCEACGKAT DPGRLLLCDD
CDISYHTYCL DPPLQTVPKG GWKCKWCVWC RHCGATSAGL RCEWQNNYTQ CAPCASLSSC
PVCCRNYREE DLILQCRQCD RWMHAVCQNL NTEEEVENVA DIGFDCSMCR PYMPVSNVPS
SDCCDSSLVA QIVTKVKELD PPKTYTQDGV CLTESGMSQL QSLTVTAPRR KRTKPKLKLK
IINQNSVAVL QTPPDIQSEH SRDGEMDDSR EGELMDCDGK SESSPEREAG DDETKGIEGT
DAIKKRKRKP YRPGIGGFMV RQRSRTGQGK AKRSVVRKDS SGSISEQLPS RDDGWREQLP
DTLVDEPVSV AENTDKIKKR YRKRKNKLEE TFPAYLQEAF FGKDLLDTSR QNKLSVDNLS
EDAAQLSFKT GFLDPSSDPL LSSSSTSAKP GTQGTADDPL ADISEVLNTD DDILGIISDD
LAKSVDHSDI GPTTADASSL PQPGVSQSSR PLTEEQLDGI LSPELDKMVT DGAILGKLYK
IPELGGKDVE DLFTAVLSPA TTQPAPLPQP PPPPQLLPMH NQDVFSRMPL MNGLIGPSPH
LPHNSLPPGS GLGTFPAIAQ SPYTDVRDKS PAFNAIASDP NSSWAPTTPS MEGENDTLSN
AQRSTLKWEK EEALGEMATV APVLYTNINF PNLKEEFPDW TTRVKQIAKL WRKASSQERA
PYVQKARDNR AALRINKVQM SNDSMKRQQQ QDSIDPSSRI DSDLFKDPLK QRESEHEQEW
KFRQQMRQKS KQQAKIEATQ KLEQVKNEQQ QQQQQQQQQQ QQQLASQHLL VAPGSDTPSS
GAQSPLTPQA GNGNVSPAQT FHKDLFSKHL PGTPASTPSD GVFVKPQPPP PPSTPSRIPV
QESLSQSQNS QPPSPQMFSP GSSHSRPPSP VDPYAKMVGT PRPPPGGHSF PRRNSVTPVE
NCVPLSSVPR PIHMNETSAT RPSPARDLCA SSMTNSDPYA KPPDTPRPMM TDQFSKPFSL
PRSPVISEQS TKGPLTTGTS DHFTKPSPRT DAFQRQRLPD PYAGPSLTPA PLGNGPFKTP
LHPPPSQDPY GSVSQTSRRL SVDPYERPAL TPRPVDNFSH SQSNDPYSHP PLTPHPAMTE
SFTHASRAFP QPGTISRSAS QDPYSQPPGT PRPLIDSYSQ TSGTARSNPD PYSQPPGTPR
PNTIDPYSQQ PPTPRPSPQT DMFVSSVANQ RHTDPYTHHL GPPRPGISVP YSQPPAVPRP
RTSEGFTRPS SARPALMPNQ DPFLQAAQNR VPGLPGPLIR PPDTCSQTPR PPGPGRIDTF
THASSSAVRD PYDQPPVTPR PHSESFGTSQ VVHDLVDRPV PGSEGNFSTS SNLPVSSQGQ
QFSSVSQLPG PVPTSGGTDT QNTVNMSQAD TEKLRQRQKL REIILQQQQQ KKIASRQEKG
PQDTAVVPHP VPLPHWQPES INQAFTRPPP PYPGSTRSPV IPPLGPRYAV FPKDQRGPYP
PEVAGMGMRP HGFRFGFPGA GHGPMPSQDR FHVPQQIQGS GIPPHIRRPM SMEMPRPSNN
PPLNNPVGLP QHFPPQGLPV QQHNILGQAF IELRHRAPDG RSRLPFAASP SSVIESPSHP
RHGNFLPRPD FPGPRHTDPI RQPSQCLSNQ LPVHPNLEQV PPSQQEQGHP AHQSSIVMRP
LNHPLSGEFS EAPLSTSTPA ETSPDNLEIA GQSSAGLEEK LDSDDPSVKE LDVKDLEGVE
VKDLDDEDLE NLNLDTEDGK GDDLDTLDNL ETNDPNLDDL LRSGEFDIIA YTDPELDLGD
KKSMFNEELD LNVPIDDKLD NQCASVEPKT RDQGDKTMVL EDKDLPQRKS SVSSEIKTEA
LSPYSKEEIQ SEIKNHDDSR GDADTACSQA ASAQTNHSDR GKTALLTTDQ DMLEKRCNQE
NAGPVVSAIQ GSTPLPARDV MNSCDITGST PVLSSLLSNE KCDDSDIRPS GSSPPSLPIS
PSTHGSSLPP TLIVPPSPLL DNTVNSNVTV VPRINHAFSQ GVPVNPGFIQ GQSSVNHNLG
TGKPTNQTVP LTNQSSTMSG PQQLMIPQTL AQQNRERPLL LEEQPLLLQD LLDQERQEQQ
QQRQMQAMIR QRSEPFFPNI DFDAITDPIM KAKMVALKGI NKVMAQNSLG MPPMVMSRFP
FMGPSVAGTQ NNDGQTLVPQ AVAQDGSITH QISRPNPPNF GPGFVNDSQR KQYEEWLQET
QQLLQMQQKY LEEQIGAHRK SKKALSAKQR TAKKAGREFP EEDAEQLKHV TEQQSMVQKQ
LEQIRKQQKE HAELIEDYRI KQQQQQQQCA LAPPILMPGV QPQPPLVPGA TSLTMSQPNF
PMVPQQLQHQ QHTAVISGHT SPARMPSLPG WQSNSASAHL PLNPPRIQPP IAQLSLKTCT
PAPGTVSSAN PQNGPPPRVE FDDNNPFSES FQERERKERL REQQERQRVQ LMQEVDRQRA
LQQRMEMEQH CLMGAELANR TPVSQMPFYG SDRPCDFLQP PRPLQQSPQH QQQIGPVLQQ
QNVQQGSVNS PPNQTFMQTN EQRQVGPPSF VPDSPSASGG SPNFHSVKPG HGNLPGSSFQ
QSPLRPPFTP ILPGTSPVAN SNVPCGQDPA VTQGQNYSGS SQSLIQLYSD IIPEEKGKKK
RTRKKKKDDD AESGKAPSTP HSDCAAPLTP GLSETTSTPA VSSPSELPQQ RQQEPVEPVP
VPTPNVSAGQ PCIESENKLP NSEFIKETSN QQTHVNAEAD KPSVETPNKT EEIKLEKAET
QPSQEDTKVE EKTGNKIKDI VAGPVSSIQC PSHPVGTPTT KGDTGNELLK HLLKNKKASS
LLTQKPEGTL SSDESSTKDG KLIEKQSPAE GLQTLGAQMQ GGFGGGNSQL PKTDGASENK
KQRSKRTQRT GEKAAPRSKK RKKDEEEKQA MYSSSDSFTH LKQQNNLSNP PTPPASLPPT
PPPMACQKMA NGFATTEELA GKAGVLVSHE VARALGPKPF QLPFRPQDDL LARAIAQGPK
TVDVPASLPT PPHNNHEELR IQDHYGDRDT PDSFVPSSSP ESVVGVEVNK YPDLSLVKEE
PPEPVPSPII PILPSISGKN SESRRNDIKT EPGTLFFTSP FGSSPNGPRS GLISVAITLH
PTAAENISSV VAAFSDLLHV RIPNSYEVSN APDVPPMGLV SSHRVNPSLE YRQHLLLRGP
PPGSANPPRL ATSYRLKQPN VPFPPTSNGL SGYKDSSHGP AEGASLRPQW CCHCKVVILG
SGVRKSCKDL TFVNKGSREN TKRMEKDIVF CSNNCFILYS SAAQAKNSDN KESLPSLPQS
PMKEPSKAFH QYSNNISTLD VHCLPQFQEK VSPPASPPIS FPPAFEAAKV ESKPDELKVT
VKLKPRLRTV PVGLEDCRPL NKKWRGMKWK KWSIHIVIPK GTFKPPCEDE IDEFLKKLGT
CLKPDPVPKD CRKCCFCHEE GDGLTDGPAR LLNLDLDLWV HLNCALWSTE VYETQAGALI
NVELALRRGL QMKCVFCHKT GATSGCHRFR CTNIYHFTCA TKAQCMFFKD KTMLCPMHKP
KGIHEQQLSY FAVFRRVYVQ RDEVRQIASI VQRGERDHTF RVGSLIFHTI GQLLPQQMQA
FHSPKALFPV GYEASRLYWS TRYANRRCRY LCSIEEKDGR PVFVIRIVEQ GHEDLVLSDS
SPKDVWDKIL EPVACVRKKS EMLQLFPAYL KGEDLFGLTV SAVARIAESL PGVEACENYT
FRYGRNPLME LPLAVNPTGC ARSEPKMSAH VKRFVLRPHT LNSTSTSKSF QSTVTGELNA
PYSKQFVHSK SSQYRRMKTE WKSNVYLARS RIQGLGLYAA RDIEKHTMVI EYIGTIIRNE
VANRKEKLYE SQNRGVYMFR MDNDHVIDAT LTGGPARYIN HSCAPNCVAE VVTFERGHKI
IISSNRRIQK GEELCYDYKF DFEDDQHKIP CHCGAVNCRK WMN
