ID   E1BKN0_BOVIN            Unreviewed;      2711 AA.
AC   E1BKN0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=[histone H3]-lysine(4) N-methyltransferase {ECO:0000256|ARBA:ARBA00023620};
DE            EC=2.1.1.364 {ECO:0000256|ARBA:ARBA00023620};
GN   Name=KMT2B {ECO:0000313|Ensembl:ENSBTAP00000003584.5,
GN   ECO:0000313|VGNC:VGNC:30691};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000003584.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000003584.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003584.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000003584.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003584.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024515};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC         Evidence={ECO:0000256|ARBA:ARBA00024515};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_003587289.1; XM_003587241.4.
DR   RefSeq; XP_015322912.1; XM_015467426.1.
DR   SMR; E1BKN0; -.
DR   STRING; 9913.ENSBTAP00000003584; -.
DR   PaxDb; 9913-ENSBTAP00000003584; -.
DR   Ensembl; ENSBTAT00000003584.6; ENSBTAP00000003584.5; ENSBTAG00000002763.6.
DR   GeneID; 785776; -.
DR   KEGG; bta:785776; -.
DR   CTD; 9757; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002763; -.
DR   VGNC; VGNC:30691; KMT2B.
DR   eggNOG; KOG1084; Eukaryota.
DR   GeneTree; ENSGT00940000161496; -.
DR   HOGENOM; CLU_000208_1_0_1; -.
DR   InParanoid; E1BKN0; -.
DR   OMA; TTRYIHF; -.
DR   OrthoDB; 5490909at2759; -.
DR   TreeFam; TF319820; -.
DR   Reactome; R-BTA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-BTA-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000002763; Expressed in blood and 104 other cell types or tissues.
DR   ExpressionAtlas; E1BKN0; baseline.
DR   GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0044665; C:MLL1/2 complex; IEA:Ensembl.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045322; F:unmethylated CpG binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd05493; Bromo_ALL-1; 1.
DR   CDD; cd15694; ePHD_KMT2B; 1.
DR   CDD; cd15589; PHD1_KMT2B; 1.
DR   CDD; cd15591; PHD2_KMT2B; 1.
DR   CDD; cd15593; PHD3_KMT2B; 1.
DR   CDD; cd19170; SET_KMT2A_2B; 1.
DR   Gene3D; 3.30.160.360; -; 2.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR047219; KMT2A_2B_SET.
DR   InterPro; IPR041959; KMT2B_ePHD.
DR   InterPro; IPR016569; MeTrfase_trithorax.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR002857; Znf_CXXC.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45838:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE 2B; 1.
DR   PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   PIRSF; PIRSF010354; Methyltransferase_trithorax; 6.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR010354-51};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR010354-50};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR010354-51};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00509}.
FT   DOMAIN          953..1000
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51058"
FT   DOMAIN          1196..1247
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1244..1298
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1330..1391
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1573..1681
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          2571..2687
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          2695..2711
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1540..1561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1801..1974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2007..2027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2044..2156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2204..2226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2276..2408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..378
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..449
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..588
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..630
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..679
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1085
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1808..1822
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1851
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1955..1969
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2127..2152
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2207..2226
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2391..2408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2581
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         2583
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         2625
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         2648..2649
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         2651
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         2699
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         2700
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         2701
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         2706
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ   SEQUENCE   2711 AA;  293366 MW;  BED4A79F7DA60E24 CRC64;
     MAAAAGGGSC PGPGSARGRF PGRPRGSGGG GGRGGRGNGA ERVRVALRRG GGAAGPGGAE
     PGEDTALLRL LGLHRGLRRL RRLWAGPRIQ RGRGRGRGRG WGPSRGCLLE EESSDGESDD
     EEFQGFHSDE DAASSSLRSA LRSQRGRAPR GRGRKHKTTP LPPPRLADVA PAPPKTPARK
     RGEEGTERMV QALTELLRRA QAPPAPRSRA CESSTPRRSR GRPPGRPAGP CRKKQQAVVV
     AEAAVTIPRP EPPPPVVPVK HRTGSWKCKE GPGPGPGTPK RGGQSGRGGR GGRGRGRGRL
     PLVIKFVSKA KKMKMGQLSL GLESGQGQDQ HEESWQDAPQ GRVGSGQGEG PCWRKEQKLE
     EEGEEEKEEE DEEEERAVAE EAMVLAEEKE EAKLPSPPLT PPAPPPPPSL PPASASPPSP
     LCPPPPPVSP PPPPTPPPPR APEEQEESPP PVVPATCSRK RGRPPLTPSQ RAEREAARAG
     PEGTSPPTPV PSTATGGPLE DSPTVAPKST TFLKNIRQFI MPVVSARSSR VIKTPRRFMD
     EDPPKPPKVE VSPTLRPPIA TSPLAPQEPA PAPSPPRAPT PPSTPVPLPE KRRSILREPT
     FRWTSLTREL PPPPPAPPPA PPPLPAPVTP SRRPLLLRAP QFTPSEAHLK IYESVLTTPP
     LGAPEAPEPE PPPADDSPAE PEPRALGRTN HLSLPRFAPV VATPIKAEMP SPGAPAPSSG
     QQPHAQLQQP LQALQTQLLP PALPPQQSLL QPQLQLQPPP QQAPPLEKAR IAGLGSLPLS
     GVEEKMFSLL KRAKVQLIKI DQQQQQKVAS LMPPSPGGQM EEVVGTVKQI PDRGSVKSED
     ESVETKRERP SGPESPVQGP RIKHVCRHAA VALGQARAMV PEDVPRLSAL PLRDRQDLNA
     EDTSSASETE SVPSQSQPGK VESTGPGGDS EPAGSGGTLA HAPRRSLPSH HGKKMRMARC
     GHCRGCLRVQ DCGSCVNCLD KPKFGGPNTK KQCCVYRKCD KIEARKMERL AKKGRTIVKT
     LLPWDSDESP EASPGPPGPR RGAGAGGPRE EVVAPPGPEE QDSFLLQRKS ARRCVKQRPS
     YDIFEDSDDS DPGGPPAPRR RTPRENELPV PEPEEQSRPR KPTLQPVLQL KARRRLDKDA
     LAPGPFASFP NGWTGKQKSP DGVHRVRVDF KEDCDLENVW LMGGLSVLTS VPGGPPMVCL
     LCASKGLHEL VFCQVCCDPF HPFCLEEAER PLPQHHDTWC CRRCKFCHVC GRKGRGSKHL
     LECERCRHAY HPACLGPSYP TRATRKRRHW ICSACVRCKS CGATPGKNWD VEWSGDYSLC
     PRCTQLFEKG NYCPICTRCY EDNDYESKMM QCAQCDHWVH AKCEGLSDED YEILSGLPDS
     VLYTCGPCAG ATHPRWREAL SGALQGGLRQ VLQGLLSSKV AGPLLLCTQC GQEGQQLHPG
     PCDLHAVRRR FEEGHYKSVH SFMEDVVGIL MRHSEEGEML ERRAGGQTKG LLLKLLESAF
     GWFDAHDPKY WRRSTRLPNG VLPNAVLPPS LDHVYAQWRQ QEPETPESGQ PPGDPSTAFQ
     GKDSAAFSHL EDPRQCALCL KYGDADSKEA GRLLYIGQNE WTHVNCAIWS AEVFEENDGS
     LKNVHAAVAR GRQMRCELCL KPGATVGCCL SSCLSNFHFM CARASYCIFQ DDKKVFCQKH
     TDLLDGKEIV NPDGFDVLRR VYVDFEGINF KRKFLTGLEP DAINVLIGSI RIDSLGTLSD
     LSDCEGRLFP IGYQCSRLYW STVDARRRCW YRCRILEYRP WGPREEPVHL EAAEENQTIV
     HSPAPCSEPP DHVDPPPDTD ALIPRAPEHH PPVQNPDPPP RLDPSSAPPP APRSFSGARI
     KVPNYSPSRR PLGGVSFGPL PSPGSPSSLT HHIPTVGDPD FPAPPRRSRR PSPLASRLPP
     SRRASPPLRT SPQLRVPPPT SVVRALTPTS GELAPPSRAP SPPPPPEDLG PDFEDMEVVS
     GLSAADLDFA ASLLGTEPFQ EEIVAAGAGG SSHGGLGDSS EEEAGPTPRY VHFPVTVVSG
     PALAPGALPG APRIEQLDGV DDGTDSEAEA VQQPRGQGTP TSGPGAGRAG VIGAAGDRAR
     PPEDLPSEIV DFVLKNLGGP GEGGAGPREE PLPPAPPLAN GSQPPQGLPP NPADPTRTFA
     WLPGPPGVRV LSLGPAPEPP KPAASKIILV NKLGQVFVKM AGEGEPVSPP VKPPPLPPPM
     PPTAPTSWTL PPGPLLGVLP VVGVVRPAPP PPPPPLTLVL SSGPPSPPRQ AIRVKRVSTF
     SGRSPPAPPP SKTPRLEEDG ESLEDPPQGP GPCGSGFSRV RMKTPTVRGV LDLDDSGELT
     AEESPRPLQD RSPLLPLPEG GPPRAPDGPP DLLLESQWHH YSGEASSSEE EPPSPEDKEN
     QAPKRAGPHL RFEISSEDGF SVEAESLEGA WRTLIEKVQE ARGHARLRHL SFSGMSGARL
     LGIHHDAVIF LAEQLPGAQR CQHYKFRYHQ QGEGQEEPPL NPHGAARAEV YLRKCTFDMF
     NFLASQHRVL PEGATCDEEE DEVQLRSTRR ATSLELPMAM RFRHLKKTSK EAVGVYRSAI
     HGRGLFCKRN IDAGEMVIEY SGIVIRSVLT DKREKFYDGK GIGCYMFRMD DFDVVDATMH
     GNAARFINHS CEPNCFSRVI HVEGQKHIVI FALRRILRGE ELTYDYKFPI EDASNKLPCN
     CGAKRCRRFL N
//