ID M3W5T8_FELCA Unreviewed; 2194 AA.
AC M3W5T8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 71.
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|VGNC:VGNC:63161};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000005933.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000005933.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005933.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000005933.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005933.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000005933.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005933.6};
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04004572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000005933; -.
DR PaxDb; 9685-ENSFCAP00000005933; -.
DR Ensembl; ENSFCAT00000006383.6; ENSFCAP00000005933.6; ENSFCAG00000006381.6.
DR VGNC; VGNC:63161; KMT2B.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000161496; -.
DR HOGENOM; CLU_000208_1_0_1; -.
DR InParanoid; M3W5T8; -.
DR OMA; TTRYIHF; -.
DR Proteomes; UP000011712; Chromosome E2.
DR Bgee; ENSFCAG00000006381; Expressed in uterus and 10 other cell types or tissues.
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; 5.
DR PRINTS; PR01217; PRICHEXTENSN.
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; 3.
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:UP000011712};
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 436..483
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 679..730
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 727..781
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 813..874
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1056..1164
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2054..2170
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2178..2194
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2064
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2066
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2131..2132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 2194 AA; 239108 MW; F570BBDD8DE974AC CRC64;
MPVVSARSSR VIKTPRRFMD EDPPKPLKVE VSPTLRPPVA MSPLAPPEPA PAPSPPRAPT
PPSTPVPLPE KRRSILREPT FRWTSLTREL PPPPPAPPPA PPPLPAPVTP SRRPLLLRAP
QFTPSEAHLK IYESVLTTPL GAPEAPEPEP PPADDSPAEP EPRAVGRTNH LSLPRFAPVV
ATPVKAEVPL PGAPTLSNGQ QPQPQAQLQQ PLQALQTQLL PQTLPPQQPQ LQPQLQLQPQ
PPPQQPPPLE KARVAGLGSL PLSGVEEKMF SLLKRAKVQL FKIDQQQQQK VASLLPPSPG
GQMEEVVGTV KQLSDRGSVR SEDESMETKR ERPSGPESPV QGPRIKHVCR HAAVALGQAR
AMVPEDVPRL SALPLRDRQD IATEDTSSAS ETESVPSRSR RGKVESAGPG GDSEPAGSGG
TLAQTPRRSL PSHHGKKMRM ARCGHCRGCL RVQDCGSCVN CLDKPKFGGP NTKKQCCVYR
KCDKIEARKM ERLAKKGRTI VKTLLPWDSD ESPEASPGPP GPRRGAGAGG PREEVVAPPG
PEEQDSLLLQ RKSARRCVKQ RPSYDIFEDS DDSEPGGPPA PRRRTPRENE LPVPEPEEQS
RPRKPTLQPV LQLKARRRLD KDALAPGPFT SFPNGWTGKQ KSPDGVHRVR VDFKEDCDLE
NVWLMGGLSV LTSVPGGPPM VCLLCASKGL HELVFCQVCC DPFHPFCLEE AERPLPQHHD
TWCCRRCKFC HVCGRKGRGS KHLLECERCR HAYHPACLGP SYPTRATRKR RHWICSACVR
CKSCGATPGK NWDVEWSGDY SLCPRCTQLY EKGNFCPICT RCYEDNDYES KMMQCAQCDH
WVHAKCEGLS DEDYEILSGL PDSVLYTCGP CAGATHPRWR EALSGALQGG LRQVLQGLLS
SKVAGPLLLC TQCGQAGKQL HPGPCDLQAV SRRFEEGHYK SVHSFMEDMV GILMKHSEEG
ETPERRAGGQ MKGLLLKLLE SAFGWFDAHD PKYWRRSTRL PNGVLPNAVL PPSLDHVYAQ
WRQQEPETPE SGQPPGDPSA AFQGKDPAAF SHLEDPRQCA LCLKYGDADS KEAGRLLYIG
QNEWTHVNCA IWSAEVFEEN DGSLKNVHAA VARGRQMRCE LCLKPGATVG CCLSSCLSNF
HFMCARASYC IFQDDKKVFC QKHTDLLDGK EIVTPDGFDV LRRVYVDFEG INFKRKFLTG
LEPDAINVLI GSIRIDSLGT LSDLSDCEGR LFPIGYQCSR LYWSTVDARR RCWYRCRILE
YRPWGPREEP VHLEAAEENQ TIVHSPTPSS EPPDHVDPPP DTDALIPGAP EHHSPVQNLD
PPLRPDLSIA PPPAPRSFSG ARIKVPNYSP SRRPLGGVSF GPLPSPGSPS SLTHHIPTVG
DLDFPAPPRR SRRPSPLTPR LPPSRRASPP LRTSPQLRVP PPTSVVRALT PTSGELAPPG
PAPSPPPPPE DLGPDFEDME VVSGLSAADL DFAASLLGTE PFQEEIVAAG AVGSSHGGPG
DSSEEEASPT PRYVHFPVTV VSGPALAPGA LPGTPRIEQL DGVDDGTDSE AEAVQQPRGQ
GTPPSGPGVG RAGVIGAAGD RTRPPEDLPS EIVDFVLKNL GGPGEGGAGP REEPLPPAPP
LANGSQPSQG LPPSPADPTR TFAWLPGAPG VRVLSLGPAP EPPKPATSKI ILVNKLGQVF
VKMAGEGEPV SPPVKQPPLP PPIPPTAPAS WTLPPGPLLG VLPVVGVVRP APPPPPPPLT
LVLSSGPPSP PHQAIRVKRV STFSGRSPPA PPPNKTPRLE EDGESLEDAP QGPGLSGSGF
SRVRMKTPTV RGVLDLDEPG EPTGEESPRP LQDRSPLLSL PEGGPPRAPD GPPDLLLESQ
WHHYSGEASS SEEEPPSPED KENQAPKRAG PHLRFEISSE DGFSVEAESL EGAWRTLIEK
VQEARGHARL RHLSFSGMSG ARLLGIHHDA VIFLAEQLPG AQRCQHYKFR YHQQGEGQEE
PPLNPHGAAR AEVYLRKCTF DMFNFLASQH RVLPEGATCD EEEDEVQLRS TRRATSLELP
MAMRFRHLKK TSKEAVGVYR SAIHGRGLFC KRNIDAGEMV IEYSGIVIRS VLTDKREKFY
DGKGIGCYMF RMDDFDVVDA TMHGNAARFI NHSCEPNCFS RVIHVEGQKH IVIFALRRIL
RGEELTYDYK FPIEDASNKL PCNCGAKRCR RFLN
//
