ID G3I6I9_CRIGR Unreviewed; 1475 AA.
AC G3I6I9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=[histone H3]-lysine(4) N-methyltransferase {ECO:0000256|ARBA:ARBA00023620};
DE EC=2.1.1.364 {ECO:0000256|ARBA:ARBA00023620};
GN ORFNames=I79_019113 {ECO:0000313|EMBL:EGW10394.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW10394.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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 EMBL; JH001370; EGW10394.1; -; Genomic_DNA.
DR STRING; 10029.G3I6I9; -.
DR InParanoid; G3I6I9; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd15698; ePHD2_KMT2D; 1.
DR CDD; cd19209; SET_KMT2D; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR041964; KMT2D_ePHD2.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037890; SET_KMT2D.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45888:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2D; 1.
DR PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
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.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:EGW10394.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGW10394.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 967..1075
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1335..1451
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1459..1475
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 161026 MW; 65538B2D59E0C812 CRC64;
MSVEPGEVKP SVSGDSQLLL VQSQAQAQPT PVQLQPPLRL PGQPQQQQVN LLHTTGGGNH
GQQLGSSSEV PSVPHLLNQP SVSLGEQPGP MTQNLLGSQQ PLGLDRPIQN NTGPQPPKTG
PVPQSGQGLP GVGVMPTVGQ LRAQLQGVLA KNPQLRHLSP QQQQQLQALL MQRQLQQSQA
VRQTPPIQEP GSQPSPLQGL LGCQPQSGGF SGSQTGPLQE LGAGPRPQGP PRLPVPQGAL
STGPVLGPVH PTPPPSSPQE PKRPSQLPSP SAQPTPTHPG TPKPQGPTLE LPPGRVSPAA
AQLADTFFGK GLGPWDPSDN LTEAQKPEQS SLVSGHLEQV NGQVVQESPQ LSIKQEPREE
SCALGAQAVK READGEPGGT PGTSNHLLLA GSRSEAGHLL LQKLLRAKNV QLGAGRGPEG
PRSEINGHID SKLSGLEQKL QGPSSSKEDA TTRKPLTAKP KRVQKTSDRL VSSRKKLRKE
DGVRANEALL KQLKQELSQL PLTEPTITAN FSLFAPFGSG CLVSGQSQLR GAFGSGALHA
GLDYYSQLLT KNNLSNPPTP PSSLPPTPPP SVQQKMVNGV TPSDELGEHP KDAASAQDTE
GTLRNAAEVK SLDLLAALPT PPHNQTEDVR MESDEDSDSP DSIVPASSPE SILGEEAPRF
PQLGSGRWEQ DTRALSPVIP IIPRASIPVF PDTKPYGTLD LEVPGKLPAT AWEKSKGSEV
SVMLTVSAAA AKNLNGVMVA VAELLSMKIP NSYEVLFPDS PARVGLQPKK VEAEGPGGKE
KGLSAKGPDT GPDWLRQFDA VLPGYTLKSQ LDILSLLKQE SPAPEPSTQH SYTYNVSNLD
VRQLSAPPPE EPSPPPSPLA PSPASPPAEP LVELQAEPSA EPPIPSPLPL ASSPESARPK
PRARPPEESE DSRPPRLKKW KGVRWKRLRL LLTIQKGSGR QEGEREVAEF MEQLGTALKP
NKVPRDMRRC CFCHEEGDGA TDGPARLLNL DLDLWVHLNC ALWSTEVYET QGGALMNVEV
ALHRGLLTKC SLCQRTGATS SCNRMRCPNV YHFACAIRAK CMFFKDKTML CPMHKIKGPC
EQELSSFAVF RRVYIERDEV KQIASIIQRG ERLHMFRVGG LVFHAIGQLL PHQMADFHSA
TALYPVGYEA TRIYWSLRTN NRRCCYRCSI SENNGRPEFV IKVIEQGLED LVFTDASPQA
VWNRIIEPVA AMRKEADMLR LFPEYLKGEE LFGLTVHAVL RIAESLPGVE SCQNYLFRYG
RHPLMELPLM INPTGCARSE PKILTHYKRP HTLNSTSMSK AYQSTFTGET NTPYSKQFVH
SKSSQYRRLR TEWKNNVYLA RSRIQGLGLY AAKDLEKHTM VIEYIGTIIR NEVANRREKI
YEEQNRGIYM FRINNEHVID ATLTGGPARY INHSCAPNCV AEVVTFDKED KIIIISSRRI
PKGEELTYDY QFDFEDDQHK IPCHCGAWNC RKWMN
//
