ID G3RY49_GORGO Unreviewed; 2535 AA.
AC G3RY49;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
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:ENSGGOP00000020736.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000020736.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000020736.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000020736.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000020736.2}
RP IDENTIFICATION.
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 EMBL; CABD030113210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030113213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000025977.2; ENSGGOP00000020736.2; ENSGGOG00000016796.3.
DR GeneTree; ENSGT00940000161496; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000016796; Expressed in cerebellum and 5 other cell types or tissues.
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:0045322; F:unmethylated CpG binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 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; 7.
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; 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:UP000001519};
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 862..909
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1104..1155
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1152..1206
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1238..1299
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1481..1589
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2395..2511
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2519..2535
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..1996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2101..2232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2215..2232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2405
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2407
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2449
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2472..2473
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2524
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 2535 AA; 274962 MW; C26273295C911945 CRC64;
GGGGRGGRGN GAERVRVALR RGGGATGPGG AEPGEDTALL RLLGLRRGLR RLRRLWRRGR
GRGRGRGWGP SRGCVPEEES SDGESDEEEF QGFHSDEDVA PSSLRSALRS QRGRAPRGRG
RKHKTTPLPP PRLADVAPTP PKTPARKRGE EGTERMVQAL TELLRRAQAP QAPRSRACEP
STPRRSRGRP PGRPAGPCRR KQQAVVVAEA AVTIPKPEPP PPVVPVKHQT GSWKCKEGPG
PGPGTPRRGG QSSRGGRGSR GRGRGGGLPF VIKFVSRAKK VKMGQLSLGL ESGQGQGQHE
ESWQDAPQRR VGSGQGGSPC WKKQEQKLDD EEEEKKEEEE KDKEEGEEKE ERAVAEEMMP
AAEKEEAKLP PPPLTPPAPS PPPPLPPPST SPPPPLCPPP PPPVSPPPLP SPPPPPAQEE
QEESPPPVVP ATCSRKRGRP PLTPSQRAER EAARAGPEGT SPPTPTPSTA TGGPPEDSPT
VAPKSTTFLK NIRQFIMPVV SARSSRVIKT PRRFMDEDPP KPPKVEVSPV LRPPITTSPP
VPQEPAPVPS PPRFTPSEAH LKIYESVLTP PPLGAPEAPE PEPPPADDSP AEPEPRAVGR
TNHLSLLPRF APVVTTPVKA EVSPHGAPAL SNGPQTQAQL LQPLQALQTQ LLPQALPPPQ
PQLQPPPSPQ QMPPLEKARI AGVGSLPLSG VEEKMFSLLK RAKVQLFKID QQQQQKVAAS
MPLSPGGQME EVAGAVKQIS DRGPVRSEDE SVEAKRERPS GPESPVQGPR IKHVCRHAAV
ALGQARAMVP EDVPRLSALP LRDRQDLATE DTSSASETES VPSRSRRGKV EAAGPGGESE
PTGSGGTLAH TPRRSLPSHH GKKMRMARCG HCRGCLRVQD CGSCVNCLDK PKFGGPNTKK
QCCVYRKCDK IEARKMERLA KKGRTIVKTL LPWDSDESPE ASPGPPGPRR GAGAGGPREE
VVAPPGPEEQ DSLLQRKSAR RCVKQRPSYD IFEDSDDSEP GGPPAPRRRT PRENELPLPE
PEEQSRPRKP TLQPVLQLKA RRRLDKDALA PGPFASFPNG WTGKQKSPDG VHRVRVDFKE
DCDLENVWLM GGLSVLTSVP GGPPMVCLLC ASKGLHELVF CQVCCDPFHP FCLEEAERPL
PQHHDTWCCR RCKFCHVCGR KGRGSKHLLE CERCRHAYHP ACLGPSYPTR ATRKRRHWIC
SACVRCKSCG ATPGKNWDVE WSGDYSLCPR CTQLYEKGNY CPICTRCYED NDYESKMMQC
AQCDHWVHAK CEGLNPVGTP ILSGLPDSVL YTCGPCAGAA QPRWREALSG ALQGGLRQVL
QGLLSSKVVG PLLLCTQCGP DGKQLHPGPC GLQAVSQRFE DGHYKSVHSF MEDMVGILMR
HSEEGETPER RAGGQMKGLL LKLLESAFGW FDAHDPKYWR RSTRLPNGVL PNAVLPPSLD
HVYAQWRQQE PETPESGQPP GDPSAALQGK DPAAFSHLED PRQCALCLKY GDADSKEAGR
LLYIGQNEWT HVNCAIWSAE VFEENDGSLK NVHAAVARGR QMRCELCLKP GATVGCCLSS
CLSNFHFMCA RASYCIFQDD KKVFCQKHTD LLDGKEIVNP DGFDVLRRVY VDFEGINFKR
KFLTGLEPDA INVLIGSIRI DSLGTLSDLS DCEGRLFPIG YQCSRLYWST VDARRRCWYR
CRILEYRPWG PREEPAHLEA AEENQTIVHS PAPSSEPPGG EDPPLDTDVL VPGVPERHSP
IQNLDPPLRP DSGSAPPPAP RSFSGARIKV PNYSPSRRPL GGVSFGPLPS PGSPSSLTHH
IPTVGDPDFP APPRRSRRPS PLVPRPPPSR WASPPLKTSP QLRVPPPTSV VTALTPTSGE
LAPPGPAPSP PPPEDLGPDF EDMEVVSGLS AADLDFAASL LGTEPFQEEI VAAGAMGSSH
GGPGDSSEEE SSPTSRYIHF PVTVVSAPGL APSTTPGAPR IEQLDGVDDG TDSEAEAVQQ
PRGQGTPPSG PGVVRAGVLG AAGDRARPPE DLPSEIVDFV LKNLGGPGDG GAGPREESLP
AAPPLANGSQ PSQGLTASPA DPTRTFAWLP GAPGVRVLSL GPAPDSGPAS PPRQAIRVKR
VSTFSGRSPP APPPYKAPRL DEDGEASEDT PQVPGLGSGG FSRVRMKTPT VRGVLDLDQP
GEPAGEESPG PLQERSPLLP LPEGGLPQVP DGPPDLLLES QWHHYSGEAS SSEEEPPSPD
DKENQAPKRT GPHLRFEISS EDGFSVEAES LEGAWRTLIE KVQEARGHAR LRHLSFSGMS
GARLLGIHHD AVIFLAEQLP GAQRCQHYKF RYHQQGEGQE EPPLNPHGAA RAEVYLRKCT
FDMFNFLASQ HRVLPEGATC DEEEDEVQLR STRRATSLEL PMAMRFRHLK KTSKEAVGVY
RSAIHGRGLF CKRNIDAGEM VIEYSGIVIR SVLTDKREKF YDGKGIGCYM FRMDDFDVVD
ATMHGNAARF INHSCEPNCF SRVIHVEGQK HIVIFALRRI LRGEELTYDY KFPIEDASNK
LPCNCGAKRC RRFLN
//
