TRX_DROME
ID TRX_DROME Reviewed; 3726 AA.
AC P20659; A4V2V9; A4V2W0; Q27255; Q27327; Q8INF9; Q960R2; Q9VFL1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Histone-lysine N-methyltransferase trithorax;
DE EC=2.1.1.355 {ECO:0000269|PubMed:12408863};
DE AltName: Full=Cysteine methyltransferase KMT2A {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:24235145};
DE AltName: Full=Lysine N-methyltransferase 2A;
GN Name=trx {ECO:0000303|PubMed:2107543}; Synonyms=KMT2A; ORFNames=CG8651;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RX PubMed=2107543; DOI=10.1073/pnas.87.6.2112;
RA Mazo A.M., Huang D.-H., Mozer B.A., Dawid I.B.;
RT "The trithorax gene, a trans-acting regulator of the bithorax complex in
RT Drosophila, encodes a protein with zinc-binding domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2112-2116(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=7924996; DOI=10.1242/dev.120.7.1907;
RA Sedkov Y., Tillib S., Mizrokhi L., Mazo A.;
RT "The bithorax complex is regulated by trithorax earlier during Drosophila
RT embryogenesis than is the Antennapedia complex, correlating with a
RT bithorax-like expression pattern of distinct early trithorax transcripts.";
RL Development 120:1907-1917(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8555104; DOI=10.1016/0925-4773(95)00429-7;
RA Tillib S., Sedkov Y., Mizrokhi L., Mazo A.;
RT "Conservation of structure and expression of the trithorax gene between
RT Drosophila virilis and Drosophila melanogaster.";
RL Mech. Dev. 53:113-122(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2970-3726 (ISOFORMS A/B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP INTERACTION WITH ASH1.
RX PubMed=10454589; DOI=10.1128/mcb.19.9.6441;
RA Rozovskaia T., Tillib S., Smith S., Sedkov Y., Rozenblatt-Rosen O.,
RA Petruk S., Yano T., Nakamura T., Ben-Simchon L., Gildea J., Croce C.M.,
RA Shearn A., Canaani E., Mazo A.;
RT "Trithorax and ASH1 interact directly and associate with the trithorax
RT group-responsive bxd region of the Ultrabithorax promoter.";
RL Mol. Cell. Biol. 19:6441-6447(1999).
RN [8]
RP INTERACTION WITH ASH1.
RX PubMed=10656681; DOI=10.1038/sj.onc.1203307;
RA Rozovskaia T., Rozenblatt-Rosen O., Sedkov Y., Burakov D., Yano T.,
RA Nakamura T., Petruck S., Ben-Simchon L., Croce C.M., Mazo A., Canaani E.;
RT "Self-association of the SET domains of human ALL-1 and of Drosophila
RT TRITHORAX and ASH1 proteins.";
RL Oncogene 19:351-357(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7958911; DOI=10.1101/gad.8.20.2478;
RA Kuzin B., Tillib S., Sedkov Y., Mizrokhi L., Mazo A.;
RT "The Drosophila trithorax gene encodes a chromosomal protein and directly
RT regulates the region-specific homeotic gene fork head.";
RL Genes Dev. 8:2478-2490(1994).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [11]
RP FUNCTION, INTERACTION WITH NUP98, AND DISRUPTION PHENOTYPE.
RX PubMed=25310983; DOI=10.1016/j.celrep.2014.09.002;
RA Pascual-Garcia P., Jeong J., Capelson M.;
RT "Nucleoporin Nup98 associates with Trx/MLL and NSL histone-modifying
RT complexes and regulates Hox gene expression.";
RL Cell Rep. 9:433-442(2014).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, METHYLATION AT CYS-3641, AND MUTAGENESIS OF
RP CYS-3641.
RX PubMed=24235145; DOI=10.1074/jbc.m113.501064;
RA Patel A., Vought V.E., Swatkoski S., Viggiano S., Howard B.,
RA Dharmarajan V., Monteith K.E., Kupakuwana G., Namitz K.E., Shinsky S.A.,
RA Cotter R.J., Cosgrove M.S.;
RT "Automethylation activities within the mixed lineage leukemia-1 (MLL1) core
RT complex reveal evidence supporting a 'two-active site' model for multiple
RT histone H3 lysine 4 methylation.";
RL J. Biol. Chem. 289:868-884(2014).
CC -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' of histone
CC H3 (H3K4me) (PubMed:12408863). H3K4me represents a specific tag for
CC epigenetic transcriptional activation (PubMed:12408863). Functions in
CC segment determination through interaction with genes of bithorax (BX-C)
CC and antennapedia (ANT-C) complexes (PubMed:2107543, PubMed:7958911).
CC Acts as an activator of BX-C (PubMed:7924996). Involved in the very
CC early regulation of homeotic genes expressed only in the posterior
CC region of the embryo (PubMed:7924996, PubMed:25310983). Also has auto-
CC methylation activity on Cys-3641 (PubMed:24235145).
CC {ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:2107543,
CC ECO:0000269|PubMed:24235145, ECO:0000269|PubMed:25310983,
CC ECO:0000269|PubMed:7924996, ECO:0000269|PubMed:7958911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000269|PubMed:12408863};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60277;
CC Evidence={ECO:0000269|PubMed:12408863};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82612;
CC Evidence={ECO:0000269|PubMed:24235145};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545;
CC Evidence={ECO:0000269|PubMed:24235145};
CC -!- SUBUNIT: Interacts (via SET domain) with ash1 (via SET domain)
CC (PubMed:10454589, PubMed:10656681). Interacts with Nup98
CC (PubMed:25310983). {ECO:0000269|PubMed:10454589,
CC ECO:0000269|PubMed:10656681, ECO:0000269|PubMed:25310983}.
CC -!- INTERACTION:
CC P20659; Q9V3G3: cyp33; NbExp=2; IntAct=EBI-591327, EBI-128445;
CC P20659; P20659: trx; NbExp=7; IntAct=EBI-591327, EBI-591327;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:7958911}. Chromosome {ECO:0000269|PubMed:7958911}.
CC Note=Binds to 16 discrete sites on larval salivary gland polytene
CC chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=D;
CC IsoId=P20659-1; Sequence=Displayed;
CC Name=B; Synonyms=C, E;
CC IsoId=P20659-2; Sequence=VSP_006665;
CC -!- TISSUE SPECIFICITY: Maternal isoforms are expressed in syncytial
CC blastoderm, confined to the ventral region fated to become mesoderm. An
CC additional broad domain of expression arises during cellularization and
CC is quickly resolved into four pair-rule-like stripes in the posterior
CC half of the embryo. {ECO:0000269|PubMed:7924996}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:7924996}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down in the larva results in
CC decreased expression of Hox genes such as Ubx and Antp.
CC {ECO:0000269|PubMed:25310983}.
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=AAK93328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M31617; AAA29025.1; -; mRNA.
DR EMBL; Z50152; CAA90514.1; -; Genomic_DNA.
DR EMBL; Z50152; CAA90513.1; -; Genomic_DNA.
DR EMBL; Z31725; CAA83516.1; -; Genomic_DNA.
DR EMBL; Z31725; CAA83515.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55041.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13599.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13600.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13601.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52951.1; -; Genomic_DNA.
DR EMBL; AY051904; AAK93328.1; ALT_INIT; mRNA.
DR PIR; A35085; A35085.
DR RefSeq; NP_001014621.1; NM_001014621.2. [P20659-2]
DR RefSeq; NP_476769.1; NM_057421.3. [P20659-1]
DR RefSeq; NP_476770.1; NM_057422.3. [P20659-2]
DR RefSeq; NP_599108.1; NM_134281.2. [P20659-2]
DR RefSeq; NP_599109.1; NM_134282.2. [P20659-1]
DR SMR; P20659; -.
DR BioGRID; 66813; 50.
DR ELM; P20659; -.
DR IntAct; P20659; 14.
DR MINT; P20659; -.
DR STRING; 7227.FBpp0082406; -.
DR PaxDb; P20659; -.
DR PRIDE; P20659; -.
DR DNASU; 41737; -.
DR EnsemblMetazoa; FBtr0082947; FBpp0082406; FBgn0003862. [P20659-1]
DR EnsemblMetazoa; FBtr0082948; FBpp0082407; FBgn0003862. [P20659-2]
DR EnsemblMetazoa; FBtr0082949; FBpp0082408; FBgn0003862. [P20659-2]
DR EnsemblMetazoa; FBtr0082950; FBpp0082409; FBgn0003862. [P20659-1]
DR EnsemblMetazoa; FBtr0100277; FBpp0099668; FBgn0003862. [P20659-2]
DR GeneID; 41737; -.
DR KEGG; dme:Dmel_CG8651; -.
DR UCSC; CG8651-RC; d. melanogaster.
DR UCSC; CG8651-RD; d. melanogaster.
DR CTD; 41737; -.
DR FlyBase; FBgn0003862; trx.
DR VEuPathDB; VectorBase:FBgn0003862; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000163756; -.
DR InParanoid; P20659; -.
DR OMA; FPWFTSS; -.
DR PhylomeDB; P20659; -.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR SignaLink; P20659; -.
DR BioGRID-ORCS; 41737; 0 hits in 3 CRISPR screens.
DR ChiTaRS; trx; fly.
DR GenomeRNAi; 41737; -.
DR PRO; PR:P20659; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003862; Expressed in eye disc (Drosophila) and 53 other tissues.
DR Genevisible; P20659; DM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0044665; C:MLL1/2 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0008023; C:transcription elongation factor complex; IPI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:FlyBase.
DR GO; GO:0106363; F:protein-cysteine methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IC:FlyBase.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0007482; P:haltere development; IGI:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:FlyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR GO; GO:0016571; P:histone methylation; TAS:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR016569; MeTrfase_trithorax.
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; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 2.
DR SMART; SM00184; RING; 4.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 4.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW Developmental protein; DNA-binding; Metal-binding; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..3726
FT /note="Histone-lysine N-methyltransferase trithorax"
FT /id="PRO_0000124874"
FT DOMAIN 1884..1941
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 3386..3470
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 3588..3704
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 3710..3726
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DNA_BIND 759..884
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 1266..1347
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1348..1393
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1421..1482
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1734..1774
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1795..1842
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2068..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2283..2302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2649..2669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2866..2894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3029..3096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3347..3381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..588
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3029..3088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3598
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 3600
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 3642
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 3665..3666
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 3668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 3714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 3716
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT BINDING 3721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q03164"
FT MOD_RES 3641
FT /note="S-methylcysteine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24235145"
FT VAR_SEQ 1..368
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_006665"
FT MUTAGEN 3641
FT /note="C->S: Abolished auto-methylation."
FT /evidence="ECO:0000269|PubMed:24235145"
FT CONFLICT 239..249
FT /note="GTTSEATTSGL -> LEQLVKQQPLV (in Ref. 1; AAA29025, 2;
FT CAA90513 and 3; CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="N -> K (in Ref. 1; AAA29025, 2; CAA90513 and 3;
FT CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> L (in Ref. 1; AAA29025, 2; CAA90513 and 3;
FT CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="G -> R (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="E -> Q (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="V -> A (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="N -> I (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="T -> A (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="K -> P (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1529..1530
FT /note="KL -> NV (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1594
FT /note="S -> P (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1627
FT /note="A -> E (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1690
FT /note="T -> A (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2010
FT /note="E -> Q (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2025
FT /note="P -> PWLTSPLKFLGLSTHGGLLLWLLLGVVVRLKQGG (in Ref. 1;
FT AAA29025)"
FT /evidence="ECO:0000305"
FT CONFLICT 2341
FT /note="S -> R (in Ref. 2; CAA90513/CAA90514 and 3;
FT CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2365
FT /note="S -> N (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2392
FT /note="S -> G (in Ref. 2; CAA90513/CAA90514 and 3;
FT CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 3157
FT /note="E -> Q (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 3234
FT /note="A -> R (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
FT CONFLICT 3690
FT /note="L -> V (in Ref. 1; AAA29025, 2; CAA90513/CAA90514
FT and 3; CAA83515/CAA83516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3726 AA; 400098 MW; E3DDB8F062BD7796 CRC64;
MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG SSAAREKGNN
CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG SGSSGSGSTN GGSVNGGTHH
KSAANLDKEA VTKDQNGDGD KTRGNVSSAP SGKLSAAASG KALSKSSRTF SASTSVTSSG
RSSGSSPDGN SGASSDGASS GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSGT
TSEATTSGLS GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK
FKNLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPIASGS TPSVEGGIGV GGVVSPGEDA
ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP PAMASSGDGS SPKSGADTGP
STSSTTAKQK KTVTFRNVLE TSDDKSVVKR FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE
CIVRPSILSK ILNKNSNIDK LNSLKFRSAG ASSSSSNQES GSSSNVFGLS RAFGAPMDED
DEGGVTFRRN DSPEDQNNAE DDEMDDDDDD EEAEEDDENE DDNDEAVSEK SAETEKSAGA
DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG DSKGKNVFGT
SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGN FVLRQPRLQF QADNQQATFT
APKACPTSPS AIPKPANSLA TSSFGSLAST NSSTVTPTPS ACSICSAVVS SKEVTQARKY
GVVACDVCRK FFSKMTKKSI SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK
KFYKDRCTAC WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF
TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL RPAILENPLF
LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE KLLSPTQAGT KKSGAAEAQV
EEVQPQKEEA PQTSTTTQPS ASNGASHGVP QAELAGETNA TGDTLKRQRI DLKGPRVKHV
CRSASIVLGQ PLATFGEDQQ PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS
CKTSPVGDES KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA
SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV CQTGFGLIVT
ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN LKHGSFEDTT LMGSLLETTV
NASTGPSSSL NQLTQRLNWL CPRCTVCYTC NMSSGSKVKC QKCQKNYHST CLGTSKRLLG
ADRPLICVNC LKCKSCSTTK VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM
MECGDCGQWV HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE
FKASLYSVLK LLSKSRQACA LLKLSPRKKL RCTCGASSNQ GKLQPKALQF SSGSDNGLGS
DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKSLPCSCQ QHISHSQSFS LVDIKQKIAG
NSYVSLAEFN YDMSQVIQQS NCDELDIAYK ELLSEQFPWF QNETKACTDA LEEDMFESCS
GGNYEDLQDT GGVSASVYNE HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC
RKSGEGLSGE EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC
GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA NGSPSVTYES
NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI VPRFSDSYEA VVPINFLCSR
LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL DVGRNYTVDH TNPNSKEVQL GMAQIARWHT
SLARSEFLEN GGTDWSGEFP NPNSCVPPDE NTEEEPQQQA DLLPPELKDA IFEDLPHELL
DGISMLDIFL YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN
TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR RKLSKNLAEG
VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG SVRSKSFTWS AAKRYFEKSE
GREEAAKMRI MQMDGVDDSI TEFRIISGDG NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL
PSCSPTMSSN ETESDVSGQG MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ
SLGSLGQFGL QGLQQLQLQP QSLGSGFFLS QPNPATQANT DDLQIYANSL QSLAANLGGG
FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ ATNTDKKIML
PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL QPHPQQHQQQ QQTQVQQPIT
VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ PQNIISFVTG DGSQGQPLQY ISIPTAGEYK
PQPQPTATPT FLTTAPGAGA TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL
IQPQTIQLGG GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV
QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV LNNTGDASSA
GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS TSMDYTSPVM VTAKIPPVTQ
IKRTNAQAKA AGISGVGKVP PQPQVVNKVL PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG
TGTTCGAPPS IASKPLQKKT NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL
QQQIPAVVVN QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII
TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN PMQQQAPSTT
SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE QPIIHQMTSA SVSKCYAQKS
TLPSPVYEAE LKVSSVLESI VPDVTMDAIL EEQPVTESIY TEGLYEKNSP GESKTEQLLL
QQQQREQLNQ QLVNNGYLLD KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMATSACND
HEMSDSEEPA VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS
APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE QRTVSQEQEQ
SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT YKSSSITEIW EKVFEAVQVA
RRAHGLTPLP EGPLADMGGI QMIGLKTNAL KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA
ANGAHGGNLG GSSASAALSV SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF
SWLASRHRKQ PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR
GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL VVDATMRGNA
ARFINHCCEP NCYSKVVDIL GHKHIIIFAL RRIVQGEELT YDYKFPFEDE KIPCSCGSKR
CRKYLN
