P20659 (TRX_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase trithorax
EC=2.1.1.43

Alternative name(s):
Lysine N-methyltransferase 2A

Gene names

Name:	trx
Synonyms:	KMT2A
ORF Names:	CG8651

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	3726 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Functions in segment determination through interaction with genes of bithorax (BX-C) and antennapedia (ANT-C) complexes. Acts as an activator of BX-C. Involved in the very early regulation of homeotic genes expressed only in the posterior region of the embryo. Ref.1 Ref.2 Ref.9
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.10
Subunit structure	Interacts with ash1 via its SET domain. Ref.7 Ref.8
Subcellular location	Nucleus. Chromosome. Note: Binds to 16 discrete sites on larval salivary gland polytene chromosomes. Ref.9
Tissue specificity	Maternal isoforms are expressed in syncytial blastoderm, confined to the ventral region fated to become mesoderm. An additional broad domain of expression arises during cellularization and is quickly resolved into four pair-rule-like stripes in the posterior half of the embryo. Ref.2
Developmental stage	Expressed both maternally and zygotically. Ref.2
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 1 nuclear receptor DNA-binding domain. Contains 5 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 SET domain.
Sequence caution	The sequence AAK93328.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Activator Chromatin regulator Developmental protein Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from mutant phenotype PubMed 18516287. Source: FlyBase germ cell migration Inferred from mutant phenotype PubMed 9435287. Source: FlyBase histone H3 acetylation Inferred from mutant phenotype PubMed 17174895. Source: FlyBase histone H3-K4 methylation Inferred from direct assay Ref.10. Source: FlyBase positive regulation of transcription elongation from RNA polymerase II promoter Inferred from direct assay PubMed 17174895. Source: FlyBase regulation of response to DNA damage stimulus Inferred from genetic interaction PubMed 18612247. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1/2 complex Inferred from direct assay PubMed 21875999. Source: FlyBase microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase polytene chromosome Inferred from direct assay PubMed 12524522PubMed 21875999. Source: FlyBase transcription elongation factor complex Inferred from physical interaction PubMed 17174895. Source: FlyBase
Molecular_function	chromatin binding Inferred from direct assay PubMed 17174895. Source: FlyBase histone methyltransferase activity (H3-K4 specific) Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay PubMed 11313484. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from direct assay PubMed 21177970. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		7	EBI-591327,EBI-591327
cyp33	Q9V3G3	2	EBI-591327,EBI-128445

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P20659-1)

Also known as: D;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P20659-2)

Also known as: C; E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-368: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3726	3726	Histone-lysine N-methyltransferase trithorax		PRO_0000124874
Regions
	Domain	1884 – 1941	58	FYR N-terminal
	Domain	3386 – 3470	85	FYR C-terminal
	Domain	3587 – 3708	122	SET
	Domain	3710 – 3726	17	Post-SET
	DNA binding	759 – 884	126	Nuclear receptor
	Zinc finger	1266 – 1347	82	PHD-type 1
	Zinc finger	1348 – 1393	46	PHD-type 2
	Zinc finger	1421 – 1482	62	PHD-type 3
	Zinc finger	1734 – 1793	60	PHD-type 4; atypical
	Zinc finger	1794 – 1844	51	PHD-type 5; atypical
	Region	3665 – 3666	2	S-adenosyl-L-methionine binding By similarity
	Compositional bias	512 – 516	5	Poly-Ser
	Compositional bias	565 – 570	6	Poly-Asp
	Compositional bias	661 – 664	4	Poly-Ser
	Compositional bias	905 – 910	6	Poly-Ser
	Compositional bias	1576 – 1582	7	Poly-Gln
	Compositional bias	2298 – 3027	730	Gln-rich
	Compositional bias	3032 – 3040	9	Poly-Ser
	Compositional bias	3181 – 3184	4	Poly-Gln
	Compositional bias	3220 – 3225	6	Poly-Glu
Sites
	Metal binding	3668	1	Zinc By similarity
	Metal binding	3714	1	Zinc By similarity
	Metal binding	3716	1	Zinc By similarity
	Metal binding	3721	1	Zinc By similarity
	Binding site	3598	1	S-adenosyl-L-methionine By similarity
	Binding site	3600	1	S-adenosyl-L-methionine By similarity
	Binding site	3642	1	S-adenosyl-L-methionine By similarity
Natural variations
	Alternative sequence	1 – 368	368	Missing in isoform B.		VSP_006665
Experimental info
	Sequence conflict	239 – 249	11	GTTSEATTSGL → LEQLVKQQPLV in AAA29025. Ref.1
	Sequence conflict	239 – 249	11	GTTSEATTSGL → LEQLVKQQPLV in CAA90513. Ref.2
	Sequence conflict	239 – 249	11	GTTSEATTSGL → LEQLVKQQPLV in CAA83516. Ref.3
	Sequence conflict	303	1	N → K in AAA29025. Ref.1
	Sequence conflict	303	1	N → K in CAA90513. Ref.2
	Sequence conflict	303	1	N → K in CAA83516. Ref.3
	Sequence conflict	337	1	A → L in AAA29025. Ref.1
	Sequence conflict	337	1	A → L in CAA90513. Ref.2
	Sequence conflict	337	1	A → L in CAA83516. Ref.3
	Sequence conflict	521	1	G → R in AAA29025. Ref.1
	Sequence conflict	521	1	G → R in CAA90513. Ref.2
	Sequence conflict	521	1	G → R in CAA90514. Ref.2
	Sequence conflict	521	1	G → R in CAA83515. Ref.3
	Sequence conflict	521	1	G → R in CAA83516. Ref.3
	Sequence conflict	578	1	E → Q in AAA29025. Ref.1
	Sequence conflict	578	1	E → Q in CAA90513. Ref.2
	Sequence conflict	578	1	E → Q in CAA90514. Ref.2
	Sequence conflict	578	1	E → Q in CAA83515. Ref.3
	Sequence conflict	578	1	E → Q in CAA83516. Ref.3
	Sequence conflict	587	1	V → A in AAA29025. Ref.1
	Sequence conflict	587	1	V → A in CAA90513. Ref.2
	Sequence conflict	587	1	V → A in CAA90514. Ref.2
	Sequence conflict	587	1	V → A in CAA83515. Ref.3
	Sequence conflict	587	1	V → A in CAA83516. Ref.3
	Sequence conflict	700	1	N → I in AAA29025. Ref.1
	Sequence conflict	700	1	N → I in CAA90513. Ref.2
	Sequence conflict	700	1	N → I in CAA90514. Ref.2
	Sequence conflict	700	1	N → I in CAA83515. Ref.3
	Sequence conflict	700	1	N → I in CAA83516. Ref.3
	Sequence conflict	720	1	T → A in AAA29025. Ref.1
	Sequence conflict	720	1	T → A in CAA90513. Ref.2
	Sequence conflict	720	1	T → A in CAA90514. Ref.2
	Sequence conflict	720	1	T → A in CAA83515. Ref.3
	Sequence conflict	720	1	T → A in CAA83516. Ref.3
	Sequence conflict	1073	1	K → P in AAA29025. Ref.1
	Sequence conflict	1073	1	K → P in CAA90513. Ref.2
	Sequence conflict	1073	1	K → P in CAA90514. Ref.2
	Sequence conflict	1073	1	K → P in CAA83515. Ref.3
	Sequence conflict	1073	1	K → P in CAA83516. Ref.3
	Sequence conflict	1529 – 1530	2	KL → NV in AAA29025. Ref.1
	Sequence conflict	1529 – 1530	2	KL → NV in CAA90513. Ref.2
	Sequence conflict	1529 – 1530	2	KL → NV in CAA90514. Ref.2
	Sequence conflict	1529 – 1530	2	KL → NV in CAA83515. Ref.3
	Sequence conflict	1529 – 1530	2	KL → NV in CAA83516. Ref.3
	Sequence conflict	1594	1	S → P in AAA29025. Ref.1
	Sequence conflict	1594	1	S → P in CAA90513. Ref.2
	Sequence conflict	1594	1	S → P in CAA90514. Ref.2
	Sequence conflict	1594	1	S → P in CAA83515. Ref.3
	Sequence conflict	1594	1	S → P in CAA83516. Ref.3
	Sequence conflict	1627	1	A → E in AAA29025. Ref.1
	Sequence conflict	1627	1	A → E in CAA90513. Ref.2
	Sequence conflict	1627	1	A → E in CAA90514. Ref.2
	Sequence conflict	1627	1	A → E in CAA83515. Ref.3
	Sequence conflict	1627	1	A → E in CAA83516. Ref.3
	Sequence conflict	1690	1	T → A in AAA29025. Ref.1
	Sequence conflict	1690	1	T → A in CAA90513. Ref.2
	Sequence conflict	1690	1	T → A in CAA90514. Ref.2
	Sequence conflict	1690	1	T → A in CAA83515. Ref.3
	Sequence conflict	1690	1	T → A in CAA83516. Ref.3
	Sequence conflict	2010	1	E → Q in AAA29025. Ref.1
	Sequence conflict	2010	1	E → Q in CAA90513. Ref.2
	Sequence conflict	2010	1	E → Q in CAA90514. Ref.2
	Sequence conflict	2010	1	E → Q in CAA83515. Ref.3
	Sequence conflict	2010	1	E → Q in CAA83516. Ref.3
	Sequence conflict	2025	1	P → PWLTSPLKFLGLSTHGGLLL WLLLGVVVRLKQGG in AAA29025. Ref.1
	Sequence conflict	2341	1	S → R in CAA90513. Ref.2
	Sequence conflict	2341	1	S → R in CAA90514. Ref.2
	Sequence conflict	2341	1	S → R in CAA83515. Ref.3
	Sequence conflict	2341	1	S → R in CAA83516. Ref.3
	Sequence conflict	2365	1	S → N in AAA29025. Ref.1
	Sequence conflict	2365	1	S → N in CAA90513. Ref.2
	Sequence conflict	2365	1	S → N in CAA90514. Ref.2
	Sequence conflict	2365	1	S → N in CAA83515. Ref.3
	Sequence conflict	2365	1	S → N in CAA83516. Ref.3
	Sequence conflict	2392	1	S → G in CAA90513. Ref.2
	Sequence conflict	2392	1	S → G in CAA90514. Ref.2
	Sequence conflict	2392	1	S → G in CAA83515. Ref.3
	Sequence conflict	2392	1	S → G in CAA83516. Ref.3
	Sequence conflict	3157	1	E → Q in AAA29025. Ref.1
	Sequence conflict	3157	1	E → Q in CAA90513. Ref.2
	Sequence conflict	3157	1	E → Q in CAA90514. Ref.2
	Sequence conflict	3157	1	E → Q in CAA83515. Ref.3
	Sequence conflict	3157	1	E → Q in CAA83516. Ref.3
	Sequence conflict	3234	1	A → R in AAA29025. Ref.1
	Sequence conflict	3234	1	A → R in CAA90513. Ref.2
	Sequence conflict	3234	1	A → R in CAA90514. Ref.2
	Sequence conflict	3234	1	A → R in CAA83515. Ref.3
	Sequence conflict	3234	1	A → R in CAA83516. Ref.3
	Sequence conflict	3690	1	L → V in AAA29025. Ref.1
	Sequence conflict	3690	1	L → V in CAA90513. Ref.2
	Sequence conflict	3690	1	L → V in CAA90514. Ref.2
	Sequence conflict	3690	1	L → V in CAA83515. Ref.3
	Sequence conflict	3690	1	L → V in CAA83516. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (D) [UniParc]. Last modified March 2, 2010. Version 4. Checksum: E3DDB8F062BD7796	FASTA	3,726	400,098
	10 20 30 40 50 60 MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG SSAAREKGNN 70 80 90 100 110 120 CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG SGSSGSGSTN GGSVNGGTHH 130 140 150 160 170 180 KSAANLDKEA VTKDQNGDGD KTRGNVSSAP SGKLSAAASG KALSKSSRTF SASTSVTSSG 190 200 210 220 230 240 RSSGSSPDGN SGASSDGASS GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSGT 250 260 270 280 290 300 TSEATTSGLS GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK 310 320 330 340 350 360 FKNLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPIASGS TPSVEGGIGV GGVVSPGEDA 370 380 390 400 410 420 ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP PAMASSGDGS SPKSGADTGP 430 440 450 460 470 480 STSSTTAKQK KTVTFRNVLE TSDDKSVVKR FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE 490 500 510 520 530 540 CIVRPSILSK ILNKNSNIDK LNSLKFRSAG ASSSSSNQES GSSSNVFGLS RAFGAPMDED 550 560 570 580 590 600 DEGGVTFRRN DSPEDQNNAE DDEMDDDDDD EEAEEDDENE DDNDEAVSEK SAETEKSAGA 610 620 630 640 650 660 DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG DSKGKNVFGT 670 680 690 700 710 720 SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGN FVLRQPRLQF QADNQQATFT 730 740 750 760 770 780 APKACPTSPS AIPKPANSLA TSSFGSLAST NSSTVTPTPS ACSICSAVVS SKEVTQARKY 790 800 810 820 830 840 GVVACDVCRK FFSKMTKKSI SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK 850 860 870 880 890 900 KFYKDRCTAC WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF 910 920 930 940 950 960 TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL RPAILENPLF 970 980 990 1000 1010 1020 LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE KLLSPTQAGT KKSGAAEAQV 1030 1040 1050 1060 1070 1080 EEVQPQKEEA PQTSTTTQPS ASNGASHGVP QAELAGETNA TGDTLKRQRI DLKGPRVKHV 1090 1100 1110 1120 1130 1140 CRSASIVLGQ PLATFGEDQQ PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS 1150 1160 1170 1180 1190 1200 CKTSPVGDES KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA 1210 1220 1230 1240 1250 1260 SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV CQTGFGLIVT 1270 1280 1290 1300 1310 1320 ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN LKHGSFEDTT LMGSLLETTV 1330 1340 1350 1360 1370 1380 NASTGPSSSL NQLTQRLNWL CPRCTVCYTC NMSSGSKVKC QKCQKNYHST CLGTSKRLLG 1390 1400 1410 1420 1430 1440 ADRPLICVNC LKCKSCSTTK VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM 1450 1460 1470 1480 1490 1500 MECGDCGQWV HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE 1510 1520 1530 1540 1550 1560 FKASLYSVLK LLSKSRQACA LLKLSPRKKL RCTCGASSNQ GKLQPKALQF SSGSDNGLGS 1570 1580 1590 1600 1610 1620 DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKSLPCSCQ QHISHSQSFS LVDIKQKIAG 1630 1640 1650 1660 1670 1680 NSYVSLAEFN YDMSQVIQQS NCDELDIAYK ELLSEQFPWF QNETKACTDA LEEDMFESCS 1690 1700 1710 1720 1730 1740 GGNYEDLQDT GGVSASVYNE HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC 1750 1760 1770 1780 1790 1800 RKSGEGLSGE EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC 1810 1820 1830 1840 1850 1860 GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA NGSPSVTYES 1870 1880 1890 1900 1910 1920 NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI VPRFSDSYEA VVPINFLCSR 1930 1940 1950 1960 1970 1980 LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL DVGRNYTVDH TNPNSKEVQL GMAQIARWHT 1990 2000 2010 2020 2030 2040 SLARSEFLEN GGTDWSGEFP NPNSCVPPDE NTEEEPQQQA DLLPPELKDA IFEDLPHELL 2050 2060 2070 2080 2090 2100 DGISMLDIFL YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN 2110 2120 2130 2140 2150 2160 TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR RKLSKNLAEG 2170 2180 2190 2200 2210 2220 VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG SVRSKSFTWS AAKRYFEKSE 2230 2240 2250 2260 2270 2280 GREEAAKMRI MQMDGVDDSI TEFRIISGDG NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL 2290 2300 2310 2320 2330 2340 PSCSPTMSSN ETESDVSGQG MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ 2350 2360 2370 2380 2390 2400 SLGSLGQFGL QGLQQLQLQP QSLGSGFFLS QPNPATQANT DDLQIYANSL QSLAANLGGG 2410 2420 2430 2440 2450 2460 FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ ATNTDKKIML 2470 2480 2490 2500 2510 2520 PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL QPHPQQHQQQ QQTQVQQPIT 2530 2540 2550 2560 2570 2580 VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ PQNIISFVTG DGSQGQPLQY ISIPTAGEYK 2590 2600 2610 2620 2630 2640 PQPQPTATPT FLTTAPGAGA TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL 2650 2660 2670 2680 2690 2700 IQPQTIQLGG GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV 2710 2720 2730 2740 2750 2760 QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV LNNTGDASSA 2770 2780 2790 2800 2810 2820 GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS TSMDYTSPVM VTAKIPPVTQ 2830 2840 2850 2860 2870 2880 IKRTNAQAKA AGISGVGKVP PQPQVVNKVL PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG 2890 2900 2910 2920 2930 2940 TGTTCGAPPS IASKPLQKKT NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL 2950 2960 2970 2980 2990 3000 QQQIPAVVVN QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII 3010 3020 3030 3040 3050 3060 TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN PMQQQAPSTT 3070 3080 3090 3100 3110 3120 SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE QPIIHQMTSA SVSKCYAQKS 3130 3140 3150 3160 3170 3180 TLPSPVYEAE LKVSSVLESI VPDVTMDAIL EEQPVTESIY TEGLYEKNSP GESKTEQLLL 3190 3200 3210 3220 3230 3240 QQQQREQLNQ QLVNNGYLLD KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMATSACND 3250 3260 3270 3280 3290 3300 HEMSDSEEPA VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS 3310 3320 3330 3340 3350 3360 APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE QRTVSQEQEQ 3370 3380 3390 3400 3410 3420 SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT YKSSSITEIW EKVFEAVQVA 3430 3440 3450 3460 3470 3480 RRAHGLTPLP EGPLADMGGI QMIGLKTNAL KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA 3490 3500 3510 3520 3530 3540 ANGAHGGNLG GSSASAALSV SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF 3550 3560 3570 3580 3590 3600 SWLASRHRKQ PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR 3610 3620 3630 3640 3650 3660 GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL VVDATMRGNA 3670 3680 3690 3700 3710 3720 ARFINHCCEP NCYSKVVDIL GHKHIIIFAL RRIVQGEELT YDYKFPFEDE KIPCSCGSKR CRKYLN
	Isoform B (C) (E) [UniParc]. Checksum: 1382F25255A47E5B	FASTA	3,358	364,664
	10 20 30 40 50 60 MPNEVARDPS PSSCTAAANG AASGKGSASN GPPAMASSGD GSSPKSGADT GPSTSSTTAK 70 80 90 100 110 120 QKKTVTFRNV LETSDDKSVV KRFYNPDIRI PIVSIMKKDS LNRPLNYSRG GECIVRPSIL 130 140 150 160 170 180 SKILNKNSNI DKLNSLKFRS AGASSSSSNQ ESGSSSNVFG LSRAFGAPMD EDDEGGVTFR 190 200 210 220 230 240 RNDSPEDQNN AEDDEMDDDD DDEEAEEDDE NEDDNDEAVS EKSAETEKSA GADERDPDEK 250 260 270 280 290 300 QLVMDSHFVL PKRSTRSSRI IKPNKRLLEE GAISTKKPLS LGDSKGKNVF GTSSSSAGST 310 320 330 340 350 360 ASTFSASTNL KLGKETFFNF GTLKPNSSAA GNFVLRQPRL QFQADNQQAT FTAPKACPTS 370 380 390 400 410 420 PSAIPKPANS LATSSFGSLA STNSSTVTPT PSACSICSAV VSSKEVTQAR KYGVVACDVC 430 440 450 460 470 480 RKFFSKMTKK SISANSSTAN TSSGSQQYLQ CKGNEGSPCS IHSAKSQLKN FKKFYKDRCT 490 500 510 520 530 540 ACWLKKCMIS FQLPAAHRSR LSAILPPGMR GEAAAREEKS AELLSPTGSL RFTSTASSSS 550 560 570 580 590 600 PSVVASTSVK WKSSGDSTSA LTSIKPNPLA ENNVTFGSTP LLRPAILENP LFLKISNAAD 610 620 630 640 650 660 QKLAAAEAIS PSLTKKNSKQ EKEKVKESEQ SEKLLSPTQA GTKKSGAAEA QVEEVQPQKE 670 680 690 700 710 720 EAPQTSTTTQ PSASNGASHG VPQAELAGET NATGDTLKRQ RIDLKGPRVK HVCRSASIVL 730 740 750 760 770 780 GQPLATFGED QQPEDAADMQ QEIAAPVPSA IMEPSPEKPT HIVTDENDNC ASCKTSPVGD 790 800 810 820 830 840 ESKPSKSSGS AQAEVKKATA LGKEGTASAA GGSSAKVTTR NAAVASNLIV AASKKQRNGD 850 860 870 880 890 900 IATSSSVTQS SNQTQGRKTK EHRQQRTLIS IDFWENYDPA EVCQTGFGLI VTETVAQRAL 910 920 930 940 950 960 CFLCGSTGLD PLIFCACCCE PYHQYCVQDE YNLKHGSFED TTLMGSLLET TVNASTGPSS 970 980 990 1000 1010 1020 SLNQLTQRLN WLCPRCTVCY TCNMSSGSKV KCQKCQKNYH STCLGTSKRL LGADRPLICV 1030 1040 1050 1060 1070 1080 NCLKCKSCST TKVSKFVGNL PMCTGCFKLR KKGNFCPICQ RCYDDNDFDL KMMECGDCGQ 1090 1100 1110 1120 1130 1140 WVHSKCEGLS DEQYNLLSTL PESIEFICKK CARRNESSKI KAEEWRQAVM EEFKASLYSV 1150 1160 1170 1180 1190 1200 LKLLSKSRQA CALLKLSPRK KLRCTCGASS NQGKLQPKAL QFSSGSDNGL GSDGESQNSD 1210 1220 1230 1240 1250 1260 DVYEFKDQQQ QQQQRNANMN KPRVKSLPCS CQQHISHSQS FSLVDIKQKI AGNSYVSLAE 1270 1280 1290 1300 1310 1320 FNYDMSQVIQ QSNCDELDIA YKELLSEQFP WFQNETKACT DALEEDMFES CSGGNYEDLQ 1330 1340 1350 1360 1370 1380 DTGGVSASVY NEHSTSQAES RSGVLDIPLE EVDDFGSCGI KMRLDTRMCL FCRKSGEGLS 1390 1400 1410 1420 1430 1440 GEEARLLYCG HDCWVHTNCA MWSAEVFEEI DGSLQNVHSA VARGRMIKCT VCGNRGATVG 1450 1460 1470 1480 1490 1500 CNVRSCGEHY HYPCARSIDC AFLTDKSMYC PAHAKNGNAL KANGSPSVTY ESNFEVSRPV 1510 1520 1530 1540 1550 1560 YVELDRKRKK LIEPARVQFH IGSLEVRQLG AIVPRFSDSY EAVVPINFLC SRLYWSSKEP 1570 1580 1590 1600 1610 1620 WKIVEYTVRT TIQNSSSTLT ALDVGRNYTV DHTNPNSKEV QLGMAQIARW HTSLARSEFL 1630 1640 1650 1660 1670 1680 ENGGTDWSGE FPNPNSCVPP DENTEEEPQQ QADLLPPELK DAIFEDLPHE LLDGISMLDI 1690 1700 1710 1720 1730 1740 FLYDDKTDLF AISEQSKDGT QAMTSNQAQN QNQQAGGANS VSICDEDTRN SNTSLGNGWP 1750 1760 1770 1780 1790 1800 ASNPVEDAML SAARNSSQVQ MLKTLAWPKL DGNSAMATAI KRRKLSKNLA EGVFLTLSSQ 1810 1820 1830 1840 1850 1860 QRNKKEMATV AGVSRRQSIS ETSVEGVATT SGSVRSKSFT WSAAKRYFEK SEGREEAAKM 1870 1880 1890 1900 1910 1920 RIMQMDGVDD SITEFRIISG DGNLSTAQFS GQVKCDRCQC TYRNYDAFQR HLPSCSPTMS 1930 1940 1950 1960 1970 1980 SNETESDVSG QGMTNNATQI SAESLNELQK QLLANAGGLN YLQSATSFPQ VQSLGSLGQF 1990 2000 2010 2020 2030 2040 GLQGLQQLQL QPQSLGSGFF LSQPNPATQA NTDDLQIYAN SLQSLAANLG GGFTLAQPTV 2050 2060 2070 2080 2090 2100 TAPAQPQLIA VSTNPDGTQQ FIQIPQTMQA TTTPTATYQT LQATNTDKKI MLPLTAAGKP 2110 2120 2130 2140 2150 2160 LKTVATKAAQ QAAVKQRQLK SGHQVKPIQA KLQPHPQQHQ QQQQTQVQQP ITVMGQNLLQ 2170 2180 2190 2200 2210 2220 PQLLFQSSTQ TQAPQIILPQ AQPQNIISFV TGDGSQGQPL QYISIPTAGE YKPQPQPTAT 2230 2240 2250 2260 2270 2280 PTFLTTAPGA GATYLQTDAS GNLVLTTTPS NSGLQMLTAQ SLQAQPQVIG TLIQPQTIQL 2290 2300 2310 2320 2330 2340 GGGADGNQPG SNQQPLILGG TGGGSSGLEF ATTSPQVILA TQPMYYGLET IVQNTVMSSQ 2350 2360 2370 2380 2390 2400 QFVSTAMPGM LSQNASFSAT TTQVFQASKI EPIVDLPAGY VVLNNTGDAS SAGTFLNAAS 2410 2420 2430 2440 2450 2460 VLQQQTQDDT TTQILQNANF QFQSVPTSSG ASTSMDYTSP VMVTAKIPPV TQIKRTNAQA 2470 2480 2490 2500 2510 2520 KAAGISGVGK VPPQPQVVNK VLPTSIVTQQ SQVQVKNSNL KQSQVKGKAA SGTGTTCGAP 2530 2540 2550 2560 2570 2580 PSIASKPLQK KTNMIRPIHK LEVKPKVMKP TPKVQNQNHS LLQQQQQQQP QLQQQIPAVV 2590 2600 2610 2620 2630 2640 VNQVPKVTIS QQRIPAQTQQ QQLQQAQMIH IPQQQQPLQQ QQVQVQPSMP IITLAEAPVV 2650 2660 2670 2680 2690 2700 QSQFVMEPQA LEQQELANRV QHFSTSSSSS SSNCSLPTNV VNPMQQQAPS TTSSSTTRPT 2710 2720 2730 2740 2750 2760 NRVLPMQQRQ EPAPLSNECP VVSSPTPPKP VEQPIIHQMT SASVSKCYAQ KSTLPSPVYE 2770 2780 2790 2800 2810 2820 AELKVSSVLE SIVPDVTMDA ILEEQPVTES IYTEGLYEKN SPGESKTEQL LLQQQQREQL 2830 2840 2850 2860 2870 2880 NQQLVNNGYL LDKHTFQVEP MDTDVYREED LEEEEDEDDD FSLKMATSAC NDHEMSDSEE 2890 2900 2910 2920 2930 2940 PAVKDKISKI LDNLTNDDCA DSIATATTME VDASAGYQQM VEDVLATTAA QSAPTEEFEG 2950 2960 2970 2980 2990 3000 ALETAAVEAA ATYINEMADA HVLDLKQLQN GVELELRRRK EEQRTVSQEQ EQSKAAIVPT 3010 3020 3030 3040 3050 3060 AAAPEPPQPI QEPKKMTGPH LLYEIQSEDG FTYKSSSITE IWEKVFEAVQ VARRAHGLTP 3070 3080 3090 3100 3110 3120 LPEGPLADMG GIQMIGLKTN ALKYLIEQLP GVEKCSKYTP KYHKRNGNVS TAANGAHGGN 3130 3140 3150 3160 3170 3180 LGGSSASAAL SVSGGDSHGL LDYGSDQDEL EENAYDCARC EPYSNRSEYD MFSWLASRHR 3190 3200 3210 3220 3230 3240 KQPIQVFVQP SDNELVPRRG TGSNLPMAMK YRTLKETYKD YVGVFRSHIH GRGLYCTKDI 3250 3260 3270 3280 3290 3300 EAGEMVIEYA GELIRSTLTD KRERYYDSRG IGCYMFKIDD NLVVDATMRG NAARFINHCC 3310 3320 3330 3340 3350 EPNCYSKVVD ILGHKHIIIF ALRRIVQGEE LTYDYKFPFE DEKIPCSCGS KRCRKYLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains." Mazo A.M., Huang D.-H., Mozer B.A., Dawid I.B. Proc. Natl. Acad. Sci. U.S.A. 87:2112-2116(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION.
[2]	"The bithorax complex is regulated by trithorax earlier during Drosophila embryogenesis than is the Antennapedia complex, correlating with a bithorax-like expression pattern of distinct early trithorax transcripts." Sedkov Y., Tillib S., Mizrokhi L., Mazo A. Development 120:1907-1917(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[3]	"Conservation of structure and expression of the trithorax gene between Drosophila virilis and Drosophila melanogaster." Tillib S., Sedkov Y., Mizrokhi L., Mazo A. Mech. Dev. 53:113-122(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Oregon-R. Tissue: Embryo.
[4]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[6]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2970-3726 (ISOFORMS A/B). Strain: Berkeley. Tissue: Embryo.
[7]	"Trithorax and ASH1 interact directly and associate with the trithorax group-responsive bxd region of the Ultrabithorax promoter." Rozovskaia T., Tillib S., Smith S., Sedkov Y., Rozenblatt-Rosen O., Petruk S., Yano T., Nakamura T., Ben-Simchon L., Gildea J., Croce C.M., Shearn A., Canaani E., Mazo A. Mol. Cell. Biol. 19:6441-6447(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASH1.
[8]	"Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins." Rozovskaia T., Rozenblatt-Rosen O., Sedkov Y., Burakov D., Yano T., Nakamura T., Petruck S., Ben-Simchon L., Croce C.M., Mazo A., Canaani E. Oncogene 19:351-357(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASH1.
[9]	"The Drosophila trithorax gene encodes a chromosomal protein and directly regulates the region-specific homeotic gene fork head." Kuzin B., Tillib S., Sedkov Y., Mizrokhi L., Mazo A. Genes Dev. 8:2478-2490(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Drosophila Enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites." Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Cell 111:185-196(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYMATIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31617 mRNA. Translation: AAA29025.1. Z50152 Genomic DNA. Translation: CAA90514.1. Z50152 Genomic DNA. Translation: CAA90513.1. Z31725 Genomic DNA. Translation: CAA83516.1. Z31725 Genomic DNA. Translation: CAA83515.1. AE014297 Genomic DNA. Translation: AAF55041.2. AE014297 Genomic DNA. Translation: AAN13599.1. AE014297 Genomic DNA. Translation: AAN13600.1. AE014297 Genomic DNA. Translation: AAN13601.1. AE014297 Genomic DNA. Translation: AAX52951.1. AY051904 mRNA. Translation: AAK93328.1. Different initiation.
PIR	A35085.
RefSeq	NP_001014621.1. NM_001014621.2. NP_476769.1. NM_057421.3. NP_476770.1. NM_057422.3. NP_599108.1. NM_134281.2. NP_599109.1. NM_134282.2.
UniGene	Dm.6437.
3D structure databases
ProteinModelPortal	P20659.
SMR	P20659. Positions 1269-1294, 1346-1399, 1420-1523, 3566-3726.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20659. 6 interactions.
MINT	MINT-907260.
Proteomic databases
PaxDb	P20659.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082947; FBpp0082406; FBgn0003862. FBtr0082950; FBpp0082409; FBgn0003862.
GeneID	41737.
KEGG	dme:Dmel_CG8651.
Organism-specific databases
CTD	41737.
FlyBase	FBgn0003862. trx.
Phylogenomic databases
eggNOG	COG2940.
GeneTree	ENSGT00690000101661.
InParanoid	P20659.
KO	K09186.
OMA	RQPRLQF.
OrthoDB	EOG4X3FG4.
PhylomeDB	P20659.
Gene expression databases
Bgee	P20659.
GermOnline	CG8651. Drosophila melanogaster.
Family and domain databases
Gene3D	3.30.40.10. 3 hits.
InterPro	IPR003889. FYrich_C. IPR003888. FYrich_N. IPR015722. Histone-lysine_MeTfrase. IPR016569. MeTrfase_trithorax. IPR003616. Post-SET_dom. IPR001214. SET_dom. IPR011011. Znf_FYVE_PHD. IPR001628. Znf_hrmn_rcpt. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
PANTHER	PTHR22884:SF10. PTHR22884:SF10. 1 hit.
Pfam	PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 1 hit. PF00856. SET. 1 hit. [Graphical view]
PIRSF	PIRSF010354. Methyltransferase_trithorax. 1 hit.
SMART	SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00249. PHD. 4 hits. SM00508. PostSET. 2 hits. SM00184. RING. 4 hits. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 3 hits.
PROSITE	PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. Uncertain. PS50868. POST_SET. 1 hit. PS50280. SET. 1 hit. PS01359. ZF_PHD_1. 4 hits. PS50016. ZF_PHD_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	41737.
NextBio	825306.

Entry information

Entry name

TRX_DROME

Accession

Primary (citable) accession number: P20659
Secondary accession number(s): A4V2V9 , A4V2W0, Q27255, Q27327, Q8INF9, Q960R2, Q9VFL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	March 2, 2010
Last modified:	May 1, 2013
This is version 149 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project