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P20659 (TRX_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length3726 AA.
Sequence statusComplete.
Protein existenceEvidence 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 class V-like SAM-binding methyltransferase superfamily. 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 processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionActivator
Chromatin regulator
Developmental protein
Methyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon 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

histone 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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1/2 complex

Inferred from direct assay PubMed 21875999. Source: FlyBase

histone methyltransferase complex

Inferred from direct assay Ref.10. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from direct assay Ref.10PubMed 17174895. 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_functionchromatin binding

Inferred from direct assay PubMed 17174895. Source: FlyBase

histone methyltransferase activity (H3-K4 specific)

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from physical interaction Ref.8PubMed 11313484. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11976948. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 11313484. Source: UniProtKB

protein phosphatase 1 binding

Inferred from physical interaction PubMed 17007873. Source: FlyBase

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

itself7EBI-591327,EBI-591327
cyp33Q9V3G32EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 37263726Histone-lysine N-methyltransferase trithorax
PRO_0000124874

Regions

Domain1884 – 194158FYR N-terminal
Domain3386 – 347085FYR C-terminal
Domain3588 – 3704117SET
Domain3710 – 372617Post-SET
DNA binding759 – 884126Nuclear receptor
Zinc finger1266 – 134782PHD-type 1
Zinc finger1348 – 139346PHD-type 2
Zinc finger1421 – 148262PHD-type 3
Zinc finger1734 – 179360PHD-type 4; atypical
Zinc finger1794 – 184451PHD-type 5; atypical
Region3665 – 36662S-adenosyl-L-methionine binding By similarity
Compositional bias512 – 5165Poly-Ser
Compositional bias565 – 5706Poly-Asp
Compositional bias661 – 6644Poly-Ser
Compositional bias905 – 9106Poly-Ser
Compositional bias1576 – 15827Poly-Gln
Compositional bias2298 – 3027730Gln-rich
Compositional bias3032 – 30409Poly-Ser
Compositional bias3181 – 31844Poly-Gln
Compositional bias3220 – 32256Poly-Glu

Sites

Metal binding36681Zinc By similarity
Metal binding37141Zinc By similarity
Metal binding37161Zinc By similarity
Metal binding37211Zinc By similarity
Binding site35981S-adenosyl-L-methionine By similarity
Binding site36001S-adenosyl-L-methionine By similarity
Binding site36421S-adenosyl-L-methionine By similarity

Natural variations

Alternative sequence1 – 368368Missing in isoform B.
VSP_006665

Experimental info

Sequence conflict239 – 24911GTTSEATTSGL → LEQLVKQQPLV in AAA29025. Ref.1
Sequence conflict239 – 24911GTTSEATTSGL → LEQLVKQQPLV in CAA90513. Ref.2
Sequence conflict239 – 24911GTTSEATTSGL → LEQLVKQQPLV in CAA83516. Ref.3
Sequence conflict3031N → K in AAA29025. Ref.1
Sequence conflict3031N → K in CAA90513. Ref.2
Sequence conflict3031N → K in CAA83516. Ref.3
Sequence conflict3371A → L in AAA29025. Ref.1
Sequence conflict3371A → L in CAA90513. Ref.2
Sequence conflict3371A → L in CAA83516. Ref.3
Sequence conflict5211G → R in AAA29025. Ref.1
Sequence conflict5211G → R in CAA90513. Ref.2
Sequence conflict5211G → R in CAA90514. Ref.2
Sequence conflict5211G → R in CAA83515. Ref.3
Sequence conflict5211G → R in CAA83516. Ref.3
Sequence conflict5781E → Q in AAA29025. Ref.1
Sequence conflict5781E → Q in CAA90513. Ref.2
Sequence conflict5781E → Q in CAA90514. Ref.2
Sequence conflict5781E → Q in CAA83515. Ref.3
Sequence conflict5781E → Q in CAA83516. Ref.3
Sequence conflict5871V → A in AAA29025. Ref.1
Sequence conflict5871V → A in CAA90513. Ref.2
Sequence conflict5871V → A in CAA90514. Ref.2
Sequence conflict5871V → A in CAA83515. Ref.3
Sequence conflict5871V → A in CAA83516. Ref.3
Sequence conflict7001N → I in AAA29025. Ref.1
Sequence conflict7001N → I in CAA90513. Ref.2
Sequence conflict7001N → I in CAA90514. Ref.2
Sequence conflict7001N → I in CAA83515. Ref.3
Sequence conflict7001N → I in CAA83516. Ref.3
Sequence conflict7201T → A in AAA29025. Ref.1
Sequence conflict7201T → A in CAA90513. Ref.2
Sequence conflict7201T → A in CAA90514. Ref.2
Sequence conflict7201T → A in CAA83515. Ref.3
Sequence conflict7201T → A in CAA83516. Ref.3
Sequence conflict10731K → P in AAA29025. Ref.1
Sequence conflict10731K → P in CAA90513. Ref.2
Sequence conflict10731K → P in CAA90514. Ref.2
Sequence conflict10731K → P in CAA83515. Ref.3
Sequence conflict10731K → P in CAA83516. Ref.3
Sequence conflict1529 – 15302KL → NV in AAA29025. Ref.1
Sequence conflict1529 – 15302KL → NV in CAA90513. Ref.2
Sequence conflict1529 – 15302KL → NV in CAA90514. Ref.2
Sequence conflict1529 – 15302KL → NV in CAA83515. Ref.3
Sequence conflict1529 – 15302KL → NV in CAA83516. Ref.3
Sequence conflict15941S → P in AAA29025. Ref.1
Sequence conflict15941S → P in CAA90513. Ref.2
Sequence conflict15941S → P in CAA90514. Ref.2
Sequence conflict15941S → P in CAA83515. Ref.3
Sequence conflict15941S → P in CAA83516. Ref.3
Sequence conflict16271A → E in AAA29025. Ref.1
Sequence conflict16271A → E in CAA90513. Ref.2
Sequence conflict16271A → E in CAA90514. Ref.2
Sequence conflict16271A → E in CAA83515. Ref.3
Sequence conflict16271A → E in CAA83516. Ref.3
Sequence conflict16901T → A in AAA29025. Ref.1
Sequence conflict16901T → A in CAA90513. Ref.2
Sequence conflict16901T → A in CAA90514. Ref.2
Sequence conflict16901T → A in CAA83515. Ref.3
Sequence conflict16901T → A in CAA83516. Ref.3
Sequence conflict20101E → Q in AAA29025. Ref.1
Sequence conflict20101E → Q in CAA90513. Ref.2
Sequence conflict20101E → Q in CAA90514. Ref.2
Sequence conflict20101E → Q in CAA83515. Ref.3
Sequence conflict20101E → Q in CAA83516. Ref.3
Sequence conflict20251P → PWLTSPLKFLGLSTHGGLLL WLLLGVVVRLKQGG in AAA29025. Ref.1
Sequence conflict23411S → R in CAA90513. Ref.2
Sequence conflict23411S → R in CAA90514. Ref.2
Sequence conflict23411S → R in CAA83515. Ref.3
Sequence conflict23411S → R in CAA83516. Ref.3
Sequence conflict23651S → N in AAA29025. Ref.1
Sequence conflict23651S → N in CAA90513. Ref.2
Sequence conflict23651S → N in CAA90514. Ref.2
Sequence conflict23651S → N in CAA83515. Ref.3
Sequence conflict23651S → N in CAA83516. Ref.3
Sequence conflict23921S → G in CAA90513. Ref.2
Sequence conflict23921S → G in CAA90514. Ref.2
Sequence conflict23921S → G in CAA83515. Ref.3
Sequence conflict23921S → G in CAA83516. Ref.3
Sequence conflict31571E → Q in AAA29025. Ref.1
Sequence conflict31571E → Q in CAA90513. Ref.2
Sequence conflict31571E → Q in CAA90514. Ref.2
Sequence conflict31571E → Q in CAA83515. Ref.3
Sequence conflict31571E → Q in CAA83516. Ref.3
Sequence conflict32341A → R in AAA29025. Ref.1
Sequence conflict32341A → R in CAA90513. Ref.2
Sequence conflict32341A → R in CAA90514. Ref.2
Sequence conflict32341A → R in CAA83515. Ref.3
Sequence conflict32341A → R in CAA83516. Ref.3
Sequence conflict36901L → V in AAA29025. Ref.1
Sequence conflict36901L → V in CAA90513. Ref.2
Sequence conflict36901L → V in CAA90514. Ref.2
Sequence conflict36901L → V in CAA83515. Ref.3
Sequence conflict36901L → V in CAA83516. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A (D) [UniParc].

Last modified March 2, 2010. Version 4.
Checksum: E3DDB8F062BD7796

FASTA3,726400,098
        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 

« Hide

Isoform B (C) (E) [UniParc].

Checksum: 1382F25255A47E5B
Show »

FASTA3,358364,664

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRA35085.
RefSeqNP_001014621.1. NM_001014621.2. [P20659-2]
NP_476769.1. NM_057421.3. [P20659-1]
NP_476770.1. NM_057422.3. [P20659-2]
NP_599108.1. NM_134281.2. [P20659-2]
NP_599109.1. NM_134282.2. [P20659-1]
UniGeneDm.6437.

3D structure databases

ProteinModelPortalP20659.
SMRP20659. Positions 1267-1296, 1343-1403, 1420-1523, 1737-1842, 3566-3726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66813. 36 interactions.
IntActP20659. 6 interactions.
MINTMINT-907260.

Proteomic databases

PaxDbP20659.
PRIDEP20659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082947; FBpp0082406; FBgn0003862. [P20659-1]
FBtr0082950; FBpp0082409; FBgn0003862. [P20659-1]
GeneID41737.
KEGGdme:Dmel_CG8651.
UCSCCG8651-RC. d. melanogaster.

Organism-specific databases

CTD41737.
FlyBaseFBgn0003862. trx.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00740000115089.
InParanoidP20659.
KOK09186.
OMAARCEPYS.
OrthoDBEOG75XGJZ.
PhylomeDBP20659.

Enzyme and pathway databases

SignaLinkP20659.

Gene expression databases

BgeeP20659.

Family and domain databases

Gene3D3.30.40.10. 3 hits.
InterProIPR003889. FYrich_C.
IPR003888. FYrich_N.
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]
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTSM00542. 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]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 4 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41737.
NextBio825306.
PROP20659.

Entry information

Entry nameTRX_DROME
AccessionPrimary (citable) accession number: P20659
Secondary accession number(s): A4V2V9 expand/collapse secondary AC list , A4V2W0, Q27255, Q27327, Q8INF9, Q960R2, Q9VFL1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 160 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase