Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20659

- TRX_DROME

UniProt

P20659 - TRX_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone-lysine N-methyltransferase trithorax

Gene

trx

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei3598 – 35981S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei3600 – 36001S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei3642 – 36421S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi3668 – 36681ZincBy similarity
Metal bindingi3714 – 37141ZincBy similarity
Metal bindingi3716 – 37161ZincBy similarity
Metal bindingi3721 – 37211ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi759 – 884126Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1266 – 134782PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1348 – 139346PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1421 – 148262PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1734 – 179360PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1794 – 184451PHD-type 5; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: FlyBase
  2. histone methyltransferase activity (H3-K4 specific) Source: InterPro
  3. identical protein binding Source: IntAct
  4. protein homodimerization activity Source: UniProtKB
  5. protein phosphatase 1 binding Source: FlyBase
  6. sequence-specific DNA binding Source: InterPro
  7. sequence-specific DNA binding transcription factor activity Source: InterPro
  8. transcription regulatory region DNA binding Source: FlyBase
  9. zinc ion binding Source: FlyBase

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. germ cell migration Source: FlyBase
  3. histone H3 acetylation Source: FlyBase
  4. histone H3-K4 methylation Source: FlyBase
  5. histone methylation Source: FlyBase
  6. positive regulation of transcription elongation from RNA polymerase II promoter Source: FlyBase
  7. regulation of response to DNA damage stimulus Source: FlyBase
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

SignaLinkiP20659.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase trithorax (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 2A
Gene namesi
Name:trx
Synonyms:KMT2A
ORF Names:CG8651
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003862. trx.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosome 1 Publication
Note: Binds to 16 discrete sites on larval salivary gland polytene chromosomes.

GO - Cellular componenti

  1. histone methyltransferase complex Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. MLL1/2 complex Source: FlyBase
  4. nucleus Source: FlyBase
  5. polytene chromosome Source: FlyBase
  6. transcription elongation factor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 37263726Histone-lysine N-methyltransferase trithoraxPRO_0000124874Add
BLAST

Proteomic databases

PaxDbiP20659.
PRIDEiP20659.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP20659.

Interactioni

Subunit structurei

Interacts with ash1 via its SET domain.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-591327,EBI-591327
cyp33Q9V3G32EBI-591327,EBI-128445

Protein-protein interaction databases

BioGridi66813. 37 interactions.
IntActiP20659. 6 interactions.
MINTiMINT-907260.

Structurei

3D structure databases

ProteinModelPortaliP20659.
SMRiP20659. Positions 1267-1297, 1344-1396, 1420-1523, 1737-1842, 3566-3726.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1884 – 194158FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3386 – 347085FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3588 – 3704117SETPROSITE-ProRule annotationAdd
BLAST
Domaini3710 – 372617Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3665 – 36662S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi512 – 5165Poly-Ser
Compositional biasi565 – 5706Poly-Asp
Compositional biasi661 – 6644Poly-Ser
Compositional biasi905 – 9106Poly-Ser
Compositional biasi1576 – 15827Poly-Gln
Compositional biasi2298 – 3027730Gln-richAdd
BLAST
Compositional biasi3032 – 30409Poly-Ser
Compositional biasi3181 – 31844Poly-Gln
Compositional biasi3220 – 32256Poly-Glu

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation
Contains 5 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1266 – 134782PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1348 – 139346PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1421 – 148262PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1734 – 179360PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1794 – 184451PHD-type 5; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
InParanoidiP20659.
KOiK09186.
OMAiARCEPYS.
OrthoDBiEOG75XGJZ.
PhylomeDBiP20659.

Family and domain databases

Gene3Di3.30.40.10. 3 hits.
InterProiIPR003889. 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]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTiSM00542. 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]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS51543. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: P20659-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG
60 70 80 90 100
SSAAREKGNN CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG
110 120 130 140 150
SGSSGSGSTN GGSVNGGTHH KSAANLDKEA VTKDQNGDGD KTRGNVSSAP
160 170 180 190 200
SGKLSAAASG KALSKSSRTF SASTSVTSSG RSSGSSPDGN SGASSDGASS
210 220 230 240 250
GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSGT TSEATTSGLS
260 270 280 290 300
GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK
310 320 330 340 350
FKNLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPIASGS TPSVEGGIGV
360 370 380 390 400
GGVVSPGEDA ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP
410 420 430 440 450
PAMASSGDGS SPKSGADTGP STSSTTAKQK KTVTFRNVLE TSDDKSVVKR
460 470 480 490 500
FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE CIVRPSILSK ILNKNSNIDK
510 520 530 540 550
LNSLKFRSAG ASSSSSNQES GSSSNVFGLS RAFGAPMDED DEGGVTFRRN
560 570 580 590 600
DSPEDQNNAE DDEMDDDDDD EEAEEDDENE DDNDEAVSEK SAETEKSAGA
610 620 630 640 650
DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG
660 670 680 690 700
DSKGKNVFGT SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGN
710 720 730 740 750
FVLRQPRLQF QADNQQATFT APKACPTSPS AIPKPANSLA TSSFGSLAST
760 770 780 790 800
NSSTVTPTPS ACSICSAVVS SKEVTQARKY GVVACDVCRK FFSKMTKKSI
810 820 830 840 850
SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK KFYKDRCTAC
860 870 880 890 900
WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF
910 920 930 940 950
TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL
960 970 980 990 1000
RPAILENPLF LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE
1010 1020 1030 1040 1050
KLLSPTQAGT KKSGAAEAQV EEVQPQKEEA PQTSTTTQPS ASNGASHGVP
1060 1070 1080 1090 1100
QAELAGETNA TGDTLKRQRI DLKGPRVKHV CRSASIVLGQ PLATFGEDQQ
1110 1120 1130 1140 1150
PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS CKTSPVGDES
1160 1170 1180 1190 1200
KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA
1210 1220 1230 1240 1250
SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV
1260 1270 1280 1290 1300
CQTGFGLIVT ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN
1310 1320 1330 1340 1350
LKHGSFEDTT LMGSLLETTV NASTGPSSSL NQLTQRLNWL CPRCTVCYTC
1360 1370 1380 1390 1400
NMSSGSKVKC QKCQKNYHST CLGTSKRLLG ADRPLICVNC LKCKSCSTTK
1410 1420 1430 1440 1450
VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM MECGDCGQWV
1460 1470 1480 1490 1500
HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE
1510 1520 1530 1540 1550
FKASLYSVLK LLSKSRQACA LLKLSPRKKL RCTCGASSNQ GKLQPKALQF
1560 1570 1580 1590 1600
SSGSDNGLGS DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKSLPCSCQ
1610 1620 1630 1640 1650
QHISHSQSFS LVDIKQKIAG NSYVSLAEFN YDMSQVIQQS NCDELDIAYK
1660 1670 1680 1690 1700
ELLSEQFPWF QNETKACTDA LEEDMFESCS GGNYEDLQDT GGVSASVYNE
1710 1720 1730 1740 1750
HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC RKSGEGLSGE
1760 1770 1780 1790 1800
EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC
1810 1820 1830 1840 1850
GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA
1860 1870 1880 1890 1900
NGSPSVTYES NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI
1910 1920 1930 1940 1950
VPRFSDSYEA VVPINFLCSR LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL
1960 1970 1980 1990 2000
DVGRNYTVDH TNPNSKEVQL GMAQIARWHT SLARSEFLEN GGTDWSGEFP
2010 2020 2030 2040 2050
NPNSCVPPDE NTEEEPQQQA DLLPPELKDA IFEDLPHELL DGISMLDIFL
2060 2070 2080 2090 2100
YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN
2110 2120 2130 2140 2150
TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR
2160 2170 2180 2190 2200
RKLSKNLAEG VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG
2210 2220 2230 2240 2250
SVRSKSFTWS AAKRYFEKSE GREEAAKMRI MQMDGVDDSI TEFRIISGDG
2260 2270 2280 2290 2300
NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL PSCSPTMSSN ETESDVSGQG
2310 2320 2330 2340 2350
MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ SLGSLGQFGL
2360 2370 2380 2390 2400
QGLQQLQLQP QSLGSGFFLS QPNPATQANT DDLQIYANSL QSLAANLGGG
2410 2420 2430 2440 2450
FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ
2460 2470 2480 2490 2500
ATNTDKKIML PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL
2510 2520 2530 2540 2550
QPHPQQHQQQ QQTQVQQPIT VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ
2560 2570 2580 2590 2600
PQNIISFVTG DGSQGQPLQY ISIPTAGEYK PQPQPTATPT FLTTAPGAGA
2610 2620 2630 2640 2650
TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL IQPQTIQLGG
2660 2670 2680 2690 2700
GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV
2710 2720 2730 2740 2750
QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV
2760 2770 2780 2790 2800
LNNTGDASSA GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS
2810 2820 2830 2840 2850
TSMDYTSPVM VTAKIPPVTQ IKRTNAQAKA AGISGVGKVP PQPQVVNKVL
2860 2870 2880 2890 2900
PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG TGTTCGAPPS IASKPLQKKT
2910 2920 2930 2940 2950
NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL QQQIPAVVVN
2960 2970 2980 2990 3000
QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII
3010 3020 3030 3040 3050
TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN
3060 3070 3080 3090 3100
PMQQQAPSTT SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE
3110 3120 3130 3140 3150
QPIIHQMTSA SVSKCYAQKS TLPSPVYEAE LKVSSVLESI VPDVTMDAIL
3160 3170 3180 3190 3200
EEQPVTESIY TEGLYEKNSP GESKTEQLLL QQQQREQLNQ QLVNNGYLLD
3210 3220 3230 3240 3250
KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMATSACND HEMSDSEEPA
3260 3270 3280 3290 3300
VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS
3310 3320 3330 3340 3350
APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE
3360 3370 3380 3390 3400
QRTVSQEQEQ SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT
3410 3420 3430 3440 3450
YKSSSITEIW EKVFEAVQVA RRAHGLTPLP EGPLADMGGI QMIGLKTNAL
3460 3470 3480 3490 3500
KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA ANGAHGGNLG GSSASAALSV
3510 3520 3530 3540 3550
SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF SWLASRHRKQ
3560 3570 3580 3590 3600
PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR
3610 3620 3630 3640 3650
GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL
3660 3670 3680 3690 3700
VVDATMRGNA ARFINHCCEP NCYSKVVDIL GHKHIIIFAL RRIVQGEELT
3710 3720
YDYKFPFEDE KIPCSCGSKR CRKYLN
Length:3,726
Mass (Da):400,098
Last modified:March 2, 2010 - v4
Checksum:iE3DDB8F062BD7796
GO
Isoform B (identifier: P20659-2) [UniParc]FASTAAdd to Basket

Also known as: C, E

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

Show »
Length:3,358
Mass (Da):364,664
Checksum:i1382F25255A47E5B
GO

Sequence cautioni

The sequence AAK93328.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 24911GTTSEATTSGL → LEQLVKQQPLV in AAA29025. (PubMed:2107543)CuratedAdd
BLAST
Sequence conflicti239 – 24911GTTSEATTSGL → LEQLVKQQPLV in CAA90513. (PubMed:7924996)CuratedAdd
BLAST
Sequence conflicti239 – 24911GTTSEATTSGL → LEQLVKQQPLV in CAA83516. (PubMed:8555104)CuratedAdd
BLAST
Sequence conflicti303 – 3031N → K in AAA29025. (PubMed:2107543)Curated
Sequence conflicti303 – 3031N → K in CAA90513. (PubMed:7924996)Curated
Sequence conflicti303 – 3031N → K in CAA83516. (PubMed:8555104)Curated
Sequence conflicti337 – 3371A → L in AAA29025. (PubMed:2107543)Curated
Sequence conflicti337 – 3371A → L in CAA90513. (PubMed:7924996)Curated
Sequence conflicti337 – 3371A → L in CAA83516. (PubMed:8555104)Curated
Sequence conflicti521 – 5211G → R in AAA29025. (PubMed:2107543)Curated
Sequence conflicti521 – 5211G → R in CAA90513. (PubMed:7924996)Curated
Sequence conflicti521 – 5211G → R in CAA90514. (PubMed:7924996)Curated
Sequence conflicti521 – 5211G → R in CAA83515. (PubMed:8555104)Curated
Sequence conflicti521 – 5211G → R in CAA83516. (PubMed:8555104)Curated
Sequence conflicti578 – 5781E → Q in AAA29025. (PubMed:2107543)Curated
Sequence conflicti578 – 5781E → Q in CAA90513. (PubMed:7924996)Curated
Sequence conflicti578 – 5781E → Q in CAA90514. (PubMed:7924996)Curated
Sequence conflicti578 – 5781E → Q in CAA83515. (PubMed:8555104)Curated
Sequence conflicti578 – 5781E → Q in CAA83516. (PubMed:8555104)Curated
Sequence conflicti587 – 5871V → A in AAA29025. (PubMed:2107543)Curated
Sequence conflicti587 – 5871V → A in CAA90513. (PubMed:7924996)Curated
Sequence conflicti587 – 5871V → A in CAA90514. (PubMed:7924996)Curated
Sequence conflicti587 – 5871V → A in CAA83515. (PubMed:8555104)Curated
Sequence conflicti587 – 5871V → A in CAA83516. (PubMed:8555104)Curated
Sequence conflicti700 – 7001N → I in AAA29025. (PubMed:2107543)Curated
Sequence conflicti700 – 7001N → I in CAA90513. (PubMed:7924996)Curated
Sequence conflicti700 – 7001N → I in CAA90514. (PubMed:7924996)Curated
Sequence conflicti700 – 7001N → I in CAA83515. (PubMed:8555104)Curated
Sequence conflicti700 – 7001N → I in CAA83516. (PubMed:8555104)Curated
Sequence conflicti720 – 7201T → A in AAA29025. (PubMed:2107543)Curated
Sequence conflicti720 – 7201T → A in CAA90513. (PubMed:7924996)Curated
Sequence conflicti720 – 7201T → A in CAA90514. (PubMed:7924996)Curated
Sequence conflicti720 – 7201T → A in CAA83515. (PubMed:8555104)Curated
Sequence conflicti720 – 7201T → A in CAA83516. (PubMed:8555104)Curated
Sequence conflicti1073 – 10731K → P in AAA29025. (PubMed:2107543)Curated
Sequence conflicti1073 – 10731K → P in CAA90513. (PubMed:7924996)Curated
Sequence conflicti1073 – 10731K → P in CAA90514. (PubMed:7924996)Curated
Sequence conflicti1073 – 10731K → P in CAA83515. (PubMed:8555104)Curated
Sequence conflicti1073 – 10731K → P in CAA83516. (PubMed:8555104)Curated
Sequence conflicti1529 – 15302KL → NV in AAA29025. (PubMed:2107543)Curated
Sequence conflicti1529 – 15302KL → NV in CAA90513. (PubMed:7924996)Curated
Sequence conflicti1529 – 15302KL → NV in CAA90514. (PubMed:7924996)Curated
Sequence conflicti1529 – 15302KL → NV in CAA83515. (PubMed:8555104)Curated
Sequence conflicti1529 – 15302KL → NV in CAA83516. (PubMed:8555104)Curated
Sequence conflicti1594 – 15941S → P in AAA29025. (PubMed:2107543)Curated
Sequence conflicti1594 – 15941S → P in CAA90513. (PubMed:7924996)Curated
Sequence conflicti1594 – 15941S → P in CAA90514. (PubMed:7924996)Curated
Sequence conflicti1594 – 15941S → P in CAA83515. (PubMed:8555104)Curated
Sequence conflicti1594 – 15941S → P in CAA83516. (PubMed:8555104)Curated
Sequence conflicti1627 – 16271A → E in AAA29025. (PubMed:2107543)Curated
Sequence conflicti1627 – 16271A → E in CAA90513. (PubMed:7924996)Curated
Sequence conflicti1627 – 16271A → E in CAA90514. (PubMed:7924996)Curated
Sequence conflicti1627 – 16271A → E in CAA83515. (PubMed:8555104)Curated
Sequence conflicti1627 – 16271A → E in CAA83516. (PubMed:8555104)Curated
Sequence conflicti1690 – 16901T → A in AAA29025. (PubMed:2107543)Curated
Sequence conflicti1690 – 16901T → A in CAA90513. (PubMed:7924996)Curated
Sequence conflicti1690 – 16901T → A in CAA90514. (PubMed:7924996)Curated
Sequence conflicti1690 – 16901T → A in CAA83515. (PubMed:8555104)Curated
Sequence conflicti1690 – 16901T → A in CAA83516. (PubMed:8555104)Curated
Sequence conflicti2010 – 20101E → Q in AAA29025. (PubMed:2107543)Curated
Sequence conflicti2010 – 20101E → Q in CAA90513. (PubMed:7924996)Curated
Sequence conflicti2010 – 20101E → Q in CAA90514. (PubMed:7924996)Curated
Sequence conflicti2010 – 20101E → Q in CAA83515. (PubMed:8555104)Curated
Sequence conflicti2010 – 20101E → Q in CAA83516. (PubMed:8555104)Curated
Sequence conflicti2025 – 20251P → PWLTSPLKFLGLSTHGGLLL WLLLGVVVRLKQGG in AAA29025. (PubMed:2107543)Curated
Sequence conflicti2341 – 23411S → R in CAA90513. (PubMed:7924996)Curated
Sequence conflicti2341 – 23411S → R in CAA90514. (PubMed:7924996)Curated
Sequence conflicti2341 – 23411S → R in CAA83515. (PubMed:8555104)Curated
Sequence conflicti2341 – 23411S → R in CAA83516. (PubMed:8555104)Curated
Sequence conflicti2365 – 23651S → N in AAA29025. (PubMed:2107543)Curated
Sequence conflicti2365 – 23651S → N in CAA90513. (PubMed:7924996)Curated
Sequence conflicti2365 – 23651S → N in CAA90514. (PubMed:7924996)Curated
Sequence conflicti2365 – 23651S → N in CAA83515. (PubMed:8555104)Curated
Sequence conflicti2365 – 23651S → N in CAA83516. (PubMed:8555104)Curated
Sequence conflicti2392 – 23921S → G in CAA90513. (PubMed:7924996)Curated
Sequence conflicti2392 – 23921S → G in CAA90514. (PubMed:7924996)Curated
Sequence conflicti2392 – 23921S → G in CAA83515. (PubMed:8555104)Curated
Sequence conflicti2392 – 23921S → G in CAA83516. (PubMed:8555104)Curated
Sequence conflicti3157 – 31571E → Q in AAA29025. (PubMed:2107543)Curated
Sequence conflicti3157 – 31571E → Q in CAA90513. (PubMed:7924996)Curated
Sequence conflicti3157 – 31571E → Q in CAA90514. (PubMed:7924996)Curated
Sequence conflicti3157 – 31571E → Q in CAA83515. (PubMed:8555104)Curated
Sequence conflicti3157 – 31571E → Q in CAA83516. (PubMed:8555104)Curated
Sequence conflicti3234 – 32341A → R in AAA29025. (PubMed:2107543)Curated
Sequence conflicti3234 – 32341A → R in CAA90513. (PubMed:7924996)Curated
Sequence conflicti3234 – 32341A → R in CAA90514. (PubMed:7924996)Curated
Sequence conflicti3234 – 32341A → R in CAA83515. (PubMed:8555104)Curated
Sequence conflicti3234 – 32341A → R in CAA83516. (PubMed:8555104)Curated
Sequence conflicti3690 – 36901L → V in AAA29025. (PubMed:2107543)Curated
Sequence conflicti3690 – 36901L → V in CAA90513. (PubMed:7924996)Curated
Sequence conflicti3690 – 36901L → V in CAA90514. (PubMed:7924996)Curated
Sequence conflicti3690 – 36901L → V in CAA83515. (PubMed:8555104)Curated
Sequence conflicti3690 – 36901L → V in CAA83516. (PubMed:8555104)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 368368Missing in isoform B. CuratedVSP_006665Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA35085.
RefSeqiNP_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]
UniGeneiDm.6437.

Genome annotation databases

EnsemblMetazoaiFBtr0082947; FBpp0082406; FBgn0003862. [P20659-1]
FBtr0082950; FBpp0082409; FBgn0003862. [P20659-1]
GeneIDi41737.
KEGGidme:Dmel_CG8651.
UCSCiCG8651-RC. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi A35085.
RefSeqi NP_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 ]
UniGenei Dm.6437.

3D structure databases

ProteinModelPortali P20659.
SMRi P20659. Positions 1267-1297, 1344-1396, 1420-1523, 1737-1842, 3566-3726.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66813. 37 interactions.
IntActi P20659. 6 interactions.
MINTi MINT-907260.

Proteomic databases

PaxDbi P20659.
PRIDEi P20659.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082947 ; FBpp0082406 ; FBgn0003862 . [P20659-1 ]
FBtr0082950 ; FBpp0082409 ; FBgn0003862 . [P20659-1 ]
GeneIDi 41737.
KEGGi dme:Dmel_CG8651.
UCSCi CG8651-RC. d. melanogaster.

Organism-specific databases

CTDi 41737.
FlyBasei FBgn0003862. trx.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000119228.
InParanoidi P20659.
KOi K09186.
OMAi ARCEPYS.
OrthoDBi EOG75XGJZ.
PhylomeDBi P20659.

Enzyme and pathway databases

SignaLinki P20659.

Miscellaneous databases

GenomeRNAii 41737.
NextBioi 825306.
PROi P20659.

Gene expression databases

Bgeei P20659.

Family and domain databases

Gene3Di 3.30.40.10. 3 hits.
InterProi IPR003889. 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 ]
Pfami PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTi 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 ]
SUPFAMi SSF57903. SSF57903. 2 hits.
PROSITEi PS51543. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. 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.

Entry informationi

Entry nameiTRX_DROME
AccessioniPrimary (citable) accession number: P20659
Secondary accession number(s): A4V2V9
, A4V2W0, Q27255, Q27327, Q8INF9, Q960R2, Q9VFL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 2, 2010
Last modified: November 26, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3