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P20659

- TRX_DROME

UniProt

P20659 - TRX_DROME

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
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (02 Mar 2010)
      Previous versions | rss
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    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 binding Source: IntAct
    5. protein homodimerization activity Source: UniProtKB
    6. protein phosphatase 1 binding Source: FlyBase
    7. sequence-specific DNA binding Source: InterPro
    8. sequence-specific DNA binding transcription factor activity Source: InterPro
    9. transcription regulatory region DNA binding Source: FlyBase
    10. zinc ion binding Source: InterPro

    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

    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

    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. 36 interactions.
    IntActiP20659. 6 interactions.
    MINTiMINT-907260.

    Structurei

    3D structure databases

    ProteinModelPortaliP20659.
    SMRiP20659. Positions 1267-1296, 1343-1403, 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.
    GeneTreeiENSGT00740000115089.
    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

    MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG     50
    SSAAREKGNN CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG 100
    SGSSGSGSTN GGSVNGGTHH KSAANLDKEA VTKDQNGDGD KTRGNVSSAP 150
    SGKLSAAASG KALSKSSRTF SASTSVTSSG RSSGSSPDGN SGASSDGASS 200
    GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSGT TSEATTSGLS 250
    GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK 300
    FKNLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPIASGS TPSVEGGIGV 350
    GGVVSPGEDA ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP 400
    PAMASSGDGS SPKSGADTGP STSSTTAKQK KTVTFRNVLE TSDDKSVVKR 450
    FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE CIVRPSILSK ILNKNSNIDK 500
    LNSLKFRSAG ASSSSSNQES GSSSNVFGLS RAFGAPMDED DEGGVTFRRN 550
    DSPEDQNNAE DDEMDDDDDD EEAEEDDENE DDNDEAVSEK SAETEKSAGA 600
    DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG 650
    DSKGKNVFGT SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGN 700
    FVLRQPRLQF QADNQQATFT APKACPTSPS AIPKPANSLA TSSFGSLAST 750
    NSSTVTPTPS ACSICSAVVS SKEVTQARKY GVVACDVCRK FFSKMTKKSI 800
    SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK KFYKDRCTAC 850
    WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF 900
    TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL 950
    RPAILENPLF LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE 1000
    KLLSPTQAGT KKSGAAEAQV EEVQPQKEEA PQTSTTTQPS ASNGASHGVP 1050
    QAELAGETNA TGDTLKRQRI DLKGPRVKHV CRSASIVLGQ PLATFGEDQQ 1100
    PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS CKTSPVGDES 1150
    KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA 1200
    SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV 1250
    CQTGFGLIVT ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN 1300
    LKHGSFEDTT LMGSLLETTV NASTGPSSSL NQLTQRLNWL CPRCTVCYTC 1350
    NMSSGSKVKC QKCQKNYHST CLGTSKRLLG ADRPLICVNC LKCKSCSTTK 1400
    VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM MECGDCGQWV 1450
    HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE 1500
    FKASLYSVLK LLSKSRQACA LLKLSPRKKL RCTCGASSNQ GKLQPKALQF 1550
    SSGSDNGLGS DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKSLPCSCQ 1600
    QHISHSQSFS LVDIKQKIAG NSYVSLAEFN YDMSQVIQQS NCDELDIAYK 1650
    ELLSEQFPWF QNETKACTDA LEEDMFESCS GGNYEDLQDT GGVSASVYNE 1700
    HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC RKSGEGLSGE 1750
    EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC 1800
    GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA 1850
    NGSPSVTYES NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI 1900
    VPRFSDSYEA VVPINFLCSR LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL 1950
    DVGRNYTVDH TNPNSKEVQL GMAQIARWHT SLARSEFLEN GGTDWSGEFP 2000
    NPNSCVPPDE NTEEEPQQQA DLLPPELKDA IFEDLPHELL DGISMLDIFL 2050
    YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN 2100
    TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR 2150
    RKLSKNLAEG VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG 2200
    SVRSKSFTWS AAKRYFEKSE GREEAAKMRI MQMDGVDDSI TEFRIISGDG 2250
    NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL PSCSPTMSSN ETESDVSGQG 2300
    MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ SLGSLGQFGL 2350
    QGLQQLQLQP QSLGSGFFLS QPNPATQANT DDLQIYANSL QSLAANLGGG 2400
    FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ 2450
    ATNTDKKIML PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL 2500
    QPHPQQHQQQ QQTQVQQPIT VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ 2550
    PQNIISFVTG DGSQGQPLQY ISIPTAGEYK PQPQPTATPT FLTTAPGAGA 2600
    TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL IQPQTIQLGG 2650
    GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV 2700
    QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV 2750
    LNNTGDASSA GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS 2800
    TSMDYTSPVM VTAKIPPVTQ IKRTNAQAKA AGISGVGKVP PQPQVVNKVL 2850
    PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG TGTTCGAPPS IASKPLQKKT 2900
    NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL QQQIPAVVVN 2950
    QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII 3000
    TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN 3050
    PMQQQAPSTT SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE 3100
    QPIIHQMTSA SVSKCYAQKS TLPSPVYEAE LKVSSVLESI VPDVTMDAIL 3150
    EEQPVTESIY TEGLYEKNSP GESKTEQLLL QQQQREQLNQ QLVNNGYLLD 3200
    KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMATSACND HEMSDSEEPA 3250
    VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS 3300
    APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE 3350
    QRTVSQEQEQ SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT 3400
    YKSSSITEIW EKVFEAVQVA RRAHGLTPLP EGPLADMGGI QMIGLKTNAL 3450
    KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA ANGAHGGNLG GSSASAALSV 3500
    SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF SWLASRHRKQ 3550
    PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR 3600
    GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL 3650
    VVDATMRGNA ARFINHCCEP NCYSKVVDIL GHKHIIIFAL RRIVQGEELT 3700
    YDYKFPFEDE KIPCSCGSKR CRKYLN 3726
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 1267-1296, 1343-1403, 1420-1523, 1737-1842, 3566-3726.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66813. 36 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 ENSGT00740000115089.
    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

    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: October 1, 2014
    This is version 161 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