ASH1_DROME
ID ASH1_DROME Reviewed; 2226 AA.
AC Q9VW15; A8WHI9; M9NFL0; Q24189; Q8MQX5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Histone-lysine N-methyltransferase ash1;
DE EC=2.1.1.354 {ECO:0000269|PubMed:13679578};
DE AltName: Full=Absent small and homeotic disks protein 1;
DE AltName: Full=Lysine N-methyltransferase 2H;
GN Name=ash1; Synonyms=KMT2H; ORFNames=CG8887;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-1284 AND ASN-1473.
RX PubMed=8725238; DOI=10.1093/genetics/143.2.913;
RA Tripoulas N., LaJeunesse D., Gildea J., Shearn A.;
RT "The Drosophila ash1 gene product, which is localized at specific sites on
RT polytene chromosomes, contains a SET domain and a PHD finger.";
RL Genetics 143:913-928(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1120.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7982557; DOI=10.1093/genetics/137.4.1027;
RA Tripoulas N.A., Hersperger E., La Jeunesse D., Shearn A.;
RT "Molecular genetic analysis of the Drosophila melanogaster gene absent,
RT small or homeotic discs1 (ash1).";
RL Genetics 137:1027-1038(1994).
RN [6]
RP SUBUNIT.
RX PubMed=9735357; DOI=10.1242/dev.125.20.3955;
RA Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M., Shearn A.,
RA Tamkun J.W.;
RT "The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of
RT distinct protein complexes.";
RL Development 125:3955-3966(1998).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TRX.
RX PubMed=10454589; DOI=10.1128/mcb.19.9.6441;
RA Rozovskaia T., Tillib S., Smith S., Sedkov Y., Rozenblatt-Rosen O.,
RA Petruk S., Yano T., Nakamura T., Ben-Simchon L., Gildea J., Croce C.M.,
RA Shearn A., Canaani E., Mazo A.;
RT "Trithorax and ASH1 interact directly and associate with the trithorax
RT group-responsive bxd region of the Ultrabithorax promoter.";
RL Mol. Cell. Biol. 19:6441-6447(1999).
RN [8]
RP INTERACTION WITH NEJ.
RX PubMed=11094082; DOI=10.1128/mcb.20.24.9317-9330.2000;
RA Bantignies F., Goodman R.H., Smolik S.M.;
RT "Functional interaction between the coactivator Drosophila CREB-binding
RT protein and ASH1, a member of the trithorax group of chromatin modifiers.";
RL Mol. Cell. Biol. 20:9317-9330(2000).
RN [9]
RP INTERACTION WITH TRX.
RX PubMed=10656681; DOI=10.1038/sj.onc.1203307;
RA Rozovskaia T., Rozenblatt-Rosen O., Sedkov Y., Burakov D., Yano T.,
RA Nakamura T., Petruck S., Ben-Simchon L., Croce C.M., Mazo A., Canaani E.;
RT "Self-association of the SET domains of human ALL-1 and of Drosophila
RT TRITHORAX and ASH1 proteins.";
RL Oncogene 19:351-357(2000).
RN [10]
RP RETRACTED PAPER.
RX PubMed=12397363; DOI=10.1038/nature01126;
RA Beisel C., Imhof A., Greene J., Kremmer E., Sauer F.;
RT "Histone methylation by the Drosophila epigenetic transcriptional regulator
RT Ash1.";
RL Nature 419:857-862(2002).
RN [11]
RP RETRACTION NOTICE OF PUBMED:12397363.
RX PubMed=25874679; DOI=10.1038/nature14421;
RA Beisel C., Imhof A., Greene J., Kremmer E., Sauer F.;
RL Nature 521:110-110(2015).
RN [12]
RP FUNCTION, SET DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=13679578; DOI=10.1073/pnas.1933593100;
RA Byrd K.N., Shearn A.;
RT "ASH1, a Drosophila trithorax group protein, is required for methylation of
RT lysine 4 residues on histone H3.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11535-11540(2003).
RN [13]
RP FUNCTION.
RX PubMed=15031712; DOI=10.1038/sj.embor.7400111;
RA Klymenko T., Mueller J.;
RT "The histone methyltransferases Trithorax and Ash1 prevent transcriptional
RT silencing by Polycomb group proteins.";
RL EMBO Rep. 5:373-377(2004).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16882982; DOI=10.1101/gad.388706;
RA Papp B., Mueller J.;
RT "Histone trimethylation and the maintenance of transcriptional ON and OFF
RT states by trxG and PcG proteins.";
RL Genes Dev. 20:2041-2054(2006).
RN [15]
RP RETRACTED PAPER.
RX PubMed=16497925; DOI=10.1126/science.1117705;
RA Sanchez-Elsner T., Gou D., Kremmer E., Sauer F.;
RT "Noncoding RNAs of trithorax response elements recruit Drosophila Ash1 to
RT Ultrabithorax.";
RL Science 311:1118-1123(2006).
RN [16]
RP RETRACTION NOTICE OF PUBMED:16497925.
RX PubMed=24876484; DOI=10.1126/science.344.6187.981-a;
RA McNutt M.;
RL Science 344:981-981(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-136; SER-138;
RP THR-200; THR-201; SER-740; SER-831 AND SER-977, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Trithorax group (TrxG) protein that has histone
CC methyltransferase activity (PubMed:13679578, PubMed:16882982).
CC Specifically trimethylates 'Lys-4' of histone H3 (H3K4me3), a specific
CC tag for epigenetic transcriptional activation (PubMed:13679578,
CC PubMed:16882982). TrxG proteins are generally required to maintain the
CC transcriptionally active state of homeotic genes throughout
CC development. Does not act as a coactivator required for transcriptional
CC activation, but specifically prevents inappropriate Polycomb Group
CC (PcG) silencing of homeotic genes in cells in which they must stay
CC transcriptionally active (PubMed:15031712).
CC {ECO:0000269|PubMed:13679578, ECO:0000269|PubMed:15031712,
CC ECO:0000269|PubMed:16882982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000269|PubMed:13679578};
CC -!- SUBUNIT: Component of a large multiprotein complex distinct from
CC complexes containing ash2 or brm (PubMed:9735357). Interacts (via SET
CC domain) with trx (via SET domain) (PubMed:10454589, PubMed:10656681).
CC Interacts with nej/cbp (PubMed:11094082). {ECO:0000269|PubMed:10454589,
CC ECO:0000269|PubMed:10656681, ECO:0000269|PubMed:11094082,
CC ECO:0000269|PubMed:9735357}.
CC -!- INTERACTION:
CC Q9VW15; Q9VW15: ash1; NbExp=3; IntAct=EBI-124480, EBI-124480;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000269|PubMed:10454589,
CC ECO:0000269|PubMed:8725238}. Note=Localizes at the promoter of active
CC genes. {ECO:0000269|PubMed:16882982}.
CC -!- TISSUE SPECIFICITY: Expressed throughout development but is present at
CC higher levels during the embryonic and pupal stages than during the
CC larval stages. During the larval stages it accumulates primarily in
CC imaginal disks. {ECO:0000269|PubMed:7982557}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. During
CC oogenesis it accumulates in the nurse cells of developing egg chambers.
CC {ECO:0000269|PubMed:7982557}.
CC -!- DOMAIN: The SET domain is sufficient for methyltransferase activity.
CC {ECO:0000269|PubMed:13679578}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: Was reported to trimethylate H3 'Lys-9' and H4 'Lys-20'
CC (PubMed:12397363). Was also reported to bind non-coding RNAs of
CC trithorax response element (TRE) (PubMed:16497925). However, both
CC papers were retracted because some data, results and conclusions are
CC not reliable. {ECO:0000305|PubMed:12397363,
CC ECO:0000305|PubMed:16497925}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01100.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM52758.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=ABX00757.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U49439; AAB01100.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014296; AAF49140.3; -; Genomic_DNA.
DR EMBL; AE014296; AFH04505.1; -; Genomic_DNA.
DR EMBL; AY122246; AAM52758.1; ALT_SEQ; mRNA.
DR EMBL; BT031135; ABX00757.1; ALT_FRAME; mRNA.
DR PIR; S71490; S71490.
DR RefSeq; NP_001246834.1; NM_001259905.1.
DR RefSeq; NP_524160.2; NM_079436.3.
DR AlphaFoldDB; Q9VW15; -.
DR SMR; Q9VW15; -.
DR BioGRID; 65403; 19.
DR DIP; DIP-23637N; -.
DR IntAct; Q9VW15; 2.
DR STRING; 7227.FBpp0297151; -.
DR iPTMnet; Q9VW15; -.
DR PaxDb; Q9VW15; -.
DR PRIDE; Q9VW15; -.
DR DNASU; 40133; -.
DR EnsemblMetazoa; FBtr0306009; FBpp0297151; FBgn0005386.
DR EnsemblMetazoa; FBtr0306010; FBpp0297152; FBgn0005386.
DR GeneID; 40133; -.
DR KEGG; dme:Dmel_CG8887; -.
DR CTD; 40133; -.
DR FlyBase; FBgn0005386; ash1.
DR VEuPathDB; VectorBase:FBgn0005386; -.
DR eggNOG; KOG1083; Eukaryota.
DR GeneTree; ENSGT00940000172679; -.
DR HOGENOM; CLU_229222_0_0_1; -.
DR InParanoid; Q9VW15; -.
DR OMA; HCYICEL; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q9VW15; -.
DR SignaLink; Q9VW15; -.
DR BioGRID-ORCS; 40133; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40133; -.
DR PRO; PR:Q9VW15; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0005386; Expressed in egg cell and 20 other tissues.
DR Genevisible; Q9VW15; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IPI:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:FlyBase.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:FlyBase.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:FlyBase.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IMP:FlyBase.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IMP:FlyBase.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; IMP:FlyBase.
DR GO; GO:0010452; P:histone H3-K36 methylation; IDA:FlyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR GO; GO:0016571; P:histone methylation; IDA:FlyBase.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0018991; P:oviposition; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR CDD; cd05525; Bromo_ASH1; 1.
DR CDD; cd15548; PHD_ASH1L; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR043320; Bromo_ASH1L.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR043319; PHD_ASH1L.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; Developmental protein;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2226
FT /note="Histone-lysine N-methyltransferase ash1"
FT /id="PRO_0000259518"
FT DOMAIN 1339..1387
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1390..1506
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1514..1530
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 1952..2072
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DNA_BIND 261..273
FT /note="A.T hook 1"
FT DNA_BIND 1065..1077
FT /note="A.T hook 2"
FT DNA_BIND 1095..1107
FT /note="A.T hook 3"
FT ZN_FING 1857..1903
FT /note="PHD-type"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2205..2226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2208..2226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 1284
FT /note="E->K: In ash1-21; induces lethality between prepupal
FT and late pupal stages."
FT /evidence="ECO:0000269|PubMed:8725238"
FT MUTAGEN 1473
FT /note="N->I: In ash1-10; induces lethality between prepupal
FT and late pupal stages."
FT /evidence="ECO:0000269|PubMed:8725238"
FT CONFLICT 163
FT /note="A -> G (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> G (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="P -> T (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="SS -> RR (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="A -> P (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001
FT /note="Q -> K (in Ref. 4; AAM52758)"
FT /evidence="ECO:0000305"
FT CONFLICT 1191
FT /note="L -> V (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="F -> L (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1993
FT /note="H -> Q (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2031
FT /note="R -> P (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2034
FT /note="V -> L (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2038
FT /note="T -> P (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2041
FT /note="C -> S (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2044
FT /note="R -> P (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2145
FT /note="R -> C (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2169
FT /note="L -> H (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
FT CONFLICT 2181
FT /note="I -> V (in Ref. 1; AAB01100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2226 AA; 246266 MW; 0ACBB0BF404848F2 CRC64;
MSCSQNETAA AKVLETQRAQ ESGSENEETD SITDQSSQSK SIKSATQFSV QRSDTDGLRM
RISAIRPTLG VVATKKPPKS RKMSTQDTES GCSEAKNRAV SKKVKVKRKK LASSSGISKS
DKVSKSKKSQ ISAFSSDSED DLPLKVHQQR APRVLLSAII QAAQSASKPT LDIGISSSDN
ELPNLVQAAI KRVESDTEDT TVEGSFRKAA KDKNLPQYQS TLLQDFMEKT QMLGQTVNAK
LAEEKVAKAK EETLVQTAVP RKRRGRPKKV VPTVPAPGNS GPAINESADS GVISTTSTTQ
STTPSPKMQN ENAVPTGSLP IASSSKPKID MAYLDKRMYA TERVLYPPPR SKRRQNNKKT
ACSSSNKEEL QLDPLWREID VNKKFRLRSM SVGAASGTGA STTICSKVLA AKSGYVSDYG
SVRHQRSSHN HNSGYKSDAS CKSRYSTKSC MSRRSRAKSC GYRSDCKESG KSGLRMRRKR
RASMLLKSSA DDTVEDQDIL QLAGLSLGQS SEESNEYISK PSLKSLPTTS ASKKYGEINR
YVTTGQYFGR GGSLSATNPD NFISKMMNQR KETPAPSKSS CKIKSRRSSA ASMCSSYVSG
VSRMRRRHRR KSFSHNKSLN IDSKLLTEIE IITSTFNSRC RIQDDRLTGS SGKEKLLADA
NKLQATLAAP SPAQQLTLNG GGPASTLSKP LKRGLKKRKL SEPLVDFAML SASASGTPNG
SGSSNGNTKR RHKKSQSNDS SSPDDHKLPL KKRHYLLTPG ERPPAEVAFA NGKLNAEAWA
AAAAAAKSTA STKSQAQFNA RSVKSALTPK KRHLLEQPTS VSGAGSSASN SPLRIVVDNN
SISGGKLLDI SPSSLCSLKQ QRRGGAAKQK VSAAKDLVQL QSPAGSYPPP GVFEPSVELE
IQIPLSKLNE SVITKAEVES PLLSALDIKE DTKKEVGQRV VETLLHKTGG NLLLKRKRKK
INRTGFPTVR RKKRKVSVEQ QTTAVIDEHE PEFDPDDEPL QSLRETRSSN NVNVQAAPNP
PLDCERVPQA GEARETFVAR TNQKAPRLSV VALERLQRPQ TPARGRPRGR KPKNREQAEA
APQPPPKSEP EIRPAKKRGR QPKQPVLEEP PPTPPPQQKK NKMEPNIRLP DGIDPNTNFS
CKIRLKRRKN LEAGTQPKKE KPVQPVTVEE IPPEIPVSQE EIDAEAEAKR LDSIPTEHDP
LPASESHNPG PQDYASCSES SEDKASTTSL RKLSKVKKTY LVAGLFSNHY KQSLMPPPAK
VNKKPGLEEQ VGPASLLPPP PYCEKYLRRT EMDFELPYDI WWAYTNSKLP TRNVVPSWNY
RKIRTNVYAE SVRPNLAGFD HPTCNCKNQG EKSCLDNCLN RMVYTECSPS NCPAGEKCRN
QKIQRHAVAP GVERFMTADK GWGVRTKLPI AKGTYILEYV GEVVTEKEFK QRMASIYLND
THHYCLHLDG GLVIDGQRMG SDCRFVNHSC EPNCEMQKWS VNGLSRMVLF AKRAIEEGEE
LTYDYNFSLF NPSEGQPCRC NTPQCRGVIG GKSQRVKPLP AVEAKPSGEG LSGRNGRQRK
QKAKKHAQRQ AGKDISSAVA VAKLQPLSEK EKKLVRQFNT FLVRNFEKIR RCKAKRASDA
AATASSPALG TTNGDIPGRR PSTPSSPSLA AQISALCSPR NIKTRGLTQA VHDPELEKMA
KMAVVLRDIC SAMETLKMSD LLTTVSSKKK KPIKTTLSGK LGSTAATSKV EFRSIQAQVE
QGHYKTPQEF DDHMQQLFVE AKQQHGDDEG KEKALQSLKD SYEQQKIASY VQLVEILGDS
ESLQSFKPKE VLSSEEEPGK IAVKKSPGAK ERDSPIVPLK VTPPPLLPIE ASPDEDVIRC
ICGLYKDEGL MIQCSKCMVW QHTECTKADI DADNYQCERC EPREVDREIP LEEFTEEGHR
YYLSLMRGDL QVRQGDAVYV LRDIPIKDES GKVLPTKKHT YETIGAIDYQ ECDIFRVEHL
WKNELGKRFI FGHHFLRPHE TFHEPSRRFY PNEVVRVSLY EVVPIELVIG RCWVLDRTTF
CKGRPMECND EDHCYICELR VDKTARFFSK AKANHPACTK SYAFRKFPEK IKISKSYAPH
DVDPSLLKTR KQKTELDVGA GPTTMHKVSG RQEQHQAKMV GRKPRGISAP ADATAVHVVT
PVAPNKQMLK KRKSRLENVL ITMKLKCLDA QTAQEQPIDL SYLLSGRGAR QRKTQQSSSS
STANST
