SPT5H_DROME
ID SPT5H_DROME Reviewed; 1078 AA.
AC Q9V460; Q8IGQ1; Q8T0P5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
DE AltName: Full=dSpt5;
GN Name=Spt5; ORFNames=CG7626;
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 [MRNA] (ISOFORM A), AND SUBCELLULAR LOCATION.
RX PubMed=11040216; DOI=10.1101/gad.831900;
RA Kaplan C.D., Morris J.R., Wu C.-T., Winston F.;
RT "Spt5 and spt6 are associated with active transcription and have
RT characteristics of general elongation factors in D. melanogaster.";
RL Genes Dev. 14:2623-2634(2000).
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] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 408-1078 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11040217; DOI=10.1101/gad.844200;
RA Andrulis E.D., Guzman E., Doering P., Werner J., Lis J.T.;
RT "High-resolution localization of Drosophila Spt5 and Spt6 at heat shock
RT genes in vivo: roles in promoter proximal pausing and transcription
RT elongation.";
RL Genes Dev. 14:2635-2649(2000).
RN [7]
RP INTERACTION WITH THE EXOSOME COMPLEX.
RX PubMed=12490954; DOI=10.1038/nature01181;
RA Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P.,
RA Lis J.T.;
RT "The RNA processing exosome is linked to elongating RNA polymerase II in
RT Drosophila.";
RL Nature 420:837-841(2002).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12782658; DOI=10.1101/gad.1091403;
RA Wu C.-H., Yamaguchi Y., Benjamin L.R., Horvat-Gordon M., Washinsky J.,
RA Enerly E., Larsson J., Lambertsson A., Handa H., Gilmour D.;
RT "NELF and DSIF cause promoter proximal pausing on the hsp70 promoter in
RT Drosophila.";
RL Genes Dev. 17:1402-1414(2003).
RN [9]
RP INTERACTION WITH SPT6; RNA POLYMERASE II AND THE FACT COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12934007; DOI=10.1126/science.1085712;
RA Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S., Reinberg D.,
RA Lis J.T.;
RT "Tracking FACT and the RNA polymerase II elongation complex through
RT chromatin in vivo.";
RL Science 301:1094-1096(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLY-994.
RX PubMed=15380072; DOI=10.1016/j.cub.2004.08.066;
RA Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H.,
RA Ish-Horowicz D.;
RT "Locus-specific requirements for Spt5 in transcriptional activation and
RT repression in Drosophila.";
RL Curr. Biol. 14:1680-1684(2004).
RN [11]
RP INTERACTION WITH SPT4 AND RNA POLYMERASE II.
RX PubMed=15056674; DOI=10.1074/jbc.m402956200;
RA Zhang Z., Wu C.-H., Gilmour D.S.;
RT "Analysis of polymerase II elongation complexes by native gel
RT electrophoresis. Evidence for a novel carboxyl-terminal domain-mediated
RT termination mechanism.";
RL J. Biol. Chem. 279:23223-23228(2004).
RN [12]
RP INTERACTION WITH TRX, AND SUBCELLULAR LOCATION.
RX PubMed=14730313; DOI=10.1038/ncb1088;
RA Smith S.T., Petruk S., Sedkov Y., Cho E., Tillib S., Canaani E., Mazo A.;
RT "Modulation of heat shock gene expression by the TAC1 chromatin-modifying
RT complex.";
RL Nat. Cell Biol. 6:162-167(2004).
RN [13]
RP FUNCTION.
RX PubMed=15741180; DOI=10.1093/nar/gki274;
RA Wu C.-H., Lee C., Fan R., Smith M.J., Yamaguchi Y., Handa H., Gilmour D.S.;
RT "Molecular characterization of Drosophila NELF.";
RL Nucleic Acids Res. 33:1269-1279(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-76; SER-90; THR-162;
RP THR-808; THR-815; THR-847; THR-855; THR-867 AND THR-868, AND IDENTIFICATION
RP BY MASS 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: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates transcription elongation by RNA
CC polymerase II. DSIF enhances transcriptional pausing at sites proximal
CC to the promoter, which may facilitate the assembly of an elongation
CC competent RNA polymerase II complex. DSIF may also promote
CC transcriptional elongation within coding regions. DSIF is required for
CC the transcriptional induction of heat shock response genes and
CC regulation of genes which control anterior-posterior patterning during
CC embryonic development. {ECO:0000269|PubMed:12782658,
CC ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:15741180}.
CC -!- SUBUNIT: Interacts with Spt6. Interacts with Spt4 to form DSIF. DSIF
CC interacts with trx, RNA polymerase II and with the FACT complex, which
CC is composed of dre4/Spt16 and Ssrp/Ssrp1. DSIF can also interact with
CC the exosome, a complex with 3'-5' exoribonuclease activity which is
CC composed of at least Csl4, Dis3, Mtr3, Rrp4, Rrp6, Rrp40, Rrp42, Rrp46
CC and Ski6. DSIF may also interact with the positive transcription
CC elongation factor b complex (P-TEFb complex), which is composed of Cdk9
CC and cyclin-T (CycT). {ECO:0000269|PubMed:12490954,
CC ECO:0000269|PubMed:12934007, ECO:0000269|PubMed:14730313,
CC ECO:0000269|PubMed:15056674}.
CC -!- INTERACTION:
CC Q9V460; Q9TVQ5: spt4; NbExp=2; IntAct=EBI-134850, EBI-165626;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes predominantly
CC to transcriptionally active regions of polytene chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9V460-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V460-2; Sequence=VSP_016285;
CC -!- PTM: Phosphorylated. Phosphorylation by P-TEFb alleviates
CC transcriptional pausing (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39285.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL39285.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF222864; AAF34689.1; -; mRNA.
DR EMBL; AE013599; AAF57561.1; -; Genomic_DNA.
DR EMBL; AY069140; AAL39285.1; ALT_SEQ; mRNA.
DR EMBL; BT001668; AAN71423.1; -; mRNA.
DR EMBL; BT023840; AAZ86761.1; -; mRNA.
DR RefSeq; NP_652610.1; NM_144353.4. [Q9V460-1]
DR AlphaFoldDB; Q9V460; -.
DR SMR; Q9V460; -.
DR BioGRID; 72729; 22.
DR DIP; DIP-59538N; -.
DR IntAct; Q9V460; 7.
DR STRING; 7227.FBpp0085716; -.
DR iPTMnet; Q9V460; -.
DR PaxDb; Q9V460; -.
DR PRIDE; Q9V460; -.
DR DNASU; 53442; -.
DR EnsemblMetazoa; FBtr0086531; FBpp0085716; FBgn0040273. [Q9V460-1]
DR GeneID; 53442; -.
DR KEGG; dme:Dmel_CG7626; -.
DR UCSC; CG7626-RA; d. melanogaster. [Q9V460-1]
DR CTD; 53442; -.
DR FlyBase; FBgn0040273; Spt5.
DR VEuPathDB; VectorBase:FBgn0040273; -.
DR eggNOG; KOG1999; Eukaryota.
DR GeneTree; ENSGT00440000037640; -.
DR HOGENOM; CLU_003537_0_0_1; -.
DR InParanoid; Q9V460; -.
DR OMA; VGYMNTP; -.
DR PhylomeDB; Q9V460; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-72086; mRNA Capping.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR BioGRID-ORCS; 53442; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 53442; -.
DR PRO; PR:Q9V460; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0040273; Expressed in oviduct (Drosophila) and 23 other tissues.
DR Genevisible; Q9V460; DM.
DR GO; GO:0032044; C:DSIF complex; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0007549; P:dosage compensation; IMP:FlyBase.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1078
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208473"
FT DOMAIN 309..336
FT /note="KOW 1"
FT DOMAIN 460..487
FT /note="KOW 2"
FT DOMAIN 513..545
FT /note="KOW 3"
FT DOMAIN 635..668
FT /note="KOW 4"
FT DOMAIN 740..773
FT /note="KOW 5"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..307
FT /note="Interaction with Spt4"
FT /evidence="ECO:0000250"
FT REGION 350..461
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 815
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT MOD_RES 825
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT MOD_RES 847
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 855
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 868
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 488..603
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_016285"
FT MUTAGEN 994
FT /note="G->D: In allele WO49; impedes segmental patterning
FT of the embryo and the heat shock response."
FT /evidence="ECO:0000269|PubMed:15380072"
SQ SEQUENCE 1078 AA; 119445 MW; 0B917AEE0C0ADD13 CRC64;
MSDSEVSNMS DSGSEDGSIS NKSQRSARSK SRSRSRSGSR GSRSVSRSRS RSQSGHSRSG
SESPQRRDNR GKSDESGEEE EEPPGEDIDS EEYDEEENDD HPRKKKKKER FGGFIIDEAE
VDDEVDEDDE WEEGANEIGI VGNEIDELGP TARDIEIRRR GTNLWDTQKE DEIEEYLRKK
YADESIAKRH FGDGGEEMSD EITQQTLLPG IKDPNLWMVK CRIGEEKATA LLLMRKYLTY
LNTDDPLQIK SIIAPEGVKG YIYLEAYKQT HVKTCIDNVG NLRMGKWKQE MVPIKEMTDV
LKVVKEQVGL KVKQWVRLKR GLYKDDIAQV DYVDLAQNQV HLKLLPRIDY TRMRGALRTT
ATESDDSKRK KKRRPAAKPF DPEAVRAIGG EVHSDGDFLL FEGNRYSRKG FLYKNFTMSA
ILSDGVKPTL AELERFEESP EEVNLEIMGT VKDDPTMAHS FSMGDNVEVC VGDLENLQAK
IVAIDGTMIT VMPKHQDLKD PLIFKASELR KYFKTGDHAR VLAGRYEGET GLIIRVEPTR
VVLVSDLTNH ELEVLPRDLQ LCSDVATGVD CLGQFQWGDM VQLDSQNVGV IVRLERENFH
VLGMNGKCIE CKPTALHKRK ENRHTVALDA DQNQIRRRDV VKVMEGPHAG RSGEIKHLYR
SLAFLHCRMY TENGGIFVCK TRHLQLAGGS KTTVSNAGIV GGLGFMSPRI QSPMHPSGGR
GARGGARGGR GGFRVTRDRE ILGKTIKISG GPYKGAVGIV KDATESTARV ELHTSCQTIS
VDRNHIAIVG VTGKEGSVST YGRTPARTPG YGAQTPSYTA AGSKTPLVGS QTPNWDTDTR
TPYGTMTPSH DGSMTPRHGA WDPTANTTPA RNNDFDYSLE EPSPSPGYNP STPGYQMTSQ
FAPQTPGTLY GSDRSYSPFN PSPSPAPSPY PVGYMNTPSP STYSPNTPGG IPQSPYNPQT
PGASLDSSMG DWCTTDIEVR IHTHDDTDLV GQTGIIRTVS NGVCSVFLRQ EDRSVSIVSE
HLAPVLPCNG DEFKIIYGDD RESVGRVLSK DGDVFVCRIN EEIKLLPINF LCKMKSID
