BRM_DROME
ID BRM_DROME Reviewed; 1638 AA.
AC P25439; A4V1Z7; A4V1Z8; Q9VUW5; Q9VUW6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=ATP-dependent helicase brm;
DE EC=3.6.4.12;
DE AltName: Full=Homeotic gene regulator;
DE AltName: Full=Protein brahma;
GN Name=brm; ORFNames=CG5942;
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), FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1346755; DOI=10.1016/0092-8674(92)90191-e;
RA Tamkun J.W., Deuring R., Scott M.P., Kissinger M., Pattatucci A.M.,
RA Kaufman T.C., Kennison J.A.;
RT "Brahma: a regulator of Drosophila homeotic genes structurally related to
RT the yeast transcriptional activator SNF2/SWI2.";
RL Cell 68:561-572(1992).
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, AND ALTERNATIVE SPLICING.
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 A).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION IN A BRAHMA COMPLEX WITH OSA AND SNR1.
RX PubMed=10601025; DOI=10.1093/emboj/18.24.7029;
RA Collins R.T., Furukawa T., Tanese N., Treisman J.E.;
RT "Osa associates with the Brahma chromatin remodeling complex and promotes
RT the activation of some target genes.";
RL EMBO J. 18:7029-7040(1999).
RN [7]
RP FUNCTION AS COACTIVATOR, AND IDENTIFICATION IN A BRAHMA COMPLEX WITH OSA;
RP MOR; SNR1; DALAO; BAP55; BAP60 AND ACT42A.
RX PubMed=10809665;
RA Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.;
RT "The Drosophila brahma complex is an essential coactivator for the
RT trithorax group protein zeste.";
RL Genes Dev. 14:1058-1071(2000).
RN [8]
RP INTERACTION WITH ASF1.
RX PubMed=12381660; DOI=10.1101/gad.231202;
RA Moshkin Y.M., Armstrong J.A., Maeda R.K., Tamkun J.W., Verrijzer P.,
RA Kennison J.A., Karch F.;
RT "Histone chaperone ASF1 cooperates with the Brahma chromatin-remodelling
RT machinery.";
RL Genes Dev. 16:2621-2626(2002).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE BRM-HDAC3-ERM COMPLEX, INTERACTION WITH ERM
RP AND HDAC3, AND DISRUPTION PHENOTYPE.
RX PubMed=24618901; DOI=10.7554/elife.01906;
RA Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K., Aw S.S.,
RA Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C., Wang H.;
RT "The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in
RT Drosophila type II neuroblast lineages.";
RL Elife 3:E01906-E01906(2014).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-698; SER-1407;
RP SER-1411; SER-1591 AND SER-1594, AND IDENTIFICATION 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: Transcriptional regulator (PubMed:1346755). Acts as a
CC coactivator, assisting one or more dedicated transcriptional activators
CC of ANTC and BXC homeotic gene clusters (PubMed:1346755). Can counteract
CC the repressive effect of Polycomb protein (PubMed:1346755). ATPase
CC subunit of the Brahma complex, a multiprotein complex which is the
CC equivalent of the yeast SWI/SNF complex and acts by remodeling the
CC chromatin by catalyzing an ATP-dependent alteration in the structure of
CC nucleosomal DNA (PubMed:1346755). This complex can both serve as a
CC transcriptional coactivator or corepressor, depending on the context
CC (PubMed:10809665). In type II neuroblast lineage, as part of the Brm
CC remodeling complex, suppresses the formation of ectopic neuroblasts
CC probably through interaction with erm and HDAC3 (PubMed:24618901).
CC {ECO:0000269|PubMed:10809665, ECO:0000269|PubMed:1346755,
CC ECO:0000269|PubMed:24618901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the Brahma complex, which is composed of brm,
CC osa, mor, Snr1/Bap45, dalao/Bap111, Bap55, Bap60 and Act42A/Bap47
CC (PubMed:10601025, PubMed:10809665). Interacts with asf1
CC (PubMed:12381660). Associates with the brm-HDAC3-erm repressor complex,
CC composed of brm, HDAC3 and erm (PubMed:24618901). Interacts with erm
CC and HDAC3 (PubMed:24618901). {ECO:0000269|PubMed:10601025,
CC ECO:0000269|PubMed:10809665, ECO:0000269|PubMed:12381660,
CC ECO:0000269|PubMed:24618901}.
CC -!- INTERACTION:
CC P25439; Q7KPY3: mor; NbExp=3; IntAct=EBI-868480, EBI-1182199;
CC P25439; Q8IN94: osa; NbExp=4; IntAct=EBI-868480, EBI-115993;
CC P25439; Q24090: Snr1; NbExp=4; IntAct=EBI-868480, EBI-151570;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B;
CC IsoId=P25439-1; Sequence=Displayed;
CC Name=C; Synonyms=D;
CC IsoId=P25439-2; Sequence=VSP_000555;
CC -!- DEVELOPMENTAL STAGE: Highest expression in unfertilized eggs and early
CC embryos. {ECO:0000269|PubMed:1346755}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in larval brains results
CC in the formation of ectopic neuroblasts in type II neuroblast lineage.
CC Simultaneous RNAi-mediated knockdown of HDAC3 or erm in type II
CC neuroblasts results in a more severe phenotype of ectopic neuroblasts.
CC {ECO:0000269|PubMed:24618901}.
CC -!- MISCELLANEOUS: 'Brahma' means 'fate' in India.
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DR EMBL; M85049; AAA19661.1; -; mRNA.
DR EMBL; AE014296; AAF49557.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49558.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11773.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11774.1; -; Genomic_DNA.
DR EMBL; AY095048; AAM11376.1; -; mRNA.
DR EMBL; BT009972; AAQ22441.1; -; mRNA.
DR PIR; A42091; A42091.
DR RefSeq; NP_536745.4; NM_080497.5. [P25439-2]
DR RefSeq; NP_536746.1; NM_080498.3. [P25439-1]
DR RefSeq; NP_730088.1; NM_168640.2. [P25439-2]
DR RefSeq; NP_730089.1; NM_168641.1. [P25439-1]
DR AlphaFoldDB; P25439; -.
DR SMR; P25439; -.
DR BioGRID; 65055; 112.
DR DIP; DIP-36728N; -.
DR IntAct; P25439; 17.
DR MINT; P25439; -.
DR STRING; 7227.FBpp0305757; -.
DR iPTMnet; P25439; -.
DR PaxDb; P25439; -.
DR PRIDE; P25439; -.
DR DNASU; 39744; -.
DR EnsemblMetazoa; FBtr0075523; FBpp0075278; FBgn0000212. [P25439-2]
DR EnsemblMetazoa; FBtr0075524; FBpp0075279; FBgn0000212. [P25439-2]
DR EnsemblMetazoa; FBtr0075525; FBpp0075280; FBgn0000212. [P25439-1]
DR EnsemblMetazoa; FBtr0075526; FBpp0075281; FBgn0000212. [P25439-1]
DR GeneID; 39744; -.
DR KEGG; dme:Dmel_CG5942; -.
DR CTD; 39744; -.
DR FlyBase; FBgn0000212; brm.
DR VEuPathDB; VectorBase:FBgn0000212; -.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000154821; -.
DR InParanoid; P25439; -.
DR OMA; YGPGHRY; -.
DR PhylomeDB; P25439; -.
DR Reactome; R-DME-1266695; Interleukin-7 signaling.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-3247509; Chromatin modifying enzymes.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; P25439; -.
DR BioGRID-ORCS; 39744; 0 hits in 3 CRISPR screens.
DR ChiTaRS; brm; fly.
DR GenomeRNAi; 39744; -.
DR PRO; PR:P25439; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000212; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P25439; baseline and differential.
DR Genevisible; P25439; DM.
DR GO; GO:0035060; C:brahma complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0043697; P:cell dedifferentiation; IGI:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0035172; P:hemocyte proliferation; TAS:FlyBase.
DR GO; GO:0043974; P:histone H3-K27 acetylation; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030088; SMARCA2.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF541; PTHR10799:SF541; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Bromodomain;
KW Chromatin regulator; Developmental protein; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1638
FT /note="ATP-dependent helicase brm"
FT /id="PRO_0000074310"
FT DOMAIN 173..208
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 501..573
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 785..950
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1102..1263
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1443..1513
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 900..903
FT /note="DEGH box"
FT COMPBIAS 1..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 798..805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1594
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 81..85
FT /note="IFSKG -> S (in isoform C)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_000555"
FT CONFLICT 687
FT /note="D -> Y (in Ref. 1; AAA19661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1638 AA; 185089 MW; A4494B29F4F2E42A CRC64;
MASPSPANSP MPPPQAPSPM APPSQSPAPS PHSPYPHQQP GPLQGPPPPG HPGAYGHPMQ
HGPPGQGPPG HHMPPHHQGM IFSKGPHMGM QMPPTGPNMS PYQTHGMPPN APTQPCIVSP
GGPPGGPPPP ERSSQENLHA LQRAIDSMEE KGLQEDPRYS QLLAMRATSK HQHLNGNQVN
LLRTQITAYR LLARNKPISM QMQQALQAAQ QQPPPGPPIG PPGAPGGPPP GSQHAGQPPV
PPQQQQQPPP SAGTPPQCST PPASNPYGPP VPGQKMQVAP PPPHMQQGQP LPPQPPQVGG
PPPIQQQQPP QQQQQQSQPP PPEPHQHQLP NGGKPLSMGP SGGQPLIPSS PMQPQVRGTL
PGMPPGSQVP QPGGGPQRQV PPAGMPMPKP NRITTVAKPV GLDPITLLQE RENRIAARIS
LRMQELQRLP ATMSEDLRLQ AAIELRALRV LNFQRQLRME FVQCTRRDTT LETALNIKLY
KRTKRQGLRE ARATEKLEKQ QKLEAERKRR QKHLEFLAAV LQHGKDLREF HRNNKAQLAR
MNKAVMNHHA NAEREQKKEQ ERIEKERMRR LMAEDEEGYR KLIDQKKDKR LAFLLSQTDE
YISNLTQMVK QHKDDQMKKK EEEGKRLIQF KKELLMSGEY IGIDEGSIVA DMRVHVVEQC
TGKKLTGDDA PMLKHLHRWL NMHPGWDWID DEEDSCGSND DHKPKVEEQP TATEDATDKA
QATGNDEDAK DLITKAKVED DEYRTEEQTY YSIAHTIHEK VVEQASIMVN GTLKEYQIKG
LEWLVSLYNN NLNGILADEM GLGKTIQTIS LVTYLMDRKK VMGPYLIIVP LSTLPNWVLE
FEKWAPAVGV VSYKGSPQGR RLLQNQMRAT KFNVLLTTYE YVIKDKAVLA KIQWKYMIID
EGHRMKNHHC KLTQVLNTHY IAPYRLLLTG TPLQNKLPEL WALLNFLLPS IFKSCSTFEQ
WFNAPFATTG EKVELNEEET ILIIRRLHKV LRPFLLRRLK KEVEHQLPDK VEYIIKCDMS
ALQRVLYKHM QSKGVLLTDG SEKGKHGKGG AKALMNTIVQ LRKLCNHPFM FQHIEEKYCD
HTGGHGVVSG PDLYRVSGKF ELLDRILPKL KATNHRVLLF CQMTQCMTII EDYLGWRQFG
YLRLDGTTKA EDRGELLRKF NAKGSDVFVF LLSTRAGGLG LNLQTADTVV IFDSDWNPHQ
DLQAQDRAHR IGQRNEVRVL RLMTVNSVEE RILAAARYKL NMDEKVIQAG MFDQKSTGSE
RQQFLQTILH QDDNEEEEEN EVPDDEMINM MIARSEEEIE IFKRMDAERK KEDEEIHPGR
ERLIDESELP DWLTKDDDEV ERFHYQYDED TILGRGSRQR KEVDYTDSLT EKEWLKAIDD
GAEFDEEEEE DDSKRKRRKR KNRKEESDDD SLILKRRRRQ NLDKRSKKQM HKIMSAVIKH
NQDGRTLSEP FMKLPSRQRL PDYYEIIKRP VDIKKILQRI EDCKYADLNE LEKDFMQLCQ
NAQIYNEEAS LIYLDSIALQ KVFVGARQRI TAAADAAAVA AGDNTGEAHG NGGSDNSDND
DDDGGDDGSD DEEIATTSAA AVKMKLKLNK SLASAPATPT QSSSNVSSGA ATTSKKQTRR
KRSQKKYTIS DDDDDDMD
