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Database: UniProt
Entry: M9MS40_DROME
LinkDB: M9MS40_DROME
Original site: M9MS40_DROME 
ID   M9MS40_DROME            Unreviewed;      3282 AA.
AC   M9MS40;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=nej {ECO:0000313|EMBL:ADV37657.1,
GN   ECO:0000313|FlyBase:FBgn0261617};
GN   Synonyms=anon-WO0147981.11 {ECO:0000313|EMBL:ADV37657.1},
GN   anon-WO03040301.89 {ECO:0000313|EMBL:ADV37657.1}, CBP
GN   {ECO:0000313|EMBL:ADV37657.1}, Cbp {ECO:0000313|EMBL:ADV37657.1}, cbp
GN   {ECO:0000313|EMBL:ADV37657.1}, CBP/p300 {ECO:0000313|EMBL:ADV37657.1},
GN   CBP_ {ECO:0000313|EMBL:ADV37657.1}, CG15321
GN   {ECO:0000313|EMBL:ADV37657.1}, Crbp {ECO:0000313|EMBL:ADV37657.1},
GN   dCBP {ECO:0000313|EMBL:ADV37657.1}, dKAT3
GN   {ECO:0000313|EMBL:ADV37657.1}, dmCBP {ECO:0000313|EMBL:ADV37657.1},
GN   Dmel\CG15319 {ECO:0000313|EMBL:ADV37657.1}, l(1)G0112
GN   {ECO:0000313|EMBL:ADV37657.1}, l(1)G0350
GN   {ECO:0000313|EMBL:ADV37657.1}, l(1)G0470
GN   {ECO:0000313|EMBL:ADV37657.1}, Nej {ECO:0000313|EMBL:ADV37657.1}, nej
GN   CBP {ECO:0000313|EMBL:ADV37657.1}, Nejire
GN   {ECO:0000313|EMBL:ADV37657.1}, P300 {ECO:0000313|EMBL:ADV37657.1},
GN   p300 {ECO:0000313|EMBL:ADV37657.1}, p300/CBP
GN   {ECO:0000313|EMBL:ADV37657.1};
GN   ORFNames=CG15319 {ECO:0000313|EMBL:ADV37657.1,
GN   ECO:0000313|FlyBase:FBgn0261617}, Dmel_CG15319
GN   {ECO:0000313|EMBL:ADV37657.1};
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 {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AE014298; ADV37657.1; -; Genomic_DNA.
DR   RefSeq; NP_001188575.1; NM_001201646.2.
DR   SMR; M9MS40; -.
DR   STRING; 7227.FBpp0291862; -.
DR   PaxDb; 7227-FBpp0291862; -.
DR   EnsemblMetazoa; FBtr0302722; FBpp0291862; FBgn0261617.
DR   GeneID; 43856; -.
DR   KEGG; dme:Dmel_CG15319; -.
DR   AGR; FB:FBgn0261617; -.
DR   CTD; 43856; -.
DR   FlyBase; FBgn0261617; nej.
DR   VEuPathDB; VectorBase:FBgn0261617; -.
DR   eggNOG; KOG1778; Eukaryota.
DR   GeneTree; ENSGT00940000166210; -.
DR   InParanoid; M9MS40; -.
DR   OMA; TPNQGMH; -.
DR   OrthoDB; 5490807at2759; -.
DR   PhylomeDB; M9MS40; -.
DR   Reactome; R-DME-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR   Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-DME-3214847; HATs acetylate histones.
DR   Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR   Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DME-6782135; Dual incision in TC-NER.
DR   Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR   Reactome; R-DME-6811555; PI5P Regulates TP53 Acetylation.
DR   Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   Reactome; R-DME-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR   Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-DME-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   Reactome; R-DME-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR   Reactome; R-DME-9701898; STAT3 nuclear events downstream of ALK signaling.
DR   Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-DME-9759194; Nuclear events mediated by NFE2L2.
DR   BioGRID-ORCS; 43856; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; nej; fly.
DR   GenomeRNAi; 43856; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0261617; Expressed in cleaving embryo and 21 other cell types or tissues.
DR   ExpressionAtlas; M9MS40; baseline and differential.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:FlyBase.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:1990226; F:histone methyltransferase binding; IPI:FlyBase.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR   GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:FlyBase.
DR   GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase.
DR   GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR   GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR   GO; GO:0045466; P:R7 cell differentiation; IMP:FlyBase.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR   GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR   CDD; cd05495; Bromo_cbp_like; 1.
DR   CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR   CDD; cd15557; PHD_CBP_p300; 1.
DR   CDD; cd15802; RING_CBP-p300; 1.
DR   CDD; cd02337; ZZ_CBP; 1.
DR   Gene3D; 2.10.110.40; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR   Gene3D; 1.20.1020.10; TAZ domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR031162; CBP_P300_HAT.
DR   InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR   InterPro; IPR003101; KIX_dom.
DR   InterPro; IPR036529; KIX_dom_sf.
DR   InterPro; IPR010303; RING_CBP-p300.
DR   InterPro; IPR038547; RING_CBP-p300_sf.
DR   InterPro; IPR035898; TAZ_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000197; Znf_TAZ.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR   PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF08214; HAT_KAT11; 1.
DR   Pfam; PF02172; KIX; 1.
DR   Pfam; PF06001; RING_CBP-p300; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57933; TAZ domain; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS50952; KIX; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ADV37657.1};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9MS40};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADV37657.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          514..600
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   DOMAIN          944..1023
FT                   /note="KIX"
FT                   /evidence="ECO:0000259|PROSITE:PS50952"
FT   DOMAIN          1721..1793
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1951..2334
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          2336..2384
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          2398..2479
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   ZN_FING         514..600
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT   ZN_FING         2398..2479
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT   REGION          33..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1636..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2211..2250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2686..2741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2861..2963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3005..3034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3096..3240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2176..2203
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        112..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1563..1580
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2220..2236
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2727..2741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2878..2948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3096..3145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3154..3173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3174..3196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3282 AA;  341431 MW;  3A5A472BB9EF3918 CRC64;
     MMADHLDEPP QKRVKMDPTD ISYFLEENLP DELVSSNSGW SDQLTGGAGG GNGGGGASGV
     TTNPTSGPNP GGGPNKPAAQ GPGSGTGGVG VGVNVGVGGV VGVGVVPSQM NGAGGGNGSG
     TGGDDGSGNG SGAGNRISQM QHQQLQHLLQ QQQQGQKGAM VVPGMQQLGS KSPNLQSPNQ
     GGMQQVVGTQ MGMVNSMPMS ISNNGNNGMN AIPGMNTIAQ GNLGNMVLTN SVGGGMGGMV
     NHLKQQPGGG GGGMINSVSV PGGPGAGAGG VGAGGGGAVA ANQGMHMQNG PMMGRMVGQQ
     HMLRGPHLMG ASGGAGGPGN GPGGGGPRMQ NPNMQMNFRP FAAQLNSLPY GVGQYGGPGG
     GNNPQQQQQQ QQQQLLAQQM AQRGGVVPGM PQGNRPVGTV VPMSTLGGDG SGPAGQLVSG
     NPQQQQMLAQ QQTGAMGPRP PQPNQLLGHP GQQQQQQQQP GTSQQQQQQQ GVGIGGAGVV
     ANAGTVAGVP AVAGGGAGGA VQSSGPGGAN RDVPDDRKRQ IQQQLMLLLH AHKCNRRENL
     NPNREVCNVN YCKAMKSVLA HMGTCKQSKD CTMQHCASSR QILLHYKTCQ NSGCVICYPF
     RQNHSVFQNA NVPPGGGPAG IGGAPPGGGG AGGGAAGAGG NLQQQQQQQQ QQQQNQQPNL
     TGLVVDGKQG QQVAPGGGQN TAIVLPQQQG AGGAPGAPKT PADMVQQLTQ QQQQQQQQVH
     QQQVQQQELR RFDGMSQQVV AGGMQQQQQQ GLPPVIRIQG AQPAVRVLGP GGPGGPSGPN
     VLPNDVNSLH QQQQQMLQQQ QQQGQNRRRG GLATMVEQQQ QHQQQQQQPN PAQLGGNIPA
     PLSVNVGGFG NTNFGGAAAG GAVGANDKQQ LKVAQVHPQS HGVGAGGASA GAGASGGQVA
     AGSSVLMPAD TTGSGNAGNP NQNAGGVAGG AGGGNGGNTG PPGDNEKDWR ESVTADLRNH
     LVHKLVQAIF PTSDPTTMQD KRMHNLVSYA EKVEKDMYEM AKSRSEYYHL LAEKIYKIQK
     ELEEKRLKRK EQHQQMLMQQ QGVANPVAGG AAGGAGSAAG VAGGVVLPQQ QQQQQQQQQQ
     QGQQPLQSCI HPSISPMGGV MPPQQLRPQG PPGILGQQTA AGLGVGVGVT NNMVTMRSHS
     PGGNMLALQQ QQRMQFPQQQ QQQPPGSGAG KMLVGPPGPS PGGMVVNPAL SPYQTTNVLT
     SPVPGQQQQQ QFINANGGTG ANPQLSEIMK QRHIHQQQQQ QQQQQQQGML LPQSPFSNST
     PLQQQQQQQQ QQQQQQQATS NSFSSPMQQQ QQGQQQQQQK PGSVLNNMPP TPTSLEALNA
     GAGAPGTGGS ASNVTVSAPS PSPGFLSNGP SIGTPSNNNN NSSANNNPPS VSSLMQQPLS
     NRPGTPPYIP ASPVPATSAS GLAASSTPAS AAATCASSGS GSNSSSGATA AGASSTSSSS
     SAGSGTPLSS VSTPTSATMA TSSGGGGGGG GNAGGGSSTT PASNPLLLMS GGTAGGGTGA
     TTTTSTSSSS RMMSSSSSLS SQMAALEAAA RDNDDETPSP SGENTNGSGG SGNAGGMASK
     GKLDSIKQDD DIKKEFMDDS CGGNNDSSQM DCSTGGGKGK NVNNDGTSMI KMEIKTEDGL
     DGEVKIKTEA MDVDEAGGST AGEHHGEGGG GSGVGGGKDN INGAHDGGAT GGAVDIKPKT
     ETKPLVPEPL APNAGDKKKK CQFNPEELRT ALLPTLEKLY RQEPESVPFR YPVDPQALGI
     PDYFEIVKKP MDLGTIRTNI QNGKYSDPWE YVDDVWLMFD NAWLYNRKTS RVYRYCTKLS
     EVFEAEIDPV MQALGYCCGR KYTFNPQVLC CYGKQLCTIP RDAKYYSYQN SLKEYGVASN
     RYTYCQKCFN DIQGDTVTLG DDPLQSQTQI KKDQFKEMKN DHLELEPFVN CQECGRKQHQ
     ICVLWLDSIW PGGFVCDNCL KKKNSKRKEN KFNAKRLPTT KLGVYIETRV NNFLKKKEAG
     AGEVHIRVVS SSDKCVEVKP GMRRRFVEQG EMMNEFPYRA KALFAFEEVD GIDVCFFGMH
     VQEYGSECPA PNTRRVYIAY LDSVHFFRPR QYRTAVYHEI LLGYMDYVKQ LGYTMAHIWA
     CPPSEGDDYI FHCHPTDQKI PKPKRLQEWY KKMLDKGMIE RIIQDYKDIL KQAMEDKLGS
     AAELPYFEGD FWPNVLEESI KELDQEEEEK RKQAEAAEAA AAANLFSIEE NEVSGDGKKK
     GQKKAKKSNK SKAAQRKNSK KSNEHQSGND LSTKIYATME KHKEVFFVIR LHSAQSAASL
     APIQDPDPLL TCDLMDGRDA FLTLARDKHF EFSSLRRAQF STLSMLYELH NQGQDKFVYT
     CNHCKTAVET RYHCTVCDDF DLCIVCKEKV GHQHKMEKLG FDIDDGSALA DHKQANPQEA
     RKQSIQRCIQ SLAHACQCRD ANCRLPSCQK MKLVVQHTKN CKRKPNGGCP ICKQLIALCC
     YHAKNCEEQK CPVPFCPNIK HKLKQQQSQQ KFQQQQLLRR RVALMSRTAA PAALQGPAAV
     SGPTVVSGGV PVVGMSGVAV SQQVIPGQAG ILPPGAGGMS PSTVAVPSPV SGGAGAGGMG
     GMTSPHPHQP GIGMKPGGGH SPSPNVLQVV KQVQEEAARQ QVSHGGGFGK GVPMAPPVMN
     RPMGGAGPNQ NVVNQLGGMG VGVGGVGGVG VGGVGGVGVN QLNSGGGNTP GAPISGPGMN
     VNHLMSMDQW GGGGAGGGGA NPGGGNPQAR YANNTGGMRQ PTHVMQTNLI PPQQQQQMMG
     GLGGPNQLGG GQMPVGGQHG GMGMGMGAPP MAGTVGGVRP SPGAGGGGGS ATGGGLNTQQ
     LALIMQKIKN NPTNESNQHI LAILKQNPQI MAAIIKQRQQ SQNNAAAGGG APGPGGALQQ
     QQAGNGPQNP QQQQQQQQQQ QVMQQQQMQH MMNQQQGGGG PQQMNPNQQQ QQQQVNLMQQ
     QQQGGPGGPG SGLPTRMPNM PNALGMLQSL PPNMSPGVST QGGMVPNQNW NKMRYMQMSQ
     YPPPYPQRQR GPHMGGAGPG PGQQQFPGGG GGAGNFNAGG AGGAGGVVGV GGVPGGAGTV
     PGGDQYSMAN AAAASNMLQQ QQGQVGVGVG VGVKPGPGQQ QQQMGVGMPP GMQQQQQQQQ
     PLQQQQMMQV AMPNANAQNP SAVVGGPNAQ VMGPPTPHSL QQQLMQSARS SPPIRSPQPT
     PSPRSAPSPR AAPSASPRAQ PSPHHVMSSH SPAPQGPPHD GMHNHGMHHQ SPLPGVPQDV
     GVGVGVGVGV GVNVNVGNVG VGNAGGALPD ASDQLTKFVE RL
//
DBGET integrated database retrieval system