SET_DROME
ID SET_DROME Reviewed; 269 AA.
AC P53997; Q540W9; Q9VFA5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein SET;
GN Name=Set; ORFNames=CG4299;
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].
RX PubMed=7622566; DOI=10.1083/jcb.130.3.661;
RA Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., Murray A.W.;
RT "Members of the NAP/SET family of proteins interact specifically with B-
RT type cyclins.";
RL J. Cell Biol. 130:661-673(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377,
RC ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MEL01, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18,
RC MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-148 AND SER-152, AND
RP 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 -!- SUBUNIT: Interacts specifically with B-type cyclins.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; U30470; AAA74264.1; -; mRNA.
DR EMBL; AM294381; CAL26311.1; -; Genomic_DNA.
DR EMBL; AM294382; CAL26312.1; -; Genomic_DNA.
DR EMBL; AM294383; CAL26313.1; -; Genomic_DNA.
DR EMBL; AM294384; CAL26314.1; -; Genomic_DNA.
DR EMBL; AM294385; CAL26315.1; -; Genomic_DNA.
DR EMBL; AM294386; CAL26316.1; -; Genomic_DNA.
DR EMBL; AM294387; CAL26317.1; -; Genomic_DNA.
DR EMBL; AM294388; CAL26318.1; -; Genomic_DNA.
DR EMBL; AM294389; CAL26319.1; -; Genomic_DNA.
DR EMBL; AM294390; CAL26320.1; -; Genomic_DNA.
DR EMBL; FM245455; CAR93381.1; -; Genomic_DNA.
DR EMBL; FM245456; CAR93382.1; -; Genomic_DNA.
DR EMBL; FM245457; CAR93383.1; -; Genomic_DNA.
DR EMBL; FM245458; CAR93384.1; -; Genomic_DNA.
DR EMBL; FM245459; CAR93385.1; -; Genomic_DNA.
DR EMBL; FM245460; CAR93386.1; -; Genomic_DNA.
DR EMBL; FM245461; CAR93387.1; -; Genomic_DNA.
DR EMBL; FM245462; CAR93388.1; -; Genomic_DNA.
DR EMBL; FM245463; CAR93389.1; -; Genomic_DNA.
DR EMBL; FM245464; CAR93390.1; -; Genomic_DNA.
DR EMBL; FM245465; CAR93391.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55155.1; -; Genomic_DNA.
DR EMBL; AY118922; AAM50782.1; -; mRNA.
DR RefSeq; NP_650438.2; NM_142181.3.
DR AlphaFoldDB; P53997; -.
DR SMR; P53997; -.
DR BioGRID; 66908; 6.
DR DIP; DIP-19697N; -.
DR IntAct; P53997; 2.
DR STRING; 7227.FBpp0082521; -.
DR iPTMnet; P53997; -.
DR PaxDb; P53997; -.
DR PRIDE; P53997; -.
DR DNASU; 41844; -.
DR EnsemblMetazoa; FBtr0083062; FBpp0082521; FBgn0014879.
DR GeneID; 41844; -.
DR KEGG; dme:Dmel_CG4299; -.
DR UCSC; CG4299-RA; d. melanogaster.
DR CTD; 6418; -.
DR FlyBase; FBgn0014879; Set.
DR VEuPathDB; VectorBase:FBgn0014879; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000169229; -.
DR HOGENOM; CLU_051687_4_0_1; -.
DR InParanoid; P53997; -.
DR OMA; WPVALMN; -.
DR OrthoDB; 1191764at2759; -.
DR PhylomeDB; P53997; -.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR BioGRID-ORCS; 41844; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Set; fly.
DR GenomeRNAi; 41844; -.
DR PRO; PR:P53997; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0014879; Expressed in wing disc and 51 other tissues.
DR Genevisible; P53997; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..269
FT /note="Protein SET"
FT /id="PRO_0000185665"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..269
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 15
FT /note="Missing (in Ref. 1; AAA74264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30995 MW; 05F88CB85933BB09 CRC64;
MSSVPKRAKL DGAPADGNTS AAAGNNEEES EALEQIDACQ NEIDALNEKA SEEILKVEQK
YNKLRKPCYE KRSELVKRIP NFWVTSFINH PQVSGILDEE EEECLHALNK LEVEEFEDIK
SGYRINFHFD ENPYFENKVL TKEFHLNSAA ASENGDWPAS TSTPIKWKEG KNLLKLLLTK
PYGNKKKRNS EYKTFFDWFS DNTDPVNDEI AELIKDDLWP NPLQYYLVPD IEVEPEDEED
NEDNDEEAFD DEDGEDGEGE EEEEDEDDK