HMG2_DROME
ID HMG2_DROME Reviewed; 393 AA.
AC Q24537; A4V4L8; Q23998; Q24285; Q95SD7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=High mobility group protein DSP1;
DE AltName: Full=Protein dorsal switch 1;
GN Name=Dsp1; Synonyms=ssrp2; ORFNames=CG12223;
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 E).
RC TISSUE=Embryo;
RX PubMed=8072548; DOI=10.1038/371175a0;
RA Lehming N., Thanos D., Brickman J.M., Ma J., Maniatis T., Ptashne M.;
RT "An HMG-like protein that can switch a transcriptional activator to a
RT repressor.";
RL Nature 371:175-179(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS D AND E).
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=9031641; DOI=10.1016/s0378-1119(96)00616-6;
RA Canaple L., Decoville M., Leng M., Locker D.L.D.;
RT "The Drosophila DSP1 gene encoding an HMG 1-like protein: genomic
RT organization, evolutionary conservation and expression.";
RL Gene 184:285-290(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Ovary;
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).
CC -!- FUNCTION: Binds preferentially single-stranded DNA and unwinds double-
CC stranded DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=E;
CC IsoId=Q24537-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q24537-2; Sequence=VSP_002183;
CC Name=A; Synonyms=B, C;
CC IsoId=Q24537-3; Sequence=VSP_002184;
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57212.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U13881; AAA50238.1; -; mRNA.
DR EMBL; X89811; CAA61938.1; -; Genomic_DNA.
DR EMBL; X81456; CAA57212.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAF48594.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09394.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09395.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09396.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65386.1; -; Genomic_DNA.
DR EMBL; AY060841; AAL28389.1; -; mRNA.
DR PIR; JC6179; JC6179.
DR PIR; S50068; S50068.
DR RefSeq; NP_001285322.1; NM_001298393.1. [Q24537-2]
DR RefSeq; NP_542446.2; NM_080715.4. [Q24537-3]
DR RefSeq; NP_727959.2; NM_167502.3. [Q24537-2]
DR RefSeq; NP_727960.1; NM_167503.3. [Q24537-3]
DR RefSeq; NP_727961.1; NM_167504.2. [Q24537-3]
DR RefSeq; NP_996485.1; NM_206762.3. [Q24537-1]
DR AlphaFoldDB; Q24537; -.
DR SMR; Q24537; -.
DR BioGRID; 72866; 25.
DR DIP; DIP-29511N; -.
DR IntAct; Q24537; 11.
DR STRING; 7227.FBpp0288398; -.
DR PaxDb; Q24537; -.
DR DNASU; 117294; -.
DR EnsemblMetazoa; FBtr0089259; FBpp0088318; FBgn0278608. [Q24537-3]
DR EnsemblMetazoa; FBtr0089260; FBpp0088319; FBgn0278608. [Q24537-3]
DR EnsemblMetazoa; FBtr0089261; FBpp0088320; FBgn0278608. [Q24537-3]
DR EnsemblMetazoa; FBtr0089262; FBpp0089257; FBgn0278608. [Q24537-2]
DR EnsemblMetazoa; FBtr0089263; FBpp0089258; FBgn0278608. [Q24537-1]
DR EnsemblMetazoa; FBtr0339766; FBpp0308813; FBgn0278608. [Q24537-2]
DR GeneID; 117294; -.
DR KEGG; dme:Dmel_CG12223; -.
DR UCSC; CG12223-RB; d. melanogaster.
DR CTD; 117294; -.
DR FlyBase; FBgn0278608; Dsp1.
DR VEuPathDB; VectorBase:FBgn0278608; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000153299; -.
DR InParanoid; Q24537; -.
DR OMA; QWWYPGG; -.
DR Reactome; R-DME-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-DME-163282; Mitochondrial transcription initiation.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-5620971; Pyroptosis.
DR Reactome; R-DME-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q24537; -.
DR BioGRID-ORCS; 117294; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Dsp1; fly.
DR GenomeRNAi; 117294; -.
DR PRO; PR:Q24537; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0278608; Expressed in wing disc and 35 other tissues.
DR ExpressionAtlas; Q24537; baseline and differential.
DR Genevisible; Q24537; DM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0008301; F:DNA binding, bending; IDA:FlyBase.
DR GO; GO:0003697; F:single-stranded DNA binding; NAS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:FlyBase.
DR GO; GO:0032502; P:developmental process; IMP:FlyBase.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; NAS:UniProtKB.
DR GO; GO:0035218; P:leg disc development; IMP:FlyBase.
DR GO; GO:0008348; P:negative regulation of antimicrobial humoral response; IMP:FlyBase.
DR GO; GO:0017055; P:negative regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007379; P:segment specification; IMP:FlyBase.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017967; HMG_boxA_CS.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS00353; HMG_BOX_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..393
FT /note="High mobility group protein DSP1"
FT /id="PRO_0000048543"
FT DNA_BIND 179..249
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 271..339
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 153..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 8..15
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002184"
FT VAR_SEQ 8..14
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_002183"
FT CONFLICT 129
FT /note="Q -> T (in Ref. 1; AAA50238)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..257
FT /note="VVG -> LWD (in Ref. 1; AAA50238)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> R (in Ref. 1; AAA50238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44935 MW; FD270250B723FD31 CRC64;
MEHFHQIQQT IQHYQQQLAA QQQQQVQQQQ LQQHQVVVQQ NQQQAHQNSS NTTAGVGTQQ
LFTYKMASSF PNPATTMAQV VATSNAAGTT GYDYRLNMAQ AAAAAAVPGS QWWYSAANQG
QVDANTAAQL QHQQQQQQQQ QQQQQQQHQQ QQQMQQQQQQ QNVINSASPM SRVKADAKPR
GRMTAYAYFV QTCREEHKKK HPDETVIFAE FSRKCAERWK TMVDKEKKRF HEMAEKDKQR
YEAEMQNYVP PKGAVVGRGK KRKQIKDPNA PKRSLSAFFW FCNDERNKVK ALNPEFGVGD
IAKELGRKWS DVDPEVKQKY ESMAERDKAR YEREMTEYKT SGKIAMSAPS MQASMQAQAQ
KAALLAAAAQ QQHQQLEEQH DDDDGDGDDD ENQ
