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Protein

High mobility group protein DSP1

Gene

Dsp1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Binds preferentially single-stranded DNA and unwinds double-stranded DNA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi179 – 24971HMG box 1PROSITE-ProRule annotationAdd
BLAST
DNA bindingi271 – 33969HMG box 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • DNA binding, bending Source: FlyBase
  • single-stranded DNA binding Source: UniProtKB
  • TBP-class protein binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • chromatin remodeling Source: FlyBase
  • developmental process Source: FlyBase
  • DNA unwinding involved in DNA replication Source: UniProtKB
  • leg disc development Source: FlyBase
  • negative regulation of antimicrobial humoral response Source: FlyBase
  • negative regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • positive regulation of DNA binding Source: FlyBase
  • segment specification Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-211227. Activation of DNA fragmentation factor.
SignaLinkiQ24537.

Names & Taxonomyi

Protein namesi
Recommended name:
High mobility group protein DSP1
Alternative name(s):
Protein dorsal switch 1
Gene namesi
Name:Dsp1
Synonyms:ssrp2
ORF Names:CG12223
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0278608. Dsp1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393High mobility group protein DSP1PRO_0000048543Add
BLAST

Proteomic databases

PaxDbiQ24537.
PRIDEiQ24537.

Expressioni

Gene expression databases

BgeeiQ24537.
ExpressionAtlasiQ24537. differential.
GenevisibleiQ24537. DM.

Interactioni

GO - Molecular functioni

  • TBP-class protein binding Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi72866. 11 interactions.
DIPiDIP-29511N.
IntActiQ24537. 1 interaction.
STRINGi7227.FBpp0288398.

Structurei

3D structure databases

ProteinModelPortaliQ24537.
SMRiQ24537. Positions 178-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 162156Gln-richAdd
BLAST
Compositional biasi99 – 1068Poly-Ala
Compositional biasi376 – 39116Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the HMGB family.Curated
Contains 2 HMG box DNA-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00760000119164.
InParanoidiQ24537.
KOiK10802.
OrthoDBiEOG7WHHBQ.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
PROSITEiPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform E (identifier: Q24537-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEHFHQIQQT IQHYQQQLAA QQQQQVQQQQ LQQHQVVVQQ NQQQAHQNSS
60 70 80 90 100
NTTAGVGTQQ LFTYKMASSF PNPATTMAQV VATSNAAGTT GYDYRLNMAQ
110 120 130 140 150
AAAAAAVPGS QWWYSAANQG QVDANTAAQL QHQQQQQQQQ QQQQQQQHQQ
160 170 180 190 200
QQQMQQQQQQ QNVINSASPM SRVKADAKPR GRMTAYAYFV QTCREEHKKK
210 220 230 240 250
HPDETVIFAE FSRKCAERWK TMVDKEKKRF HEMAEKDKQR YEAEMQNYVP
260 270 280 290 300
PKGAVVGRGK KRKQIKDPNA PKRSLSAFFW FCNDERNKVK ALNPEFGVGD
310 320 330 340 350
IAKELGRKWS DVDPEVKQKY ESMAERDKAR YEREMTEYKT SGKIAMSAPS
360 370 380 390
MQASMQAQAQ KAALLAAAAQ QQHQQLEEQH DDDDGDGDDD ENQ
Length:393
Mass (Da):44,935
Last modified:November 1, 1996 - v1
Checksum:iFD270250B723FD31
GO
Isoform D (identifier: Q24537-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-14: Missing.

Show »
Length:386
Mass (Da):44,036
Checksum:iF0B018B47D2ECE54
GO
Isoform A (identifier: Q24537-3) [UniParc]FASTAAdd to basket

Also known as: B, C

The sequence of this isoform differs from the canonical sequence as follows:
     8-15: Missing.

Note: No experimental confirmation available.
Show »
Length:385
Mass (Da):43,908
Checksum:iE1837A90D2F850F9
GO

Sequence cautioni

The sequence CAA57212.1 differs from that shown. Reason: Frameshift at position 31. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291Q → T in AAA50238 (PubMed:8072548).Curated
Sequence conflicti255 – 2573VVG → LWD in AAA50238 (PubMed:8072548).Curated
Sequence conflicti368 – 3681A → R in AAA50238 (PubMed:8072548).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei8 – 158Missing in isoform A. 1 PublicationVSP_002184
Alternative sequencei8 – 147Missing in isoform D. CuratedVSP_002183

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13881 mRNA. Translation: AAA50238.1.
X89811 Genomic DNA. Translation: CAA61938.1.
X81456 mRNA. Translation: CAA57212.1. Frameshift.
AE014298 Genomic DNA. Translation: AAF48594.2.
AE014298 Genomic DNA. Translation: AAN09394.2.
AE014298 Genomic DNA. Translation: AAN09395.1.
AE014298 Genomic DNA. Translation: AAN09396.1.
AE014298 Genomic DNA. Translation: AAS65386.1.
AY060841 mRNA. Translation: AAL28389.1.
PIRiJC6179.
S50068.
RefSeqiNP_001285322.1. NM_001298393.1. [Q24537-2]
NP_542446.2. NM_080715.4. [Q24537-3]
NP_727959.2. NM_167502.3. [Q24537-2]
NP_727960.1. NM_167503.3. [Q24537-3]
NP_727961.1. NM_167504.2. [Q24537-3]
NP_996485.1. NM_206762.3. [Q24537-1]
UniGeneiDm.2879.

Genome annotation databases

EnsemblMetazoaiFBtr0089263; FBpp0089258; FBgn0011764. [Q24537-1]
GeneIDi117294.
KEGGidme:Dmel_CG12223.
UCSCiCG12223-RB. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13881 mRNA. Translation: AAA50238.1.
X89811 Genomic DNA. Translation: CAA61938.1.
X81456 mRNA. Translation: CAA57212.1. Frameshift.
AE014298 Genomic DNA. Translation: AAF48594.2.
AE014298 Genomic DNA. Translation: AAN09394.2.
AE014298 Genomic DNA. Translation: AAN09395.1.
AE014298 Genomic DNA. Translation: AAN09396.1.
AE014298 Genomic DNA. Translation: AAS65386.1.
AY060841 mRNA. Translation: AAL28389.1.
PIRiJC6179.
S50068.
RefSeqiNP_001285322.1. NM_001298393.1. [Q24537-2]
NP_542446.2. NM_080715.4. [Q24537-3]
NP_727959.2. NM_167502.3. [Q24537-2]
NP_727960.1. NM_167503.3. [Q24537-3]
NP_727961.1. NM_167504.2. [Q24537-3]
NP_996485.1. NM_206762.3. [Q24537-1]
UniGeneiDm.2879.

3D structure databases

ProteinModelPortaliQ24537.
SMRiQ24537. Positions 178-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi72866. 11 interactions.
DIPiDIP-29511N.
IntActiQ24537. 1 interaction.
STRINGi7227.FBpp0288398.

Proteomic databases

PaxDbiQ24537.
PRIDEiQ24537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089263; FBpp0089258; FBgn0011764. [Q24537-1]
GeneIDi117294.
KEGGidme:Dmel_CG12223.
UCSCiCG12223-RB. d. melanogaster.

Organism-specific databases

CTDi117294.
FlyBaseiFBgn0278608. Dsp1.

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00760000119164.
InParanoidiQ24537.
KOiK10802.
OrthoDBiEOG7WHHBQ.

Enzyme and pathway databases

ReactomeiR-DME-211227. Activation of DNA fragmentation factor.
SignaLinkiQ24537.

Miscellaneous databases

ChiTaRSiDsp1. fly.
GenomeRNAii117294.
PROiQ24537.

Gene expression databases

BgeeiQ24537.
ExpressionAtlasiQ24537. differential.
GenevisibleiQ24537. DM.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
PROSITEiPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An HMG-like protein that can switch a transcriptional activator to a repressor."
    Lehming N., Thanos D., Brickman J.M., Ma J., Maniatis T., Ptashne M.
    Nature 371:175-179(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E).
    Tissue: Embryo.
  2. "The Drosophila DSP1 gene encoding an HMG 1-like protein: genomic organization, evolutionary conservation and expression."
    Canaple L., Decoville M., Leng M., Locker D.L.D.
    Gene 184:285-290(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS D AND E).
    Strain: Canton-S.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Ovary.

Entry informationi

Entry nameiHMG2_DROME
AccessioniPrimary (citable) accession number: Q24537
Secondary accession number(s): A4V4L8
, Q23998, Q24285, Q95SD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.