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Protein

High mobility group protein D

Gene

HmgD

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

Functioni

Binds preferentially single-stranded DNA and unwinds double-stranded DNA. Prefers sites containing the sequence 5'-ttg-3'. Facilitates DNA bending. Associated with early embryonic chromatin in the absence of histone H1.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi5 – 7167HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • AT DNA binding Source: FlyBase
  • DNA binding Source: FlyBase
  • DNA binding, bending Source: FlyBase

GO - Biological processi

  • chromatin organization Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • muscle organ development Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
High mobility group protein D
Short name:
HMG-D
Gene namesi
Name:HmgD
ORF Names:CG17950
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004362. HmgD.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112High mobility group protein DPRO_0000048552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei12 – 121Phosphotyrosine1 Publication
Modified residuei103 – 1031Phosphoserine2 Publications
Modified residuei111 – 1111Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ05783.
PRIDEiQ05783.

PTM databases

iPTMnetiQ05783.

Expressioni

Developmental stagei

Present in all stages of development.1 Publication

Gene expression databases

BgeeiQ05783.
ExpressionAtlasiQ05783. differential.
GenevisibleiQ05783. DM.

Interactioni

Protein-protein interaction databases

BioGridi63106. 19 interactions.
DIPiDIP-22805N.
IntActiQ05783. 1 interaction.
MINTiMINT-843935.
STRINGi7227.FBpp0071625.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2515Combined sources
Beta strandi27 – 293Combined sources
Helixi32 – 4514Combined sources
Helixi50 – 7021Combined sources
Turni71 – 733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7JNMR-A1-74[»]
1HMANMR-A2-74[»]
1QRVX-ray2.20A/B2-74[»]
3NM9X-ray2.85A/D/G/J/M/P2-74[»]
ProteinModelPortaliQ05783.
SMRiQ05783. Positions 2-74.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05783.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 11212Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the HMGB family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00560000076898.
InParanoidiQ05783.
OMAiDSIKREN.
OrthoDBiEOG7QVM5F.
PhylomeDBiQ05783.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKPKRPLS AYMLWLNSAR ESIKRENPGI KVTEVAKRGG ELWRAMKDKS
60 70 80 90 100
EWEAKAAKAK DDYDRAVKEF EANGGSSAAN GGGAKKRAKP AKKVAKKSKK
110
EESDEDDDDE SE
Length:112
Mass (Da):12,416
Last modified:February 1, 1995 - v1
Checksum:i3F537CCFD62FEC9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77023 mRNA. Translation: AAA28609.1.
X71138 mRNA. Translation: CAA50468.1.
AM294353 Genomic DNA. Translation: CAL26283.1.
AM294354 Genomic DNA. Translation: CAL26284.1.
AM294355 Genomic DNA. Translation: CAL26285.1.
AM294356 Genomic DNA. Translation: CAL26286.1.
AM294357 Genomic DNA. Translation: CAL26287.1.
AM294358 Genomic DNA. Translation: CAL26288.1.
AM294359 Genomic DNA. Translation: CAL26289.1.
AM294360 Genomic DNA. Translation: CAL26290.1.
AM294361 Genomic DNA. Translation: CAL26291.1.
AM294362 Genomic DNA. Translation: CAL26292.1.
AM294363 Genomic DNA. Translation: CAL26293.1.
AE013599 Genomic DNA. Translation: AAF46759.1.
AY118333 mRNA. Translation: AAM48362.1.
PIRiA44382.
RefSeqiNP_001163244.1. NM_001169773.2.
NP_001286696.1. NM_001299767.1.
NP_726109.1. NM_166479.2.
NP_726110.1. NM_166480.2.
UniGeneiDm.7318.

Genome annotation databases

EnsemblMetazoaiFBtr0071708; FBpp0071625; FBgn0004362.
FBtr0071709; FBpp0071626; FBgn0004362.
FBtr0301410; FBpp0290624; FBgn0004362.
FBtr0345487; FBpp0311598; FBgn0004362.
GeneIDi37481.
KEGGidme:Dmel_CG17950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77023 mRNA. Translation: AAA28609.1.
X71138 mRNA. Translation: CAA50468.1.
AM294353 Genomic DNA. Translation: CAL26283.1.
AM294354 Genomic DNA. Translation: CAL26284.1.
AM294355 Genomic DNA. Translation: CAL26285.1.
AM294356 Genomic DNA. Translation: CAL26286.1.
AM294357 Genomic DNA. Translation: CAL26287.1.
AM294358 Genomic DNA. Translation: CAL26288.1.
AM294359 Genomic DNA. Translation: CAL26289.1.
AM294360 Genomic DNA. Translation: CAL26290.1.
AM294361 Genomic DNA. Translation: CAL26291.1.
AM294362 Genomic DNA. Translation: CAL26292.1.
AM294363 Genomic DNA. Translation: CAL26293.1.
AE013599 Genomic DNA. Translation: AAF46759.1.
AY118333 mRNA. Translation: AAM48362.1.
PIRiA44382.
RefSeqiNP_001163244.1. NM_001169773.2.
NP_001286696.1. NM_001299767.1.
NP_726109.1. NM_166479.2.
NP_726110.1. NM_166480.2.
UniGeneiDm.7318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7JNMR-A1-74[»]
1HMANMR-A2-74[»]
1QRVX-ray2.20A/B2-74[»]
3NM9X-ray2.85A/D/G/J/M/P2-74[»]
ProteinModelPortaliQ05783.
SMRiQ05783. Positions 2-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63106. 19 interactions.
DIPiDIP-22805N.
IntActiQ05783. 1 interaction.
MINTiMINT-843935.
STRINGi7227.FBpp0071625.

PTM databases

iPTMnetiQ05783.

Proteomic databases

PaxDbiQ05783.
PRIDEiQ05783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071708; FBpp0071625; FBgn0004362.
FBtr0071709; FBpp0071626; FBgn0004362.
FBtr0301410; FBpp0290624; FBgn0004362.
FBtr0345487; FBpp0311598; FBgn0004362.
GeneIDi37481.
KEGGidme:Dmel_CG17950.

Organism-specific databases

CTDi37481.
FlyBaseiFBgn0004362. HmgD.

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00560000076898.
InParanoidiQ05783.
OMAiDSIKREN.
OrthoDBiEOG7QVM5F.
PhylomeDBiQ05783.

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiHmgD. fly.
EvolutionaryTraceiQ05783.
GenomeRNAii37481.
NextBioi803865.
PROiQ05783.

Gene expression databases

BgeeiQ05783.
ExpressionAtlasiQ05783. differential.
GenevisibleiQ05783. DM.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A high-mobility-group protein and its cDNAs from Drosophila melanogaster."
    Wagner C.R., Hamana K., Elgin S.C.R.
    Mol. Cell. Biol. 12:1915-1923(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-77, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "dHMG-Z, a second HMG-1-related protein in Drosophila melanogaster."
    Ner S.S., Churchill M.E.A., Searles M.A., Travers A.A.
    Nucleic Acids Res. 21:4369-4371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  3. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
    Proeschel M., Zhang Z., Parsch J.
    Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84 and ZBMEL95.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "HMG-D, the Drosophila melanogaster homologue of HMG 1 protein, is associated with early embryonic chromatin in the absence of histone H1."
    Ner S.S., Travers A.A.
    EMBO J. 13:1817-1822(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG."
    Churchill M.E.A., Jones D.N.M., Glaser T., Hefner H., Searles M.A., Travers A.A.
    EMBO J. 14:1264-1275(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; TYR-12; SER-103 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster."
    Jones D.N.M., Searles M.A., Shaw G.L., Churchill M.E.A., Ner S.S., Keeler J., Travers A.A., Neuhaus D.
    Structure 2:609-627(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-74.

Entry informationi

Entry nameiHMGD_DROME
AccessioniPrimary (citable) accession number: Q05783
Secondary accession number(s): Q540Z0, Q9W2D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.