Q05783 (HMGD_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High mobility group protein D
Short name=HMG-D

Gene names

Name:	HmgD
ORF Names:	CG17950

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7 Ref.8
Subcellular location	Nucleus. Chromosome Ref.1 Ref.7 Ref.8.
Developmental stage	Present in all stages of development. Ref.1
Sequence similarities	Belongs to the HMGB family. Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin organization Inferred from direct assay Ref.8. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype. Source: FlyBase muscle organ development Inferred from mutant phenotype. Source: FlyBase
Cellular component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	AT DNA binding Inferred from direct assay Ref.8. Source: FlyBase DNA binding, bending Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 112

112

High mobility group protein D

PRO_0000048552

Regions

DNA binding

5 – 71

67

HMG box

Compositional bias

101 – 112

12

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

10

1

Phosphoserine Ref.10

Modified residue

12

1

Phosphotyrosine Ref.10

Modified residue

103

1

Phosphoserine Ref.9 Ref.10

Modified residue

111

1

Phosphoserine Ref.9 Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

112

Helix Strand Turn

Details...

Helix

11 – 25

15

Helix

32 – 45

14

Helix

50 – 70

21

Turn

71 – 73

3

Sequences

	Sequence		Length	Mass (Da)
	Q05783 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 3F537CCFD62FEC9F	FASTA	112	12,416
	10 20 30 40 50 60 MSDKPKRPLS AYMLWLNSAR ESIKRENPGI KVTEVAKRGG ELWRAMKDKS EWEAKAAKAK 70 80 90 100 110 DDYDRAVKEF EANGGSSAAN GGGAKKRAKP AKKVAKKSKK EESDEDDDDE SE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1373803] [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: 8414994] [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: 16951084] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[6]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] 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: 8168480] [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: 7720717] [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: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-111, 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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; TYR-12; SER-103 AND SER-111, 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: 7922039] [Abstract] Cited for: STRUCTURE BY NMR OF 2-74.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A44382.

RefSeq

NP_001163244.1. NM_001169773.1.
NP_726109.1. NM_166479.1.
NP_726110.1. NM_166480.1.

UniGene

Dm.7318.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E7J	NMR	-	A	1-74	[»]
1HMA	NMR	-	A	2-74	[»]
1QRV	X-ray	2.20	A/B	2-74	[»]
3NM9	X-ray	2.85	A/D/G/J/M/P	2-74	[»]

ProteinModelPortal

Q05783.

SMR

Q05783. Positions 2-74.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-22805N.

IntAct

Q05783. 1 interaction.

MINT

MINT-843935.

STRING

Q05783.

Proteomic databases

PRIDE

Q05783.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0071708; FBpp0071625; FBgn0004362.
FBtr0071709; FBpp0071626; FBgn0004362.
FBtr0301410; FBpp0290624; FBgn0004362.

GeneID

37481.

KEGG

dme:Dmel_CG17950.

Organism-specific databases

CTD

37481.

FlyBase

FBgn0004362. HmgD.

Phylogenomic databases

eggNOG

inNOG11573.

GeneTree

EMGT00050000003536.

InParanoid

Q05783.

OMA

ELWRAMK.

OrthoDB

EOG4TX98R.

PhylomeDB

Q05783.

Gene expression databases

Bgee

Q05783.

GermOnline

CG17950. Drosophila melanogaster.

Family and domain databases

InterPro

IPR000910. HMG_HMG1/HMG2.
IPR009071. HMG_superfamily.
[Graphical view]

Gene3D

G3DSA:1.10.30.10. HMG-box. 1 hit.

Pfam

PF00505. HMG_box. 1 hit.
[Graphical view]

SMART

SM00398. HMG. 1 hit.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 1 hit.

PROSITE

PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

803865.

Entry information

Entry name

HMGD_DROME

Accession

Primary (citable) accession number: Q05783
Secondary accession number(s): Q540Z0, Q9W2D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project