Q9V424 (Q9V424_DROME) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
MBD-like, isoform B EMBL AAF54401.1

Submitted name:
Methyl-CpG binding domain-like protein EMBL AAD55391.1

Gene names

Name:	MBD-like EMBL AAF54401.1 FlyBase FBgn0027950
ORF Names:	CG8208 FlyBase FBgn0027950, Dmel_CG8208 EMBL AAF54401.1

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	226 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Traceable author statement. Source: FlyBase negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: FlyBase
Cellular component	NuRD complex Inferred from physical interaction. Source: FlyBase polytene chromosome Inferred from direct assay. Source: FlyBase
Molecular function	histone deacetylase binding Inferred from physical interaction. Source: FlyBase methyl-CpG binding Inferred from direct assay. Source: FlyBase transcription corepressor activity Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9V424 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 26F2DD296442B4D3	FASTA	226	25,293
	10 20 30 40 50 60 MQMNPSVTIE RKRVDCSVLP KGWQRDEVRK SGSSANNNAS SNNNSSATAS SNNNNNKVDV 70 80 90 100 110 120 FYYSRALRTD VSLVPPIRQT ASIFKQPVTV IRNHKQDPAK AKNEPKHGTR EKPKQLFWEK 130 140 150 160 170 180 RLERLRACHD SGEELDDISL PKTIRTVGPN VNEQTVLQSV ATALHMLNAG VHGQSSTKAD 190 200 210 220 LTKNAMAFMN PEQPLMHAVI ISEDDIRKQE DRVGVARRKL QDALKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., 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., WoodageT, 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., 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.
[2]	"The Mi-2 histone deacetylase complex couples DNA methylation to chromatin remodeling and histone deacetylation." Wade P.A., Gegonne A., Jones P.L., Ballestar E., Aubry F., Wolffe A.P. Nat. Genet. 0:0-0(1999) Cited for: NUCLEOTIDE SEQUENCE.
[3]	"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: NUCLEOTIDE SEQUENCE. Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF171098 mRNA. Translation: AAD55391.1. AE014297 Genomic DNA. Translation: AAF54401.1.
RefSeq	NP_649907.1. NM_141650.2.
UniGene	Dm.1126.
3D structure databases
ProteinModelPortal	Q9V424.
SMR	Q9V424. Positions 10-65, 196-225.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V424. 1 interaction.
STRING	Q9V424.
Proteomic databases
PRIDE	Q9V424.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082068; FBpp0081546; FBgn0027950.
GeneID	41151.
KEGG	dme:Dmel_CG8208.
NMPDR	fig|7227.3.peg.11907.
UCSC	CG8208-RB. d. melanogaster.
Organism-specific databases
CTD	41151.
FlyBase	FBgn0027950. MBD-like.
Phylogenomic databases
eggNOG	inNOG10121.
GeneTree	EMGT00050000015116.
InParanoid	Q9V424.
OrthoDB	EOG4Q575H.
Gene expression databases
ArrayExpress	Q9V424.
Bgee	Q9V424.
Family and domain databases
InterPro	IPR016177. DNA-bd_integrase-typ. IPR001739. Methyl_CpG_DNA-bd. [Graphical view]
KO	K11590.
Pfam	PF01429. MBD. 1 hit. [Graphical view]
SUPFAM	SSF54171. DNA-binding_integrase-type. 1 hit.
ProtoNet	Search...
Other
NextBio	822427.

Entry information

Entry name

Q9V424_DROME

Accession

Primary (citable) accession number: Q9V424

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)