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Reviewed, UniProtKB/Swiss-Prot Q9VEX9 (SAP18_DROME)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Histone deacetylase complex subunit SAP18
Alternative name(s):
    Sin3-associated polypeptide, 18 kDa
    Bicoid-interacting protein 1
    dSAP18
Gene names
Name: Bin1
Synonyms: SAP18
ORF Names: CG6046
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in the tethering of the SIN3 complex to core histone proteins. Interacts with bicoid (bcd) to repress transcription of bicoid target genes in the anterior tip of the embryo; a process known as retraction. Interacts with Trl and binds to Polycomb response elements at the bithorax complex. May contribute to the regulation of other homeotic gene expressions. Ref.1 Ref.6

Subunit structure

Forms a complex with SIN3 and histone deacetylase By similarity. Interacts with the N-terminal residues of TRL. Interacts with BCD; in vitro and yeast cells.

Subcellular location

Nucleus. Ref.1 Ref.6

Developmental stage

Expressed both maternally and zygotically. Ref.1

Sequence similarities

Belongs to the SAP18 family.

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Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionDevelopmental protein
Repressor
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmulticellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-dependent Ref.1

Inferred from direct assay. Source: FlyBase

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.1 Ref.6

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150Histone deacetylase complex subunit SAP18
PRO_0000220978

Experimental info

Sequence conflict571T → A in AAL48535. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q9VEX9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 94947F206D8FA0AD

FASTA15017,288
        10         20         30         40         50         60 
MANVESMIVE EKTQVKQIDR EKTCPMLLRV FCSTGRHHSV SEYMFGNVPT NELQIYTWQD 

        70         80         90        100        110        120 
ATLHELTSLV RDVNPDTRKK GTYFDFAVVY PNFRSNHFQM REIGVTCTGQ KGIDDNKTLA 

       130        140        150 
QAKFSIGDFL DISITPPNRL PPTARRQRPY

« Hide

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References

« Hide 'large scale' references
[1]"Drosophila SAP18, a member of the Sin3/Rpd3 histone deacetylase complex, interacts with Bicoid and inhibits its activity."
Zhu W., Foehr M., Jaynes J.B., Hanes S.D.
Dev. Genes Evol. 211:109-117(2001) [PubMed: 11455422] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCD, DEVELOPMENTAL STAGE.
[2]"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. expand/collapse author list , 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.
[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. expand/collapse author list , 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.
[4]"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.
[5]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[6]"The GAGA factor of Drosophila interacts with SAP18, a Sin3-associated polypeptide."
Espinas M.L., Canudas S., Fanti L., Pimpinelli S., Casanova J., Azorin F.
EMBO Rep. 1:253-259(2000) [PubMed: 11256608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-150, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRL.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF297546 mRNA. Translation: AAG34996.1.
AE014297 Genomic DNA. Translation: AAF55284.1.
AY070913 mRNA. Translation: AAL48535.1.
BT025229 mRNA. Translation: ABF17920.1.
AJ278500 mRNA. Translation: CAB95728.1.
RefSeqNP_524377.1.
UniGeneDm.20197

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:19160N.
IntActQ9VEX9. 25 interactions.

Proteomic databases

PRIDEQ9VEX9.

Genome annotation databases

EnsemblFBgn0024491. Drosophila melanogaster. [Contig view]
GeneID41965.
KEGGdme:Dmel_CG6046.
NMPDRfig|7227.3.peg.13108.

Organism-specific databases

FlyBaseFBgn0024491. Bin1.

Phylogenomic databases

HOGENOMQ9VEX9.
OMAQ9VEX9. FAIVYPD.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-011892-MON.

Gene expression databases

ArrayExpressQ9VEX9.
GermOnlineCG6046. Drosophila melanogaster.

Family and domain databases

InterProIPR017250. Hist_deAcase_cplx_SAP18_su.
IPR010516. SAP18.
[Graphical view]
PANTHERPTHR13082. SAP18. 1 hit.
PfamPF06487. SAP18. 1 hit.
[Graphical view]
PIRSFPIRSF037637. HDAC_SAP18. 1 hit.
ProtoNetSearch...

Other Resources

NextBio826507.

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Entry information

Entry nameSAP18_DROME
AccessionPrimary (citable) accession number: Q9VEX9
Secondary accession number(s): Q1LYZ7, Q8SZF6, Q9N9Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents