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Reviewed, UniProtKB/Swiss-Prot O88574 (SAP30_MOUSE)

Last modified November 24, 2009. Version 55. 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

Names and origin

Protein namesRecommended name:
    Histone deacetylase complex subunit SAP30
Alternative name(s):
    Sin3-associated polypeptide, 30 kDa
    Sin3 corepressor complex subunit SAP30
Gene names
Name: Sap30
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. Ref.1 UniProtKB O75446

Subunit structure

Interacts with HCFC1 By similarity. A component of the histone deacetylase complex that includes at least SIN3A, HDAC1 and HDAC2. Interacts with SIN3A, SIN3B, HDAC1, HDAC2, RBBP4 and NCOR1. Ref.1 UniProtKB O75446

Subcellular location

Nucleus.

Sequence similarities

Belongs to the SAP30 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processregulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Histone deacetylase complex subunit SAP30
PRO_0000097583

Regions

Region1 – 129129Interaction with NCOR1
Region130 – 22091Interaction with SIN3A
Compositional bias15 – 5945Ala-rich

Amino acid modifications

Modified residue1041N6-acetyllysine By similarity
Modified residue1311Phosphoserine By similarity
Modified residue1381Phosphoserine By similarity
Modified residue1451Phosphothreonine By similarity
Modified residue1691Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88574-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: A9D4CBDAB97BBD8C

FASTA22023,231
        10         20         30         40         50         60 
MNGFTPEEMS RGGDAAAAVA AVVAAAAAAA SAGNGNAAGG GAEVPGAGAV SASGPPGAAG 

        70         80         90        100        110        120 
PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI ELDKSARHLY ICDYHKNLIQ 

       130        140        150        160        170        180 
SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE 

       190        200        210        220 
IVGCHFKSIP VNEKDTLTCF IYSVRNDKNK SDLKADSGVH 

« Hide

References

« Hide 'large scale' references
[1]"SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors."
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N.
Mol. Cell 2:33-42(1998) [PubMed: 9702189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NCOR1; SIN3A; SIN3B; HDAC1; HDAC2 AND RBBP4.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver and Thymus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Mouse scrapie responsive gene 1 (Scrg1): genomic organization, physical linkage to sap30, genetic mapping on chromosome 8, and expression in neuronal primary cell cultures."
Dron M., Tartare X., Guillo F., Haik S., Barbin G., Maury C., Tovey M., Dandoy-Dron F.
Genomics 70:140-149(2000) [PubMed: 11087671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-220.
Strain: C57BL/6N.
Tissue: Liver.

Cross-references

Sequence databases

AF075136 mRNA. Translation: AAC26007.1.
AK010928 mRNA. Translation: BAB27273.1.
AK088745 mRNA. Translation: BAC40543.1.
CH466569 Genomic DNA. Translation: EDL28616.1.
BC132081 mRNA. Translation: AAI32082.1.
BC132087 mRNA. Translation: AAI32088.1.
AJ251216 Genomic DNA. Translation: CAC24848.1.
IPIIPI00132028.
RefSeqNP_068560.1.
UniGeneMm.118

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO88574. 6 interactions.
STRINGO88574.

PTM databases

PhosphoSiteO88574.

Proteomic databases

PRIDEO88574.

Genome annotation databases

EnsemblENSMUST00000034022; ENSMUSP00000034022; ENSMUSG00000031609; Mus musculus. [Genome view]
GeneID60406.
KEGGmmu:60406.
UCSCuc009lsu.1. mouse.

Organism-specific databases

CTD60406.
MGIMGI:1929129. Sap30.

Phylogenomic databases

HOGENOMO88574.
HOVERGENO88574.
OMAFTPDEMS
OrthoDBEOG934ZRN

Gene expression databases

ArrayExpressO88574.
BgeeO88574.
GenevestigatorO88574.
GermOnlineENSMUSG00000031609. Mus musculus.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio314849.
SOURCESearch...

Entry information

Entry nameSAP30_MOUSE
AccessionPrimary (citable) accession number: O88574
Secondary accession number(s): A2RSE9, Q99JB9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1998
Last modified: November 24, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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