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O88574 (SAP30_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase complex subunit SAP30
Alternative name(s):
30 kDa Sin3-associated polypeptide
Sin3 corepressor complex subunit SAP30
Sin3-associated polypeptide p30
Gene names
Name:Sap30
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
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. Interacts directly with SAMSN1. Ref.1 Ref.7 UniProtKB O75446

Subcellular location

Nucleus Ref.1.

Sequence similarities

Belongs to the SAP30 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ncor1Q609743EBI-593511,EBI-349004
Sin3aQ605206EBI-593511,EBI-349034

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Histone deacetylase complex subunit SAP30
PRO_0000097583

Regions

Zinc finger67 – 11549Atypical
Region1 – 129129Interaction with NCOR1
Region130 – 22091Interaction with SIN3A
Compositional bias15 – 5945Ala-rich

Amino acid modifications

Modified residue1311Phosphoserine Ref.6
Modified residue1381Phosphoserine By similarity
Modified residue1451Phosphothreonine By similarity

Secondary structure

........... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O88574 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-220.
Strain: C57BL/6N.
Tissue: Liver.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"SLy2 targets the nuclear SAP30/HDAC1 complex."
Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., Schmitz I., Beer-Hammer S.
Int. J. Biochem. Cell Biol. 42:1472-1481(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAMSN1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22316.1.
RefSeqNP_068560.1. NM_021788.2.
UniGeneMm.118.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LD7NMR-A130-220[»]
ProteinModelPortalO88574.
SMRO88574. Positions 64-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208559. 4 interactions.
IntActO88574. 7 interactions.
MINTMINT-4968448.
STRING10090.ENSMUSP00000034022.

PTM databases

PhosphoSiteO88574.

Proteomic databases

MaxQBO88574.
PRIDEO88574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034022; ENSMUSP00000034022; ENSMUSG00000031609.
GeneID60406.
KEGGmmu:60406.
UCSCuc009lsu.2. mouse.

Organism-specific databases

CTD8819.
MGIMGI:1929129. Sap30.

Phylogenomic databases

eggNOGNOG81414.
GeneTreeENSGT00390000006633.
HOGENOMHOG000007811.
HOVERGENHBG057907.
InParanoidA2RSE9.
OMAKIDSGVH.
OrthoDBEOG7P5T35.
PhylomeDBO88574.
TreeFamTF324135.

Enzyme and pathway databases

ReactomeREACT_200794. Mus musculus biological processes.

Gene expression databases

BgeeO88574.
GenevestigatorO88574.

Family and domain databases

InterProIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERPTHR13286. PTHR13286. 1 hit.
PfamPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO88574.
NextBio314849.
PROO88574.
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: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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