Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O88574

- SAP30_MOUSE

UniProt

O88574 - SAP30_MOUSE

Protein

Histone deacetylase complex subunit SAP30

Gene

Sap30

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri67 – 11549AtypicalAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    2. skeletal muscle cell differentiation Source: MGI
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase complex subunit SAP30
    Alternative name(s):
    30 kDa Sin3-associated polypeptide
    Sin3 corepressor complex subunit SAP30
    Sin3-associated polypeptide p30
    Gene namesi
    Name:Sap30Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1929129. Sap30.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: MGI
    2. Sin3 complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Histone deacetylase complex subunit SAP30PRO_0000097583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei138 – 1381PhosphoserineBy similarity
    Modified residuei145 – 1451PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO88574.
    PRIDEiO88574.

    PTM databases

    PhosphoSiteiO88574.

    Expressioni

    Gene expression databases

    BgeeiO88574.
    GenevestigatoriO88574.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ncor1Q609743EBI-593511,EBI-349004
    Sin3aQ605206EBI-593511,EBI-349034

    Protein-protein interaction databases

    BioGridi208559. 4 interactions.
    IntActiO88574. 7 interactions.
    MINTiMINT-4968448.
    STRINGi10090.ENSMUSP00000034022.

    Structurei

    Secondary structure

    1
    220
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi135 – 1384
    Beta strandi151 – 1533
    Helixi155 – 16410
    Helixi175 – 18612
    Helixi193 – 20614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LD7NMR-A130-220[»]
    ProteinModelPortaliO88574.
    SMRiO88574. Positions 64-220.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO88574.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 129129Interaction with NCOR1Add
    BLAST
    Regioni130 – 22091Interaction with SIN3AAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi15 – 5945Ala-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SAP30 family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri67 – 11549AtypicalAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG81414.
    GeneTreeiENSGT00390000006633.
    HOGENOMiHOG000007811.
    HOVERGENiHBG057907.
    InParanoidiA2RSE9.
    OMAiKIDSGVH.
    OrthoDBiEOG7P5T35.
    PhylomeDBiO88574.
    TreeFamiTF324135.

    Family and domain databases

    InterProiIPR024145. His_deAcase_SAP30/SAP30L.
    IPR025718. SAP30_Sin3-bd.
    IPR025717. SAP30_zn-finger.
    [Graphical view]
    PANTHERiPTHR13286. PTHR13286. 1 hit.
    PfamiPF13867. SAP30_Sin3_bdg. 1 hit.
    PF13866. zf-SAP30. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88574-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGFTPEEMS RGGDAAAAVA AVVAAAAAAA SAGNGNAAGG GAEVPGAGAV    50
    SASGPPGAAG PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI 100
    ELDKSARHLY ICDYHKNLIQ SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL 150
    YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE IVGCHFKSIP VNEKDTLTCF 200
    IYSVRNDKNK SDLKADSGVH 220
    Length:220
    Mass (Da):23,231
    Last modified:November 1, 1998 - v1
    Checksum:iA9D4CBDAB97BBD8C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS22316.1.
    RefSeqiNP_068560.1. NM_021788.2.
    UniGeneiMm.118.

    Genome annotation databases

    EnsembliENSMUST00000034022; ENSMUSP00000034022; ENSMUSG00000031609.
    GeneIDi60406.
    KEGGimmu:60406.
    UCSCiuc009lsu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS22316.1.
    RefSeqi NP_068560.1. NM_021788.2.
    UniGenei Mm.118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LD7 NMR - A 130-220 [» ]
    ProteinModelPortali O88574.
    SMRi O88574. Positions 64-220.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208559. 4 interactions.
    IntActi O88574. 7 interactions.
    MINTi MINT-4968448.
    STRINGi 10090.ENSMUSP00000034022.

    PTM databases

    PhosphoSitei O88574.

    Proteomic databases

    MaxQBi O88574.
    PRIDEi O88574.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034022 ; ENSMUSP00000034022 ; ENSMUSG00000031609 .
    GeneIDi 60406.
    KEGGi mmu:60406.
    UCSCi uc009lsu.2. mouse.

    Organism-specific databases

    CTDi 8819.
    MGIi MGI:1929129. Sap30.

    Phylogenomic databases

    eggNOGi NOG81414.
    GeneTreei ENSGT00390000006633.
    HOGENOMi HOG000007811.
    HOVERGENi HBG057907.
    InParanoidi A2RSE9.
    OMAi KIDSGVH.
    OrthoDBi EOG7P5T35.
    PhylomeDBi O88574.
    TreeFami TF324135.

    Enzyme and pathway databases

    Reactomei REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

    EvolutionaryTracei O88574.
    NextBioi 314849.
    PROi O88574.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88574.
    Genevestigatori O88574.

    Family and domain databases

    InterProi IPR024145. His_deAcase_SAP30/SAP30L.
    IPR025718. SAP30_Sin3-bd.
    IPR025717. SAP30_zn-finger.
    [Graphical view ]
    PANTHERi PTHR13286. PTHR13286. 1 hit.
    Pfami PF13867. SAP30_Sin3_bdg. 1 hit.
    PF13866. zf-SAP30. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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/6NImported.
      Tissue: LiverImported.
    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. Cited for: INTERACTION WITH SAMSN1.

    Entry informationi

    Entry nameiSAP30_MOUSE
    AccessioniPrimary (citable) accession number: O88574
    Secondary accession number(s): A2RSE9, Q99JB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3