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Q60520

- SIN3A_MOUSE

UniProt

Q60520 - SIN3A_MOUSE

Protein

Paired amphipathic helix protein Sin3a

Gene

Sin3a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.4 Publications

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA binding Source: MGI
    3. protein binding Source: UniProtKB
    4. protein deacetylase activity Source: Ensembl
    5. RNA polymerase II repressing transcription factor binding Source: MGI
    6. RNA polymerase II transcription corepressor activity Source: UniProtKB
    7. sequence-specific DNA binding transcription factor activity Source: MGI
    8. transcription corepressor activity Source: UniProtKB
    9. transcription factor binding Source: MGI
    10. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

    GO - Biological processi

    1. activation of innate immune response Source: Ensembl
    2. aging Source: Ensembl
    3. cellular protein localization Source: MGI
    4. cellular response to glucose stimulus Source: MGI
    5. DNA replication Source: MGI
    6. hematopoietic progenitor cell differentiation Source: MGI
    7. in utero embryonic development Source: MGI
    8. negative regulation of apoptotic process Source: MGI
    9. negative regulation of circadian rhythm Source: UniProtKB
    10. negative regulation of histone H3-K27 acetylation Source: Ensembl
    11. negative regulation of protein localization to nucleus Source: Ensembl
    12. negative regulation of transcription, DNA-templated Source: UniProtKB
    13. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    14. negative regulation of transcription regulatory region DNA binding Source: Ensembl
    15. positive regulation of chromatin silencing Source: Ensembl
    16. positive regulation of defense response to virus by host Source: Ensembl
    17. positive regulation of G2/M transition of mitotic cell cycle Source: MGI
    18. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    19. regulation of transcription, DNA-templated Source: MGI
    20. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
    21. response to methylglyoxal Source: MGI
    22. response to organonitrogen compound Source: Ensembl
    23. rhythmic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Paired amphipathic helix protein Sin3a
    Alternative name(s):
    Histone deacetylase complex subunit Sin3a
    Transcriptional corepressor Sin3a
    Gene namesi
    Name:Sin3a
    Synonyms:Kiaa4126
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:107157. Sin3a.

    Subcellular locationi

    Nucleus. Nucleusnucleolus
    Note: Recruited to the nucleolus by SAP30L.By similarity

    GO - Cellular componenti

    1. kinetochore Source: MGI
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. Sin3 complex Source: Ensembl
    5. transcriptional repressor complex Source: UniProtKB
    6. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi307 – 3071A → V: Greatly reduced binding to MAD; when associated with D-308 and A-311. 1 Publication
    Mutagenesisi308 – 3081I → D: Greatly reduced binding to MAD; when associated with V-307 and A-311. 1 Publication
    Mutagenesisi309 – 3091N → D: No effect on binding to MAD. 1 Publication
    Mutagenesisi311 – 3111V → A: Greatly reduced binding to MAD; when associated with V-307 and D-308. 1 Publication
    Mutagenesisi326 – 3261K → A: No effect on binding to MAD. 1 Publication
    Mutagenesisi329 – 3291L → A: Greatly reduced binding to MAD; when associated with A-332. 1 Publication
    Mutagenesisi332 – 3321L → A: Greatly reduced binding to MAD; when associated with A-329. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12741274Paired amphipathic helix protein Sin3aPRO_0000121538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101PhosphoserineBy similarity
    Modified residuei277 – 2771PhosphoserineBy similarity
    Modified residuei470 – 4701N6-acetyllysineBy similarity
    Modified residuei833 – 8331Phosphoserine2 Publications
    Modified residuei861 – 8611PhosphoserineBy similarity
    Modified residuei866 – 8661N6-acetyllysine1 Publication
    Modified residuei876 – 8761N6-acetyllysine1 Publication
    Modified residuei941 – 9411PhosphoserineBy similarity
    Modified residuei1113 – 11131PhosphoserineBy similarity

    Post-translational modificationi

    SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ60520.
    PaxDbiQ60520.
    PRIDEiQ60520.

    PTM databases

    PhosphoSiteiQ60520.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest levels in testis, lung and thymus.

    Gene expression databases

    ArrayExpressiQ60520.
    BgeeiQ60520.
    CleanExiMM_SIN3A.
    GenevestigatoriQ60520.

    Interactioni

    Subunit structurei

    Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1, SAP30L, SAP130, SFPQ and TOPORS. Interacts with OGT (via TPRs 1-6); the interaction mediates transcriptional repression in parallel with histone deacetylase By similarity. Interacts with BAZ2A, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3. Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30. Interacts with TET1; the interaction recruits SIN3A to gene promoters. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A.By similarity18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sap25Q1EHW44EBI-349034,EBI-937195
    Sap30O885746EBI-349034,EBI-593511
    Sox2P484323EBI-349034,EBI-2313612
    Suds3Q8BR654EBI-349034,EBI-591431
    Tet1Q3URK32EBI-349034,EBI-4291699

    Protein-protein interaction databases

    BioGridi203256. 58 interactions.
    DIPiDIP-469N.
    IntActiQ60520. 20 interactions.
    MINTiMINT-1510506.

    Structurei

    Secondary structure

    1
    1274
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi126 – 13611
    Helixi137 – 1393
    Helixi141 – 15515
    Helixi161 – 17111
    Turni172 – 1743
    Helixi176 – 1838
    Helixi302 – 31716
    Turni318 – 3203
    Helixi322 – 34423
    Beta strandi347 – 3493
    Helixi355 – 36511
    Turni366 – 3683
    Helixi370 – 3778
    Turni457 – 4604
    Helixi463 – 47513
    Helixi478 – 49215
    Helixi498 – 5047
    Helixi506 – 5094
    Helixi513 – 52311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G1ENMR-B295-383[»]
    1S5QNMR-B295-383[»]
    1S5RNMR-B295-383[»]
    2L9SNMR-B295-385[»]
    2LD7NMR-B456-528[»]
    2RMRNMR-A119-189[»]
    2RMSNMR-A119-189[»]
    ProteinModelPortaliQ60520.
    SMRiQ60520. Positions 119-189, 295-385, 454-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60520.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini119 – 18971PAH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 38384PAH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini457 – 52670PAH 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 19678Interaction with HCFC1By similarityAdd
    BLAST
    Regioni205 – 479275Interaction with RESTAdd
    BLAST
    Regioni459 – 52668Interaction with SAP30Add
    BLAST
    Regioni524 – 851328Interaction with NCOR1Add
    BLAST
    Regioni525 – 660136Interactions with SUDS3 and SAP130By similarityAdd
    BLAST
    Regioni688 – 830143Interactions with HDAC1 and ARID4BBy similarityAdd
    BLAST
    Regioni889 – 96880Interaction with OGTBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili904 – 93330Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi207 – 26559Gln-richAdd
    BLAST
    Compositional biasi218 – 28568Pro-richAdd
    BLAST
    Compositional biasi836 – 8427Poly-Glu

    Sequence similaritiesi

    Contains 3 PAH (paired amphipathic helix) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5602.
    GeneTreeiENSGT00390000007239.
    HOVERGENiHBG060425.
    InParanoidiQ570Z7.
    KOiK11644.
    OMAiNDHGGTA.
    OrthoDBiEOG7SV0TV.
    PhylomeDBiQ60520.
    TreeFamiTF106187.

    Family and domain databases

    Gene3Di1.20.1160.11. 3 hits.
    InterProiIPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view]
    PfamiPF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view]
    SMARTiSM00761. HDAC_interact. 1 hit.
    [Graphical view]
    SUPFAMiSSF47762. SSF47762. 3 hits.
    PROSITEiPS51477. PAH. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60520-2) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKRRLDDQES PVYAAQQRRI PGSTEAFSHQ HRVLAPAPPV YEAVSETMQS     50
    ATGIQYSVAP NYQVSAVPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ 100
    SHAHPAPPVA PVQGQQQFQR LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI 150
    MKEFKSQSID TPGVISRVSQ LFKGHPDLIM GFNTFLPPGY KIEVQTNDMV 200
    NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SSQSAPTPAQ PAPQPTAAKV 250
    SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ 300
    PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT 350
    PALTEQEVYA QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV 400
    RNDHGGTVKK PQLNNKPQRP SQNGCQIRRH SGTGATPPVK KKPKLMSLKE 450
    SSMADASKHG VGTESLFFDK VRKALRSAEA YENFLRCLVI FNQEVISRAE 500
    LVQLVSPFLG KFPELFNWFK NFLGYKESVH LESFPKERAT EGIAMEIDYA 550
    SCKRLGSSYR ALPKSYQQPK CTGRTPLCKE VLNDTWVSFP SWSEDSTFVS 600
    SKKTQYEEHI YRCEDERFEL DVVLETNLAT IRVLEAIQKK LSRLSAEEQA 650
    KFRLDNTLGG TSEVIHRKAL QRIYADKAAD IIDGLRKNPS IAVPIVLKRL 700
    KMKEEEWREA QRGFNKVWRE QNEKYYLKSL DHQGINFKQN DTKVLRSKSL 750
    LNEIESIYDE RQEQATEENA GVPVGPHLSL AYEDKQILED AAALIIHHVK 800
    RQTGIQKEDK YKIKQIMHHF IPDLLFAQRG DLSDVEEEEE EEMDVDEATG 850
    APKKHNGVGG SPPKSKLLFS NTAAQKLRGM DEVYNLFYVN NNWYIFMRLH 900
    QILCLRLLRI CSQAERQIEE ENREREWERE VLGIKRDKSD SPAIQLRLKE 950
    PMDVDVEDYY PAFLDMVRSL LDGNIDSSQY EDSLREMFTI HAYIAFTMDK 1000
    LIQSIVRQLQ HIVSDEVCVQ VTDLYLAENN NGATGGQLNS QTSRSLLESA 1050
    YQRKAEQLMS DENCFKLMFI QSQGQVQLTV ELLDTEEENS DDPVEAERWS 1100
    DYVERYMSSD TTSPELREHL AQKPVFLPRN LRRIRKCQRG REQQEKEGKE 1150
    GNSKKTMENV ESLDKLECRF KLNSYKMVYV IKSEDYMYRR TALLRAHQSH 1200
    ERVSKRLHQR FQAWVDKWTK EHVPREMAAE TSKWLMGEGL EGLVPCTTTC 1250
    DTETLHFVSI NKYRVKYGTV FKAP 1274
    Length:1,274
    Mass (Da):145,088
    Last modified:October 5, 2010 - v3
    Checksum:i80FE378F62ED7CB3
    GO
    Isoform 2 (identifier: Q60520-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1097-1097: E → EVWT

    Show »
    Length:1,277
    Mass (Da):145,474
    Checksum:iF578FED21F4824D3
    GO

    Sequence cautioni

    The sequence AAB01610.1 differs from that shown. Reason: The cDNA contains an internal 15bp tandem duplication.
    The sequence AAH52716.1 differs from that shown. Reason: Probable cloning artifact leading to an internal deletion.
    The sequence AAH53385.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAD90217.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441Y → H in AAB01610. (PubMed:7601471)Curated
    Sequence conflicti154 – 1541F → L in AAH53385. (PubMed:15489334)Curated
    Sequence conflicti303 – 3031E → H in AAB01610. (PubMed:7601471)Curated
    Sequence conflicti514 – 5141E → G in AAH53385. (PubMed:15489334)Curated
    Sequence conflicti720 – 7212EQ → DE in AAB01610. (PubMed:7601471)Curated
    Sequence conflicti827 – 8271A → D in AAA89119. (PubMed:8649810)Curated
    Sequence conflicti899 – 8991L → R in AAH52716. (PubMed:15489334)Curated
    Sequence conflicti912 – 9121S → F in AAH52716. (PubMed:15489334)Curated
    Sequence conflicti969 – 9691S → Q in AAB01610. (PubMed:7601471)Curated
    Sequence conflicti1047 – 10471L → V in AAB01610. (PubMed:7601471)Curated
    Sequence conflicti1205 – 12073KRL → QGK in AAA69773. (PubMed:7889570)Curated
    Sequence conflicti1205 – 12051K → KK in AAA69772. (PubMed:7889570)Curated
    Sequence conflicti1215 – 12162VD → GK in AAA69772. (PubMed:7889570)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1097 – 10971E → EVWT in isoform 2. 3 PublicationsVSP_039918

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36831 mRNA. Translation: AAB01610.1. Sequence problems.
    U22394 mRNA. Translation: AAA89119.1.
    AK220292 mRNA. Translation: BAD90217.1. Different initiation.
    BC052716 mRNA. Translation: AAH52716.1. Sequence problems.
    BC053385 mRNA. Translation: AAH53385.1. Sequence problems.
    L38620 mRNA. Translation: AAA69773.2.
    L38621 mRNA. Translation: AAA69772.2.
    CCDSiCCDS23216.1. [Q60520-2]
    CCDS52805.1. [Q60520-1]
    PIRiA56068.
    I61713.
    RefSeqiNP_001103820.1. NM_001110350.1. [Q60520-1]
    NP_001103821.1. NM_001110351.1. [Q60520-2]
    NP_035508.2. NM_011378.2. [Q60520-2]
    XP_006510953.1. XM_006510890.1. [Q60520-1]
    XP_006510954.1. XM_006510891.1. [Q60520-1]
    XP_006510955.1. XM_006510892.1. [Q60520-1]
    XP_006510956.1. XM_006510893.1. [Q60520-1]
    UniGeneiMm.15755.

    Genome annotation databases

    EnsembliENSMUST00000049169; ENSMUSP00000045044; ENSMUSG00000042557. [Q60520-2]
    ENSMUST00000167715; ENSMUSP00000130641; ENSMUSG00000042557. [Q60520-2]
    ENSMUST00000168177; ENSMUSP00000130221; ENSMUSG00000042557. [Q60520-1]
    ENSMUST00000168502; ENSMUSP00000128956; ENSMUSG00000042557. [Q60520-1]
    ENSMUST00000168678; ENSMUSP00000126601; ENSMUSG00000042557. [Q60520-2]
    GeneIDi20466.
    KEGGimmu:20466.
    UCSCiuc009ptx.2. mouse. [Q60520-1]
    uc012gtw.1. mouse. [Q60520-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36831 mRNA. Translation: AAB01610.1 . Sequence problems.
    U22394 mRNA. Translation: AAA89119.1 .
    AK220292 mRNA. Translation: BAD90217.1 . Different initiation.
    BC052716 mRNA. Translation: AAH52716.1 . Sequence problems.
    BC053385 mRNA. Translation: AAH53385.1 . Sequence problems.
    L38620 mRNA. Translation: AAA69773.2 .
    L38621 mRNA. Translation: AAA69772.2 .
    CCDSi CCDS23216.1. [Q60520-2 ]
    CCDS52805.1. [Q60520-1 ]
    PIRi A56068.
    I61713.
    RefSeqi NP_001103820.1. NM_001110350.1. [Q60520-1 ]
    NP_001103821.1. NM_001110351.1. [Q60520-2 ]
    NP_035508.2. NM_011378.2. [Q60520-2 ]
    XP_006510953.1. XM_006510890.1. [Q60520-1 ]
    XP_006510954.1. XM_006510891.1. [Q60520-1 ]
    XP_006510955.1. XM_006510892.1. [Q60520-1 ]
    XP_006510956.1. XM_006510893.1. [Q60520-1 ]
    UniGenei Mm.15755.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G1E NMR - B 295-383 [» ]
    1S5Q NMR - B 295-383 [» ]
    1S5R NMR - B 295-383 [» ]
    2L9S NMR - B 295-385 [» ]
    2LD7 NMR - B 456-528 [» ]
    2RMR NMR - A 119-189 [» ]
    2RMS NMR - A 119-189 [» ]
    ProteinModelPortali Q60520.
    SMRi Q60520. Positions 119-189, 295-385, 454-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203256. 58 interactions.
    DIPi DIP-469N.
    IntActi Q60520. 20 interactions.
    MINTi MINT-1510506.

    PTM databases

    PhosphoSitei Q60520.

    Proteomic databases

    MaxQBi Q60520.
    PaxDbi Q60520.
    PRIDEi Q60520.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049169 ; ENSMUSP00000045044 ; ENSMUSG00000042557 . [Q60520-2 ]
    ENSMUST00000167715 ; ENSMUSP00000130641 ; ENSMUSG00000042557 . [Q60520-2 ]
    ENSMUST00000168177 ; ENSMUSP00000130221 ; ENSMUSG00000042557 . [Q60520-1 ]
    ENSMUST00000168502 ; ENSMUSP00000128956 ; ENSMUSG00000042557 . [Q60520-1 ]
    ENSMUST00000168678 ; ENSMUSP00000126601 ; ENSMUSG00000042557 . [Q60520-2 ]
    GeneIDi 20466.
    KEGGi mmu:20466.
    UCSCi uc009ptx.2. mouse. [Q60520-1 ]
    uc012gtw.1. mouse. [Q60520-2 ]

    Organism-specific databases

    CTDi 25942.
    MGIi MGI:107157. Sin3a.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5602.
    GeneTreei ENSGT00390000007239.
    HOVERGENi HBG060425.
    InParanoidi Q570Z7.
    KOi K11644.
    OMAi NDHGGTA.
    OrthoDBi EOG7SV0TV.
    PhylomeDBi Q60520.
    TreeFami TF106187.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

    EvolutionaryTracei Q60520.
    NextBioi 298567.
    PROi Q60520.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60520.
    Bgeei Q60520.
    CleanExi MM_SIN3A.
    Genevestigatori Q60520.

    Family and domain databases

    Gene3Di 1.20.1160.11. 3 hits.
    InterProi IPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view ]
    Pfami PF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view ]
    SMARTi SM00761. HDAC_interact. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47762. SSF47762. 3 hits.
    PROSITEi PS51477. PAH. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A widely distributed putative mammalian transcriptional regulator containing multiple paired amphipathic helices, with similarity to yeast SIN3."
      Halleck M.S., Pownall S., Harder K.W., Duncan A.M.V., Jirik F.R., Schlegel R.A.
      Genomics 26:403-406(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: 129.
      Tissue: Teratocarcinoma.
    2. "Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression of the Myc antagonist Mxi1."
      Rao G., Alland L., Guida P., Schreiber-Agus N., Chin L., Chen K., Rochelle J.M., Seldin M.F., Skoultchi A.I., DePinho R.A.
      Oncogene 12:1165-1172(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MXI1.
      Strain: ICR.
      Tissue: Brain.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Pancreatic islet.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1146 (ISOFORM 1).
      Strain: C57BL/6Imported.
      Tissue: BrainImported and EggImported.
    5. "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3."
      Ayer D.E., Lawrence Q.A., Eisenman R.N.
      Cell 80:767-776(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1216 (ISOFORM 1), FUNCTION, INTERACTION WITH MXD1.
      Tissue: Embryo.
    6. Ayer D.E., Lawrence Q.A., Eisenman R.N.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    7. "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation."
      Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
      EMBO J. 14:5646-5659(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MXD3 AND MXD4.
    8. Cited for: INTERACTION WITH NCOR1.
    9. "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: INTERACTION WITH SAP30 AND NCOR1.
    10. "The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A."
      Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.
      J. Biol. Chem. 275:34963-34967(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD2.
    11. "The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex."
      Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C., Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.
      J. Biol. Chem. 275:9461-9467(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH REST.
    12. "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex."
      Yochum G.S., Ayer D.E.
      Mol. Cell. Biol. 21:4110-4118(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHF12.
    13. "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
      Zhou Y., Santoro R., Grummt I.
      EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAZ2A.
    14. "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex."
      Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.
      Mol. Cell. Biol. 22:2743-2750(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUDS3.
    15. "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors."
      Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M., Scheffner M., Bach I.
      Nature 416:99-103(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RLIM.
    16. "Tissue-specific regulation of retinal and pituitary precursor cell proliferation."
      Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.
      Science 297:1180-1183(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DACH1.
    17. "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."
      Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.
      Biochem. J. 369:651-657(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    19. "Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex."
      Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.
      Mol. Cancer 5:26-26(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMYD2.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    21. "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression."
      Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., Smidt M.P.
      Development 136:531-540(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR4A2.
    22. "TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity."
      Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A., Rappsilber J., Helin K.
      Nature 473:343-348(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TET1.
    23. "A molecular mechanism for circadian clock negative feedback."
      Duong H.A., Robles M.S., Knutti D., Weitz C.J.
      Science 332:1436-1439(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX.
    24. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-866 AND LYS-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    25. "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex."
      Brubaker K., Cowley S.M., Huang K., Loo L., Yochum G.S., Ayer D.E., Eisenman R.N., Radhakrishnan I.
      Cell 103:655-665(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 295-383 IN COMPLEX WITH MXD1, MUTAGENESIS OF ALA-307; ILE-308; ASN-309; VAL-311; LYS-326; LEU-329 AND LEU-332.

    Entry informationi

    Entry nameiSIN3A_MOUSE
    AccessioniPrimary (citable) accession number: Q60520
    Secondary accession number(s): Q570Z7
    , Q60820, Q62139, Q62140, Q7TPU8, Q7TSZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 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