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Q60520

- SIN3A_MOUSE

UniProt

Q60520 - SIN3A_MOUSE

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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

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 deacetylase activity Source: Ensembl
  4. RNA polymerase II repressing transcription factor binding Source: MGI
  5. RNA polymerase II transcription corepressor activity Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: MGI
  7. transcription corepressor activity Source: UniProtKB
  8. transcription factor binding Source: MGI
  9. 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
Complete GO annotation...

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. cytoplasm Source: Ensembl
  2. intercellular bridge Source: Ensembl
  3. kinetochore Source: MGI
  4. nucleus Source: UniProtKB
  5. Sin3 complex Source: Ensembl
  6. transcriptional repressor complex Source: UniProtKB
  7. transcription factor complex Source: MGI
Complete GO annotation...

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

BgeeiQ60520.
CleanExiMM_SIN3A.
ExpressionAtlasiQ60520. baseline and differential.
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. Interacts with KLF11.By similarity19 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.
InParanoidiQ60520.
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

        10         20         30         40         50
MKRRLDDQES PVYAAQQRRI PGSTEAFSHQ HRVLAPAPPV YEAVSETMQS
60 70 80 90 100
ATGIQYSVAP NYQVSAVPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ
110 120 130 140 150
SHAHPAPPVA PVQGQQQFQR LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI
160 170 180 190 200
MKEFKSQSID TPGVISRVSQ LFKGHPDLIM GFNTFLPPGY KIEVQTNDMV
210 220 230 240 250
NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SSQSAPTPAQ PAPQPTAAKV
260 270 280 290 300
SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ
310 320 330 340 350
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT
360 370 380 390 400
PALTEQEVYA QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV
410 420 430 440 450
RNDHGGTVKK PQLNNKPQRP SQNGCQIRRH SGTGATPPVK KKPKLMSLKE
460 470 480 490 500
SSMADASKHG VGTESLFFDK VRKALRSAEA YENFLRCLVI FNQEVISRAE
510 520 530 540 550
LVQLVSPFLG KFPELFNWFK NFLGYKESVH LESFPKERAT EGIAMEIDYA
560 570 580 590 600
SCKRLGSSYR ALPKSYQQPK CTGRTPLCKE VLNDTWVSFP SWSEDSTFVS
610 620 630 640 650
SKKTQYEEHI YRCEDERFEL DVVLETNLAT IRVLEAIQKK LSRLSAEEQA
660 670 680 690 700
KFRLDNTLGG TSEVIHRKAL QRIYADKAAD IIDGLRKNPS IAVPIVLKRL
710 720 730 740 750
KMKEEEWREA QRGFNKVWRE QNEKYYLKSL DHQGINFKQN DTKVLRSKSL
760 770 780 790 800
LNEIESIYDE RQEQATEENA GVPVGPHLSL AYEDKQILED AAALIIHHVK
810 820 830 840 850
RQTGIQKEDK YKIKQIMHHF IPDLLFAQRG DLSDVEEEEE EEMDVDEATG
860 870 880 890 900
APKKHNGVGG SPPKSKLLFS NTAAQKLRGM DEVYNLFYVN NNWYIFMRLH
910 920 930 940 950
QILCLRLLRI CSQAERQIEE ENREREWERE VLGIKRDKSD SPAIQLRLKE
960 970 980 990 1000
PMDVDVEDYY PAFLDMVRSL LDGNIDSSQY EDSLREMFTI HAYIAFTMDK
1010 1020 1030 1040 1050
LIQSIVRQLQ HIVSDEVCVQ VTDLYLAENN NGATGGQLNS QTSRSLLESA
1060 1070 1080 1090 1100
YQRKAEQLMS DENCFKLMFI QSQGQVQLTV ELLDTEEENS DDPVEAERWS
1110 1120 1130 1140 1150
DYVERYMSSD TTSPELREHL AQKPVFLPRN LRRIRKCQRG REQQEKEGKE
1160 1170 1180 1190 1200
GNSKKTMENV ESLDKLECRF KLNSYKMVYV IKSEDYMYRR TALLRAHQSH
1210 1220 1230 1240 1250
ERVSKRLHQR FQAWVDKWTK EHVPREMAAE TSKWLMGEGL EGLVPCTTTC
1260 1270
DTETLHFVSI NKYRVKYGTV FKAP
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 Q60520.
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

Bgeei Q60520.
CleanExi MM_SIN3A.
ExpressionAtlasi Q60520. baseline and differential.
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

« Hide 'large scale' publications
  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. Cited for: INTERACTION WITH KLF11.
  20. "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.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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 29, 2014
This is version 143 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