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Q60520 (SIN3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paired amphipathic helix protein Sin3a
Alternative name(s):
Histone deacetylase complex subunit Sin3a
Transcriptional corepressor Sin3a
Gene names
Name:Sin3a
Synonyms:Kiaa4126
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1274 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.5 Ref.12 Ref.24

Subunit structure

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. Ref.2 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23 Ref.24

Subcellular location

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

Tissue specificity

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

Post-translational modification

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

Sequence similarities

Contains 3 PAH (paired amphipathic helix) domains.

Sequence caution

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.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from mutant phenotype PubMed 15998811. Source: MGI

activation of innate immune response

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

cellular protein localization

Inferred from mutant phenotype PubMed 15998811. Source: MGI

cellular response to glucose stimulus

Inferred from direct assay PubMed 17670746. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from mutant phenotype PubMed 24029230. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 15998811. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15998811. Source: MGI

negative regulation of circadian rhythm

Inferred from mutant phenotype Ref.24. Source: UniProtKB

negative regulation of histone H3-K27 acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 10431247PubMed 12649481Ref.5. Source: MGI

negative regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.12Ref.5. Source: UniProtKB

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15998811. Source: MGI

positive regulation of chromatin silencing

Inferred from electronic annotation. Source: Ensembl

positive regulation of defense response to virus by host

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 15998811. Source: MGI

response to methylglyoxal

Inferred from direct assay PubMed 17670746. Source: MGI

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSin3 complex

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from direct assay PubMed 14519686. Source: MGI

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.12Ref.2. Source: UniProtKB

transcription factor complex

Inferred from physical interaction PubMed 17182846. Source: MGI

transcriptional repressor complex

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 14593184PubMed 15998811. Source: MGI

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 19235719. Source: MGI

RNA polymerase II transcription corepressor activity

Inferred from genetic interaction Ref.12. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 17074803PubMed 18212064. Source: MGI

protein binding

Inferred from physical interaction Ref.12Ref.13Ref.16Ref.15Ref.14Ref.20Ref.22Ref.24Ref.5Ref.2Ref.10. Source: UniProtKB

protein deacetylase activity

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 15998811. Source: MGI

transcription corepressor activity

Inferred from direct assay Ref.12Ref.5. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 14593184PubMed 15767674. Source: MGI

transcription regulatory region sequence-specific DNA binding

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q60520-2)

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.
Isoform 2 (identifier: Q60520-1)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12741274Paired amphipathic helix protein Sin3a
PRO_0000121538

Regions

Domain119 – 18971PAH 1
Domain300 – 38384PAH 2
Domain457 – 52670PAH 3
Region119 – 19678Interaction with HCFC1 By similarity UniProtKB Q96ST3
Region205 – 479275Interaction with REST
Region459 – 52668Interaction with SAP30
Region524 – 851328Interaction with NCOR1
Region525 – 660136Interactions with SUDS3 and SAP130 By similarity
Region688 – 830143Interactions with HDAC1 and ARID4B By similarity
Region889 – 96880Interaction with OGT By similarity
Coiled coil904 – 93330 Potential
Compositional bias207 – 26559Gln-rich
Compositional bias218 – 28568Pro-rich
Compositional bias836 – 8427Poly-Glu

Amino acid modifications

Modified residue101Phosphoserine By similarity
Modified residue2771Phosphoserine By similarity
Modified residue4701N6-acetyllysine By similarity
Modified residue8331Phosphoserine Ref.19 Ref.21 UniProtKB Q96ST3
Modified residue8611Phosphoserine By similarity UniProtKB Q96ST3
Modified residue8661N6-acetyllysine Ref.25
Modified residue8761N6-acetyllysine Ref.25
Modified residue9411Phosphoserine By similarity
Modified residue11131Phosphoserine By similarity

Natural variations

Alternative sequence10971E → EVWT in isoform 2.
VSP_039918

Experimental info

Mutagenesis3071A → V: Greatly reduced binding to MAD; when associated with D-308 and A-311. Ref.26
Mutagenesis3081I → D: Greatly reduced binding to MAD; when associated with V-307 and A-311. Ref.26
Mutagenesis3091N → D: No effect on binding to MAD. Ref.26
Mutagenesis3111V → A: Greatly reduced binding to MAD; when associated with V-307 and D-308. Ref.26
Mutagenesis3261K → A: No effect on binding to MAD. Ref.26
Mutagenesis3291L → A: Greatly reduced binding to MAD; when associated with A-332. Ref.26
Mutagenesis3321L → A: Greatly reduced binding to MAD; when associated with A-329. Ref.26
Sequence conflict1441Y → H in AAB01610. Ref.1
Sequence conflict1541F → L in AAH53385. Ref.4
Sequence conflict3031E → H in AAB01610. Ref.1
Sequence conflict5141E → G in AAH53385. Ref.4
Sequence conflict720 – 7212EQ → DE in AAB01610. Ref.1
Sequence conflict8271A → D in AAA89119. Ref.2
Sequence conflict8991L → R in AAH52716. Ref.4
Sequence conflict9121S → F in AAH52716. Ref.4
Sequence conflict9691S → Q in AAB01610. Ref.1
Sequence conflict10471L → V in AAB01610. Ref.1
Sequence conflict1205 – 12073KRL → QGK in AAA69773. Ref.5
Sequence conflict12051K → KK in AAA69772. Ref.5
Sequence conflict1215 – 12162VD → GK in AAA69772. Ref.5

Secondary structure

................................... 1274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 80FE378F62ED7CB3

FASTA1,274145,088
        10         20         30         40         50         60 
MKRRLDDQES PVYAAQQRRI PGSTEAFSHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVAP 

        70         80         90        100        110        120 
NYQVSAVPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR 

       130        140        150        160        170        180 
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM 

       190        200        210        220        230        240 
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SSQSAPTPAQ 

       250        260        270        280        290        300 
PAPQPTAAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ 

       310        320        330        340        350        360 
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA 

       370        380        390        400        410        420 
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP 

       430        440        450        460        470        480 
SQNGCQIRRH SGTGATPPVK KKPKLMSLKE SSMADASKHG VGTESLFFDK VRKALRSAEA 

       490        500        510        520        530        540 
YENFLRCLVI FNQEVISRAE LVQLVSPFLG KFPELFNWFK NFLGYKESVH LESFPKERAT 

       550        560        570        580        590        600 
EGIAMEIDYA SCKRLGSSYR ALPKSYQQPK CTGRTPLCKE VLNDTWVSFP SWSEDSTFVS 

       610        620        630        640        650        660 
SKKTQYEEHI YRCEDERFEL DVVLETNLAT IRVLEAIQKK LSRLSAEEQA KFRLDNTLGG 

       670        680        690        700        710        720 
TSEVIHRKAL QRIYADKAAD IIDGLRKNPS IAVPIVLKRL KMKEEEWREA QRGFNKVWRE 

       730        740        750        760        770        780 
QNEKYYLKSL DHQGINFKQN DTKVLRSKSL LNEIESIYDE RQEQATEENA GVPVGPHLSL 

       790        800        810        820        830        840 
AYEDKQILED AAALIIHHVK RQTGIQKEDK YKIKQIMHHF IPDLLFAQRG DLSDVEEEEE 

       850        860        870        880        890        900 
EEMDVDEATG APKKHNGVGG SPPKSKLLFS NTAAQKLRGM DEVYNLFYVN NNWYIFMRLH 

       910        920        930        940        950        960 
QILCLRLLRI CSQAERQIEE ENREREWERE VLGIKRDKSD SPAIQLRLKE PMDVDVEDYY 

       970        980        990       1000       1010       1020 
PAFLDMVRSL LDGNIDSSQY EDSLREMFTI HAYIAFTMDK LIQSIVRQLQ HIVSDEVCVQ 

      1030       1040       1050       1060       1070       1080 
VTDLYLAENN NGATGGQLNS QTSRSLLESA YQRKAEQLMS DENCFKLMFI QSQGQVQLTV 

      1090       1100       1110       1120       1130       1140 
ELLDTEEENS DDPVEAERWS DYVERYMSSD TTSPELREHL AQKPVFLPRN LRRIRKCQRG 

      1150       1160       1170       1180       1190       1200 
REQQEKEGKE GNSKKTMENV ESLDKLECRF KLNSYKMVYV IKSEDYMYRR TALLRAHQSH 

      1210       1220       1230       1240       1250       1260 
ERVSKRLHQR FQAWVDKWTK EHVPREMAAE TSKWLMGEGL EGLVPCTTTC DTETLHFVSI 

      1270 
NKYRVKYGTV FKAP 

« Hide

Isoform 2 [UniParc].

Checksum: F578FED21F4824D3
Show »

FASTA1,277145,474

References

« Hide 'large scale' references
[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/6.
Tissue: Brain and Egg.
[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]Erratum
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
EMBO J. 15:2030-2030(1996) [PubMed] [Europe PMC] [Abstract]
[9]"A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression."
Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.
Nature 387:43-48(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOR1.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23216.1. [Q60520-2]
CCDS52805.1. [Q60520-1]
PIRA56068.
I61713.
RefSeqNP_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]
UniGeneMm.15755.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1ENMR-B295-383[»]
1S5QNMR-B295-383[»]
1S5RNMR-B295-383[»]
2L9SNMR-B295-385[»]
2LD7NMR-B456-528[»]
2RMRNMR-A119-189[»]
2RMSNMR-A119-189[»]
ProteinModelPortalQ60520.
SMRQ60520. Positions 119-189, 295-385, 454-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203256. 58 interactions.
DIPDIP-469N.
IntActQ60520. 20 interactions.
MINTMINT-1510506.

PTM databases

PhosphoSiteQ60520.

Proteomic databases

MaxQBQ60520.
PaxDbQ60520.
PRIDEQ60520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049169; ENSMUSP00000045044; ENSMUSG00000042557. [Q60520-2]
ENSMUST00000167715; ENSMUSP00000130641; ENSMUSG00000042557. [Q60520-2]
ENSMUST00000168177; ENSMUSP00000130221; ENSMUSG00000042557. [Q60520-1]
ENSMUST00000168502; ENSMUSP00000128956; ENSMUSG00000042557. [Q60520-1]
ENSMUST00000168678; ENSMUSP00000126601; ENSMUSG00000042557. [Q60520-2]
GeneID20466.
KEGGmmu:20466.
UCSCuc009ptx.2. mouse. [Q60520-1]
uc012gtw.1. mouse. [Q60520-2]

Organism-specific databases

CTD25942.
MGIMGI:107157. Sin3a.
RougeSearch...

Phylogenomic databases

eggNOGCOG5602.
GeneTreeENSGT00390000007239.
HOVERGENHBG060425.
InParanoidQ570Z7.
KOK11644.
OMANDHGGTA.
OrthoDBEOG7SV0TV.
PhylomeDBQ60520.
TreeFamTF106187.

Enzyme and pathway databases

ReactomeREACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ60520.
BgeeQ60520.
CleanExMM_SIN3A.
GenevestigatorQ60520.

Family and domain databases

Gene3D1.20.1160.11. 3 hits.
InterProIPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]
PfamPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]
SMARTSM00761. HDAC_interact. 1 hit.
[Graphical view]
SUPFAMSSF47762. SSF47762. 3 hits.
PROSITEPS51477. PAH. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60520.
NextBio298567.
PROQ60520.
SOURCESearch...

Entry information

Entry nameSIN3A_MOUSE
AccessionPrimary (citable) accession number: Q60520
Secondary accession number(s): Q570Z7 expand/collapse secondary AC list , Q60820, Q62139, Q62140, Q7TPU8, Q7TSZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 140 of the entry and version 3 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