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Q62141 (SIN3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. 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 Sin3b
Alternative name(s):
Histone deacetylase complex subunit Sin3b
Transcriptional corepressor Sin3b
Gene names
Name:Sin3b
Synonyms:Kiaa0700
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1098 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. Ref.1 Ref.2

Subunit structure

Interacts with HCFC1 By similarity. Interacts with FOXK1/MNF, MXI1, MAD, NCOR1 and SAP30. Interaction with SUDS3 enhances the interaction with HDAC1 to form a complex. Interacts with MAD3, MAD4, MAEL, REST and SETDB1. Interacts with RNF220. Ref.1 Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Nucleus Ref.1 Ref.12.

Post-translational modification

Ubiquitinated by RNF220 that leads to proteasomal degradation. Ref.12

Sequence similarities

Contains 3 PAH (paired amphipathic helix) domains.

Sequence caution

The sequence BAD32283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q62141-4)

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.
Note: No experimental confirmation available.
Isoform 1 (identifier: Q62141-1)

The sequence of this isoform differs from the canonical sequence as follows:
     955-1098: Missing.
Isoform 2 (identifier: Q62141-2)

The sequence of this isoform differs from the canonical sequence as follows:
     275-293: KKMKLRGTKDLSIAAVGKY → VGLQLKCAVVWFGYCTAEE
     294-954: Missing.
     955-1098: Missing.
Isoform 3 (identifier: Q62141-3)

The sequence of this isoform differs from the canonical sequence as follows:
     275-302: KKMKLRGTKDLSIAAVGKYGTLQEFSFF → VLVHVWVLPAHGRSGVEAQAAGEPEARA
     303-954: Missing.
     955-1098: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Paired amphipathic helix protein Sin3b
PRO_0000121540

Regions

Domain30 – 10071PAH 1
Domain145 – 23086PAH 2
Domain283 – 36078PAH 3
Region52 – 9847Interaction with REST
Region275 – 499225Interaction with NCOR1
Region383 – 550168Interaction with SUDS3 and HDAC1

Natural variations

Alternative sequence275 – 30228KKMKL…EFSFF → VLVHVWVLPAHGRSGVEAQA AGEPEARA in isoform 3.
VSP_008227
Alternative sequence275 – 29319KKMKL…AVGKY → VGLQLKCAVVWFGYCTAEE in isoform 2.
VSP_008225
Alternative sequence294 – 954661Missing in isoform 2.
VSP_008226
Alternative sequence303 – 954652Missing in isoform 3.
VSP_008228
Alternative sequence955 – 1098144Missing in isoform 1, isoform 2 and isoform 3.
VSP_014187

Experimental info

Sequence conflict2301A → G in AAC04821. Ref.2
Sequence conflict2331S → P in AAC04821. Ref.2

Secondary structure

........................... 1098
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: A73F6DFC11EBA256

FASTA1,098126,405
        10         20         30         40         50         60 
MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE 

        70         80         90        100        110        120 
IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ 

       130        140        150        160        170        180 
DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE 

       190        200        210        220        230        240 
ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS 

       250        260        270        280        290        300 
CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKKKMKLR GTKDLSIAAV GKYGTLQEFS 

       310        320        330        340        350        360 
FFDKVRRVLK SQEVYENFLR CIALFNQELV SGSELLQLVS PFLGKFPELF AQFKSFLGVK 

       370        380        390        400        410        420 
ELSFAPPMSD RSGDGISREI DYASCKRIGS SYRALPKTYQ QPKCSGRTAI CKEVLNDTWV 

       430        440        450        460        470        480 
SFPSWSEDST FVSSKKTPYE EQLHRCEDER FELDVVLETN LATIRVLESV QKKLSRMAPE 

       490        500        510        520        530        540 
DQEKLRLDDC LGGTSEVIQR RAIHRIYGDK APEVIESLKR NPATAVPVVL KRLKAKEEEW 

       550        560        570        580        590        600 
REAQQGFNKI WREQYEKAYL KSLDHQAVNF KQNDTKALRS KSLLNEIESV YDEHQEQHSE 

       610        620        630        640        650        660 
GRSAPSSEPH LIFVYEDRQI LEDAAALISY YVKRQPAIQK EDQGTIRQLL HRFLPSLFFS 

       670        680        690        700        710        720 
QQCPGTSDDS ADERDRDRDS AEPERRRPTD EKPPADASPE PPKVLDDVYS LFFANNNWYF 

       730        740        750        760        770        780 
FLRLHQTLCA RLLKIYRQAQ KQLLEHRREQ EREQLLCEGR REKAADPAME LRLKQPSEVE 

       790        800        810        820        830        840 
LEEYYPAFLD MVRSLLEGSI DPTQYEDTLR EMFTIHAYIG FTMDKLVQNI ARQLHHLVSD 

       850        860        870        880        890        900 
DVCLKVVELY LNEQQRGAAG GNLSSRCVRA ARETSYQWKA ERCMADENCF KVMFLQRRGQ 

       910        920        930        940        950        960 
VIMTIELLDT EEAQTEDPVE VQHLARYVEQ YVGSEGASSS STEGFLLKPV FLQRNLKKFR 

       970        980        990       1000       1010       1020 
RWQCEQVRAM RGEAKSSWKR LMGVESACDV DCRFRLGTHK MVFIVNSEDY MYRRGTLCRA 

      1030       1040       1050       1060       1070       1080 
KQVQPLVLLR HHRHFEEWHG RWLEDNVTVA AAGLVQDWLM GEEEEDMVPC KTLCETAHVH 

      1090 
GLPVTRYRVQ YSRRPASP 

« Hide

Isoform 1 [UniParc].

Checksum: 31F4BE14523EA213
Show »

FASTA954109,393
Isoform 2 [UniParc].

Checksum: 11A75E8F67C818AE
Show »

FASTA29332,846
Isoform 3 [UniParc].

Checksum: 421131CCD87C88F8
Show »

FASTA30233,637

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
Tissue: Embryonic kidney.
[2]"The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian Sin3B."
Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S.
Biochem. J. 345:335-343(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH FOXK1.
Tissue: Heart.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[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] (ISOFORMS 2 AND 3).
Tissue: Mammary gland and Salivary gland.
[5]"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 MAD3 AND MAD4.
[6]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]
[7]"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.
[8]"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.
[9]"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 AND HDAC1.
[10]"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.
[11]"Mouse MAELSTROM: the link between meiotic silencing of unsynapsed chromatin and microRNA pathway?"
Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A., Cooke H.J.
Hum. Mol. Genet. 15:2324-2334(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAEL.
[12]"RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination."
Kong Q., Zeng W., Wu J., Hu W., Li C., Mao B.
Biochem. Biophys. Res. Commun. 393:708-713(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF220, SUBCELLULAR LOCATION, UBIQUITINATION.
[13]"The Mad1-Sin3B interaction involves a novel helical fold."
Spronk C.A.E., Tessari M., Kaan A.M., Jansen J.F.A., Vermeulen M., Stunnenberg H.G., Vuister G.W.
Nat. Struct. Biol. 7:1100-1104(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 148-232 IN COMPLEX WITH MAD1.
[14]"The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix."
Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.
J. Mol. Biol. 354:903-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 31-107 IN COMPLEX WITH REST, INTERACTION WITH REST.
[15]"Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 32-100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38622 mRNA. Translation: AAA69774.1.
AF038848 mRNA. Translation: AAC04821.1.
AK173005 mRNA. Translation: BAD32283.1. Different initiation.
BC020049 mRNA. Translation: AAH20049.1.
BC021160 mRNA. Translation: AAH21160.1.
PIRI61714.
RefSeqNP_001106719.1. NM_001113248.2.
NP_033214.2. NM_009188.4.
UniGeneMm.2137.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E91NMR-A148-232[»]
1PD7NMR-A148-232[»]
2CR7NMR-A32-98[»]
2CZYNMR-A31-107[»]
2F05NMR-A148-252[»]
ProteinModelPortalQ62141.
SMRQ62141. Positions 31-107, 148-232, 292-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203257. 16 interactions.
DIPDIP-470N.
IntActQ62141. 6 interactions.
MINTMINT-1510576.

PTM databases

PhosphoSiteQ62141.

Proteomic databases

PaxDbQ62141.
PRIDEQ62141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004494; ENSMUSP00000004494; ENSMUSG00000031622. [Q62141-4]
ENSMUST00000109950; ENSMUSP00000105576; ENSMUSG00000031622. [Q62141-2]
GeneID20467.
KEGGmmu:20467.
UCSCuc009mgp.2. mouse. [Q62141-4]

Organism-specific databases

CTD23309.
MGIMGI:107158. Sin3b.
RougeSearch...

Phylogenomic databases

eggNOGCOG5602.
GeneTreeENSGT00390000007239.
HOGENOMHOG000230688.
HOVERGENHBG060425.
InParanoidQ62141.
OMASEPHMVF.
OrthoDBEOG7SV0TV.
PhylomeDBQ62141.
TreeFamTF106187.

Gene expression databases

ArrayExpressQ62141.
BgeeQ62141.
CleanExMM_SIN3B.
GenevestigatorQ62141.

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

EvolutionaryTraceQ62141.
NextBio298571.
PROQ62141.
SOURCESearch...

Entry information

Entry nameSIN3B_MOUSE
AccessionPrimary (citable) accession number: Q62141
Secondary accession number(s): O54976 expand/collapse secondary AC list , Q6A013, Q8VCB8, Q8VDZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 138 of the entry and version 2 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