Q60520 (SIN3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Paired amphipathic helix protein Sin3a

Alternative name(s):
Histone deacetylase complex subunit Sin3a
Transcriptional corepressor Sin3a

Gene names

Name:	Sin3a
Synonyms:	Kiaa4126

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1274 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.2 Ref.5 Ref.12
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. 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.19 Ref.21 Ref.23
Subcellular location	Nucleus. Nucleus › nucleolus. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Molecular function	Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from mutant phenotype PubMed 15998811. Source: MGI aging Inferred from electronic annotation. Source: Compara cellular protein localization Inferred from mutant phenotype PubMed 15998811. Source: MGI cellular response to glucose stimulus Inferred from direct assay PubMed 17670746. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 15998811. Source: MGI interphase of mitotic cell cycle Inferred from mutant phenotype PubMed 15998811. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 15998811. Source: MGI regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from electronic annotation. Source: Compara response to methylglyoxal Inferred from direct assay PubMed 17670746. Source: MGI response to organic nitrogen Inferred from electronic annotation. Source: Compara
Cellular_component	Sin3 complex Inferred from electronic annotation. Source: Compara kinetochore Inferred from direct assay PubMed 14519686. Source: MGI nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Inferred from physical interaction PubMed 17182846. Source: MGI transcriptional repressor complex Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 14593184PubMed 15998811. 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 sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype PubMed 15998811. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sap25	Q1EHW4	4	EBI-349034,EBI-937195
Sap30	O88574	6	EBI-349034,EBI-593511
Sox2	P48432	3	EBI-349034,EBI-2313612
Suds3	Q8BR65	4	EBI-349034,EBI-591431
Tet1	Q3URK3	2	EBI-349034,EBI-4291699

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1274

1274

Paired amphipathic helix protein Sin3a

PRO_0000121538

Regions

Domain

119 – 189

71

PAH 1

Domain

300 – 383

84

PAH 2

Domain

457 – 526

70

PAH 3

Region

119 – 196

78

Interaction with HCFC1 By similarity UniProtKB Q96ST3

Region

205 – 479

275

Interaction with REST

Region

459 – 526

68

Interaction with SAP30

Region

524 – 851

328

Interaction with NCOR1

Region

525 – 660

136

Interactions with SUDS3 and SAP130 By similarity

Region

688 – 830

143

Interactions with HDAC1 and ARID4B By similarity

Region

889 – 968

80

Interaction with OGT By similarity

Coiled coil

904 – 933

30

Potential

Compositional bias

207 – 265

59

Gln-rich

Compositional bias

218 – 285

68

Pro-rich

Compositional bias

836 – 842

7

Poly-Glu

Amino acid modifications

Modified residue

10

1

Phosphoserine By similarity

Modified residue

277

1

Phosphoserine By similarity

Modified residue

470

1

N6-acetyllysine By similarity

Modified residue

833

1

Phosphoserine By similarity UniProtKB Q96ST3

Modified residue

861

1

Phosphoserine Ref.20 Ref.22 UniProtKB Q96ST3

Modified residue

941

1

Phosphoserine By similarity

Modified residue

1113

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1097

1

E → EVWT in isoform 2.

VSP_039918

Experimental info

Mutagenesis

307

1

A → V: Greatly reduced binding to MAD; when associated with D-308 and A-311. Ref.24

Mutagenesis

308

1

I → D: Greatly reduced binding to MAD; when associated with V-307 and A-311. Ref.24

Mutagenesis

309

1

N → D: No effect on binding to MAD. Ref.24

Mutagenesis

311

1

V → A: Greatly reduced binding to MAD; when associated with V-307 and D-308. Ref.24

Mutagenesis

326

1

K → A: No effect on binding to MAD. Ref.24

Mutagenesis

329

1

L → A: Greatly reduced binding to MAD; when associated with A-332. Ref.24

Mutagenesis

332

1

L → A: Greatly reduced binding to MAD; when associated with A-329. Ref.24

Sequence conflict

144

1

Y → H in AAB01610. Ref.1

Sequence conflict

154

1

F → L in AAH53385. Ref.4

Sequence conflict

303

1

E → H in AAB01610. Ref.1

Sequence conflict

514

1

E → G in AAH53385. Ref.4

Sequence conflict

720 – 721

2

EQ → DE in AAB01610. Ref.1

Sequence conflict

827

1

A → D in AAA89119. Ref.2

Sequence conflict

899

1

L → R in AAH52716. Ref.4

Sequence conflict

912

1

S → F in AAH52716. Ref.4

Sequence conflict

969

1

S → Q in AAB01610. Ref.1

Sequence conflict

1047

1

L → V in AAB01610. Ref.1

Sequence conflict

1205 – 1207

3

KRL → QGK in AAA69773. Ref.5

Sequence conflict

1205

1

K → KK in AAA69772. Ref.5

Sequence conflict

1215 – 1216

2

VD → GK in AAA69772. Ref.5

Secondary structure

1

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1274

Helix Strand Turn

Details...

Helix

126 – 136

11

Helix

137 – 139

3

Helix

141 – 155

15

Helix

161 – 171

11

Turn

172 – 174

3

Helix

176 – 183

8

Helix

302 – 317

16

Turn

318 – 320

3

Helix

322 – 344

23

Beta strand

347 – 349

3

Helix

355 – 365

11

Turn

366 – 368

3

Helix

370 – 377

8

Turn

457 – 460

4

Helix

463 – 475

13

Helix

478 – 492

15

Helix

498 – 504

7

Helix

506 – 509

4

Helix

513 – 523

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 80FE378F62ED7CB3	FASTA	1,274	145,088
	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
	Isoform 2 [UniParc]. Checksum: F578FED21F4824D3	FASTA	1,277	145,474
	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 DDPVEAEVWT RWSDYVERYM SSDTTSPELR EHLAQKPVFL PRNLRRIRKC 1150 1160 1170 1180 1190 1200 QRGREQQEKE GKEGNSKKTM ENVESLDKLE CRFKLNSYKM VYVIKSEDYM YRRTALLRAH 1210 1220 1230 1240 1250 1260 QSHERVSKRL HQRFQAWVDK WTKEHVPREM AAETSKWLMG EGLEGLVPCT TTCDTETLHF 1270 VSINKYRVKY GTVFKAP

References

	« Hide 'large scale' referencesShow '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]	"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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861, MASS SPECTROMETRY. Tissue: Melanoma.
[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]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861, MASS SPECTROMETRY. Tissue: Macrophage.
[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]	"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.

IPI

IPI00276051.
IPI00985713.

PIR

A56068.
I61713.

RefSeq

NP_001103820.1. NM_001110350.1.
NP_001103821.1. NM_001110351.1.
NP_035508.2. NM_011378.2.

UniGene

Mm.15755.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q60520.

SMR

Q60520. Positions 119-189, 295-385, 454-528.

ModBase

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Protein-protein interaction databases

DIP

DIP-469N.

IntAct

Q60520. 13 interactions.

MINT

MINT-1510506.

PTM databases

PhosphoSite

Q60520.

Proteomic databases

PaxDb

Q60520.

PRIDE

Q60520.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENSMUST00000049169; ENSMUSP00000045044; ENSMUSG00000042557.
ENSMUST00000167715; ENSMUSP00000130641; ENSMUSG00000042557.
ENSMUST00000168177; ENSMUSP00000130221; ENSMUSG00000042557.
ENSMUST00000168502; ENSMUSP00000128956; ENSMUSG00000042557.
ENSMUST00000168678; ENSMUSP00000126601; ENSMUSG00000042557.

GeneID

20466.

KEGG

mmu:20466.

UCSC

uc009ptx.2. mouse.
uc012gtw.1. mouse.

Organism-specific databases

CTD

25942.

MGI

MGI:107157. Sin3a.

Rouge

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Phylogenomic databases

eggNOG

COG5602.

GeneTree

ENSGT00390000007239.

HOVERGEN

HBG060425.

InParanoid

Q570Z7.

KO

K11644.

OMA

PNQNGCQ.

OrthoDB

EOG48KR9G.

Gene expression databases

ArrayExpress

Q60520.

Bgee

Q60520.

CleanEx

MM_SIN3A.

Genevestigator

Q60520.

GermOnline

ENSMUSG00000042557. Mus musculus.

Family and domain databases

Gene3D

1.20.1160.11. 3 hits.

InterPro

IPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]

Pfam

PF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]

SMART

SM00761. HDAC_interact. 1 hit.
[Graphical view]

SUPFAM

SSF47762. PAH. 3 hits.

PROSITE

PS51477. PAH. 3 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q60520.

NextBio

298567.

SOURCE

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Entry information

Entry name

SIN3A_MOUSE

Accession

Primary (citable) accession number: Q60520
Secondary accession number(s): Q570Z7 , Q60820, Q62139, Q62140, Q7TPU8, Q7TSZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program