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Protein

Paired amphipathic helix protein Sin3a

Gene

Sin3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 the 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. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (PubMed:22476904).5 Publications

GO - Molecular functioni

  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • protein deacetylase activity Source: MGI
  • RNA binding Source: Ensembl
  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II repressing transcription factor binding Source: MGI
  • RNA polymerase II transcription corepressor activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription factor binding Source: MGI
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • activation of innate immune response Source: MGI
  • aging Source: Ensembl
  • cellular protein localization Source: MGI
  • cellular response to dopamine Source: Ensembl
  • cellular response to glucose stimulus Source: MGI
  • chromatin silencing at rDNA Source: Reactome
  • DNA replication Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • histone deacetylation Source: GO_Central
  • in utero embryonic development Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of histone H3-K27 acetylation Source: MGI
  • negative regulation of protein localization to nucleus Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of transcription regulatory region DNA binding Source: MGI
  • positive regulation of chromatin silencing Source: MGI
  • positive regulation of defense response to virus by host Source: MGI
  • positive regulation of G2/M transition of mitotic cell cycle Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein deacetylation Source: MGI
  • regulation of hormone levels Source: Ensembl
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
  • response to methylglyoxal Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-573389. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:107157. Sin3a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intercellular bridge Source: MGI
  • kinetochore Source: MGI
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • Sin3 complex Source: MGI
  • transcriptional repressor complex Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi307A → V: Greatly reduced binding to MAD; when associated with D-308 and A-311. 1 Publication1
Mutagenesisi308I → D: Greatly reduced binding to MAD; when associated with V-307 and A-311. 1 Publication1
Mutagenesisi309N → D: No effect on binding to MAD. 1 Publication1
Mutagenesisi311V → A: Greatly reduced binding to MAD; when associated with V-307 and D-308. 1 Publication1
Mutagenesisi326K → A: No effect on binding to MAD. 1 Publication1
Mutagenesisi329L → A: Greatly reduced binding to MAD; when associated with A-332. 1 Publication1
Mutagenesisi332L → A: Greatly reduced binding to MAD; when associated with A-329. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001215381 – 1274Paired amphipathic helix protein Sin3aAdd BLAST1274

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineBy similarity1
Modified residuei277PhosphoserineCombined sources1
Modified residuei284PhosphothreonineCombined sources1
Modified residuei470N6-acetyllysineBy similarity1
Modified residuei833PhosphoserineCombined sources1
Modified residuei861PhosphoserineBy similarity1
Modified residuei866N6-acetyllysineCombined sources1
Modified residuei876N6-acetyllysineCombined sources1
Modified residuei941PhosphoserineBy similarity1
Modified residuei1090PhosphoserineBy similarity1
Modified residuei1113PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60520.
MaxQBiQ60520.
PaxDbiQ60520.
PeptideAtlasiQ60520.
PRIDEiQ60520.

PTM databases

iPTMnetiQ60520.
PhosphoSitePlusiQ60520.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000042557.
CleanExiMM_SIN3A.
ExpressionAtlasiQ60520. baseline and differential.
GenevisibleiQ60520. MM.

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. Interacts with PPHLN1 (By similarity). Found in a complex with YY1, GON4L and HDAC1 (PubMed:21454521). Interacts (via PAH2) with FOXK1 (PubMed:22476904).By similarity21 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

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II repressing transcription factor binding Source: MGI
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi203256. 74 interactors.
DIPiDIP-469N.
IntActiQ60520. 34 interactors.
MINTiMINT-1510506.
STRINGi10090.ENSMUSP00000128956.

Structurei

Secondary structure

11274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi126 – 136Combined sources11
Helixi137 – 139Combined sources3
Helixi141 – 155Combined sources15
Helixi161 – 171Combined sources11
Turni172 – 174Combined sources3
Helixi176 – 183Combined sources8
Helixi302 – 317Combined sources16
Turni318 – 320Combined sources3
Helixi322 – 344Combined sources23
Beta strandi347 – 349Combined sources3
Helixi355 – 365Combined sources11
Turni366 – 368Combined sources3
Helixi370 – 377Combined sources8
Turni457 – 460Combined sources4
Helixi463 – 475Combined sources13
Helixi478 – 492Combined sources15
Helixi498 – 504Combined sources7
Helixi506 – 509Combined sources4
Helixi513 – 523Combined sources11
Helixi616 – 641Combined sources26
Helixi646 – 651Combined sources6
Turni660 – 662Combined sources3
Helixi663 – 673Combined sources11
Helixi675 – 677Combined sources3
Helixi678 – 685Combined sources8
Helixi689 – 713Combined sources25
Helixi715 – 723Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1ENMR-B295-383[»]
1S5QNMR-B295-383[»]
1S5RNMR-B295-383[»]
2L9SNMR-B295-385[»]
2LD7NMR-B456-528[»]
2N2HNMR-B608-729[»]
2RMRNMR-A119-189[»]
2RMSNMR-A119-189[»]
ProteinModelPortaliQ60520.
SMRiQ60520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60520.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini119 – 189PAH 1PROSITE-ProRule annotationAdd BLAST71
Domaini300 – 383PAH 2PROSITE-ProRule annotationAdd BLAST84
Domaini457 – 526PAH 3PROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni119 – 196Interaction with HCFC1By similarityAdd BLAST78
Regioni205 – 479Interaction with REST1 PublicationAdd BLAST275
Regioni459 – 526Interaction with SAP301 PublicationAdd BLAST68
Regioni524 – 851Interaction with NCOR1Add BLAST328
Regioni525 – 660Interactions with SUDS3 and SAP130By similarityAdd BLAST136
Regioni688 – 830Interactions with HDAC1 and ARID4BBy similarityAdd BLAST143
Regioni889 – 968Interaction with OGTBy similarityAdd BLAST80

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili904 – 933Sequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi207 – 265Gln-richAdd BLAST59
Compositional biasi218 – 285Pro-richAdd BLAST68
Compositional biasi836 – 842Poly-Glu7

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG4204. Eukaryota.
COG5602. LUCA.
GeneTreeiENSGT00390000007239.
HOVERGENiHBG060425.
InParanoidiQ60520.
KOiK11644.
OMAiEENCFKI.
OrthoDBiEOG091G03HY.
PhylomeDBiQ60520.
TreeFamiTF106187.

Family and domain databases

Gene3Di1.20.1160.11. 3 hits.
InterProiIPR013194. HDAC_interact_dom.
IPR003822. PAH.
IPR031693. Sin3_C.
[Graphical view]
PfamiPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
PF16879. Sin3a_C. 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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti144Y → H in AAB01610 (PubMed:7601471).Curated1
Sequence conflicti154F → L in AAH53385 (PubMed:15489334).Curated1
Sequence conflicti303E → H in AAB01610 (PubMed:7601471).Curated1
Sequence conflicti514E → G in AAH53385 (PubMed:15489334).Curated1
Sequence conflicti720 – 721EQ → DE in AAB01610 (PubMed:7601471).Curated2
Sequence conflicti827A → D in AAA89119 (PubMed:8649810).Curated1
Sequence conflicti899L → R in AAH52716 (PubMed:15489334).Curated1
Sequence conflicti912S → F in AAH52716 (PubMed:15489334).Curated1
Sequence conflicti969S → Q in AAB01610 (PubMed:7601471).Curated1
Sequence conflicti1047L → V in AAB01610 (PubMed:7601471).Curated1
Sequence conflicti1205 – 1207KRL → QGK in AAA69773 (PubMed:7889570).Curated3
Sequence conflicti1205K → KK in AAA69772 (PubMed:7889570).Curated1
Sequence conflicti1215 – 1216VD → GK in AAA69772 (PubMed:7889570).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0399181097E → EVWT in isoform 2. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006510890.3. [Q60520-1]
XP_006510954.1. XM_006510891.3. [Q60520-1]
XP_006510955.1. XM_006510892.3. [Q60520-1]
XP_006510956.1. XM_006510893.3. [Q60520-1]
XP_011240985.1. XM_011242683.2. [Q60520-1]
XP_011240986.1. XM_011242684.2. [Q60520-1]
XP_011240987.1. XM_011242685.2. [Q60520-1]
XP_011240988.1. XM_011242686.2. [Q60520-1]
XP_017168720.1. XM_017313231.1. [Q60520-2]
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:
EMBLi
GenBanki
DDBJi
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_006510890.3. [Q60520-1]
XP_006510954.1. XM_006510891.3. [Q60520-1]
XP_006510955.1. XM_006510892.3. [Q60520-1]
XP_006510956.1. XM_006510893.3. [Q60520-1]
XP_011240985.1. XM_011242683.2. [Q60520-1]
XP_011240986.1. XM_011242684.2. [Q60520-1]
XP_011240987.1. XM_011242685.2. [Q60520-1]
XP_011240988.1. XM_011242686.2. [Q60520-1]
XP_017168720.1. XM_017313231.1. [Q60520-2]
UniGeneiMm.15755.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1ENMR-B295-383[»]
1S5QNMR-B295-383[»]
1S5RNMR-B295-383[»]
2L9SNMR-B295-385[»]
2LD7NMR-B456-528[»]
2N2HNMR-B608-729[»]
2RMRNMR-A119-189[»]
2RMSNMR-A119-189[»]
ProteinModelPortaliQ60520.
SMRiQ60520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203256. 74 interactors.
DIPiDIP-469N.
IntActiQ60520. 34 interactors.
MINTiMINT-1510506.
STRINGi10090.ENSMUSP00000128956.

PTM databases

iPTMnetiQ60520.
PhosphoSitePlusiQ60520.

Proteomic databases

EPDiQ60520.
MaxQBiQ60520.
PaxDbiQ60520.
PeptideAtlasiQ60520.
PRIDEiQ60520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi25942.
MGIiMGI:107157. Sin3a.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4204. Eukaryota.
COG5602. LUCA.
GeneTreeiENSGT00390000007239.
HOVERGENiHBG060425.
InParanoidiQ60520.
KOiK11644.
OMAiEENCFKI.
OrthoDBiEOG091G03HY.
PhylomeDBiQ60520.
TreeFamiTF106187.

Enzyme and pathway databases

ReactomeiR-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-573389. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiSin3a. mouse.
EvolutionaryTraceiQ60520.
PROiQ60520.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000042557.
CleanExiMM_SIN3A.
ExpressionAtlasiQ60520. baseline and differential.
GenevisibleiQ60520. MM.

Family and domain databases

Gene3Di1.20.1160.11. 3 hits.
InterProiIPR013194. HDAC_interact_dom.
IPR003822. PAH.
IPR031693. Sin3_C.
[Graphical view]
PfamiPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
PF16879. Sin3a_C. 1 hit.
[Graphical view]
SMARTiSM00761. HDAC_interact. 1 hit.
[Graphical view]
SUPFAMiSSF47762. SSF47762. 3 hits.
PROSITEiPS51477. PAH. 3 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.