Q60520: Paired amphipathic helix protein Sin3a (Sin3a)

Paired amphipathic helix protein Sin3a (Sin3a) is a 1274-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q60520.

Gene
Sin3a
Organism
Mus musculus
Length
1274 residues
Mean pLDDT
68.7
Model
AF-Q60520-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.7 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate29%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

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 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). Required for cortical…

Subunit structure

Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1, SAP30L, SAP130, SFPQ and TOPORS (PubMed:8649810). Interacts with OGT (via TPRs 1-6); the interaction mediates transcriptional repression in parallel with histone deacetylase (By similarity). Interacts with BAZ2A, MXD1, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3 (PubMed:10734093, PubMed:10950960,…

Subcellular location

Nucleus, Nucleus, nucleolus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
1G1ENMRB=295-383
1S5QNMRB=295-383
1S5RNMRB=295-383
2L9SNMRB=295-385
2LD7NMRB=456-528
2N2HNMRB=608-729
2RMRNMRA=119-189
2RMSNMRA=119-189

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