Summary: Histone deacetylase complex subunit SAP25
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Histone deacetylase complex subunit SAP25 Provide feedback
SAP25 is a family of proteins found in eukaryotes. SAP25 is a core component of the mSin3 co-repressor complex whose subcellular location is regulated by PML. mSin3, the transcriptional co-repressor, is associated with histone deacetylases (HDACs) and is utilised by many DNA-binding transcriptional repressors. SAP25 is a nucleo-cytoplasmic shuttling protein that is actively exported from the nucleus by a CRM1-dependent mechanism. It binds to the PAH1 domain of mSin3A, associates with the mSin3A-HDAC complex in vivo, and represses transcription when tethered to DNA [1,2].
Shiio Y, Rose DW, Aur R, Donohoe S, Aebersold R, Eisenman RN;, Mol Cell Biol. 2006;26:1386-1397.: Identification and characterization of SAP25, a novel component of the mSin3 corepressor complex. PUBMED:16449650 EPMC:16449650
Sahu SC, Swanson KA, Kang RS, Huang K, Brubaker K, Ratcliff K, Radhakrishnan I;, J Mol Biol. 2008;375:1444-1456.: Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor. PUBMED:18089292 EPMC:18089292
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR029163
In mammals, SAP25 is involved in the transcriptional repression mediated by the mSIN3 complex, which consists of at least SAP30, SAP45/Sds3, SAP130, SAP180/BCAA, RBP1, HDAC1 (histone deacetylase1), HDAC2, RbAp46, and RbAp48 [PUBMED:2259223]. The mSIN3 complex can be recruited by sequence-specific DNA binding transcription factors and chromatin-binding proteins to specific regions of the genome and regulate their transcription [PUBMED:2259223]. SAP25 binds to the the PAH1 domain of mSin3A and changes the conformation of the complex that affects its protein-protein interaction [PUBMED:2259223]. SAP25 can be actively exported from the nucleus to cytoplasm by a CRM1-dependent nuclear export pathway. Its localisation is regulated by promyelocytic leukemia protein (PML), which induces a nuclear accumulation of SAP25 [PUBMED:16449650].
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|Cellular component||nucleus (GO:0005634)|
|Biological process||regulation of transcription, DNA-templated (GO:0006355)|
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|Number in seed:||10|
|Number in full:||33|
|Average length of the domain:||188.20 aa|
|Average identity of full alignment:||65 %|
|Average coverage of the sequence by the domain:||79.47 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SAP25 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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