SAPPutative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation |
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| SMART accession number: | SM00513
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| Description: |
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| Interpro abstract (IPR003034): |
The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA binding domain found in diverse nuclear proteins involved in chromosomal organisation [(PUBMED:10694879)], including in apoptosis [(PUBMED:10490026)]. In yeast, SAP is found in the most distal N-terminal region of E3 SUMO-protein ligase SIZ1, where it is involved in nuclear localization [(PUBMED:16109721)].
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| GO function: | nucleic acid binding (GO:0003676) |
| Family alignment: |
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There are 1794
SAP domains in 1756 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Aravind L, Koonin EV
- SAP - a putative DNA-binding motif involved in chromosomal organization.
- Trends Biochem Sci. 2000; 25: 112-4
- Gohring F, Schwab BL, Nicotera P, Leist M, Fackelmayer FO
- The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown.
- EMBO J. 1997; 16: 7361-71
- Display abstract
The scaffold attachment factor A (SAF-A) is an abundant component of the nuclear scaffold and of chromatin, and also occurs in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. Evidence from previous experiments had suggested that SAF-A most likely has at least two different functions, being involved both in nuclear architecture and RNA metabolism. We now show that the protein has a novel scaffold-associated region (SAR)-specific bipartite DNA-binding domain which is independent from the previously identified RNA-binding domain, the RGG box. During apoptosis, but not during necrosis, SAF-A is cleaved in a caspase-dependent way. Cleavage occurs within the bipartite DNA-binding domain, resulting in a loss of DNA-binding activity and a concomitant detachment of SAF-A from nuclear structural sites. On the other hand, cleavage does not compromise the association of SAF-A with hnRNP complexes, indicating that the function of SAF-A in RNA metabolism is not affected in apoptosis. Our results suggest that detachment of SAF-A from SARs, caused by apoptotic proteolysis of its DNA-binding domain, is linked to the formation of oligonucleosomal-sized DNA fragments and could therefore contribute to nuclear breakdown in apoptotic cells.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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| % proteins involved | KEGG pathway ID | Description |
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| 33.33 | map04630 | Jak-STAT signaling pathway | | 33.33 | map05222 | Small cell lung cancer | | 33.33 | map04120 | Ubiquitin mediated proteolysis |
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with SAP domain which could be assigned to a KEGG orthologous group, and not all proteins containing SAP domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%. |
- Structure (3D structures containing this domain)
3D Structures of SAP domains in PDB
| PDB code | Main view | Title | | 1h1j |  | The sap domain is a dna-binding domain capable of binding s/mar dna |
| 1jeq |  | Crystal structure of the ku heterodimer |
| 1jey |  | Crystal structure of the ku heterodimer bound to dna |
| 1jjr |  | The three-dimensional structure of the c-terminal dna binding domain of human ku70 |
| 1kcf |  | Crystal structure of the yeast mitochondrial holliday junction resolvase, ydc2 |
| 1v66 |  | Solution structure of human p53 binding domain of pias-1 |
| 1zbh |  | 3'-end specific recognition of histone mrna stem-loop by 3'- exonuclease |
| 1zbu |  | Crystal structure of full-length 3'-exonuclease |
| 1zrj |  | Solution structure of the sap domain of human e1b-55kda- associated protein 5 isoform c |
| 2do1 |  | Solution structure of the sap domain of human nuclear protein hcc-1 |
| 2do5 |  | Solution structure of the sap domain of human splicing factor 3b subunit 2 |
| 2jx3 |  | Nmr solution structure of the n-terminal domain of dek |
| 2rnn |  | Solution structure of the n-terminal sap domain of sumo e3 ligases from saccharomyces cerevisiae |
| 2rno |  | Solution structure of the n-terminal sap domain of sumo e3 ligases from oryza sativa |
- Links (links to other resources describing this domain)
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