Type |
Details |
Score |
Publication |
First Author: |
Chan CW |
Year: |
2007 |
Journal: |
Biochem J |
Title: |
A novel member of the SAF (scaffold attachment factor)-box protein family inhibits gene expression and induces apoptosis. |
Volume: |
407 |
Issue: |
3 |
Pages: |
355-62 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
SLTM belongs to the scaffold attachment factor B (SAFB) family. When overexpressed, it acts as a general inhibitor of transcription that eventually leads to apoptosis [, ].Scaffold attachment factor B (SAFB) family members include SAFB1, SAFB2 and SAFB-like transcriptional modulator, SLTM. They contain an N-terminal DNA-binding (SAF-A/B, Acinus and PIAS, SAP) domain, an RNA-binding domain (RBD) and an C-terminal arginine/glycine motif RGG/RG domain. Their RGG/RG domain, which partially overlaps with a putative coiled-coil domain, is most conserved and is likely to be involved in protein-protein interactions []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
44
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
169
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Garee JP |
Year: |
2010 |
Journal: |
J Cell Biochem |
Title: |
SAFB1's multiple functions in biological control-lots still to be done! |
Volume: |
109 |
Issue: |
2 |
Pages: |
312-9 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
SAFB1 belongs to the scaffold attachment factor B (SAFB) family. It has many functions such as transcriptional repression and RNA splicing. It may also have a role in chromatin organization. It is involved in in numerous cellular processes including cell growth, stress response, and apoptosis []. It plays an important role in cancer, particularly in breast tumorigenesis []. Scaffold attachment factor B (SAFB) family members include SAFB1, SAFB2 and SAFB-like transcriptional modulator, SLTM. They contain an N-terminal DNA-binding (SAF-A/B, Acinus and PIAS, SAP) domain, an RNA-binding domain (RBD) and an C-terminal arginine/glycine motif RGG/RG domain. Their RGG/RG domain, which partially overlaps with a putative coiled-coil domain, is most conserved and is likely to be involved in protein-protein interactions []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
374
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
62
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1031
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
937
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
939
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
664
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1031
 |
Fragment?: |
false |
|
•
•
•
•
•
|