PROSITE documentation PDOC50804SCAN box profile
This domain of around 80 amino acid residues has been called LeR because it is a leucine rich region [1], or SCAN box from the first letter of the names of the four proteins initially found to contain it (SRE-ZBP, CTfin-51, AW-1, Number 18 cDNA) [2]. The SCAN box is essentially found in the N-terminal part of transcription factors containing a zinc finger of the C2H2 type (see <PDOC00028>). These proteins can either activate or repress transcription, although isolated recombinant SCAN boxes do not modulate significantly the transcription [1,2]. In addition to these zinc finger transcription factors, an isolated SCAN box without adjacent zinc finger motifs has been identified in some proteins [3,4].
The SCAN box is enriched in hydrophobic and negatively charged residues with a L-X(6)-L motif at its core. This core is flanked by A, E, L, M, H and C residues that are frequently found in α-helices [2]. Predictions of the secondary structure of the domain suggest the presence of at least three α-helices that are separated from one another by short looped regions bounded by proline residues [5]. It has been shown to be a selective oligomerization domain that mediates homotypic and heterotypic interactions between SCAN box containing proteins [4,5].
The following zinc-finger proteins have been shown to contain a SCAN box:
- CTfin-51, a mouse protein that has been shown to be a strong transcriptional activator.
- SRE-ZBP, a human transcription factor that could function as a repressor of c-fos transcription.
- Zinc finger proteins ZNF24, ZNF165, ZNF174, ZNF191, ZNF192, ZNF193, ZNF202, ZNF215, ZNF232, ZNF263, ZFP-29, ZFP-38, and ZFP-95.
And a number of proteins devoid of C2H2-type zinc-finger domain:
- PGC-2 (PPAR-γ coactivator 2) [3], a human protein that binds to and increases the transcriptional activity of the nuclear receptor PPAR-γ.
- SDP1 (SCAN-domain protein 1) [4], a protein that interacts with the SCAN box of the zinc finger protein ZNF202.
The profile we developed spans the complete SCAN box.
Last update:December 2001 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Pengue G. Calabro V. Bartoli P.C. Pagliuca A. Lania L. |
Title | Repression of transcriptional activity at a distance by the evolutionarily conserved KRAB domain present in a subfamily of zinc finger proteins. | |
Source | Nucleic Acids Res. 22:2908-2914(1994). | |
PubMed ID | 8065901 |
2 | Authors | Williams A.J. Khachigian L.M. Shows T. Collins T. |
Title | Isolation and characterization of a novel zinc-finger protein with transcription repressor activity. | |
Source | J. Biol. Chem. 270:22143-22152(1995). | |
PubMed ID | 7673192 |
3 | Authors | Castillo G. Brun R.P. Rosenfield J.K. Hauser S. Park C.W. Troy A.E. Wright M.E. Spiegelman B.M. |
Title | An adipogenic cofactor bound by the differentiation domain of PPARgamma. | |
Source | EMBO J. 18:3676-3687(1999). | |
PubMed ID | 10393183 | |
DOI | 10.1093/emboj/18.13.3676 |
4 | Authors | Schumacher C. Wang H. Honer C. Ding W. Koehn J. Lawrence Q. Coulis C.M. Wang L.L. Ballinger D. Bowen B.R. Wagner S. |
Title | The SCAN domain mediates selective oligomerization. | |
Source | J. Biol. Chem. 275:17173-17179(2000). | |
PubMed ID | 10747874 | |
DOI | 10.1074/jbc.M000119200 |
5 | Authors | Williams A.J. Blacklow S.C. Collins T. |
Title | The zinc finger-associated SCAN box is a conserved oligomerization domain. | |
Source | Mol. Cell. Biol. 19:8526-8535(1999). | |
PubMed ID | 10567577 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)