ATF5 (activating transcription factor 5)

Other alias	ATFX
	FLJ34666
	HMFN0395
HGNC (Hugo)	ATF5
LocusID (NCBI)	22809
Atlas_Id	50361
Location	19q13.33  [Link to chromosome band 19q13]
Location_base_pair	Starts at 49929143 and ends at 49933936 bp from pter ( according to hg19-Feb_2009)  [Mapping ATF5.png]
Local_order	Refer to mapping diagram.
	Mapping diagram. Base on Human Mar. 2006 (NCBI36/hg18) Assembly.

	DNA structure diagram. Relative size of the 4 exons of ATF5. Exon 1 and 2 are untranslated exons (NCBI reference sequence NM_012068.4). Blue area is non-coding region and pink is coding region.
Description	The ATF5 gene spans a total genomic size of 5219 bases and is composed of four exons.
Transcription	The human ATF5 transcript is 2268 bp in size (NM_012068.4) and contains 4 exons. Exon 1 and 2 are non-coding exons and the size of open reading frame is 849 bp.

	Protein structure diagram.
Description	ATF5 consists of 282 amino acid with MW of 30.69 kDa (NCBI reference sequence NP_036200.2).
Expression	Northern blot analysis revealed ubiquitous expression of ATF5, with highest levels in liver, lung, adipose tissue, heart, and skeletal muscle.
Localisation	Nucleus and cytoplasm.
Function	ATF5 is a member of basic-region leucine zipper (bZIP) proteins family which binds the cAMP response element (CRE) consensus sequence: 5'GTGACGT(C/A)(G/A). This sequence is present in many viral and cellular promoters. ATF within or between subgroups can form homo- or hetero-dimer through the bZIP domain and the dimer can then bind to the DNA through the basic-motif and function as a transcription factor. Recently, another novel ATF5 consensus DNA binding sequence (CYTCTYCCTTW) was found in C6 glioma and MCF7 using a cyclic amplification and selection of targets (CASTing) approach (Li et al., 2009). ATF5 is linked to many cellular function including cell cycle progression, metabolite homeostasis (Al Sarraj et al., 2005; Watatani et al., 2007), cellular differentiation and apoptosis. It involves in the proliferation and differentiation of neural cells (Angelastro et al., 2003; Angelastro et al., 2005; Mason et al., 2005) and has been shown to take part in the skeletal development of mouse limb (Shinomura et al., 2006; Satake at al., 2009). Data from various groups also suggested that ATF5 can function as anti-apoptotic factor (Devireddy et al., 2001; Persengiev et al., 2002; Nishioka et al., 2009). Coimmunoprecipitation and GST pull-down analyses confirmed the association of the C-terminal bZIP motif of ATF5 with the PRL-1 PTPase domain and adjacent residues of PTP4A1 in vitro. SDS-PAGE analysis showed that PRL-1 dephosphorylates ATF5 in vitro (Peters et al., 2001). ATF5 has been shown to interact with various proteins including Cyclin D3 (Liu et al., 2004), GABAB receptors (White et al., 2000), HTLV-1 viral protein Tax (Forgacs et al., 2005), E2 ubiguitin-conjugating enzyme Cdc34, PRL-1 and DISC1 (Morris et al., 2003; Fujii et al., 2007; Tomppo et al., 2009). It is a target of Cdc34-dependent ubiquitin-mediated proteolysis (Pati et al., 1999). Study indicates that during stress condition, eIF2 is phosphorylated and subsequently direct ATF5 translation in cell (Watatani et al., 2008; Zhou et al., 2008). Recent study of the promoter of ATF5 also suggested that its transcription is regulated by EBF1 (Wei et al., 2010).
Homology	ATF5 gene is highly conserved in mammals. Protein identity percentage of human ATF5 compared with chimpanzee, cow, mouse, and rat is 98.9, 88.0, 87.5 and 88.9 respectively.

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