Q8R0S1
uniprot
Q8R0S1
canonical
amino_acid_sequence
MGDDRPFVCSAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKASDDDEKKGAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTTKPVVISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQIGSPTGSLPLVMHLANGQTMPMLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNNSGSISPSGHPMPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQNQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLGK
uniprot
proteins
function
FUNCTION: Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation (PubMed:29490055). In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recruiting histone H3K9 tri- and di-methyltransferases thus silencing the transcription of target genes such as Htr5b, STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes (PubMed:19893493, PubMed:30826729, PubMed:31294895). Phosphorylation of ATF7 disrupts interactions with histone methyltransferase and enhances the association with coactivators containing histone acetyltransferase and/or histone demethylase, leading to disruption of the heterochromatin-like structure and subsequently transcriptional activation (PubMed:19893493). In response to TNF, which is induced by various stresses, phosphorylated ATF7 and telomerase are released from telomeres leading to telomere shortening (PubMed:29490055). Also plays a role in maintaining epithelial regenerative capacity and protecting against cell death during intestinal epithelial damage and repair (PubMed:31958521). {ECO:0000269|PubMed:19893493, ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:30826729, ECO:0000269|PubMed:31294895, ECO:0000269|PubMed:31958521}.
uniprot
proteins
mass_dalton
44608
uniprot
proteins
post_translational_modification
PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity (By similarity). Social isolation stress as well as TNF also induce the phosphorylation of ATF7 (PubMed:19893493, PubMed:29490055). Phosphorylated in proliferating colonic and small intestinal epithelial cells (PubMed:31958521). {ECO:0000250|UniProtKB:P17544, ECO:0000269|PubMed:19893493, ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:31958521}.; PTM: Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase. {ECO:0000250|UniProtKB:P17544}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19893493
uniprot
proteins
pubmed
29490055
uniprot
proteins
pubmed
30826729
uniprot
proteins
pubmed
31294895
uniprot
proteins
pubmed
31958521
uniprot
proteins
sequence_length
413
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:19893493}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P17544}. Chromosome, telomere {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery. {ECO:0000250|UniProtKB:P17544}.
uniprot
proteins