ATF7
entrez
11016
canonical
uniprot
P17544
canonical
ensembl
ENSG00000170653
resolver
ensp
ENSP00000387406
resolver
ensp
ENSP00000399465
resolver
ensp
ENSP00000456858
resolver
ensp
ENSP00000465192
resolver
ensp
ENSP00000523790
resolver
ensp
ENSP00000593914
resolver
genesymbol
ATF7
resolver
genesymbol_syn
ATFA
resolver
hgnc
HGNC:792
resolver
uniprot
A5D6Y4
resolver
uniprot
B2RMP1
resolver
uniprot
B4DQL4
resolver
uniprot
Q13814
resolver
uniprot
Q8IVR8
resolver
uniprot
Q9UD83
resolver
uniprot_entry
ATF7_HUMAN
resolver
uniprot_sec
A5D6Y4
resolver
uniprot_sec
B2RMP1
resolver
uniprot_sec
B4DQL4
resolver
uniprot_sec
Q13814
resolver
uniprot_sec
Q8IVR8
resolver
uniprot_sec
Q9UD83
resolver
amino_acid_sequence
MGDDRPFVCNAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKAADEDEKKAAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNSSGSISPSGHPIPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQSQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLESPKESSEPTGSPAPVIQHSSATAPSNGLSVRSAAEAVATSVLTQMASQRTELSMPIQSHVIMTPQSQSAGR
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 STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes (By similarity). Stress induces ATF7 phosphorylation that 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q8R0S1, ECO:0000269|PubMed:29490055}.; FUNCTION: [Isoform 4]: Acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter.; FUNCTION: [Isoform 5]: Acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation. {ECO:0000269|PubMed:21858082}.
uniprot
proteins
mass_dalton
51757
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="C->A: Severely reduced TAF12-mediated enhancement of transcriptional activity."; /evidence="ECO:0000269|PubMed:15735663"; MUTAGEN 14; /note="C->A: Greatly reduced JNK2- or adenovirus E1A-mediated transactivation. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-51; A-53 and G-101."; /evidence="ECO:0000269|PubMed:10376527"; MUTAGEN 22; /note="D->K: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness."; /evidence="ECO:0000269|PubMed:8417352"; MUTAGEN 27; /note="H->N: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness."; /evidence="ECO:0000269|PubMed:8417352"; MUTAGEN 33; /note="M->D: Severely reduced TAF12-induced transcriptional activity; when associated with S-35."; /evidence="ECO:0000269|PubMed:15735663"; MUTAGEN 35; /note="L->S: Severely reduced TAF12-induced transcriptional activity; when associated with D-33."; /evidence="ECO:0000269|PubMed:15735663"; MUTAGEN 51; /note="T->A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-53. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-53 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-53 and G-101."; /evidence="ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"; MUTAGEN 51; /note="T->D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53."; /evidence="ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"; MUTAGEN 53; /note="T->A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-51. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-51 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and G-101."; /evidence="ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"; MUTAGEN 53; /note="T->D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51."; /evidence="ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"; MUTAGEN 101; /note="T->G: Some reduction in transactivation but, completely abolishes MAPK9-mediated activation. Abolishes MAPK9-mediated and greatly reduces adenovirus E1A-mediated transactivation; when associated with A-51 and A-53. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and A-53."; /evidence="ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:18950637"; MUTAGEN 107; /note="K->R: Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter."; /evidence="ECO:0000269|PubMed:18950637"; MUTAGEN 145; /note="T->A: No effect on transactivation; when associated with A-147."; /evidence="ECO:0000269|PubMed:10376527"; MUTAGEN 147; /note="T->A: No effect on transactivation; when associated with A-145."; /evidence="ECO:0000269|PubMed:10376527
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. {ECO:0000269|PubMed:18950637}.; PTM: Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase.; 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 (PubMed:18950637). Social isolation stress as well as TNF also induce the phosphorylation of ATF7 (PubMed:29490055). Phosphorylated in proliferating colonic and small intestinal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q8R0S1, ECO:0000269|PubMed:18950637, ECO:0000269|PubMed:29490055}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
10376527
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15735663
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
1694576
uniprot
proteins
pubmed
17264123
uniprot
proteins
pubmed
1827203
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18950637
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21858082
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29490055
uniprot
proteins
pubmed
8288576
uniprot
proteins
pubmed
8290251
uniprot
proteins
pubmed
8417352
uniprot
proteins
sequence_length
483
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:17264123}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17264123}. Chromosome, telomere {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:21858082}.
uniprot
proteins