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Cyclic AMP-dependent transcription factor ATF-7 (cAMP-dependent transcription factor ATF-7) (Activating transcription factor 7) (Transcription factor ATF-A)

 ATF7_HUMAN              Reviewed;         494 AA.
P17544; A5D6Y4; B2RMP1; B4DQL4; Q13814; Q8IVR8; Q9UD83;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
28-MAR-2018, entry version 185.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-7;
Short=cAMP-dependent transcription factor ATF-7;
AltName: Full=Activating transcription factor 7;
AltName: Full=Transcription factor ATF-A;
Name=ATF7; Synonyms=ATFA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix carcinoma;
PubMed=1694576; DOI=10.1093/nar/18.12.3467;
Gaire M., Chatton B., Kedinger C.;
"Isolation and characterization of two novel, closely related ATF cDNA
clones from HeLa cells.";
Nucleic Acids Res. 18:3467-3473(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Chatton B., Gaire M., Goetz J., Hauss C., Kedinger C.;
"ATF-a1, a new member of the human ATF family.";
Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY,
AND SUBUNIT.
TISSUE=Cervix carcinoma;
PubMed=8288576;
Pescini R., Kaszubska W., Whelan J., DeLamarter J.F.,
Hooft van Huijsduijnen R.;
"ATF-a0, a novel variant of the ATF/CREB transcription factor family,
forms a dominant transcription inhibitor in ATF-a heterodimers.";
J. Biol. Chem. 269:1159-1165(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBUNIT, AND FUNCTION.
PubMed=1827203; DOI=10.1073/pnas.88.9.3720;
Hai T., Curran T.;
"Cross-family dimerization of transcription factors Fos/Jun and
ATF/CREB alters DNA binding specificity.";
Proc. Natl. Acad. Sci. U.S.A. 88:3720-3724(1991).
[9]
INTERACTION WITH HUMAN ADENOVIRUS 2 E1A, ZINC-BINDING, AND MUTAGENESIS
OF ASP-22 AND HIS-27.
PubMed=8417352; DOI=10.1128/MCB.13.1.561;
Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J.,
Kedinger C.;
"Transcriptional activation by the adenovirus larger E1a product is
mediated by members of the cellular transcription factor ATF family
which can directly associate with E1a.";
Mol. Cell. Biol. 13:561-570(1993).
[10]
SUBUNIT, AND FUNCTION.
PubMed=8290251;
Chatton B., Bocco J.L., Goetz J., Gaire M., Lutz Y., Kedinger C.;
"Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family
and modulate its transcriptional activity.";
Oncogene 9:375-385(1994).
[11]
INTERACTION WITH JUN; MAPK9 AND HUMAN ADENOVIRUS 2 E1A, SUBUNIT,
FUNCTION, AND MUTAGENESIS OF CYS-14; THR-51; THR-53; THR-112; THR-156
AND THR-158.
PubMed=10376527; DOI=10.1038/sj.onc.1202723;
De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F.,
Kedinger C., Chatton B.;
"Role of the ATFa/JNK2 complex in Jun activation.";
Oncogene 18:3491-3500(1999).
[12]
INTERACTION WITH TAF4 AND TAF12, FUNCTION, TRANSACTIVATION DOMAIN, AND
MUTAGENESIS OF CYS-9; MET-33; LEU-35; THR-51 AND THR-53.
PubMed=15735663; DOI=10.1038/sj.onc.1208565;
Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C.,
Chatton B.;
"A functional interaction between ATF7 and TAF12 that is modulated by
TAF4.";
Oncogene 24:3472-3483(2005).
[13]
SUMOYLATION AT LYS-118, SUBCELLULAR LOCATION, INTERACTION WITH TAF12,
AND FUNCTION.
PubMed=17264123; DOI=10.1093/nar/gkl1168;
Hamard P.J., Boyer-Guittaut M., Camuzeaux B., Dujardin D., Hauss C.,
Oelgeschlager T., Vigneron M., Kedinger C., Chatton B.;
"Sumoylation delays the ATF7 transcription factor subcellular
localization and inhibits its transcriptional activity.";
Nucleic Acids Res. 35:1134-1144(2007).
[14]
PHOSPHORYLATION AT THR-51; THR-53 AND THR-112, SUMOYLATION AT LYS-118,
FUNCTION, AND MUTAGENESIS OF THR-51; THR-53; THR-112 AND LYS-118.
PubMed=18950637; DOI=10.1016/j.jmb.2008.10.008;
Camuzeaux B., Diring J., Hamard P.J., Oulad-Abdelghani M., Donzeau M.,
Vigneron M., Kedinger C., Chatton B.;
"p38beta2-mediated phosphorylation and sumoylation of ATF7 are
mutually exclusive.";
J. Mol. Biol. 384:980-991(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
FUNCTION (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM 5).
PubMed=21858082; DOI=10.1371/journal.pone.0023351;
Diring J., Camuzeaux B., Donzeau M., Vigneron M., Rosa-Calatrava M.,
Kedinger C., Chatton B.;
"A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and
ATF2 phosphorylation and transcriptional activity.";
PLoS ONE 6:E23351-E23351(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Plays important functions in early cell signaling. Binds
the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-
3'), a sequence present in many viral and cellular promoters.
Activator of the NF-ELAM1/delta-A site of the E-selectin promoter.
Has no intrinsic transcriptional activity, but activates
transcription on formation of JUN or FOS heterodimers. Also can
bind TRE promoter sequences when heterodimerized with members of
the JUN family.
-!- 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.
-!- SUBUNIT: Homodimer; binds DNA as homodimer. Heterodimer;
heterodimerizes with other members of ATF family and with JUN
family members. Interacts with JNK2; the interaction does not
phosphorylate ATF7 but acts as a docking site for other ATF-
associated partners such as JUN family members. Interacts (via its
transactivation domain) with TAF12 (isoforms TAFII15 and TAFII20);
the interaction potentiates the transactivation activity (isoform
TAFII20 only) and is inhibited by ATF7 sumoylation. Interacts with
TAF4; the interaction inhibits the TAF12-dependent
transactivation. Interacts with adenovirus 2 E1A; the interaction
enhances the ATF7-mediated viral transactivation activity which
requires the zinc-binding domains of both E1A and ATF7. Interacts
with MAPK9; the interaction does not phosphorylate ATF7 but acts
as a docking site for ATF7-associated partners such as JUN.
{ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:15735663,
ECO:0000269|PubMed:17264123, ECO:0000269|PubMed:1827203,
ECO:0000269|PubMed:8288576, ECO:0000269|PubMed:8290251,
ECO:0000269|PubMed:8417352}.
-!- INTERACTION:
P18847:ATF3; NbExp=2; IntAct=EBI-765623, EBI-712767;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-765623, EBI-749265;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-765623, EBI-10175124;
P06734:FCER2; NbExp=3; IntAct=EBI-765623, EBI-10199985;
P01100:FOS; NbExp=4; IntAct=EBI-765623, EBI-852851;
P15408:FOSL2; NbExp=2; IntAct=EBI-765623, EBI-3893419;
P0C746:HBZ (xeno); NbExp=2; IntAct=EBI-765623, EBI-10890294;
P05412:JUN; NbExp=6; IntAct=EBI-765623, EBI-852823;
P17275:JUNB; NbExp=2; IntAct=EBI-765623, EBI-748062;
P17535:JUND; NbExp=2; IntAct=EBI-765623, EBI-2682803;
Q9DGW5:MDV005 (xeno); NbExp=2; IntAct=EBI-765623, EBI-10889526;
Q9NX40:OCIAD1; NbExp=2; IntAct=EBI-765623, EBI-2683029;
Q8WW34:TMEM239; NbExp=3; IntAct=EBI-765623, EBI-9675724;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978, ECO:0000269|PubMed:17264123}. Nucleus,
nucleoplasm {ECO:0000269|PubMed:17264123}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=3; Synonyms=ATF-A1;
IsoId=P17544-1; Sequence=Displayed;
Name=1; Synonyms=ATF-A;
IsoId=P17544-2; Sequence=VSP_000594, VSP_000595;
Name=2; Synonyms=ATF-A-delta;
IsoId=P17544-3; Sequence=VSP_000595;
Name=4; Synonyms=ATF-A0;
IsoId=P17544-4; Sequence=VSP_000594, VSP_034543;
Name=5; Synonyms=ATF-4;
IsoId=P17544-5; Sequence=VSP_042469;
Name=6;
IsoId=P17544-6; Sequence=VSP_000594;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in heart, lung and skeletal muscle.
Isoform 4 is expressed in various tissues including heart, brain,
placenta, lung and skeletal muscle. Highest levels in skeletal
muscle. Lowest in lung and placenta. {ECO:0000269|PubMed:8288576}.
-!- 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.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; X52943; CAA37118.1; -; mRNA.
EMBL; X57197; CAA40483.1; -; mRNA.
EMBL; AK298853; BAG60976.1; -; mRNA.
EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96723.1; -; Genomic_DNA.
EMBL; CH471054; EAW96724.1; -; Genomic_DNA.
EMBL; BC042363; AAH42363.1; -; mRNA.
EMBL; BC136302; AAI36303.1; -; mRNA.
EMBL; BC140006; AAI40007.1; -; mRNA.
CCDS; CCDS44906.1; -. [P17544-6]
CCDS; CCDS58238.1; -. [P17544-5]
PIR; S12741; S12741.
RefSeq; NP_001123532.1; NM_001130060.1. [P17544-2]
RefSeq; NP_001193611.1; NM_001206682.1. [P17544-5]
RefSeq; NP_001193612.1; NM_001206683.1. [P17544-5]
RefSeq; NP_006847.1; NM_006856.2. [P17544-6]
RefSeq; XP_005268644.1; XM_005268587.3. [P17544-6]
RefSeq; XP_016874211.1; XM_017018722.1. [P17544-6]
UniGene; Hs.12286; -.
UniGene; Hs.633602; -.
ProteinModelPortal; P17544; -.
SMR; P17544; -.
BioGrid; 116206; 39.
CORUM; P17544; -.
ELM; P17544; -.
IntAct; P17544; 30.
MINT; P17544; -.
STRING; 9606.ENSP00000329212; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; P17544; -.
PhosphoSitePlus; P17544; -.
BioMuta; ATF7; -.
DMDM; 12643393; -.
EPD; P17544; -.
MaxQB; P17544; -.
PaxDb; P17544; -.
PeptideAtlas; P17544; -.
PRIDE; P17544; -.
DNASU; 11016; -.
Ensembl; ENST00000420353; ENSP00000399465; ENSG00000170653. [P17544-6]
Ensembl; ENST00000456903; ENSP00000387406; ENSG00000170653. [P17544-6]
Ensembl; ENST00000548118; ENSP00000456858; ENSG00000170653. [P17544-5]
Ensembl; ENST00000548446; ENSP00000449938; ENSG00000170653. [P17544-1]
Ensembl; ENST00000591397; ENSP00000465192; ENSG00000170653. [P17544-5]
GeneID; 11016; -.
KEGG; hsa:11016; -.
UCSC; uc001sdz.4; human. [P17544-1]
CTD; 11016; -.
DisGeNET; 11016; -.
EuPathDB; HostDB:ENSG00000170653.18; -.
GeneCards; ATF7; -.
H-InvDB; HIX0201838; -.
HGNC; HGNC:792; ATF7.
HPA; HPA003384; -.
MIM; 606371; gene.
neXtProt; NX_P17544; -.
OpenTargets; ENSG00000170653; -.
PharmGKB; PA25092; -.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00390000020106; -.
HOGENOM; HOG000220894; -.
HOVERGEN; HBG004300; -.
InParanoid; P17544; -.
KO; K09045; -.
OMA; EDCMERR; -.
OrthoDB; EOG091G0AO8; -.
PhylomeDB; P17544; -.
SIGNOR; P17544; -.
ChiTaRS; ATF7; human.
GeneWiki; ATF7; -.
GenomeRNAi; 11016; -.
PRO; PR:P17544; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000170653; -.
CleanEx; HS_ATF7; -.
ExpressionAtlas; P17544; baseline and differential.
Genevisible; P17544; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; NAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISM:NTNU_SB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR016378; TF_CRE-BP1-typ.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00170; bZIP_1; 1.
PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
SMART; SM00338; BRLZ; 1.
SMART; SM00355; ZnF_C2H2; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Host-virus interaction; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 494 Cyclic AMP-dependent transcription factor
ATF-7.
/FTId=PRO_0000076592.
DOMAIN 343 406 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
ZN_FING 7 31 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1 296 Transactivation domain.
REGION 336 494 Essential for binding adenovirus 2 E1A.
REGION 345 365 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 371 399 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 51 51 Phosphothreonine; by MAPK11.
{ECO:0000269|PubMed:18950637}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000269|PubMed:18950637}.
MOD_RES 112 112 Phosphothreonine.
{ECO:0000269|PubMed:18950637}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 118 118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:17264123,
ECO:0000269|PubMed:18950637}.
VAR_SEQ 89 99 Missing (in isoform 1, isoform 4 and
isoform 6). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1694576,
ECO:0000303|PubMed:8288576}.
/FTId=VSP_000594.
VAR_SEQ 100 494 AAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSP
PLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTLP
SPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGP
PVQMPSVISLARPVSMVPNIPGIPGPPVNSSGSISPSGHPI
PSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQS
QILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDER
RQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLS
NEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLESPKE
SSEPTGSPAPVIQHSSATAPSNGLSVRSAAEAVATSVLTQM
ASQRTELSMPIQSHVIMTPQSQSAGR -> VFRPRLFLLCF
GIIFLIG (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042469.
VAR_SEQ 125 145 Missing (in isoform 1 and isoform 2).
{ECO:0000303|PubMed:1694576}.
/FTId=VSP_000595.
VAR_SEQ 146 321 Missing (in isoform 4).
{ECO:0000303|PubMed:8288576}.
/FTId=VSP_034543.
MUTAGEN 9 9 C->A: Severely reduced TAF12-mediated
enhancement of transcriptional activity.
{ECO:0000269|PubMed:15735663}.
MUTAGEN 14 14 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-112.
{ECO:0000269|PubMed:10376527}.
MUTAGEN 22 22 D->K: No effect on binding adenovirus 2
E1A. Abolishes ATF7-mediated E1A
responsiveness.
{ECO:0000269|PubMed:8417352}.
MUTAGEN 27 27 H->N: No effect on binding adenovirus 2
E1A. Abolishes ATF7-mediated E1A
responsiveness.
{ECO:0000269|PubMed:8417352}.
MUTAGEN 33 33 M->D: Severely reduced TAF12-induced
transcriptional activity; when associated
with S-35. {ECO:0000269|PubMed:15735663}.
MUTAGEN 35 35 L->S: Severely reduced TAF12-induced
transcriptional activity; when associated
with D-33. {ECO:0000269|PubMed:15735663}.
MUTAGEN 51 51 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-112. Abolishes adenovirus 2 E1A-
mediated transactivation; when associated
with A-14; A-53 and G-112.
{ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:15735663,
ECO:0000269|PubMed:18950637}.
MUTAGEN 51 51 T->D: Completely abolishes MAPK9- and
adenovirus E1A-mediated transactivation;
when associated with D-53.
{ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:15735663,
ECO:0000269|PubMed:18950637}.
MUTAGEN 53 53 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-112. Abolishes adenovirus 2 E1A-
mediated transactivation; when associated
with A-14; A-51 and G-112.
{ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:15735663,
ECO:0000269|PubMed:18950637}.
MUTAGEN 53 53 T->D: Completely abolishes MAPK9- and
adenovirus E1A-mediated transactivation;
when associated with D-51.
{ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:15735663,
ECO:0000269|PubMed:18950637}.
MUTAGEN 112 112 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.
{ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:18950637}.
MUTAGEN 118 118 K->R: Abolishes sumoylation. Exclusive
nucleoplasmic location. Increase in
binding the E-selectin promoter.
{ECO:0000269|PubMed:18950637}.
MUTAGEN 156 156 T->A: No effect on transactivation; when
associated with A-158.
{ECO:0000269|PubMed:10376527}.
MUTAGEN 158 158 T->A: No effect on transactivation; when
associated with A-156.
{ECO:0000269|PubMed:10376527}.
CONFLICT 12 12 P -> T (in Ref. 7; AAH42363).
{ECO:0000305}.
SEQUENCE 494 AA; 52967 MW; 511EAF79C6503300 CRC64;
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
CEEVGLFNEL ASSFEHEFKK AADEDEKKAR SRTVAKKLVA AAGPLDMSLP STPDIKIKEE
EPVEVDSSPP DSPASSPCSP PLKEKEVTPK PVLISTPTPT IVRPGSLPLH LGYDPLHPTL
PSPTSVITQA PPSNRQMGSP TGSLPLVMHL ANGQTMPVLP GPPVQMPSVI SLARPVSMVP
NIPGIPGPPV NSSGSISPSG HPIPSEAKMR LKATLTHQVS SINGGCGMVV GTASTMVTAR
PEQSQILIQH PDAPSPAQPQ VSPAQPTPST GGRRRRTVDE DPDERRQRFL ERNRAAASRC
RQKRKLWVSS LEKKAEELTS QNIQLSNEVT LLRNEVAQLK QLLLAHKDCP VTALQKKTQG
YLESPKESSE PTGSPAPVIQ HSSATAPSNG LSVRSAAEAV ATSVLTQMAS QRTELSMPIQ
SHVIMTPQSQ SAGR


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