ATF1_HUMAN
ID ATF1_HUMAN Reviewed; 271 AA.
AC P18846; B4DRF9; P25168; Q9H4A8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-1;
DE Short=cAMP-dependent transcription factor ATF-1;
DE AltName: Full=Activating transcription factor 1;
DE AltName: Full=Protein TREB36;
GN Name=ATF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2196176; DOI=10.1002/j.1460-2075.1990.tb07434.x;
RA Yoshimura T., Fujisawa J., Yoshida M.;
RT "Multiple cDNA clones encoding nuclear proteins that bind to the tax-
RT dependent enhancer of HTLV-1: all contain a leucine zipper structure and
RT basic amino acid domain.";
RL EMBO J. 9:2537-2542(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1655749; DOI=10.1016/s0021-9258(18)55078-x;
RA Rehfuss R.P., Walton K.M., Loriaux M.M., Goodman R.H.;
RT "The cAMP-regulated enhancer-binding protein ATF-1 activates transcription
RT in response to cAMP-dependent protein kinase A.";
RL J. Biol. Chem. 266:18431-18434(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-271 (ISOFORM 1).
RX PubMed=2516827; DOI=10.1101/gad.3.12b.2083;
RA Hai T., Liu F., Coukos W.J., Green M.R.;
RT "Transcription factor ATF cDNA clones: an extensive family of leucine
RT zipper proteins able to selectively form DNA-binding heterodimers.";
RL Genes Dev. 3:2083-2090(1989).
RN [7]
RP ERRATUM OF PUBMED:2516827.
RA Hai T., Liu F., Coukos W.J., Green M.R.;
RL Genes Dev. 4:682-682(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-246 (ISOFORM 1), CHROMOSOMAL TRANSLOCATION
RP WITH FUS, AND ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
RX PubMed=11063792; DOI=10.1016/s0165-4608(00)00237-5;
RA Waters B.L., Panagopoulos I., Allen E.F.;
RT "Genetic characterization of angiomatoid fibrous histiocytoma identifies
RT fusion of the FUS and ATF-1 genes induced by a chromosomal translocation
RT involving bands 12q13 and 16p11.";
RL Cancer Genet. Cytogenet. 121:109-116(2000).
RN [9]
RP PHOSPHORYLATION AT SER-63, AND PHOSPHORYLATION BY CAMK1.
RX PubMed=8621702; DOI=10.1074/jbc.271.6.3066;
RA Sun P., Lou L., Maurer R.A.;
RT "Regulation of activating transcription factor-1 and the cAMP response
RT element-binding protein by Ca2+/calmodulin-dependent protein kinases type
RT I, II, and IV.";
RL J. Biol. Chem. 271:3066-3073(1996).
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH EWSR1, AND ASSOCIATION WITH ANGIOMATOID
RP FIBROUS HISTIOCYTOMA.
RX PubMed=15884099; DOI=10.1002/gcc.20201;
RA Hallor K.H., Mertens F., Jin Y., Meis-Kindblom J.M., Kindblom L.-G.,
RA Behrendtz M., Kalen A., Mandahl N., Panagopoulos I.;
RT "Fusion of the EWSR1 and ATF1 genes without expression of the MITF-M
RT transcript in angiomatoid fibrous histiocytoma.";
RL Genes Chromosomes Cancer 44:97-102(2005).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-63 BY CDK3, INTERACTION WITH CDK3, AND
RP MUTAGENESIS OF SER-63.
RX PubMed=18794154; DOI=10.1158/0008-5472.can-08-1137;
RA Zheng D., Cho Y.-Y., Lau A.T.Y., Zhang J., Ma W.-Y., Bode A.M., Dong Z.;
RT "Cyclin-dependent kinase 3-mediated activating transcription factor 1
RT phosphorylation enhances cell transformation.";
RL Cancer Res. 68:7650-7660(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP FUNCTION AS REPRESSOR, PHOSPHORYLATION AT SER-198 BY HIPK2, AND INTERACTION
RP WITH HIPK2.
RX PubMed=20980392; DOI=10.1242/jcs.073627;
RA Hailemariam K., Iwasaki K., Huang B.W., Sakamoto K., Tsuji Y.;
RT "Transcriptional regulation of ferritin and antioxidant genes by HIPK2
RT under genotoxic stress.";
RL J. Cell Sci. 123:3863-3871(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP INTERACTION WITH MOTS-C, AND SUBCELLULAR LOCATION.
RX PubMed=29983246; DOI=10.1016/j.cmet.2018.06.008;
RA Kim K.H., Son J.M., Benayoun B.A., Lee C.;
RT "The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to
RT Regulate Nuclear Gene Expression in Response to Metabolic Stress.";
RL Cell Metab. 28:516-524(2018).
CC -!- FUNCTION: This protein binds the cAMP response element (CRE)
CC (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral
CC and cellular promoters. Binds to the Tax-responsive element (TRE) of
CC HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes.
CC Represses the expression of FTH1 and other antioxidant detoxification
CC genes. Triggers cell proliferation and transformation.
CC {ECO:0000269|PubMed:18794154, ECO:0000269|PubMed:20980392}.
CC -!- SUBUNIT: Binds DNA as a dimer (PubMed:2516827). Interacts with HIPK2
CC and CDK3 (PubMed:18794154, PubMed:20980392). Interacts with MOTS-c, a
CC peptide produced by the mitochondrially encoded 12S rRNA MT-RNR1; the
CC interaction occurs in the nucleus following metabolic stress
CC (PubMed:29983246). {ECO:0000269|PubMed:18794154,
CC ECO:0000269|PubMed:20980392, ECO:0000269|PubMed:2516827,
CC ECO:0000269|PubMed:29983246}.
CC -!- INTERACTION:
CC P18846; P18846: ATF1; NbExp=2; IntAct=EBI-852794, EBI-852794;
CC P18846; P16220: CREB1; NbExp=6; IntAct=EBI-852794, EBI-711855;
CC P18846; P03372: ESR1; NbExp=3; IntAct=EBI-852794, EBI-78473;
CC P18846; P05412: JUN; NbExp=2; IntAct=EBI-852794, EBI-852823;
CC P18846; O95644: NFATC1; NbExp=3; IntAct=EBI-852794, EBI-6907210;
CC P18846; Q16649: NFIL3; NbExp=3; IntAct=EBI-852794, EBI-3951858;
CC P18846; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-852794, EBI-10890294;
CC P18846; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-852794, EBI-10889526;
CC P18846; P03259-2; Xeno; NbExp=2; IntAct=EBI-852794, EBI-7225021;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29983246}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P18846-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P18846-2; Sequence=VSP_055559;
CC -!- PTM: Phosphorylated at Ser-198 by HIPK2 in response to genotoxic
CC stress. This phosphorylation promotes transcription repression of FTH1
CC and other antioxidant detoxification genes. The CDK3-mediated
CC phosphorylation at Ser-63 promotes its transactivation and
CC transcriptional activities. Phosphorylated at Ser-63 by RPS6KA4 and
CC RPS6KA5 in response to mitogenic or stress stimuli.
CC {ECO:0000269|PubMed:18794154, ECO:0000269|PubMed:20980392,
CC ECO:0000269|PubMed:8621702}.
CC -!- DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A
CC distinct variant of malignant fibrous histiocytoma that typically
CC occurs in children and adolescents and is manifest by nodular
CC subcutaneous growth. Characteristic microscopic features include
CC lobulated sheets of histiocyte-like cells intimately associated with
CC areas of hemorrhage and cystic pseudovascular spaces, as well as a
CC striking cuffing of inflammatory cells, mimicking a lymph node
CC metastasis. Note=The gene represented in this entry may be involved in
CC disease pathogenesis. Chromosomal aberrations involving ATF1 are found
CC in patients with angiomatoid fibrous histiocytoma. Translocation
CC t(12;16)(q13;p11.2) with FUS generates a chimeric ATF1/FUS protein.
CC Translocation t(12;22)(q13;q12) with EWSR1 generates a chimeric
CC ATF1/EWSR1 protein.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC15058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ATF1ID81.html";
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DR EMBL; X55544; CAA39150.1; -; Genomic_DNA.
DR EMBL; AK299240; BAG61271.1; -; mRNA.
DR EMBL; AC013244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029619; AAH29619.1; -; mRNA.
DR EMBL; AJ295163; CAC15058.1; ALT_INIT; mRNA.
DR CCDS; CCDS8803.1; -. [P18846-1]
DR PIR; S12560; S12560.
DR RefSeq; NP_005162.1; NM_005171.4. [P18846-1]
DR RefSeq; XP_011536688.1; XM_011538386.2. [P18846-1]
DR RefSeq; XP_011536689.1; XM_011538387.2. [P18846-1]
DR RefSeq; XP_016874821.1; XM_017019332.1. [P18846-1]
DR RefSeq; XP_016874822.1; XM_017019333.1. [P18846-1]
DR RefSeq; XP_016874823.1; XM_017019334.1. [P18846-1]
DR AlphaFoldDB; P18846; -.
DR BioGRID; 106956; 50.
DR ComplexPortal; CPX-6401; bZIP transcription factor complex, ATF1-ATF1.
DR ComplexPortal; CPX-6402; bZIP transcription factor complex, ATF1-BACH1.
DR ComplexPortal; CPX-6404; bZIP transcription factor complex, ATF1-NFIL3.
DR ComplexPortal; CPX-6405; bZIP transcription factor complex, ATF1-CREB1.
DR ComplexPortal; CPX-9; bZIP transcription factor complex, ATF1-ATF4.
DR DIP; DIP-652N; -.
DR IntAct; P18846; 30.
DR MINT; P18846; -.
DR STRING; 9606.ENSP00000262053; -.
DR BindingDB; P18846; -.
DR ChEMBL; CHEMBL3255; -.
DR DrugBank; DB00852; Pseudoephedrine.
DR GlyGen; P18846; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; P18846; -.
DR PhosphoSitePlus; P18846; -.
DR BioMuta; ATF1; -.
DR DMDM; 1168542; -.
DR EPD; P18846; -.
DR jPOST; P18846; -.
DR MassIVE; P18846; -.
DR MaxQB; P18846; -.
DR PaxDb; P18846; -.
DR PeptideAtlas; P18846; -.
DR PRIDE; P18846; -.
DR ProteomicsDB; 4950; -.
DR ProteomicsDB; 53610; -. [P18846-1]
DR ABCD; P18846; 1 sequenced antibody.
DR Antibodypedia; 4260; 700 antibodies from 43 providers.
DR DNASU; 466; -.
DR Ensembl; ENST00000262053.8; ENSP00000262053.3; ENSG00000123268.9. [P18846-1]
DR GeneID; 466; -.
DR KEGG; hsa:466; -.
DR MANE-Select; ENST00000262053.8; ENSP00000262053.3; NM_005171.5; NP_005162.1.
DR UCSC; uc001rww.5; human. [P18846-1]
DR CTD; 466; -.
DR DisGeNET; 466; -.
DR GeneCards; ATF1; -.
DR HGNC; HGNC:783; ATF1.
DR HPA; ENSG00000123268; Low tissue specificity.
DR MalaCards; ATF1; -.
DR MIM; 123803; gene.
DR MIM; 612160; phenotype.
DR neXtProt; NX_P18846; -.
DR OpenTargets; ENSG00000123268; -.
DR Orphanet; 97338; Melanoma of soft tissue.
DR PharmGKB; PA25083; -.
DR VEuPathDB; HostDB:ENSG00000123268; -.
DR eggNOG; KOG3584; Eukaryota.
DR GeneTree; ENSGT00940000158200; -.
DR HOGENOM; CLU_042675_1_0_1; -.
DR InParanoid; P18846; -.
DR OMA; THISHIA; -.
DR OrthoDB; 957343at2759; -.
DR PhylomeDB; P18846; -.
DR TreeFam; TF106464; -.
DR PathwayCommons; P18846; -.
DR Reactome; R-HSA-199920; CREB phosphorylation.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P18846; -.
DR SIGNOR; P18846; -.
DR BioGRID-ORCS; 466; 26 hits in 1102 CRISPR screens.
DR ChiTaRS; ATF1; human.
DR GeneWiki; ATF1; -.
DR GenomeRNAi; 466; -.
DR Pharos; P18846; Tchem.
DR PRO; PR:P18846; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P18846; protein.
DR Bgee; ENSG00000123268; Expressed in germinal epithelium of ovary and 205 other tissues.
DR ExpressionAtlas; P18846; baseline and differential.
DR Genevisible; P18846; HS.
DR GO; GO:1990590; C:ATF1-ATF4 transcription factor complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
DR GO; GO:0014074; P:response to purine-containing compound; IDA:MGI.
DR InterPro; IPR029825; ATF1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR003102; Coactivator_CBP_pKID.
DR InterPro; IPR001630; Leuzip_CREB.
DR PANTHER; PTHR45879; PTHR45879; 1.
DR PANTHER; PTHR45879:SF2; PTHR45879:SF2; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF02173; pKID; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS50953; KID; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosomal rearrangement; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..271
FT /note="Cyclic AMP-dependent transcription factor ATF-1"
FT /id="PRO_0000076575"
FT DOMAIN 31..90
FT /note="KID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT DOMAIN 213..271
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..239
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 241..262
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 8..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 110
FT /note="Breakpoint for translocation to form chimeric
FT EWSR1/ATF1 protein"
FT SITE 112
FT /note="Breakpoint for translocation to form chimeric
FT FUS/ATF1 protein"
FT MOD_RES 63
FT /note="Phosphoserine; by CaMK1, CDK3, RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000305|PubMed:18794154,
FT ECO:0000305|PubMed:8621702"
FT MOD_RES 198
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312,
FT ECO:0000269|PubMed:20980392, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055559"
FT VARIANT 191
FT /note="P -> A (in dbSNP:rs2230674)"
FT /id="VAR_024382"
FT MUTAGEN 63
FT /note="S->A: Impaired CDK3-mediated phosphorylation and
FT altered transactivation and transcriptional activities."
FT /evidence="ECO:0000269|PubMed:18794154"
FT CONFLICT 55
FT /note="H -> A (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Missing (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29233 MW; BAFECBFFB244FCED CRC64;
MEDSHKSTTS ETAPQPGSAV QGAHISHIAQ QVSSLSESEE SQDSSDSIGS SQKAHGILAR
RPSYRKILKD LSSEDTRGRK GDGENSGVSA AVTSMSVPTP IYQTSSGQYI AIAPNGALQL
ASPGTDGVQG LQTLTMTNSG STQQGTTILQ YAQTSDGQQI LVPSNQVVVQ TASGDMQTYQ
IRTTPSATSL PQTVVMTSPV TLTSQTTKTD DPQLKREIRL MKNREAAREC RRKKKEYVKC
LENRVAVLEN QNKTLIEELK TLKDLYSNKS V
