ID ATF3_HUMAN Reviewed; 181 AA. AC P18847; Q5VTZ2; Q6ICQ9; Q7Z566; Q8WYM6; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-3 {ECO:0000305}; DE Short=cAMP-dependent transcription factor ATF-3 {ECO:0000303|PubMed:7515060}; DE AltName: Full=Activating transcription factor 3; GN Name=ATF3 {ECO:0000303|PubMed:7515060, ECO:0000312|HGNC:HGNC:785}; 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 [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION. RX PubMed=7515060; DOI=10.1016/s0021-9258(17)40754-x; RA Chen B.P.C., Liang G., Whelan J., Hai T.; RT "ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by RT alternatively spliced isoforms."; RL J. Biol. Chem. 269:15819-15826(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), SUBCELLULAR RP LOCATION, AND ALTERNATIVE SPLICING. RX PubMed=12034827; DOI=10.1093/nar/30.11.2398; RA Hashimoto Y., Zhang C., Kawauchi J., Imoto I., Adachi M.T., Inazawa J., RA Amagasa T., Hai T., Kitajima S.; RT "An alternatively spliced isoform of transcriptional repressor ATF3 and its RT induction by stress stimuli."; RL Nucleic Acids Res. 30:2398-2406(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING. RX PubMed=12881527; DOI=10.1074/jbc.m304574200; RA Pan Y., Chen H., Siu F., Kilberg M.S.; RT "Amino acid deprivation and endoplasmic reticulum stress induce expression RT of multiple activating transcription factor-3 mRNA species that, when RT overexpressed in HepG2 cells, modulate transcription by the human RT asparagine synthetase promoter."; RL J. Biol. Chem. 278:38402-38412(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-38. RG NIEHS SNPs program; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-147 (ISOFORM 5). RC TISSUE=Cerebellum, and Lung; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-181. 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 [12] RP ERRATUM OF PUBMED:2516827. RA Hai T., Liu F., Coukos W.J., Green M.R.; RL Genes Dev. 4:682-682(1990). RN [13] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-175, 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 [16] RP INTERACTION WITH KAT5. RX PubMed=25865756; DOI=10.1038/ncomms7752; RA Cui H., Guo M., Xu D., Ding Z.C., Zhou G., Ding H.F., Zhang J., Tang Y., RA Yan C.; RT "The stress-responsive gene ATF3 regulates the histone acetyltransferase RT Tip60."; RL Nat. Commun. 6:6752-6752(2015). RN [17] RP VARIANT THR-168. RX PubMed=29463886; DOI=10.1038/s41380-018-0020-x; RA Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J., RA Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C., RA Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.; RT "A set of regulatory genes co-expressed in embryonic human brain is RT implicated in disrupted speech development."; RL Mol. Psychiatry 24:1065-1078(2019). 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. Represses transcription from promoters with ATF CC sites. It may repress transcription by stabilizing the binding of CC inhibitory cofactors at the promoter. {ECO:0000269|PubMed:7515060}. CC -!- FUNCTION: [Isoform 2]: Activates transcription presumably by CC sequestering inhibitory cofactors away from the promoters. CC {ECO:0000269|PubMed:7515060}. CC -!- FUNCTION: [Isoform 3]: Stress-induced isoform, counteracts the CC transcriptional repression of isoform 1. {ECO:0000269|PubMed:12034827}. CC -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Interacts with CC KAT5; promoting KAT5 autoacetylation and KAT5 deubiquitination by USP7 CC (PubMed:25865756). {ECO:0000269|PubMed:25865756}. CC -!- INTERACTION: CC P18847; Q92870-2: APBB2; NbExp=3; IntAct=EBI-712767, EBI-21535880; CC P18847; P15336: ATF2; NbExp=5; IntAct=EBI-712767, EBI-1170906; CC P18847; P18847: ATF3; NbExp=3; IntAct=EBI-712767, EBI-712767; CC P18847; P18848: ATF4; NbExp=9; IntAct=EBI-712767, EBI-492498; CC P18847; P17544: ATF7; NbExp=3; IntAct=EBI-712767, EBI-765623; CC P18847; P54253: ATXN1; NbExp=6; IntAct=EBI-712767, EBI-930964; CC P18847; Q16520: BATF; NbExp=2; IntAct=EBI-712767, EBI-749503; CC P18847; Q9NR55: BATF3; NbExp=5; IntAct=EBI-712767, EBI-10312707; CC P18847; P49715: CEBPA; NbExp=2; IntAct=EBI-712767, EBI-1172054; CC P18847; Q15744: CEBPE; NbExp=2; IntAct=EBI-712767, EBI-3907048; CC P18847; P53567: CEBPG; NbExp=5; IntAct=EBI-712767, EBI-740209; CC P18847; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-712767, EBI-25840379; CC P18847; P35638: DDIT3; NbExp=23; IntAct=EBI-712767, EBI-742651; CC P18847; Q14192: FHL2; NbExp=3; IntAct=EBI-712767, EBI-701903; CC P18847; P01100: FOS; NbExp=2; IntAct=EBI-712767, EBI-852851; CC P18847; P05412: JUN; NbExp=9; IntAct=EBI-712767, EBI-852823; CC P18847; P17275: JUNB; NbExp=6; IntAct=EBI-712767, EBI-748062; CC P18847; P17535: JUND; NbExp=3; IntAct=EBI-712767, EBI-2682803; CC P18847; Q9ULX9: MAFF; NbExp=2; IntAct=EBI-712767, EBI-721128; CC P18847; O95644: NFATC1; NbExp=2; IntAct=EBI-712767, EBI-6907210; CC P18847; Q16236: NFE2L2; NbExp=5; IntAct=EBI-712767, EBI-2007911; CC P18847; D3DTS7: PMP22; NbExp=3; IntAct=EBI-712767, EBI-25882629; CC P18847; P37840: SNCA; NbExp=3; IntAct=EBI-712767, EBI-985879; CC P18847; Q13148: TARDBP; NbExp=6; IntAct=EBI-712767, EBI-372899; CC P18847; P09936: UCHL1; NbExp=3; IntAct=EBI-712767, EBI-714860; CC P18847-3; Q04206: RELA; NbExp=5; IntAct=EBI-9844134, EBI-73886; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, CC ECO:0000269|PubMed:12034827}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=ATF3; CC IsoId=P18847-1; Sequence=Displayed; CC Name=2; Synonyms=ATF3-delta-Zip {ECO:0000303|PubMed:7515060}; CC IsoId=P18847-2; Sequence=VSP_000592; CC Name=3; Synonyms=ATF3-delta-Zip2a/TF3-delta-Zip2b; CC IsoId=P18847-3; Sequence=VSP_043150; CC Name=4; Synonyms=ATF3-delta-Zip2c; CC IsoId=P18847-4; Sequence=VSP_043182, VSP_043150; CC Name=5; CC IsoId=P18847-5; Sequence=VSP_046966; CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/atf3/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/719/ATF3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L19871; AAA20506.1; -; mRNA. DR EMBL; AB066566; BAB84092.1; -; mRNA. DR EMBL; AB078026; BAC00495.1; -; mRNA. DR EMBL; AB078027; BAC00496.1; -; mRNA. DR EMBL; AY313927; AAP93896.1; -; mRNA. DR EMBL; BT006996; AAP35642.1; -; mRNA. DR EMBL; AY426987; AAQ93358.1; -; Genomic_DNA. DR EMBL; AK312998; BAG35834.1; -; mRNA. DR EMBL; DA589280; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR450334; CAG29330.1; -; mRNA. DR EMBL; AC092803; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93385.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93386.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93387.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93388.1; -; Genomic_DNA. DR EMBL; BC006322; AAH06322.1; -; mRNA. DR CCDS; CCDS1506.1; -. [P18847-1] DR CCDS; CCDS41464.1; -. [P18847-3] DR CCDS; CCDS55688.1; -. [P18847-4] DR CCDS; CCDS58059.1; -. [P18847-5] DR PIR; A54025; A54025. DR PIR; B54025; B54025. DR PIR; C34223; C34223. DR RefSeq; NP_001025458.1; NM_001030287.3. [P18847-1] DR RefSeq; NP_001035709.1; NM_001040619.2. [P18847-3] DR RefSeq; NP_001193413.2; NM_001206484.2. [P18847-5] DR RefSeq; NP_001193415.1; NM_001206486.2. [P18847-4] DR RefSeq; NP_001193417.2; NM_001206488.2. [P18847-5] DR RefSeq; NP_001665.1; NM_001674.3. [P18847-1] DR RefSeq; XP_005273203.1; XM_005273146.1. [P18847-1] DR RefSeq; XP_011507881.1; XM_011509579.1. [P18847-1] DR AlphaFoldDB; P18847; -. DR SMR; P18847; -. DR BioGRID; 106957; 91. DR ComplexPortal; CPX-6385; bZIP transcription factor complex, ATF3-ATF4. DR ComplexPortal; CPX-6407; bZIP transcription factor complex, ATF2-ATF3. DR ComplexPortal; CPX-6465; bZIP transcription factor complex, ATF3-ATF3. DR ComplexPortal; CPX-6466; bZIP transcription factor complex, ATF3-ATF7. DR ComplexPortal; CPX-6467; bZIP transcription factor complex, ATF3-BATF. DR ComplexPortal; CPX-6468; bZIP transcription factor complex, ATF3-BATF3. DR ComplexPortal; CPX-6469; bZIP transcription factor complex, ATF3-CEBPA. DR ComplexPortal; CPX-6470; bZIP transcription factor complex, ATF3-CEBPB. DR ComplexPortal; CPX-6471; bZIP transcription factor complex, ATF3-CEBPG. DR ComplexPortal; CPX-6472; bZIP transcription factor complex, ATF3-CEBPE. DR ComplexPortal; CPX-6473; bZIP transcription factor complex, ATF3-DDIT3. DR ComplexPortal; CPX-6474; bZIP transcription factor complex, ATF3-JUN. DR ComplexPortal; CPX-6476; bZIP transcription factor complex, ATF3-JUNB. DR ComplexPortal; CPX-6477; bZIP transcription factor complex, ATF3-FOS. DR ComplexPortal; CPX-6478; bZIP transcription factor complex, ATF3-FOSL1. DR ComplexPortal; CPX-6479; bZIP transcription factor complex, ATF3-FOSL2. DR ComplexPortal; CPX-6480; bZIP transcription factor complex, ATF3-MAFF. DR ComplexPortal; CPX-6481; bZIP transcription factor complex, ATF3-MAFG. DR CORUM; P18847; -. DR DIP; DIP-344N; -. DR IntAct; P18847; 63. DR MINT; P18847; -. DR STRING; 9606.ENSP00000344352; -. DR DrugBank; DB00852; Pseudoephedrine. DR GlyGen; P18847; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P18847; -. DR PhosphoSitePlus; P18847; -. DR BioMuta; ATF3; -. DR DMDM; 1168543; -. DR CPTAC; CPTAC-1755; -. DR EPD; P18847; -. DR jPOST; P18847; -. DR MassIVE; P18847; -. DR MaxQB; P18847; -. DR PaxDb; 9606-ENSP00000344352; -. DR PeptideAtlas; P18847; -. DR ProteomicsDB; 53611; -. [P18847-1] DR ProteomicsDB; 53612; -. [P18847-2] DR ProteomicsDB; 53613; -. [P18847-3] DR ProteomicsDB; 53614; -. [P18847-4] DR ProteomicsDB; 65367; -. DR Pumba; P18847; -. DR TopDownProteomics; P18847-1; -. [P18847-1] DR Antibodypedia; 658; 637 antibodies from 37 providers. DR DNASU; 467; -. DR Ensembl; ENST00000336937.8; ENSP00000336908.4; ENSG00000162772.18. [P18847-4] DR Ensembl; ENST00000341491.9; ENSP00000344352.4; ENSG00000162772.18. [P18847-1] DR Ensembl; ENST00000366983.5; ENSP00000355950.1; ENSG00000162772.18. [P18847-3] DR Ensembl; ENST00000366987.6; ENSP00000355954.2; ENSG00000162772.18. [P18847-1] DR Ensembl; ENST00000464547.5; ENSP00000432208.1; ENSG00000162772.18. [P18847-3] DR Ensembl; ENST00000613104.1; ENSP00000480606.1; ENSG00000162772.18. [P18847-5] DR GeneID; 467; -. DR KEGG; hsa:467; -. DR MANE-Select; ENST00000341491.9; ENSP00000344352.4; NM_001674.4; NP_001665.1. DR UCSC; uc001hjf.4; human. [P18847-1] DR AGR; HGNC:785; -. DR CTD; 467; -. DR DisGeNET; 467; -. DR GeneCards; ATF3; -. DR HGNC; HGNC:785; ATF3. DR HPA; ENSG00000162772; Low tissue specificity. DR MIM; 603148; gene. DR neXtProt; NX_P18847; -. DR OpenTargets; ENSG00000162772; -. DR PharmGKB; PA25085; -. DR VEuPathDB; HostDB:ENSG00000162772; -. DR eggNOG; KOG1414; Eukaryota. DR GeneTree; ENSGT00940000156376; -. DR HOGENOM; CLU_088612_0_2_1; -. DR InParanoid; P18847; -. DR OMA; ACMNTER; -. DR OrthoDB; 5354319at2759; -. DR PhylomeDB; P18847; -. DR TreeFam; TF326301; -. DR PathwayCommons; P18847; -. DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress. DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency. DR Reactome; R-HSA-9648895; Response of EIF2AK1 (HRI) to heme deficiency. DR SignaLink; P18847; -. DR SIGNOR; P18847; -. DR BioGRID-ORCS; 467; 17 hits in 1192 CRISPR screens. DR ChiTaRS; ATF3; human. DR GeneWiki; ATF3; -. DR GenomeRNAi; 467; -. DR Pharos; P18847; Tbio. DR PRO; PR:P18847; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P18847; Protein. DR Bgee; ENSG00000162772; Expressed in vena cava and 201 other cell types or tissues. DR ExpressionAtlas; P18847; baseline and differential. DR GO; GO:1990622; C:CHOP-ATF3 complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. 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; IGI:ParkinsonsUK-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl. DR CDD; cd14722; bZIP_ATF3; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR000837; AP-1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR23351:SF23; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-3; 1. DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1. DR Pfam; PF00170; bZIP_1; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. DR Genevisible; P18847; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; DNA-binding; Isopeptide bond; KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..181 FT /note="Cyclic AMP-dependent transcription factor ATF-3" FT /id="PRO_0000076581" FT DOMAIN 86..149 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 88..110 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 114..142 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT MOD_RES 162 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 78 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 175 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..57 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046966" FT VAR_SEQ 14..42 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12881527" FT /id="VSP_043182" FT VAR_SEQ 116..181 FT /note="KESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDER FT NLFIQQIKEGTLQS -> LQY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7515060" FT /id="VSP_000592" FT VAR_SEQ 117..181 FT /note="ESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERN FT LFIQQIKEGTLQS -> LPRPFWVQKTCIWAVDSCK (in isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|PubMed:12034827, FT ECO:0000303|PubMed:12881527" FT /id="VSP_043150" FT VARIANT 38 FT /note="T -> M (in dbSNP:rs11571541)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_048442" FT VARIANT 168 FT /note="N -> T (found in a patient with childhood apraxia of FT speech; uncertain significance)" FT /evidence="ECO:0000269|PubMed:29463886" FT /id="VAR_081532" FT CONFLICT 132 FT /note="I -> L (in Ref. 11; no nucleotide entry)" FT /evidence="ECO:0000305" SQ SEQUENCE 181 AA; 20576 MW; EC5D8F065EEE2D9C CRC64; MMLQHPGQVS ASEVSASAIV PCLSPPGSLV FEDFANLTPF VKEELRFAIQ NKHLCHRMSS ALESVTVSDR PLGVSITKAE VAPEEDERKK RRRERNKIAA AKCRNKKKEK TECLQKESEK LESVNAELKA QIEELKNEKQ HLIYMLNLHR PTCIVRAQNG RTPEDERNLF IQQIKEGTLQ S //