ATF3_HUMAN
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 03-AUG-2022, entry version 214.
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="http://atlasgeneticsoncology.org/Genes/ATF3ID719ch1q32.html";
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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; 83.
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; 61.
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; P18847; -.
DR PeptideAtlas; P18847; -.
DR PRIDE; 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 TopDownProteomics; P18847-1; -. [P18847-1]
DR Antibodypedia; 658; 579 antibodies from 37 providers.
DR DNASU; 467; -.
DR Ensembl; ENST00000336937.8; ENSP00000336908.4; ENSG00000162772.17. [P18847-4]
DR Ensembl; ENST00000341491.9; ENSP00000344352.4; ENSG00000162772.17. [P18847-1]
DR Ensembl; ENST00000366983.5; ENSP00000355950.1; ENSG00000162772.17. [P18847-3]
DR Ensembl; ENST00000366987.6; ENSP00000355954.2; ENSG00000162772.17. [P18847-1]
DR Ensembl; ENST00000464547.5; ENSP00000432208.1; ENSG00000162772.17. [P18847-3]
DR Ensembl; ENST00000613104.1; ENSP00000480606.1; ENSG00000162772.17. [P18847-5]
DR Ensembl; ENST00000613954.4; ENSP00000483576.1; ENSG00000162772.17. [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 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; PLEMSVM; -.
DR OrthoDB; 1457971at2759; -.
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; 15 hits in 1112 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 199 other tissues.
DR ExpressionAtlas; P18847; baseline and differential.
DR Genevisible; P18847; HS.
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; IDA: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:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0061394; P:regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; TAS:ParkinsonsUK-UCL.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029812; ATF3.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF23; PTHR23351:SF23; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
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 (de novo variant found in a patient with
FT childhood apraxia of speech; unknown pathological
FT 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
