BATF3_HUMAN
ID BATF3_HUMAN Reviewed; 127 AA.
AC Q9NR55;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Basic leucine zipper transcriptional factor ATF-like 3;
DE Short=B-ATF-3;
DE AltName: Full=21 kDa small nuclear factor isolated from T-cells;
DE AltName: Full=Jun dimerization protein p21SNFT;
GN Name=BATF3; Synonyms=SNFT;
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], AND FUNCTION.
RX PubMed=10878360; DOI=10.4049/jimmunol.165.2.860;
RA Iacobelli M., Wachsman W., McGuire K.L.;
RT "Repression of IL-2 promoter activity by the novel basic leucine zipper
RT p21SNFT protein.";
RL J. Immunol. 165:860-868(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH JUN.
RX PubMed=12087103; DOI=10.1074/jbc.m205048200;
RA Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L.;
RT "Correlation of transcriptional repression by p21(SNFT) with changes in
RT DNA.NF-AT complex interactions.";
RL J. Biol. Chem. 277:34967-34977(2002).
RN [6]
RP FUNCTION.
RX PubMed=15467742; DOI=10.1038/sj.onc.1208109;
RA Bower K.E., Fritz J.M., McGuire K.L.;
RT "Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro
RT invasiveness of hepatocarcinoma cells.";
RL Oncogene 23:8805-8814(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-31, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: AP-1 family transcription factor that controls the
CC differentiation of CD8(+) thymic conventional dendritic cells in the
CC immune system. Required for development of CD8-alpha(+) classical
CC dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-
CC present antigens to CD8 T-cells and produce interleukin-12 (IL12) in
CC response to pathogens (By similarity). Acts via the formation of a
CC heterodimer with JUN family proteins that recognizes and binds DNA
CC sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes.
CC {ECO:0000250, ECO:0000269|PubMed:10878360, ECO:0000269|PubMed:12087103,
CC ECO:0000269|PubMed:15467742}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with JUN family proteins.
CC Interacts with JUN. {ECO:0000269|PubMed:12087103}.
CC -!- INTERACTION:
CC Q9NR55; P21549: AGXT; NbExp=3; IntAct=EBI-10312707, EBI-727098;
CC Q9NR55; P15336: ATF2; NbExp=3; IntAct=EBI-10312707, EBI-1170906;
CC Q9NR55; P18847: ATF3; NbExp=5; IntAct=EBI-10312707, EBI-712767;
CC Q9NR55; P18848: ATF4; NbExp=2; IntAct=EBI-10312707, EBI-492498;
CC Q9NR55; Q9BYV9: BACH2; NbExp=5; IntAct=EBI-10312707, EBI-1642333;
CC Q9NR55; P49715: CEBPA; NbExp=2; IntAct=EBI-10312707, EBI-1172054;
CC Q9NR55; Q15744: CEBPE; NbExp=2; IntAct=EBI-10312707, EBI-3907048;
CC Q9NR55; P53567: CEBPG; NbExp=3; IntAct=EBI-10312707, EBI-740209;
CC Q9NR55; Q02930-3: CREB5; NbExp=5; IntAct=EBI-10312707, EBI-10192698;
CC Q9NR55; Q10586: DBP; NbExp=2; IntAct=EBI-10312707, EBI-3908088;
CC Q9NR55; P35638: DDIT3; NbExp=8; IntAct=EBI-10312707, EBI-742651;
CC Q9NR55; P35638-2: DDIT3; NbExp=3; IntAct=EBI-10312707, EBI-10173632;
CC Q9NR55; P15407: FOSL1; NbExp=3; IntAct=EBI-10312707, EBI-744510;
CC Q9NR55; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-10312707, EBI-11959863;
CC Q9NR55; Q16534: HLF; NbExp=2; IntAct=EBI-10312707, EBI-2798854;
CC Q9NR55; P05412: JUN; NbExp=7; IntAct=EBI-10312707, EBI-852823;
CC Q9NR55; P17275: JUNB; NbExp=6; IntAct=EBI-10312707, EBI-748062;
CC Q9NR55; P17535: JUND; NbExp=3; IntAct=EBI-10312707, EBI-2682803;
CC Q9NR55; Q9ULX9: MAFF; NbExp=2; IntAct=EBI-10312707, EBI-721128;
CC Q9NR55; O15525: MAFG; NbExp=2; IntAct=EBI-10312707, EBI-713514;
CC Q9NR55; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-10312707, EBI-372094;
CC Q9NR55; Q15915: ZIC1; NbExp=3; IntAct=EBI-10312707, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:12087103}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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; AF255346; AAF73966.1; -; mRNA.
DR EMBL; AL591647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93381.1; -; Genomic_DNA.
DR EMBL; BC117489; AAI17490.1; -; mRNA.
DR EMBL; BC117491; AAI17492.1; -; mRNA.
DR CCDS; CCDS1508.1; -.
DR RefSeq; NP_061134.1; NM_018664.2.
DR AlphaFoldDB; Q9NR55; -.
DR SMR; Q9NR55; -.
DR BioGRID; 120689; 55.
DR ComplexPortal; CPX-6414; bZIP transcription factor complex, ATF2-BATF3.
DR ComplexPortal; CPX-6468; bZIP transcription factor complex, ATF3-BATF3.
DR ComplexPortal; CPX-6524; bZIP transcription factor complex, ATF4-BATF3.
DR ComplexPortal; CPX-7018; bZIP transcription factor complex, BATF-BATF3.
DR ComplexPortal; CPX-7092; bZIP transcription factor complex, BATF3-BATF3.
DR ComplexPortal; CPX-7093; bZIP transcription factor complex, BACH2-BATF3.
DR ComplexPortal; CPX-7095; bZIP transcription factor complex, BATF3-CEBPA.
DR ComplexPortal; CPX-7096; bZIP transcription factor complex, BATF3-CEBPB.
DR ComplexPortal; CPX-7097; bZIP transcription factor complex, BATF3-CEBPG.
DR ComplexPortal; CPX-7098; bZIP transcription factor complex, BATF3-CEBPD.
DR ComplexPortal; CPX-7099; bZIP transcription factor complex, BATF3-CEBPE.
DR ComplexPortal; CPX-7100; bZIP transcription factor complex, BATF3-JUN.
DR ComplexPortal; CPX-7101; bZIP transcription factor complex, BATF3-JUNB.
DR ComplexPortal; CPX-7102; bZIP transcription factor complex, BATF3-JUND.
DR ComplexPortal; CPX-7103; bZIP transcription factor complex, BATF3-MAFF.
DR ComplexPortal; CPX-7105; bZIP transcription factor complex, BATF3-MAFG.
DR ComplexPortal; CPX-7106; bZIP transcription factor complex, BATF3-DDIT3.
DR ComplexPortal; CPX-7107; bZIP transcription factor complex, BATF3-HLF.
DR ComplexPortal; CPX-7108; bZIP transcription factor complex, BATF3-DBP.
DR ComplexPortal; CPX-7109; bZIP transcription factor complex, BATF3-CREB3.
DR IntAct; Q9NR55; 52.
DR MINT; Q9NR55; -.
DR STRING; 9606.ENSP00000243440; -.
DR iPTMnet; Q9NR55; -.
DR PhosphoSitePlus; Q9NR55; -.
DR BioMuta; BATF3; -.
DR DMDM; 74752916; -.
DR EPD; Q9NR55; -.
DR MassIVE; Q9NR55; -.
DR MaxQB; Q9NR55; -.
DR PaxDb; Q9NR55; -.
DR PeptideAtlas; Q9NR55; -.
DR PRIDE; Q9NR55; -.
DR ProteomicsDB; 82278; -.
DR Antibodypedia; 34609; 150 antibodies from 22 providers.
DR DNASU; 55509; -.
DR Ensembl; ENST00000243440.2; ENSP00000243440.1; ENSG00000123685.9.
DR GeneID; 55509; -.
DR KEGG; hsa:55509; -.
DR MANE-Select; ENST00000243440.2; ENSP00000243440.1; NM_018664.3; NP_061134.1.
DR UCSC; uc001hjl.3; human.
DR CTD; 55509; -.
DR DisGeNET; 55509; -.
DR GeneCards; BATF3; -.
DR HGNC; HGNC:28915; BATF3.
DR HPA; ENSG00000123685; Low tissue specificity.
DR MIM; 612470; gene.
DR neXtProt; NX_Q9NR55; -.
DR OpenTargets; ENSG00000123685; -.
DR PharmGKB; PA162377349; -.
DR VEuPathDB; HostDB:ENSG00000123685; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000161120; -.
DR HOGENOM; CLU_088612_1_1_1; -.
DR InParanoid; Q9NR55; -.
DR OMA; TMNFVTI; -.
DR OrthoDB; 1440552at2759; -.
DR PhylomeDB; Q9NR55; -.
DR TreeFam; TF332340; -.
DR PathwayCommons; Q9NR55; -.
DR SignaLink; Q9NR55; -.
DR BioGRID-ORCS; 55509; 11 hits in 1085 CRISPR screens.
DR ChiTaRS; BATF3; human.
DR GenomeRNAi; 55509; -.
DR Pharos; Q9NR55; Tbio.
DR PRO; PR:Q9NR55; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NR55; protein.
DR Bgee; ENSG00000123685; Expressed in spleen and 123 other tissues.
DR Genevisible; Q9NR55; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-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:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029818; p21SNFT.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF13; PTHR23351:SF13; 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 Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..127
FT /note="Basic leucine zipper transcriptional factor ATF-like
FT 3"
FT /id="PRO_0000326106"
FT DOMAIN 35..98
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..62
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 63..91
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 11
FT /note="V -> I (in dbSNP:rs2202683)"
FT /id="VAR_039988"
SQ SEQUENCE 127 AA; 14468 MW; 3C595D708D5D4F5F CRC64;
MSQGLPAAGS VLQRSVAAPG NQPQPQPQQQ SPEDDDRKVR RREKNRVAAQ RSRKKQTQKA
DKLHEEYESL EQENTMLRRE IGKLTEELKH LTEALKEHEK MCPLLLCPMN FVPVPPRPDP
VAGCLPR
