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Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF) (SF-HT-activated gene 2 protein) (SFA-2)

 BATF_HUMAN              Reviewed;         125 AA.
Q16520;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 156.
RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
AltName: Full=B-cell-activating transcription factor;
Short=B-ATF;
AltName: Full=SF-HT-activated gene 2 protein;
Short=SFA-2;
Name=BATF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JUN PROTEINS, AND TISSUE
SPECIFICITY.
PubMed=8570175;
Dorsey M.J., Tae H.-J., Sollenberger K.G., Mascarenhas N.T.,
Johansen L.M., Taparowsky E.J.;
"B-ATF: a novel human bZIP protein that associates with members of the
AP-1 transcription factor family.";
Oncogene 11:2255-2265(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=8630063; DOI=10.1006/bbrc.1996.0700;
Hasegawa H., Utsunomiya Y., Kishimoto K., Tange Y., Yasukawa M.,
Fujita S.;
"SFA-2, a novel bZIP transcription factor induced by human T-cell
leukemia virus type I, is highly expressed in mature lymphocytes.";
Biochem. Biophys. Res. Commun. 222:164-170(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9745044; DOI=10.1007/s003359900881;
Meyer N.P., Johansen L.M., Tae H.-J., Budde P.P., Williams K.L.,
Taparowsky E.J.;
"Genomic organization of human B-ATF, a target for regulation by EBV
and HTLV-1.";
Mamm. Genome 9:849-852(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma;
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).
[6]
INTERACTION WITH IFI35.
PubMed=8954125; DOI=10.1006/bbrc.1996.1799;
Wang X., Johansen L.M., Tae H.-J., Taparowsky E.J.;
"IFP 35 forms complexes with B-ATF, a member of the AP1 family of
transcription factors.";
Biochem. Biophys. Res. Commun. 229:316-322(1996).
[7]
TISSUE SPECIFICITY.
PubMed=10777209; DOI=10.1038/sj.onc.1203491;
Echlin D.R., Tae H.-J., Mitin N., Taparowsky E.J.;
"B-ATF functions as a negative regulator of AP-1 mediated
transcription and blocks cellular transformation by Ras and Fos.";
Oncogene 19:1752-1763(2000).
[8]
INDUCTION.
PubMed=12719594; DOI=10.1128/JVI.77.10.6029-6040.2003;
Johansen L.M., Deppmann C.D., Erickson K.D., Coffin W.F. III,
Thornton T.M., Humphrey S.E., Martin J.M., Taparowsky E.J.;
"EBNA2 and activated Notch induce expression of BATF.";
J. Virol. 77:6029-6040(2003).
[9]
INDUCTION.
PubMed=20890291; DOI=10.1038/nm.2232;
Quigley M., Pereyra F., Nilsson B., Porichis F., Fonseca C.,
Eichbaum Q., Julg B., Jesneck J.L., Brosnahan K., Imam S., Russell K.,
Toth I., Piechocka-Trocha A., Dolfi D., Angelosanto J., Crawford A.,
Shin H., Kwon D.S., Zupkosky J., Francisco L., Freeman G.J.,
Wherry E.J., Kaufmann D.E., Walker B.D., Ebert B., Haining W.N.;
"Transcriptional analysis of HIV-specific CD8+ T cells shows that PD-1
inhibits T cell function by upregulating BATF.";
Nat. Med. 16:1147-1151(2010).
-!- FUNCTION: AP-1 family transcription factor that controls the
differentiation of lineage-specific cells in the immune system:
specifically mediates the differentiation of T-helper 17 cells
(Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells
and class-switch recombination (CSR) in B-cells. Acts via the
formation of a heterodimer with JUNB that recognizes and binds DNA
sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a
complex with IRF4 (or IRF8) in immune cells, leading to
recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-
specific regulatory element, followed by cooperative binding of
BATF and IRF4 (or IRF8) and activation of genes. Controls
differentiation of T-helper cells producing interleukin-17 (Th17
cells) by binding to Th17-associated gene promoters: regulates
expression of the transcription factor RORC itself and RORC target
genes such as IL17 (IL17A or IL17B). Also involved in
differentiation of follicular T-helper cells (TfH) by directing
expression of BCL6 and MAF. In B-cells, involved in class-switch
recombination (CSR) by controlling the expression of both AICDA
and of germline transcripts of the intervening heavy-chain region
and constant heavy-chain region (I(H)-C(H)). Following infection,
can participate in CD8(+) dendritic cell differentiation via
interaction with IRF4 and IRF8 to mediate cooperative gene
activation. Regulates effector CD8(+) T-cell differentiation by
regulating expression of SIRT1. Following DNA damage, part of a
differentiation checkpoint that limits self-renewal of
hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to
differentiation of HSCs, thereby restricting self-renewal of HSCs
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-
JUNB heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP
domain) with IRF4 and IRF8; the interaction is direct (By
similarity). Also forms heterodimers with JUN and JUND. Also
interacts with IFI35. {ECO:0000250, ECO:0000269|PubMed:8570175,
ECO:0000269|PubMed:8954125}.
-!- INTERACTION:
P17676:CEBPB; NbExp=2; IntAct=EBI-749503, EBI-969696;
P53567:CEBPG; NbExp=2; IntAct=EBI-749503, EBI-740209;
P35638:DDIT3; NbExp=6; IntAct=EBI-749503, EBI-742651;
Q9HD26:GOPC; NbExp=3; IntAct=EBI-749503, EBI-349832;
P05412:JUN; NbExp=2; IntAct=EBI-749503, EBI-852823;
P17275:JUNB; NbExp=9; IntAct=EBI-749503, EBI-748062;
P17535:JUND; NbExp=2; IntAct=EBI-749503, EBI-2682803;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}. Cytoplasm {ECO:0000250}. Note=Present in the
nucleus and cytoplasm, but shows increased nuclear translocation
after activation of T-cells. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed at highest levels in lung, and at
lower levels in placenta, liver, kidney, spleen, and peripheral
blood. Detected in SW480 colorectal cancer cell line and several
hematopoietic tumor cell lines, including Raji Burkitt's lymphoma.
Strongly expressed in mature B- and T-lymphocytes. Also expressed
in moderate levels in lymph node and appendix and at low levels in
thymus and bone marrow (PubMed:10777209).
{ECO:0000269|PubMed:10777209, ECO:0000269|PubMed:8570175,
ECO:0000269|PubMed:8630063}.
-!- INDUCTION: Up-regulated by PDCD1 following infection by HIV-1
virus, leading to inhibit T-cell functions and exhaust T-cells.
Up-regulated by Epstein-Barr virus (EBV) protein EBNA2 following
infection by EBV. {ECO:0000269|PubMed:12719594,
ECO:0000269|PubMed:20890291}.
-!- PTM: Phosphorylated on serine and threonine residues and at least
one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA
binding activity and transforms it as a negative regulator of AP-1
mediated transcription (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; U15460; AAC50314.1; -; mRNA.
EMBL; D42106; BAA07686.1; -; mRNA.
EMBL; AF016898; AAC78243.1; -; Genomic_DNA.
EMBL; AC007182; AAD51372.1; -; Genomic_DNA.
EMBL; BC032294; AAH32294.1; -; mRNA.
CCDS; CCDS9843.1; -.
PIR; JC4799; JC4799.
RefSeq; NP_006390.1; NM_006399.3.
UniGene; Hs.509964; -.
ProteinModelPortal; Q16520; -.
SMR; Q16520; -.
BioGrid; 115792; 19.
DIP; DIP-52482N; -.
IntAct; Q16520; 17.
MINT; Q16520; -.
STRING; 9606.ENSP00000286639; -.
iPTMnet; Q16520; -.
PhosphoSitePlus; Q16520; -.
BioMuta; BATF; -.
DMDM; 32171340; -.
EPD; Q16520; -.
MaxQB; Q16520; -.
PaxDb; Q16520; -.
PeptideAtlas; Q16520; -.
PRIDE; Q16520; -.
ProteomicsDB; 60892; -.
DNASU; 10538; -.
Ensembl; ENST00000286639; ENSP00000286639; ENSG00000156127.
GeneID; 10538; -.
KEGG; hsa:10538; -.
UCSC; uc001xrr.4; human.
CTD; 10538; -.
DisGeNET; 10538; -.
EuPathDB; HostDB:ENSG00000156127.6; -.
GeneCards; BATF; -.
HGNC; HGNC:958; BATF.
HPA; HPA059588; -.
HPA; HPA064962; -.
MIM; 612476; gene.
neXtProt; NX_Q16520; -.
OpenTargets; ENSG00000156127; -.
PharmGKB; PA25268; -.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00390000016869; -.
HOGENOM; HOG000236325; -.
HOVERGEN; HBG039173; -.
InParanoid; Q16520; -.
KO; K09034; -.
OMA; DSNDTSY; -.
OrthoDB; EOG091G0YSM; -.
PhylomeDB; Q16520; -.
TreeFam; TF332340; -.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
GeneWiki; BATF_(gene); -.
GenomeRNAi; 10538; -.
PRO; PR:Q16520; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000156127; Expressed in 142 organ(s), highest expression level in blood.
CleanEx; HS_BATF; -.
ExpressionAtlas; Q16520; baseline and differential.
Genevisible; Q16520; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0001816; P:cytokine production; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
GO; GO:0045064; P:T-helper 2 cell differentiation; ISS:UniProtKB.
InterPro; IPR000837; AP-1.
InterPro; IPR029820; BATF.
InterPro; IPR004827; bZIP.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF14; PTHR23351:SF14; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Differentiation; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 125 Basic leucine zipper transcriptional
factor ATF-like.
/FTId=PRO_0000076595.
DOMAIN 26 89 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 28 50 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 54 75 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:O35284}.
MOD_RES 48 48 Phosphothreonine.
{ECO:0000250|UniProtKB:O35284}.
SEQUENCE 125 AA; 14120 MW; 7FD633C6F1963DF4 CRC64;
MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED
LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS
PRFQP


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