BATF_MOUSE
ID BATF_MOUSE Reviewed; 125 AA.
AC O35284; A2RT86;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
DE AltName: Full=B-cell-activating transcription factor;
DE Short=B-ATF;
GN Name=Batf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11466704;
RX DOI=10.1002/1521-4141(200105)31:5<1620::aid-immu1620>3.0.co;2-3;
RA Williams K.L., Nanda I., Lyons G.E., Kuo C.T., Schmid M., Leiden J.M.,
RA Kaplan M.H., Taparowsky E.J.;
RT "Characterization of murine BATF: a negative regulator of activator
RT protein-1 activity in the thymus.";
RL Eur. J. Immunol. 31:1620-1627(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP INDUCTION BY STAT3.
RX PubMed=12444555; DOI=10.1038/sj.onc.1205918;
RA Senga T., Iwamoto T., Humphrey S.E., Yokota T., Taparowsky E.J.,
RA Hamaguchi M.;
RT "Stat3-dependent induction of BATF in M1 mouse myeloid leukemia cells.";
RL Oncogene 21:8186-8191(2002).
RN [5]
RP SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH JUNB, PHOSPHORYLATION
RP AT SER-43 AND THR-48, AND MUTAGENESIS OF SER-43 AND THR-48.
RX PubMed=12809553; DOI=10.1042/bj20030455;
RA Deppmann C.D., Thornton T.M., Utama F.E., Taparowsky E.J.;
RT "Phosphorylation of BATF regulates DNA binding: a novel mechanism for AP-1
RT (activator protein-1) regulation.";
RL Biochem. J. 374:423-431(2003).
RN [6]
RP FUNCTION.
RX PubMed=12594265; DOI=10.4049/jimmunol.170.5.2417;
RA Williams K.L., Zullo A.J., Kaplan M.H., Brutkiewicz R.R., Deppmann C.D.,
RA Vinson C., Taparowsky E.J.;
RT "BATF transgenic mice reveal a role for activator protein-1 in NKT cell
RT development.";
RL J. Immunol. 170:2417-2426(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND INTERACTION WITH JUNB.
RX PubMed=19578362; DOI=10.1038/nature08114;
RA Schraml B.U., Hildner K., Ise W., Lee W.L., Smith W.A., Solomon B.,
RA Sahota G., Sim J., Mukasa R., Cemerski S., Hatton R.D., Stormo G.D.,
RA Weaver C.T., Russell J.H., Murphy T.L., Murphy K.M.;
RT "The AP-1 transcription factor Batf controls T(H)17 differentiation.";
RL Nature 460:405-409(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20421391; DOI=10.1084/jem.20091548;
RA Betz B.C., Jordan-Williams K.L., Wang C., Kang S.G., Liao J., Logan M.R.,
RA Kim C.H., Taparowsky E.J.;
RT "Batf coordinates multiple aspects of B and T cell function required for
RT normal antibody responses.";
RL J. Exp. Med. 207:933-942(2010).
RN [9]
RP FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=21572431; DOI=10.1038/ni.2037;
RA Ise W., Kohyama M., Schraml B.U., Zhang T., Schwer B., Basu U., Alt F.W.,
RA Tang J., Oltz E.M., Murphy T.L., Murphy K.M.;
RT "The transcription factor BATF controls the global regulators of class-
RT switch recombination in both B cells and T cells.";
RL Nat. Immunol. 12:536-543(2011).
RN [10]
RP FUNCTION.
RX PubMed=22001828; DOI=10.1038/ni.2134;
RA Rutz S., Noubade R., Eidenschenk C., Ota N., Zeng W., Zheng Y., Hackney J.,
RA Ding J., Singh H., Ouyang W.;
RT "Transcription factor c-Maf mediates the TGF-beta-dependent suppression of
RT IL-22 production in T(H)17 cells.";
RL Nat. Immunol. 12:1238-1245(2011).
RN [11]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=21873234; DOI=10.1073/pnas.1105133108;
RA Kuroda S., Yamazaki M., Abe M., Sakimura K., Takayanagi H., Iwai Y.;
RT "Basic leucine zipper transcription factor, ATF-like (BATF) regulates
RT epigenetically and energetically effector CD8 T-cell differentiation via
RT Sirt1 expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14885-14889(2011).
RN [12]
RP FUNCTION, AND INDUCTION BY STAT3.
RX PubMed=22385964; DOI=10.1016/j.cell.2012.01.040;
RA Wang J., Sun Q., Morita Y., Jiang H., Gross A., Lechel A., Hildner K.,
RA Guachalla L.M., Gompf A., Hartmann D., Schambach A., Wuestefeld T.,
RA Dauch D., Schrezenmeier H., Hofmann W.K., Nakauchi H., Ju Z., Kestler H.A.,
RA Zender L., Rudolph K.L.;
RT "A differentiation checkpoint limits hematopoietic stem cell self-renewal
RT in response to DNA damage.";
RL Cell 148:1001-1014(2012).
RN [13]
RP FUNCTION.
RX PubMed=23021777; DOI=10.1016/j.cell.2012.09.016;
RA Ciofani M., Madar A., Galan C., Sellars M., Mace K., Pauli F., Agarwal A.,
RA Huang W., Parkurst C.N., Muratet M., Newberry K.M., Meadows S.,
RA Greenfield A., Yang Y., Jain P., Kirigin F.K., Birchmeier C., Wagner E.F.,
RA Murphy K.M., Myers R.M., Bonneau R., Littman D.R.;
RT "A validated regulatory network for Th17 cell specification.";
RL Cell 151:289-303(2012).
RN [14]
RP INDUCTION BY STAT5.
RX PubMed=22318729; DOI=10.1074/jbc.m111.324046;
RA Nurieva R.I., Podd A., Chen Y., Alekseev A.M., Yu M., Qi X., Huang H.,
RA Wen R., Wang J., Li H.S., Watowich S.S., Qi H., Dong C., Wang D.;
RT "STAT5 protein negatively regulates T follicular helper (Tfh) cell
RT generation and function.";
RL J. Biol. Chem. 287:11234-11239(2012).
RN [15]
RP FUNCTION, DNA-BINDING, INTERACTION WITH IRF4; IRF8 AND JUNB, AND
RP MUTAGENESIS OF HIS-55; LEU-56; LYS-63; 69-ARG-LYS-70 AND GLU-77.
RX PubMed=22992524; DOI=10.1038/nature11531;
RA Tussiwand R., Lee W.L., Murphy T.L., Mashayekhi M., Kc W., Albring J.C.,
RA Satpathy A.T., Rotondo J.A., Edelson B.T., Kretzer N.M., Wu X., Weiss L.A.,
RA Glasmacher E., Li P., Liao W., Behnke M., Lam S.S., Aurthur C.T.,
RA Leonard W.J., Singh H., Stallings C.L., Sibley L.D., Schreiber R.D.,
RA Murphy K.M.;
RT "Compensatory dendritic cell development mediated by BATF-IRF
RT interactions.";
RL Nature 490:502-507(2012).
RN [16]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH IRF4 AND JUNB.
RX PubMed=22992523; DOI=10.1038/nature11530;
RA Li P., Spolski R., Liao W., Wang L., Murphy T.L., Murphy K.M.,
RA Leonard W.J.;
RT "BATF-JUN is critical for IRF4-mediated transcription in T cells.";
RL Nature 490:543-546(2012).
RN [17]
RP FUNCTION, DNA-BINDING, INTERACTION WITH IRF4 AND JUNB, AND MUTAGENESIS OF
RP HIS-55 AND GLU-77.
RX PubMed=22983707; DOI=10.1126/science.1228309;
RA Glasmacher E., Agrawal S., Chang A.B., Murphy T.L., Zeng W.,
RA Vander Lugt B., Khan A.A., Ciofani M., Spooner C., Rutz S., Hackney J.,
RA Nurieva R., Escalante C.R., Ouyang W., Littman D.R., Murphy K.M., Singh H.;
RT "A genomic regulatory element that directs assembly and function of immune-
RT specific AP-1-IRF complexes.";
RL Science 338:975-980(2012).
CC -!- FUNCTION: AP-1 family transcription factor that controls the
CC differentiation of lineage-specific cells in the immune system:
CC specifically mediates the differentiation of T-helper 17 cells (Th17),
CC follicular T-helper cells (TfH), CD8(+) dendritic cells and class-
CC switch recombination (CSR) in B-cells. Acts via the formation of a
CC heterodimer with JUNB that recognizes and binds DNA sequence 5'-
CC TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4
CC (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-
CC TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by
CC cooperative binding of BATF and IRF4 (or IRF8) and activation of genes.
CC Controls differentiation of T-helper cells producing interleukin-17
CC (Th17 cells) by binding to Th17-associated gene promoters: regulates
CC expression of the transcription factor RORC itself and RORC target
CC genes such as IL17 (IL17A or IL17B). Also involved in differentiation
CC of follicular T-helper cells (TfH) by directing expression of BCL6 and
CC MAF. In B-cells, involved in class-switch recombination (CSR) by
CC controlling the expression of both AICDA and of germline transcripts of
CC the intervening heavy-chain region and constant heavy-chain region
CC (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic
CC cell differentiation via interaction with IRF4 and IRF8 to mediate
CC cooperative gene activation. Regulates effector CD8(+) T-cell
CC differentiation by regulating expression of SIRT1. Following DNA
CC damage, part of a differentiation checkpoint that limits self-renewal
CC of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to
CC differentiation of HSCs, thereby restricting self-renewal of HSCs.
CC {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265,
CC ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391,
CC ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828,
CC ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707,
CC ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524,
CC ECO:0000269|PubMed:23021777}.
CC -!- SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB
CC heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain)
CC with IRF4 and IRF8; the interaction is direct. Also forms heterodimers
CC with JUN and JUND. Interacts with IFI35. {ECO:0000269|PubMed:12809553,
CC ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:22983707,
CC ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524}.
CC -!- INTERACTION:
CC O35284; Q64287: Irf4; NbExp=7; IntAct=EBI-6398523, EBI-6398485;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus
CC and cytoplasm, but shows increased nuclear translocation after
CC activation of T-cells.
CC -!- TISSUE SPECIFICITY: Detected in postnatal and adult lymphoid tissues
CC such as thymus, spleen and lymph nodes. In thymus most concentrated
CC expression is found in the immediate cortical layer. Differentially
CC expressed during T-cell development in thymus. Highly expressed in
CC Th17, Th1 and Th2 cells and in activated B-cells.
CC {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:19578362,
CC ECO:0000269|PubMed:20421391}.
CC -!- INDUCTION: Up-regulated by STAT3 in response to DNA damage. Induces by
CC IL12 at late effector stage. Down-regulated by STAT5 in follicular T-
CC helper cells (TfH). {ECO:0000269|PubMed:12444555,
CC ECO:0000269|PubMed:21873234, ECO:0000269|PubMed:22318729,
CC ECO:0000269|PubMed:22385964}.
CC -!- PTM: Phosphorylated on serine and threonine residues and at least one
CC tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding
CC activity and transforms it as a negative regulator of AP-1 mediated
CC transcription. {ECO:0000269|PubMed:12809553}.
CC -!- DISRUPTION PHENOTYPE: Mice are fertile and healthy. They display a
CC normal thymus, spleen and lymph node development, and normal CD4(+) and
CC CD8(+) T-cell development. They also show normal development of natural
CC killer T-cells, B-cells, and conventional and plasmacytoid dendritic
CC cells. They however show defects in T-helper 17 cells (Th17)
CC differentiation and are resistant to experimental autoimmune
CC encephalomyelitis. Loss of follicular T-helper cells (TfH), as well as
CC less production of antibodies with switched isotypes in B-cells is also
CC observed. {ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391,
CC ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:21873234}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AF017021; AAB70251.1; -; mRNA.
DR EMBL; AK018587; BAB31294.1; -; mRNA.
DR EMBL; BC132410; AAI32411.1; -; mRNA.
DR EMBL; BC132412; AAI32413.1; -; mRNA.
DR CCDS; CCDS26061.1; -.
DR RefSeq; NP_058047.1; NM_016767.2.
DR AlphaFoldDB; O35284; -.
DR SMR; O35284; -.
DR BioGRID; 207278; 1.
DR IntAct; O35284; 2.
DR STRING; 10090.ENSMUSP00000040706; -.
DR iPTMnet; O35284; -.
DR PhosphoSitePlus; O35284; -.
DR EPD; O35284; -.
DR PaxDb; O35284; -.
DR PRIDE; O35284; -.
DR ProteomicsDB; 273652; -.
DR Antibodypedia; 25838; 410 antibodies from 35 providers.
DR DNASU; 53314; -.
DR Ensembl; ENSMUST00000040536; ENSMUSP00000040706; ENSMUSG00000034266.
DR GeneID; 53314; -.
DR KEGG; mmu:53314; -.
DR UCSC; uc007ohd.1; mouse.
DR CTD; 10538; -.
DR MGI; MGI:1859147; Batf.
DR VEuPathDB; HostDB:ENSMUSG00000034266; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000159745; -.
DR HOGENOM; CLU_088612_4_0_1; -.
DR InParanoid; O35284; -.
DR OMA; CTGLTPQ; -.
DR OrthoDB; 1544557at2759; -.
DR PhylomeDB; O35284; -.
DR TreeFam; TF332340; -.
DR BioGRID-ORCS; 53314; 2 hits in 112 CRISPR screens.
DR PRO; PR:O35284; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35284; protein.
DR Bgee; ENSMUSG00000034266; Expressed in granulocyte and 86 other tissues.
DR Genevisible; O35284; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; IMP:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0045190; P:isotype switching; IMP:UniProtKB.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; IMP:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; IMP:UniProtKB.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IMP:UniProtKB.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029820; BATF.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF14; PTHR23351:SF14; 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; Cytoplasm; Differentiation; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..125
FT /note="Basic leucine zipper transcriptional factor ATF-
FT like"
FT /id="PRO_0000076596"
FT DOMAIN 26..89
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..50
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 54..75
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12809553"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12809553"
FT MUTAGEN 43
FT /note="S->A: Decreased phosphorylation; when associated
FT with A-48."
FT /evidence="ECO:0000269|PubMed:12809553"
FT MUTAGEN 43
FT /note="S->D: Retains the ability to dimerize with JUNB and
FT localization in the nucleus but abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:12809553"
FT MUTAGEN 48
FT /note="T->A: Decreased phosphorylation; when associated
FT with A-43."
FT /evidence="ECO:0000269|PubMed:12809553"
FT MUTAGEN 55
FT /note="H->Q: Impairs interaction with IRF4 and the
FT recruitment of IRF4 to AICE motifs, leading to defects in
FT mediate differentiation of Th17 cells. Loss of function;
FT when associated with A-56; D-63 and K-77."
FT /evidence="ECO:0000269|PubMed:22983707,
FT ECO:0000269|PubMed:22992524"
FT MUTAGEN 56
FT /note="L->A: Loss of function; when associated with Q-55;
FT D-63 and K-77."
FT /evidence="ECO:0000269|PubMed:22992524"
FT MUTAGEN 63
FT /note="K->D: Retains 50% of activity; when associated with
FT 69-Q-T-70 and K-77. Loss of function; when associated with
FT Q-55; A-56 and K-77."
FT /evidence="ECO:0000269|PubMed:22992524"
FT MUTAGEN 69..70
FT /note="RK->QT: Retains 50% of activity; when associated
FT with D-63 and K-77."
FT /evidence="ECO:0000269|PubMed:22992524"
FT MUTAGEN 77
FT /note="E->K: Does not affect interaction with IRF4 and
FT ability to mediate differentiation of Th17 cells. Retains
FT 50% of activity; when associated with D63 and 69-Q-T-70.
FT Loss of function; when associated with Q-55; A-56 and D-
FT 63."
FT /evidence="ECO:0000269|PubMed:22983707,
FT ECO:0000269|PubMed:22992524"
SQ SEQUENCE 125 AA; 14065 MW; A23B00D6E0827938 CRC64;
MPHSSDSSDS SFSRSPPPGK QDSSDDVRKV QRREKNRIAA QKSRQRQTQK ADTLHLESED
LEKQNAALRK EIKQLTEELK YFTSVLSSHE PLCSVLASGT PSPPEVVYSA HAFHQPHISS
PRFQP
