ID BACH2_MOUSE Reviewed; 839 AA.
AC P97303; A2ANU8; A2ANU9; A2RRI0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 24-JAN-2024, entry version 183.
DE RecName: Full=Transcription regulator protein BACH2;
DE AltName: Full=BTB and CNC homolog 2;
GN Name=Bach2;
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] (ISOFORM 2), FUNCTION, SUBUNIT, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=8887638; DOI=10.1128/mcb.16.11.6083;
RA Oyake T., Itoh K., Motohashi H., Hayashi N., Hoshino H., Nishizawa M.,
RA Yamamoto M., Igarashi K.;
RT "Bach proteins belong to a novel family of BTB-basic leucine zipper
RT transcription factors that interact with MafK and regulate transcription
RT through the NF-E2 site.";
RL Mol. Cell. Biol. 16:6083-6095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=10809773; DOI=10.1074/jbc.275.20.15370;
RA Hoshino H., Kobayashi A., Yoshida M., Kudo N., Oyake T., Motohashi H.,
RA Hayashi N., Yamamoto M., Igarashi K.;
RT "Oxidative stress abolishes leptomycin B-sensitive nuclear export of
RT transcription repressor Bach2 that counteracts activation of Maf
RT recognition element.";
RL J. Biol. Chem. 275:15370-15376(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=26021350; DOI=10.1242/jcs.169441;
RA Dopie J., Rajakylae E.K., Joensuu M.S., Huet G., Ferrantelli E., Xie T.,
RA Jaeaelinoja H., Jokitalo E., Vartiainen M.K.;
RT "Genome-wide RNAi screen for nuclear actin reveals a network of cofilin
RT regulators.";
RL J. Cell Sci. 128:2388-2400(2015).
RN [8]
RP FUNCTION.
RX PubMed=28530713; DOI=10.1038/ni.3753;
RA Afzali B., Groenholm J., Vandrovcova J., O'Brien C., Sun H.W.,
RA Vanderleyden I., Davis F.P., Khoder A., Zhang Y., Hegazy A.N.,
RA Villarino A.V., Palmer I.W., Kaufman J., Watts N.R., Kazemian M.,
RA Kamenyeva O., Keith J., Sayed A., Kasperaviciute D., Mueller M.,
RA Hughes J.D., Fuss I.J., Sadiyah M.F., Montgomery-Recht K., McElwee J.,
RA Restifo N.P., Strober W., Linterman M.A., Wingfield P.T., Uhlig H.H.,
RA Roychoudhuri R., Aitman T.J., Kelleher P., Lenardo M.J., O'Shea J.J.,
RA Cooper N., Laurence A.D.J.;
RT "BACH2 immunodeficiency illustrates an association between super-enhancers
RT and haploinsufficiency.";
RL Nat. Immunol. 18:813-823(2017).
CC -!- FUNCTION: Transcriptional regulator that acts as a repressor or
CC activator (PubMed:8887638). Binds to Maf recognition elements (MARE)
CC (PubMed:8887638). Plays an important role in coordinating transcription
CC activation and repression by MAFK (PubMed:8887638). Induces apoptosis
CC in response to oxidative stress through repression of the antiapoptotic
CC factor HMOX1 (By similarity). Positively regulates the nuclear import
CC of actin (PubMed:26021350). Is a key regulator of adaptive immunity,
CC crucial for the maintenance of regulatory T-cell function and B-cell
CC maturation (PubMed:28530713). {ECO:0000250|UniProtKB:Q9BYV9,
CC ECO:0000269|PubMed:26021350, ECO:0000269|PubMed:28530713}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer of
CC BACH2 and Maf-related transcription factors (PubMed:8887638).
CC {ECO:0000250|UniProtKB:Q9BYV9, ECO:0000269|PubMed:8887638}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10809773}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:10809773}.
CC Note=Nucleocytoplasmic shuttling is controlled by phosphorylation.
CC {ECO:0000250|UniProtKB:Q9BYV9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97303-2; Sequence=VSP_047933;
CC -!- TISSUE SPECIFICITY: Detected in brain and spleen.
CC {ECO:0000269|PubMed:8887638}.
CC -!- DEVELOPMENTAL STAGE: In brain, expression is lower in the adult than in
CC the neonate. {ECO:0000269|PubMed:8887638}.
CC -!- PTM: The reversible disulfide bond may provide a mechanism to regulate
CC the activity in oxidative stress responses.
CC {ECO:0000250|UniProtKB:Q9BYV9}.
CC -!- PTM: Phosphorylation at Ser-520 downstream of the PI-3K pathway
CC promotes nuclear export. {ECO:0000250|UniProtKB:Q9BYV9}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR EMBL; D86604; BAA13138.1; -; mRNA.
DR EMBL; AL732547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131642; AAI31643.1; -; mRNA.
DR CCDS; CCDS51135.1; -. [P97303-1]
DR RefSeq; NP_001103131.1; NM_001109661.1. [P97303-1]
DR RefSeq; XP_006537630.1; XM_006537567.3. [P97303-1]
DR RefSeq; XP_011248211.1; XM_011249909.2. [P97303-1]
DR AlphaFoldDB; P97303; -.
DR SMR; P97303; -.
DR BioGRID; 198295; 8.
DR IntAct; P97303; 1.
DR STRING; 10090.ENSMUSP00000103815; -.
DR iPTMnet; P97303; -.
DR PhosphoSitePlus; P97303; -.
DR EPD; P97303; -.
DR jPOST; P97303; -.
DR MaxQB; P97303; -.
DR PaxDb; 10090-ENSMUSP00000103815; -.
DR PeptideAtlas; P97303; -.
DR ProteomicsDB; 273462; -. [P97303-1]
DR ProteomicsDB; 273463; -. [P97303-2]
DR Antibodypedia; 31919; 269 antibodies from 30 providers.
DR DNASU; 12014; -.
DR Ensembl; ENSMUST00000037416.13; ENSMUSP00000043693.7; ENSMUSG00000040270.17. [P97303-2]
DR Ensembl; ENSMUST00000108180.9; ENSMUSP00000103815.3; ENSMUSG00000040270.17. [P97303-1]
DR Ensembl; ENSMUST00000171600.2; ENSMUSP00000131592.2; ENSMUSG00000040270.17. [P97303-1]
DR GeneID; 12014; -.
DR KEGG; mmu:12014; -.
DR UCSC; uc012dbf.1; mouse. [P97303-1]
DR AGR; MGI:894679; -.
DR CTD; 60468; -.
DR MGI; MGI:894679; Bach2.
DR VEuPathDB; HostDB:ENSMUSG00000040270; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00940000158228; -.
DR HOGENOM; CLU_015243_0_0_1; -.
DR InParanoid; P97303; -.
DR OMA; MMGDGMY; -.
DR OrthoDB; 382726at2759; -.
DR PhylomeDB; P97303; -.
DR TreeFam; TF326681; -.
DR BioGRID-ORCS; 12014; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Bach2; mouse.
DR PRO; PR:P97303; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P97303; Protein.
DR Bgee; ENSMUSG00000040270; Expressed in animal zygote and 245 other cell types or tissues.
DR Genevisible; P97303; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0043167; F:ion binding; EXP:DisProt.
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; ISO:MGI.
DR GO; GO:0051170; P:import into nucleus; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0090721; P:primary adaptive immune response involving T cells and B cells; ISO:MGI.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18278; BTB_POZ_BACH2; 1.
DR CDD; cd14719; bZIP_BACH; 1.
DR DisProt; DP01009; -.
DR Gene3D; 1.10.880.10; Transcription factor, Skn-1-like, DNA-binding domain; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043321; bZIP_BACH.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR46105; AGAP004733-PA; 1.
DR PANTHER; PTHR46105:SF8; TRANSCRIPTION REGULATOR PROTEIN BACH2; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Disulfide bond; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..839
FT /note="Transcription regulator protein BACH2"
FT /id="PRO_0000076457"
FT DOMAIN 37..103
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 645..708
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 150..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..666
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 670..677
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 778..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 819..839
FT /note="Nuclear export signal"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYV9"
FT DISULFID 20
FT /note="Interchain; redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9BYV9"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYV9"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYV9"
FT VAR_SEQ 421..543
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8887638"
FT /id="VSP_047933"
FT CONFLICT 220
FT /note="E -> G (in Ref. 3; AAI31643)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="P -> R (in Ref. 1; BAA13138)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="P -> R (in Ref. 1; BAA13138)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="K -> E (in Ref. 1; BAA13138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 91836 MW; 8A5321A68A07653D CRC64;
MSVDEKPGSP MYVYESTVHC ANILLGLNDQ RKKDILCDVT LIVERKEFRA HRAVLAACSE
YFWQALVGQT KDDLVVSLPE EVTARGFGPL LQFAYTAKLL LSRENIREVI RCAEFLRMHN
LEDSCFSFLQ TQLLNREDGL FVCRKDSACQ RPQEDHGNSA GEEEEEEETM DSETARMACA
TDQMLPDPIS FEATAIPVAE KEEALLPESE VPTDTKENSE KGALTQYPRY KKYQLACTKN
VYSAPSHGTS GFASTFSEDS PGNSLKPGLP MGQIKSEPPS EETEEESITL CLSGDETDIK
DRPGDVEMDR KQPSPAPTPS TPTGAACLDR SRSVSSPSCL RSLFGITKGV ESTGLPSTSQ
QPLVRSSACP FNKGISQGDL KTDYTPLAGN YGQPHVGQKD VSNFAMGSPL RGPGPETLCK
QEGELDRRSV IFSASACDQP NTPVHSYSAV SNLDKDLSEP VPKSLWVGAG QSLPSSQAYS
HSGLMADHLP GRIRPNTSCP VPIKVCPRSP PLETRTRTSS SCSSYSYAED GSGGSPCSLP
LCEFSSSPCS QGARFLATEH QEPGLMGDGM YNQVRPQIKC EQSYGTNSSD ESGSFSEADS
ESCPVQDRGQ EVKLPFPVDQ ITDLPRNDFQ MMIKMHKLTS EQLEFIHDIR RRSKNRIAAQ
RCRKRKLDCI QNLECEIRKL VCEKEKLLSE RNHLKACMGE LLDNFSCLSQ EVCRDIQSPE
QIQALHRYCP VLIPMDLPGA SVNPPPVGVE QSLAPSPCAV GGSVPCCLEP GAAPPGLPWV
PSNTSENCTS GRRLEGSDPG TFSERGPPLE ARSQSVTVDF CQEMTEKCTT DEQPRKDYA
//
