BACH1_MOUSE
ID BACH1_MOUSE Reviewed; 739 AA.
AC P97302;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription regulator protein BACH1;
DE AltName: Full=BTB and CNC homolog 1;
GN Name=Bach1;
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, SUBCELLULAR LOCATION, INTERACTION
RP WITH MAFK, AND TISSUE SPECIFICITY.
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 MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-135, AND FUNCTION.
RX PubMed=19170764; DOI=10.1111/j.1365-2443.2008.01259.x;
RA Ito N., Watanabe-Matsui M., Igarashi K., Murayama K.;
RT "Crystal structure of the Bach1 BTB domain and its regulation of
RT homodimerization.";
RL Genes Cells 14:167-178(2009).
CC -!- FUNCTION: Transcriptional regulator that acts as repressor or
CC activator, depending on the context (PubMed:8887638, PubMed:19170764).
CC Binds to NF-E2 DNA binding sites (PubMed:8887638, PubMed:19170764).
CC Plays important roles in coordinating transcription activation and
CC repression by MAFK (PubMed:8887638). Together with MAF, represses the
CC transcription of genes under the control of the NFE2L2 oxidative stress
CC pathway (By similarity). {ECO:0000250|UniProtKB:O14867,
CC ECO:0000269|PubMed:19170764, ECO:0000269|PubMed:8887638}.
CC -!- SUBUNIT: Heterodimer of BACH1 and MAFK.
CC -!- INTERACTION:
CC P97302; Q61827: Mafk; NbExp=5; IntAct=EBI-2552417, EBI-15740843;
CC P97302; P02340: Tp53; NbExp=4; IntAct=EBI-2552417, EBI-474016;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:8887638}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8887638}.
CC -!- PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:O14867}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR EMBL; D86603; BAA13137.1; -; mRNA.
DR EMBL; BC057894; AAH57894.1; -; mRNA.
DR CCDS; CCDS28293.1; -.
DR RefSeq; NP_031546.1; NM_007520.2.
DR RefSeq; XP_006522942.1; XM_006522879.3.
DR PDB; 2Z8H; X-ray; 2.50 A; A=1-135.
DR PDBsum; 2Z8H; -.
DR AlphaFoldDB; P97302; -.
DR SMR; P97302; -.
DR BioGRID; 198294; 94.
DR DIP; DIP-46342N; -.
DR IntAct; P97302; 28.
DR STRING; 10090.ENSMUSP00000026703; -.
DR iPTMnet; P97302; -.
DR PhosphoSitePlus; P97302; -.
DR jPOST; P97302; -.
DR PaxDb; P97302; -.
DR PeptideAtlas; P97302; -.
DR PRIDE; P97302; -.
DR ProteomicsDB; 277175; -.
DR Antibodypedia; 920; 386 antibodies from 39 providers.
DR DNASU; 12013; -.
DR Ensembl; ENSMUST00000026703; ENSMUSP00000026703; ENSMUSG00000025612.
DR GeneID; 12013; -.
DR KEGG; mmu:12013; -.
DR UCSC; uc007zup.1; mouse.
DR CTD; 571; -.
DR MGI; MGI:894680; Bach1.
DR VEuPathDB; HostDB:ENSMUSG00000025612; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00940000158923; -.
DR HOGENOM; CLU_015243_2_0_1; -.
DR InParanoid; P97302; -.
DR OMA; RKKCFPS; -.
DR OrthoDB; 521871at2759; -.
DR PhylomeDB; P97302; -.
DR TreeFam; TF326681; -.
DR Reactome; R-MMU-9707616; Heme signaling.
DR Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR BioGRID-ORCS; 12013; 2 hits in 109 CRISPR screens.
DR ChiTaRS; Bach1; mouse.
DR EvolutionaryTrace; P97302; -.
DR PRO; PR:P97302; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P97302; protein.
DR Bgee; ENSMUSG00000025612; Expressed in indifferent gonad and 279 other tissues.
DR ExpressionAtlas; P97302; baseline and differential.
DR Genevisible; P97302; MM.
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: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: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:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive 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:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:MGI.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0000117; P:regulation of transcription involved in G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd14719; bZIP_BACH; 1.
DR Gene3D; 3.30.710.10; -; 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 Pfam; PF00651; BTB; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..739
FT /note="Transcription regulator protein BACH1"
FT /id="PRO_0000076455"
FT DOMAIN 34..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 560..623
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 287..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..581
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 585..592
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 679..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14867"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:2Z8H"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2Z8H"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:2Z8H"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:2Z8H"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2Z8H"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2Z8H"
SQ SEQUENCE 739 AA; 81374 MW; CE2DE606B05F6E32 CRC64;
MSVSESAVFA YESSVHSTNV LLSLNDQRKK DVLCDVTVLV EGQRFRAHRS VLAACSSYFH
SRIVGQTDAE LTVTLPEEVT VKGFEPLIQF AYTAKLILSK DNVDEVCRCV EFLSVHNIEE
SCFQFLKFKF LDSTSEQQEC ARKKCFSSHC QKADFKFSFS EQKDLEIDEA DEFLEKKRVQ
TPQCDSRRCQ GSVKASPPLQ DSVSQACQSL CTDKDGALAL PSLCPKYRKF QKAFGTDKIR
TLESGVRDVH TASVQPNETS ELECFGGAQG CADLHVILKC EGMKAAMESE DTEGQDPSPQ
CPAEQPQGTP LPQDSAGPHG LYSLSALHTY EQSGDVAFAG VQSKTVKTEK PLSRPDAQDE
KPSENQDLYL KSSMGPKEDS SSLASEDRSS VEREVAEHLA KGFWSDICST DSPCQMQLSP
TVAKDGPEQG YSQRRSECPW LGIRISESPE PGQRTFTTLS SVNCPFISTL SSEGCSSNLE
IGNYDYVSEP QQEPCPYACV ISLGDDSETD TEGDSESCSA REQDCEVKLP FNAQRIISLS
RNDFQSLLKM HKLTPEQLDC IHDIRRRSKN RIAAQRCRKR KLDCIQNLES EIEKLQSEKE
SLLKERDHIL STLGETKQNL TGLCQQVCKE AALSPEQIQI LAKYSASDCP LSFLISEKGK
STPDGELAFT SVFSVSDVPP TAPPPCGRGS SAASQELVQE SPPTTAAAPE QATLLEPCRQ
SAGISDFCQQ MSDKCTTDE
