PBX1_MOUSE
ID PBX1_MOUSE Reviewed; 430 AA.
AC P41778;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Pre-B-cell leukemia transcription factor 1;
DE AltName: Full=Homeobox protein PBX1;
GN Name=Pbx1; Synonyms=Pbx-1;
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 PBX1B), PARTIAL PROTEIN SEQUENCE, AND
RP FUNCTION.
RC TISSUE=Adrenal gland;
RX PubMed=7913464; DOI=10.1016/s0021-9258(17)32223-8;
RA Kagawa N., Ogo A., Takahashi Y., Iwamatsu A., Waterman M.R.;
RT "A cAMP-regulatory sequence (CRS1) of CYP17 is a cellular target for the
RT homeodomain protein Pbx1.";
RL J. Biol. Chem. 269:18716-18719(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1A).
RA Liu Y., MacDonald R.J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PBX1A).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, AND INTERACTION WITH HOXA5; HOXB7; HOXB8; HOXC8 AND HOXD4.
RX PubMed=7791786; DOI=10.1128/mcb.15.7.3786;
RA Lu Q., Knoepfler P.S., Scheele J., Wright D.D., Kamps M.P.;
RT "Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the
RT products of multiple murine Hox genes, some of which are themselves
RT oncogenes.";
RL Mol. Cell. Biol. 15:3786-3795(1995).
RN [5]
RP INTERACTION WITH MEIS1.
RX PubMed=9315626; DOI=10.1128/mcb.17.10.5679;
RA Chang C.-P., Jacobs Y., Nakamura T., Jenkins N.A., Copeland N.G.,
RA Cleary M.L.;
RT "Meis proteins are major in vivo DNA binding partners for wild-type but not
RT chimeric Pbx proteins.";
RL Mol. Cell. Biol. 17:5679-5687(1997).
RN [6]
RP INTERACTION WITH MEIS1.
RX PubMed=9525891; DOI=10.1074/jbc.273.14.7941;
RA Bischof L.J., Kagawa N., Moskow J.J., Takahashi Y., Iwamatsu A.,
RA Buchberg A.M., Waterman M.R.;
RT "Members of the Meis1 and Pbx homeodomain protein families cooperatively
RT bind a cAMP-responsive sequence (CRS1) from bovine CYP17.";
RL J. Biol. Chem. 273:7941-7948(1998).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH PDX1 AND MEIS2.
RX PubMed=9710595; DOI=10.1128/mcb.18.9.5109;
RA Swift G.H., Liu Y., Rose S.D., Bischof L.J., Steelman S., Buchberg A.M.,
RA Wright C.V., MacDonald R.J.;
RT "An endocrine-exocrine switch in the activity of the pancreatic homeodomain
RT protein PDX1 through formation of a trimeric complex with PBX1b and MRG1
RT (MEIS2).";
RL Mol. Cell. Biol. 18:5109-5120(1998).
RN [8]
RP INTERACTION WITH HOXA9 AND MEIS1.
RX PubMed=10082572; DOI=10.1128/mcb.19.4.3051;
RA Shen W.-F., Rozenfeld S., Kwong A., Koemueves L.G., Lawrence H.J.,
RA Largman C.;
RT "HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.";
RL Mol. Cell. Biol. 19:3051-3061(1999).
RN [9]
RP INTERACTION WITH HOXD4; HOXD9; HOXD10 AND MEIS1.
RX PubMed=10523646; DOI=10.1128/mcb.19.11.7577;
RA Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U., Featherstone M.S.;
RT "PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX
RT proteins.";
RL Mol. Cell. Biol. 19:7577-7588(1999).
RN [10]
RP INTERACTION WITH MEIS2, AND IDENTIFICATION IN A COMPLEX WITH PDX1 AND
RP MEIS2.
RX PubMed=11279116; DOI=10.1074/jbc.m100678200;
RA Liu Y., MacDonald R.J., Swift G.H.;
RT "DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer
RT and cooperation with a pancreas-specific basic helix-loop-helix complex.";
RL J. Biol. Chem. 276:17985-17993(2001).
RN [11]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=12529389; DOI=10.1128/mcb.23.3.831-841.2003;
RA Chao S.H., Walker J.R., Chanda S.K., Gray N.S., Caldwell J.S.;
RT "Identification of homeodomain proteins, PBX1 and PREP1, involved in the
RT transcription of murine leukemia virus.";
RL Mol. Cell. Biol. 23:831-841(2003).
RN [12]
RP FUNCTION.
RX PubMed=19799567; DOI=10.1042/bj20090694;
RA Mojsin M., Stevanovic M.;
RT "PBX1 and MEIS1 up-regulate SOX3 gene expression by direct interaction with
RT a consensus binding site within the basal promoter region.";
RL Biochem. J. 425:107-116(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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 [14]
RP FUNCTION.
RX PubMed=22560297; DOI=10.1016/j.devcel.2012.02.009;
RA Koss M., Bolze A., Brendolan A., Saggese M., Capellini T.D., Bojilova E.,
RA Boisson B., Prall O.W., Elliott D.A., Solloway M., Lenti E., Hidaka C.,
RA Chang C.P., Mahlaoui N., Harvey R.P., Casanova J.L., Selleri L.;
RT "Congenital asplenia in mice and humans with mutations in a Pbx/Nkx2-5/p15
RT module.";
RL Dev. Cell 22:913-926(2012).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP DOMAIN, SITE, AND MUTAGENESIS OF ARG-237; ASN-286 AND ARG-290.
RX PubMed=32190943; DOI=10.1096/fj.202000121r;
RA Xu X., Zhou Y., Fu B., Zhang J., Dong Z., Zhang X., Shen N., Sun R.,
RA Tian Z., Wei H.;
RT "PBX1 promotes development of natural killer cells by binding directly to
RT the Nfil3 promoter.";
RL FASEB J. 34:6479-6492(2020).
RN [16]
RP STRUCTURE BY NMR OF 241-294.
RX PubMed=10933814; DOI=10.1021/bi0001067;
RA Sprules T., Green N., Featherstone M., Gehring K.;
RT "Conformational changes in the PBX homeodomain and C-terminal extension
RT upon binding DNA and HOX-derived YPWM peptides(,).";
RL Biochemistry 39:9943-9950(2000).
RN [17]
RP STRUCTURE BY NMR OF 233-313 IN COMPLEX WITH DNA.
RX PubMed=12409300; DOI=10.1074/jbc.m207504200;
RA Sprules T., Green N., Featherstone M., Gehring K.;
RT "Lock and key binding of the HOX YPWM peptide to the PBX homeodomain.";
RL J. Biol. Chem. 278:1053-1058(2003).
CC -!- FUNCTION: Transcription factor which binds the DNA sequence 5'-
CC TGATTGAT-3' as part of a heterodimer with HOX proteins such as HOXA1,
CC HOXA5, HOXB7 and HOXB8 (By similarity). Binds the DNA sequence 5'-
CC TGATTGAC-3' in complex with a nuclear factor which is not a class I HOX
CC protein (By similarity). Has also been shown to bind the DNA sequence
CC 5'-ATCAATCAA-3' cooperatively with HOXA5, HOXB7, HOXB8, HOXC8 and HOXD4
CC (PubMed:7791786). Acts as a transcriptional activator of PF4 in complex
CC with MEIS1 (By similarity). Also activates transcription of SOX3 in
CC complex with MEIS1 by binding to the 5'-TGATTGAC-3' consensus sequence
CC (PubMed:19799567). In natural killer cells, binds to the NFIL3 promoter
CC and acts as a transcriptional activator of NFIL3, promoting natural
CC killer cell development (PubMed:32190943). Plays a role in the cAMP-
CC dependent regulation of CYP17A1 gene expression via its cAMP-regulatory
CC sequence (CRS1) (PubMed:7913464). Probably in complex with MEIS2, is
CC involved in transcriptional regulation by KLF4 (By similarity). Acts as
CC a transcriptional activator of NKX2-5 and a transcriptional repressor
CC of CDKN2B (PubMed:22560297). Together with NKX2-5, required for spleen
CC development through a mechanism that involves CDKN2B repression
CC (PubMed:22560297). {ECO:0000250|UniProtKB:P40424,
CC ECO:0000269|PubMed:19799567, ECO:0000269|PubMed:22560297,
CC ECO:0000269|PubMed:32190943, ECO:0000269|PubMed:7791786,
CC ECO:0000269|PubMed:7913464}.
CC -!- FUNCTION: [Isoform PBX1b]: As part of a PDX1:PBX1b:MEIS2B complex in
CC pancreatic acinar cells, is involved in the transcriptional activation
CC of the ELA1 enhancer; the complex binds to the enhancer B element and
CC cooperates with the transcription factor 1 complex (PTF1) bound to the
CC enhancer A element. {ECO:0000269|PubMed:11279116}.
CC -!- FUNCTION: (Microbial infection) In complex with PREP1, binds to the 5'-
CC TGATTGAC-3' consensus sequence in the U5 region of Moloney murine
CC leukemia virus and promotes viral transcription.
CC {ECO:0000269|PubMed:12529389}.
CC -!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA
CC (PubMed:9525891, PubMed:19799567). The PBX1-MEIS1 heterodimer binds a
CC cAMP-responsive sequence in CYP17 (PubMed:9525891). It also binds a
CC consensus region in the SOX3 promoter (PubMed:19799567). PBX1 forms
CC heterotrimers with MEIS1 and a number of HOX proteins including HOXA9,
CC HOXD4, HOXD9 and HOXD10 (PubMed:9315626, PubMed:10082572,
CC PubMed:10523646, PubMed:12409300). Forms heterodimers with HOXA1,
CC HOXA5, HOXB7 and HOXB8 which bind the 5'-TGATTGAT-3' consensus sequence
CC (By similarity). Also forms heterodimers with HOXA5, HOXB7, HOXB8,
CC HOXC8 and HOXD4 which bind the 5'-ATCAATCAA-3' consensus sequence
CC (PubMed:7791786). Interacts with PBXIP1 (By similarity). Interacts with
CC TLX1 (By similarity). Interacts with FOXC1 (By similarity). Interacts
CC with MN1 (By similarity). {ECO:0000250|UniProtKB:P40424,
CC ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646,
CC ECO:0000269|PubMed:12409300, ECO:0000269|PubMed:19799567,
CC ECO:0000269|PubMed:7791786, ECO:0000269|PubMed:9315626,
CC ECO:0000269|PubMed:9525891}.
CC -!- SUBUNIT: [Isoform PBX1a]: Interacts with MEIS2 isoform Meis2D, SP1, SP3
CC and KLF4. {ECO:0000250|UniProtKB:P40424}.
CC -!- SUBUNIT: [Isoform PBX1b]: Part of a PDX1:PBX1b:MEIS2B complex; PBX1b
CC recruits MEIS2B to the complex. {ECO:0000269|PubMed:11279116,
CC ECO:0000269|PubMed:9710595}.
CC -!- INTERACTION:
CC P41778; P09631: Hoxa9; NbExp=2; IntAct=EBI-6996259, EBI-925334;
CC P41778; P09023: Hoxb6; NbExp=2; IntAct=EBI-6996259, EBI-15992861;
CC P41778; P09632: Hoxb8; NbExp=4; IntAct=EBI-6996259, EBI-925374;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32190943}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PBX1a;
CC IsoId=P41778-1; Sequence=Displayed;
CC Name=PBX1b;
CC IsoId=P41778-2; Sequence=VSP_002273, VSP_002274;
CC -!- TISSUE SPECIFICITY: Expressed constitutively in natural killer cell
CC precursors in bone marrow. {ECO:0000269|PubMed:32190943}.
CC -!- DOMAIN: The homeobox is required for PBX1 nuclear localization and for
CC transcriptional activation of NFIL3. {ECO:0000269|PubMed:32190943}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in hematopoietic cells leads
CC to a reduction in the number of natural killer cell-committed
CC progenitors in bone marrow, decreases the number of natural killer
CC cells in bone marrow and spleen and reduces NFIL3 expression in bone
CC marrow and splenic natural killer cells. {ECO:0000269|PubMed:32190943}.
CC -!- SIMILARITY: Belongs to the TALE/PBX homeobox family. {ECO:0000305}.
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DR EMBL; L27453; AAA21832.1; -; mRNA.
DR EMBL; AF020196; AAB71191.1; -; mRNA.
DR EMBL; BC058390; AAH58390.1; -; mRNA.
DR CCDS; CCDS15461.1; -. [P41778-1]
DR CCDS; CCDS15462.1; -. [P41778-2]
DR PIR; A54863; A54863.
DR RefSeq; NP_001278437.1; NM_001291508.1. [P41778-2]
DR RefSeq; NP_032809.1; NM_008783.3. [P41778-2]
DR RefSeq; NP_899198.1; NM_183355.3. [P41778-1]
DR PDB; 1DU6; NMR; -; A=241-294.
DR PDB; 1LFU; NMR; -; P=233-313.
DR PDBsum; 1DU6; -.
DR PDBsum; 1LFU; -.
DR AlphaFoldDB; P41778; -.
DR BMRB; P41778; -.
DR SMR; P41778; -.
DR BioGRID; 202037; 23.
DR CORUM; P41778; -.
DR DIP; DIP-6107N; -.
DR IntAct; P41778; 20.
DR MINT; P41778; -.
DR STRING; 10090.ENSMUSP00000135516; -.
DR iPTMnet; P41778; -.
DR PhosphoSitePlus; P41778; -.
DR MaxQB; P41778; -.
DR PaxDb; P41778; -.
DR PRIDE; P41778; -.
DR ProteomicsDB; 287793; -. [P41778-1]
DR ProteomicsDB; 287794; -. [P41778-2]
DR Antibodypedia; 1079; 424 antibodies from 37 providers.
DR DNASU; 18514; -.
DR Ensembl; ENSMUST00000072863; ENSMUSP00000072640; ENSMUSG00000052534. [P41778-2]
DR Ensembl; ENSMUST00000176540; ENSMUSP00000135516; ENSMUSG00000052534. [P41778-1]
DR Ensembl; ENSMUST00000176790; ENSMUSP00000134925; ENSMUSG00000052534. [P41778-2]
DR Ensembl; ENSMUST00000188912; ENSMUSP00000140606; ENSMUSG00000052534. [P41778-2]
DR GeneID; 18514; -.
DR KEGG; mmu:18514; -.
DR UCSC; uc007dle.2; mouse. [P41778-1]
DR CTD; 5087; -.
DR MGI; MGI:97495; Pbx1.
DR VEuPathDB; HostDB:ENSMUSG00000052534; -.
DR eggNOG; KOG0774; Eukaryota.
DR GeneTree; ENSGT00940000154374; -.
DR HOGENOM; CLU_041153_1_0_1; -.
DR InParanoid; P41778; -.
DR OMA; LAHHMTA; -.
DR OrthoDB; 804740at2759; -.
DR PhylomeDB; P41778; -.
DR TreeFam; TF314340; -.
DR BioGRID-ORCS; 18514; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pbx1; mouse.
DR EvolutionaryTrace; P41778; -.
DR PRO; PR:P41778; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P41778; protein.
DR Bgee; ENSMUSG00000052534; Expressed in rostral migratory stream and 237 other tissues.
DR ExpressionAtlas; P41778; baseline and differential.
DR Genevisible; P41778; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0005667; C:transcription regulator complex; IDA: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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0001654; P:eye development; IBA:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0001655; P:urogenital system development; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR005542; PBX.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03792; PBC; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51978; PBC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Developmental protein;
KW Differentiation; Direct protein sequencing; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Sexual differentiation; Steroidogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..430
FT /note="Pre-B-cell leukemia transcription factor 1"
FT /id="PRO_0000049236"
FT DOMAIN 38..232
FT /note="PBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT DNA_BIND 233..295
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..124
FT /note="PBC-A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT REGION 127..232
FT /note="PBC-B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT REGION 317..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 286
FT /note="Required for binding to the NFIL3 promoter"
FT /evidence="ECO:0000269|PubMed:32190943"
FT VAR_SEQ 334..347
FT /note="SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in isoform PBX1b)"
FT /evidence="ECO:0000303|PubMed:7913464"
FT /id="VSP_002273"
FT VAR_SEQ 348..430
FT /note="Missing (in isoform PBX1b)"
FT /evidence="ECO:0000303|PubMed:7913464"
FT /id="VSP_002274"
FT MUTAGEN 237
FT /note="R->A: Slightly reduced binding to NFIL3 promoter."
FT /evidence="ECO:0000269|PubMed:32190943"
FT MUTAGEN 286
FT /note="N->A: Significantly reduced binding to NFIL3
FT promoter."
FT /evidence="ECO:0000269|PubMed:32190943"
FT MUTAGEN 290
FT /note="R->A: Slightly reduced binding to NFIL3 promoter."
FT /evidence="ECO:0000269|PubMed:32190943"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1LFU"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1DU6"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1DU6"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1DU6"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:1DU6"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:1DU6"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1DU6"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:1LFU"
SQ SEQUENCE 430 AA; 46626 MW; AD3FFACBC5A9E715 CRC64;
MDEQPRLMHS HAGVGMAGHP GLSQHLQDGA GGTEGEGGRK QDIGDILQQI MTITDQSLDE
AQARKHALNC HRMKPALFNV LCEIKEKTVL SIRGAQEEEP TDPQLMRLDN MLLAEGVAGP
EKGGGSAAAA AAAAASGGAG SDNSVEHSDY RAKLSQIRQI YHTELEKYEQ ACNEFTTHVM
NLLREQSRTR PISPKEIERM VSIIHRKFSS IQMQLKQSTC EAVMILRSRF LDARRKRRNF
NKQATEILNE YFYSHLSNPY PSEEAKEELA KKCGITVSQV SNWFGNKRIR YKKNIGKFQE
EANIYAAKTA VTATNVSAHG SQANSPSTPN SAGSSSSFNM SNSGDLFMSV QSLNGDSYQG
AQVGANVQSQ VDTLRHVISQ TGGYSDGLAA SQMYSPQGIS ANGGWQDATT PSSVTSPTEG
PGSVHSDTSN
