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   16-OCT-2019, entry version 190.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1B), AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   TISSUE=Adrenal gland;
RX   PubMed=7913464;
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
RT   the 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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
RT   but not chimeric Pbx proteins.";
RL   Mol. Cell. Biol. 17:5679-5687(1997).
RN   [5]
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
RT   cooperatively bind a cAMP-responsive sequence (CRS1) from bovine
RT   CYP17.";
RL   J. Biol. Chem. 273:7941-7948(1998).
RN   [6]
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.,
RA   Buchberg A.M., Wright C.V., MacDonald R.J.;
RT   "An endocrine-exocrine switch in the activity of the pancreatic
RT   homeodomain protein PDX1 through formation of a trimeric complex with
RT   PBX1b and MRG1 (MEIS2).";
RL   Mol. Cell. Biol. 18:5109-5120(1998).
RN   [7]
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   [8]
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.,
RA   Featherstone M.S.;
RT   "PBX and MEIS as non-DNA-binding partners in trimeric complexes with
RT   HOX proteins.";
RL   Mol. Cell. Biol. 19:7577-7588(1999).
RN   [9]
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
RT   trimer and cooperation with a pancreas-specific basic helix-loop-helix
RT   complex.";
RL   J. Biol. Chem. 276:17985-17993(2001).
RN   [10]
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
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.,
RA   Bojilova E., Boisson B., Prall O.W., Elliott D.A., Solloway M.,
RA   Lenti E., Hidaka C., Chang C.P., Mahlaoui N., Harvey R.P.,
RA   Casanova J.L., Selleri L.;
RT   "Congenital asplenia in mice and humans with mutations in a Pbx/Nkx2-
RT   5/p15 module.";
RL   Dev. Cell 22:913-926(2012).
RN   [12]
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
RT   extension upon binding DNA and HOX-derived YPWM peptides(,).";
RL   Biochemistry 39:9943-9950(2000).
RN   [13]
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
RT   homeodomain.";
RL   J. Biol. Chem. 278:1053-1058(2003).
CC   -!- FUNCTION: Plays a role in the cAMP-dependent regulation of CYP17
CC       gene expression via its cAMP-regulatory sequence (CRS1) 5'-
CC       ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in
CC       complex with MEIS1. May have a role in steroidogenesis and,
CC       subsequently, sexual development and differentiation. Isoform
CC       PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar
CC       cells is involved in the transcriptional activation of the ELA1
CC       enhancer; the complex binds to the enhancer B element and
CC       cooperates with the transcription factor 1 complex (PTF1) bound to
CC       the enhancer A element. Probably in complex with MEIS2, is
CC       involved in transcriptional regulation by KLF4. Acts as a
CC       transcriptional activator of NKX2-5 and a transcriptional
CC       repressor of CDKN2B. Together with NKX2-5, it is required for
CC       spleen development through a mechanism that involves CDKN2B
CC       repression. {ECO:0000269|PubMed:22560297}.
CC   -!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA including
CC       a cAMP-responsive sequence in CYP17. Also forms heterotrimers with
CC       MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9
CC       and HOXD10. Interacts with PBXIP1 and TLX1. Isoform PBX1a
CC       interacts with MEIS2 isoform Meis2D, SP1, SP3 and KLF4. Isoform
CC       PBX1b is part of a PDX1:PBX1b:MEIS2b complex; PBX1b recruits
CC       Meis2B to the complex. Interacts with FOXC1 (By similarity).
CC       {ECO:0000250|UniProtKB:P40424, ECO:0000269|PubMed:10082572,
CC       ECO:0000269|PubMed:10523646, ECO:0000269|PubMed:11279116,
CC       ECO:0000269|PubMed:12409300, ECO:0000269|PubMed:9315626,
CC       ECO:0000269|PubMed:9525891, ECO:0000269|PubMed:9710595}.
CC   -!- INTERACTION:
CC       P09632:Hoxb8; NbExp=3; IntAct=EBI-6996259, EBI-925374;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40424}.
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: Widely distributed in steroidogenic and non-
CC       steroidogenic cells.
CC   -!- SIMILARITY: Belongs to the TALE/PBX homeobox family.
CC       {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   SMR; P41778; -.
DR   BioGrid; 202037; 23.
DR   CORUM; P41778; -.
DR   DIP; DIP-6107N; -.
DR   IntAct; P41778; 5.
DR   MINT; P41778; -.
DR   STRING; 10090.ENSMUSP00000135516; -.
DR   iPTMnet; P41778; -.
DR   PhosphoSitePlus; P41778; -.
DR   MaxQB; P41778; -.
DR   PaxDb; P41778; -.
DR   PRIDE; P41778; -.
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   eggNOG; KOG0774; Eukaryota.
DR   eggNOG; ENOG410XRVF; LUCA.
DR   GeneTree; ENSGT00940000154374; -.
DR   HOGENOM; HOG000266972; -.
DR   InParanoid; P41778; -.
DR   KO; K09355; -.
DR   OMA; STPNSAX; -.
DR   OrthoDB; 804740at2759; -.
DR   PhylomeDB; P41778; -.
DR   TreeFam; TF314340; -.
DR   ChiTaRS; Pbx1; mouse.
DR   EvolutionaryTrace; P41778; -.
DR   PRO; PR:P41778; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000052534; Expressed in 292 organ(s), highest expression level in rostral migratory stream.
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:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
DR   GO; GO:0005667; C:transcription factor 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:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor 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:0001658; P:branching involved in ureteric bud morphogenesis; IDA: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: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:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048536; P:spleen development; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Sexual differentiation; Steroidogenesis; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    430       Pre-B-cell leukemia transcription factor
FT                                1.
FT                                /FTId=PRO_0000049236.
FT   DNA_BIND    233    295       Homeobox; TALE-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00108}.
FT   COMPBIAS    127    135       Poly-Ala.
FT   VAR_SEQ     334    347       SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in
FT                                isoform PBX1b).
FT                                {ECO:0000303|PubMed:7913464}.
FT                                /FTId=VSP_002273.
FT   VAR_SEQ     348    430       Missing (in isoform PBX1b).
FT                                {ECO:0000303|PubMed:7913464}.
FT                                /FTId=VSP_002274.
FT   STRAND      236    240       {ECO:0000244|PDB:1LFU}.
FT   TURN        241    243       {ECO:0000244|PDB:1DU6}.
FT   HELIX       244    254       {ECO:0000244|PDB:1DU6}.
FT   TURN        255    257       {ECO:0000244|PDB:1DU6}.
FT   HELIX       263    273       {ECO:0000244|PDB:1DU6}.
FT   HELIX       277    287       {ECO:0000244|PDB:1DU6}.
FT   TURN        288    290       {ECO:0000244|PDB:1DU6}.
FT   HELIX       295    307       {ECO:0000244|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
//