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 06-MAR-2013, entry version 132. 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; Sciurognathi; 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 MEDLINE=94308119; 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/6; 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; 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 MEDLINE=98192578; 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; 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 MEDLINE=99182493; PubMed=10082572; 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; 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 STRUCTURE BY NMR OF 241-294. RX MEDLINE=20393887; 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 [11] 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. 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. CC -!- SUBCELLULAR LOCATION: Nucleus. 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 -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L27453; AAA21832.1; -; mRNA. DR EMBL; AF020196; AAB71191.1; -; mRNA. DR EMBL; BC058390; AAH58390.1; -; mRNA. DR IPI; IPI00115998; -. DR IPI; IPI00230237; -. DR PIR; A54863; A54863. DR RefSeq; NP_032809.1; NM_008783.2. DR RefSeq; NP_899198.1; NM_183355.2. DR UniGene; Mm.43358; -. DR UniGene; Mm.440114; -. DR PDB; 1DU6; NMR; -; A=241-294. DR PDB; 1LFU; NMR; -; P=233-313. DR PDBsum; 1DU6; -. DR PDBsum; 1LFU; -. DR ProteinModelPortal; P41778; -. DR SMR; P41778; 233-305. DR DIP; DIP-6107N; -. DR MINT; MINT-96519; -. DR STRING; P41778; -. DR PhosphoSite; P41778; -. DR PaxDb; P41778; -. DR PRIDE; P41778; -. DR Ensembl; ENSMUST00000072863; ENSMUSP00000072640; ENSMUSG00000052534. DR Ensembl; ENSMUST00000176540; ENSMUSP00000135516; ENSMUSG00000052534. DR Ensembl; ENSMUST00000176790; ENSMUSP00000134925; ENSMUSG00000052534. DR GeneID; 18514; -. DR KEGG; mmu:18514; -. DR UCSC; uc007dle.1; mouse. DR CTD; 5087; -. DR MGI; MGI:97495; Pbx1. DR eggNOG; NOG248144; -. DR GeneTree; ENSGT00390000016426; -. DR HOGENOM; HOG000266972; -. DR HOVERGEN; HBG000122; -. DR InParanoid; P41778; -. DR KO; K09355; -. DR OMA; NIQSQVD; -. DR OrthoDB; EOG45HRXQ; -. DR BindingDB; P41778; -. DR ChiTaRS; PBX1; mouse. DR EvolutionaryTrace; P41778; -. DR NextBio; 294252; -. DR Bgee; P41778; -. DR CleanEx; MM_PBX1; -. DR Genevestigator; P41778; -. DR GermOnline; ENSMUSG00000052534; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005667; C:transcription factor complex; IDA:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. DR GO; GO:0030325; P:adrenal gland development; 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:0048706; P:embryonic skeletal system development; IMP:MGI. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI. DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara. DR GO; GO:0009887; P:organ morphogenesis; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR GO; GO:0009954; P:proximal/distal pattern formation; 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:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeodomain. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR005542; PBX. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF03792; PBC; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain_like; 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 Differentiation; Direct protein sequencing; DNA-binding; Homeobox; KW Nucleus; Reference proteome; Sexual differentiation; Steroidogenesis; KW Transcription; 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 COMPBIAS 127 135 Poly-Ala. FT VAR_SEQ 334 347 SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in FT isoform PBX1b). FT /FTId=VSP_002273. FT VAR_SEQ 348 430 Missing (in isoform PBX1b). FT /FTId=VSP_002274. FT STRAND 236 240 FT TURN 241 243 FT HELIX 244 254 FT TURN 255 257 FT HELIX 263 273 FT HELIX 277 287 FT TURN 288 290 FT HELIX 295 307 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 //