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 22-APR-2020, entry version 193. 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), AND PARTIAL PROTEIN 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 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 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 [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 cooperatively RT bind a cAMP-responsive sequence (CRS1) from bovine 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., 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 [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., 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 [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 trimer RT and cooperation with a pancreas-specific basic helix-loop-helix 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 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., 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 [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 extension RT 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 homeodomain."; RL J. Biol. Chem. 278:1053-1058(2003). CC -!- FUNCTION: Plays a role in the cAMP-dependent regulation of CYP17 gene CC expression via its cAMP-regulatory sequence (CRS1) 5'-ATCAATCAA-3'. CC Acts as a transcriptional activator of PF4 in complex with MEIS1. May CC have a role in steroidogenesis and, subsequently, sexual development CC and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b CC complex in pancreatic acinar cells is involved in the transcriptional CC activation of the ELA1 enhancer; the complex binds to the enhancer B CC element and cooperates with the transcription factor 1 complex (PTF1) CC bound to 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 repressor of CC CDKN2B. Together with NKX2-5, it is required for spleen development CC through a mechanism that involves CDKN2B repression. CC {ECO:0000269|PubMed:22560297}. CC -!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA including a CC cAMP-responsive sequence in CYP17. Also forms heterotrimers with MEIS1 CC and a number of HOX proteins including HOXA9, HOXD4, HOXD9 and HOXD10. CC Interacts with PBXIP1 and TLX1. Isoform PBX1a interacts with MEIS2 CC isoform Meis2D, SP1, SP3 and KLF4. Isoform PBX1b is part of a CC PDX1:PBX1b:MEIS2b complex; PBX1b recruits Meis2B to the complex. CC Interacts with FOXC1 (By similarity). {ECO:0000250|UniProtKB:P40424, CC ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646, CC ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:12409300, CC ECO:0000269|PubMed:9315626, ECO:0000269|PubMed:9525891, CC ECO:0000269|PubMed:9710595}. CC -!- INTERACTION: CC P41778; 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. {ECO:0000305}. 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 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 Antibodypedia; 1079; 363 antibodies. 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; CLU_041153_1_0_1; -. 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 RNAct; P41778; protein. DR Bgee; ENSMUSG00000052534; Expressed in rostral migratory stream and 291 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: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:0000978; F:RNA polymerase II cis-regulatory region 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; 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 DNA_BIND 233..295 FT /note="Homeobox; TALE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT COMPBIAS 127..135 FT /note="Poly-Ala" 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 STRAND 236..240 FT /evidence="ECO:0000244|PDB:1LFU" FT TURN 241..243 FT /evidence="ECO:0000244|PDB:1DU6" FT HELIX 244..254 FT /evidence="ECO:0000244|PDB:1DU6" FT TURN 255..257 FT /evidence="ECO:0000244|PDB:1DU6" FT HELIX 263..273 FT /evidence="ECO:0000244|PDB:1DU6" FT HELIX 277..287 FT /evidence="ECO:0000244|PDB:1DU6" FT TURN 288..290 FT /evidence="ECO:0000244|PDB:1DU6" FT HELIX 295..307 FT /evidence="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 //