ID PBX1_MOUSE STANDARD; PRT; 430 AA. AC P41778; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Pre-B-cell leukemia transcription factor 1 (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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM PBX1B), AND PARTIAL PROTEIN 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 (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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 INTERACTIONS WITH HOXA9 AND MEIS1. RX 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 [7] RP INTERACTIONS 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 [8] 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 [9] 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. 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. CC -!- SUBCELLULAR LOCATION: Nuclear. 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 PIR; A54863; A54863. DR PDB; 1DU6; NMR; A=241-294. DR PDB; 1LFU; NMR; P=233-313. DR TRANSFAC; T02088; -. DR TRANSFAC; T03451; -. DR Ensembl; ENSMUSG00000052534; Mus musculus. DR MGI; MGI:97495; Pbx1. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0030325; P:adrenal gland development; IMP. DR GO; GO:0001658; P:ureteric bud branching; IDA. DR GO; GO:0001655; P:urogenital system development; IMP. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR005542; PBX. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF03792; PBX; 1. DR PRINTS; PR00024; HOMEOBOX. DR ProDom; PD000010; Homeobox; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW 3D-structure; Activator; Alternative splicing; KW Direct protein sequencing; DNA-binding; Homeobox; Nuclear protein; KW Sexual differentiation; Steroidogenesis; Transcription; KW Transcription regulation. FT DNA_BIND 233 295 Homeobox; TALE-type. FT COMPBIAS 127 135 Poly-Ala. FT VARSPLIC 334 347 SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in FT isoform PBX1b). FT /FTId=VSP_002273. FT VARSPLIC 348 430 Missing (in isoform PBX1b). FT /FTId=VSP_002274. FT TURN 241 243 FT HELIX 244 254 FT TURN 255 257 FT HELIX 263 273 FT TURN 274 274 FT HELIX 277 287 FT TURN 288 290 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 //