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Pre-B-cell leukemia transcription factor 1 (Homeobox protein PBX1)

 PBX1_MOUSE              Reviewed;         430 AA.
P41778;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
21-FEB-2002, sequence version 2.
12-SEP-2018, entry version 183.
RecName: Full=Pre-B-cell leukemia transcription factor 1;
AltName: Full=Homeobox protein PBX1;
Name=Pbx1; Synonyms=Pbx-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1B), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Adrenal gland;
PubMed=7913464;
Kagawa N., Ogo A., Takahashi Y., Iwamatsu A., Waterman M.R.;
"A cAMP-regulatory sequence (CRS1) of CYP17 is a cellular target for
the homeodomain protein Pbx1.";
J. Biol. Chem. 269:18716-18719(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1A).
Liu Y., MacDonald R.J.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PBX1A).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH MEIS1.
PubMed=9315626; DOI=10.1128/MCB.17.10.5679;
Chang C.-P., Jacobs Y., Nakamura T., Jenkins N.A., Copeland N.G.,
Cleary M.L.;
"Meis proteins are major in vivo DNA binding partners for wild-type
but not chimeric Pbx proteins.";
Mol. Cell. Biol. 17:5679-5687(1997).
[5]
INTERACTION WITH MEIS1.
PubMed=9525891; DOI=10.1074/jbc.273.14.7941;
Bischof L.J., Kagawa N., Moskow J.J., Takahashi Y., Iwamatsu A.,
Buchberg A.M., Waterman M.R.;
"Members of the Meis1 and Pbx homeodomain protein families
cooperatively bind a cAMP-responsive sequence (CRS1) from bovine
CYP17.";
J. Biol. Chem. 273:7941-7948(1998).
[6]
IDENTIFICATION IN A COMPLEX WITH PDX1 AND MEIS2.
PubMed=9710595; DOI=10.1128/MCB.18.9.5109;
Swift G.H., Liu Y., Rose S.D., Bischof L.J., Steelman S.,
Buchberg A.M., Wright C.V., MacDonald R.J.;
"An endocrine-exocrine switch in the activity of the pancreatic
homeodomain protein PDX1 through formation of a trimeric complex with
PBX1b and MRG1 (MEIS2).";
Mol. Cell. Biol. 18:5109-5120(1998).
[7]
INTERACTION WITH HOXA9 AND MEIS1.
PubMed=10082572; DOI=10.1128/MCB.19.4.3051;
Shen W.-F., Rozenfeld S., Kwong A., Koemueves L.G., Lawrence H.J.,
Largman C.;
"HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.";
Mol. Cell. Biol. 19:3051-3061(1999).
[8]
INTERACTION WITH HOXD4; HOXD9; HOXD10 AND MEIS1.
PubMed=10523646; DOI=10.1128/MCB.19.11.7577;
Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U.,
Featherstone M.S.;
"PBX and MEIS as non-DNA-binding partners in trimeric complexes with
HOX proteins.";
Mol. Cell. Biol. 19:7577-7588(1999).
[9]
INTERACTION WITH MEIS2, AND IDENTIFICATION IN A COMPLEX WITH PDX1 AND
MEIS2.
PubMed=11279116; DOI=10.1074/jbc.M100678200;
Liu Y., MacDonald R.J., Swift G.H.;
"DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b
trimer and cooperation with a pancreas-specific basic helix-loop-helix
complex.";
J. Biol. Chem. 276:17985-17993(2001).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION.
PubMed=22560297; DOI=10.1016/j.devcel.2012.02.009;
Koss M., Bolze A., Brendolan A., Saggese M., Capellini T.D.,
Bojilova E., Boisson B., Prall O.W., Elliott D.A., Solloway M.,
Lenti E., Hidaka C., Chang C.P., Mahlaoui N., Harvey R.P.,
Casanova J.L., Selleri L.;
"Congenital asplenia in mice and humans with mutations in a Pbx/Nkx2-
5/p15 module.";
Dev. Cell 22:913-926(2012).
[12]
STRUCTURE BY NMR OF 241-294.
PubMed=10933814; DOI=10.1021/bi0001067;
Sprules T., Green N., Featherstone M., Gehring K.;
"Conformational changes in the PBX homeodomain and C-terminal
extension upon binding DNA and HOX-derived YPWM peptides(,).";
Biochemistry 39:9943-9950(2000).
[13]
STRUCTURE BY NMR OF 233-313 IN COMPLEX WITH DNA.
PubMed=12409300; DOI=10.1074/jbc.M207504200;
Sprules T., Green N., Featherstone M., Gehring K.;
"Lock and key binding of the HOX YPWM peptide to the PBX
homeodomain.";
J. Biol. Chem. 278:1053-1058(2003).
-!- FUNCTION: Plays a role in the cAMP-dependent regulation of CYP17
gene expression via its cAMP-regulatory sequence (CRS1) 5'-
ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in
complex with MEIS1. May have a role in steroidogenesis and,
subsequently, sexual development and differentiation. Isoform
PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar
cells is involved in the transcriptional activation of the ELA1
enhancer; the complex binds to the enhancer B element and
cooperates with the transcription factor 1 complex (PTF1) bound to
the enhancer A element. Probably in complex with MEIS2, is
involved in transcriptional regulation by KLF4. Acts as a
transcriptional activator of NKX2-5 and a transcriptional
repressor of CDKN2B. Together with NKX2-5, it is required for
spleen development through a mechanism that involves CDKN2B
repression. {ECO:0000269|PubMed:22560297}.
-!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA including
a cAMP-responsive sequence in CYP17. Also forms heterotrimers with
MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9
and HOXD10. Interacts with PBXIP1 and TLX1. Isoform PBX1a
interacts with MEIS2 isoform Meis2D, SP1, SP3 and KLF4. Isoform
PBX1b is part of a PDX1:PBX1b:MEIS2b complex; PBX1b recruits
Meis2B to the complex. Interacts with FOXC1 (By similarity).
{ECO:0000250|UniProtKB:P40424, ECO:0000269|PubMed:10082572,
ECO:0000269|PubMed:10523646, ECO:0000269|PubMed:11279116,
ECO:0000269|PubMed:12409300, ECO:0000269|PubMed:9315626,
ECO:0000269|PubMed:9525891, ECO:0000269|PubMed:9710595}.
-!- INTERACTION:
P09632:Hoxb8; NbExp=3; IntAct=EBI-6996259, EBI-925374;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40424}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PBX1a;
IsoId=P41778-1; Sequence=Displayed;
Name=PBX1b;
IsoId=P41778-2; Sequence=VSP_002273, VSP_002274;
-!- TISSUE SPECIFICITY: Widely distributed in steroidogenic and non-
steroidogenic cells.
-!- SIMILARITY: Belongs to the TALE/PBX homeobox family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L27453; AAA21832.1; -; mRNA.
EMBL; AF020196; AAB71191.1; -; mRNA.
EMBL; BC058390; AAH58390.1; -; mRNA.
CCDS; CCDS15461.1; -. [P41778-1]
CCDS; CCDS15462.1; -. [P41778-2]
PIR; A54863; A54863.
RefSeq; NP_001278437.1; NM_001291508.1. [P41778-2]
RefSeq; NP_032809.1; NM_008783.3. [P41778-2]
RefSeq; NP_899198.1; NM_183355.3. [P41778-1]
UniGene; Mm.43358; -.
UniGene; Mm.440114; -.
PDB; 1DU6; NMR; -; A=241-294.
PDB; 1LFU; NMR; -; P=233-313.
PDBsum; 1DU6; -.
PDBsum; 1LFU; -.
ProteinModelPortal; P41778; -.
SMR; P41778; -.
BioGrid; 202037; 23.
CORUM; P41778; -.
DIP; DIP-6107N; -.
IntAct; P41778; 5.
MINT; P41778; -.
STRING; 10090.ENSMUSP00000135516; -.
iPTMnet; P41778; -.
PhosphoSitePlus; P41778; -.
MaxQB; P41778; -.
PaxDb; P41778; -.
PRIDE; P41778; -.
Ensembl; ENSMUST00000072863; ENSMUSP00000072640; ENSMUSG00000052534. [P41778-2]
Ensembl; ENSMUST00000176540; ENSMUSP00000135516; ENSMUSG00000052534. [P41778-1]
Ensembl; ENSMUST00000176790; ENSMUSP00000134925; ENSMUSG00000052534. [P41778-2]
Ensembl; ENSMUST00000188912; ENSMUSP00000140606; ENSMUSG00000052534. [P41778-2]
GeneID; 18514; -.
KEGG; mmu:18514; -.
UCSC; uc007dle.2; mouse. [P41778-1]
CTD; 5087; -.
MGI; MGI:97495; Pbx1.
eggNOG; KOG0774; Eukaryota.
eggNOG; ENOG410XRVF; LUCA.
GeneTree; ENSGT00390000016426; -.
HOGENOM; HOG000266972; -.
HOVERGEN; HBG000122; -.
InParanoid; P41778; -.
KO; K09355; -.
OMA; STPNSAX; -.
OrthoDB; EOG091G10TD; -.
PhylomeDB; P41778; -.
TreeFam; TF314340; -.
ChiTaRS; Pbx1; mouse.
EvolutionaryTrace; P41778; -.
PRO; PR:P41778; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000052534; Expressed in 292 organ(s), highest expression level in rostral migratory stream.
CleanEx; MM_PBX1; -.
ExpressionAtlas; P41778; baseline and differential.
Genevisible; P41778; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0030325; P:adrenal gland development; IMP:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0001655; P:urogenital system development; IMP:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR005542; PBX.
Pfam; PF00046; Homeobox; 1.
Pfam; PF03792; PBC; 1.
SMART; SM00389; HOX; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
DNA-binding; Homeobox; Nucleus; Reference proteome;
Sexual differentiation; Steroidogenesis; Transcription;
Transcription regulation.
CHAIN 1 430 Pre-B-cell leukemia transcription factor
1.
/FTId=PRO_0000049236.
DNA_BIND 233 295 Homeobox; TALE-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
COMPBIAS 127 135 Poly-Ala.
VAR_SEQ 334 347 SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in
isoform PBX1b).
{ECO:0000303|PubMed:7913464}.
/FTId=VSP_002273.
VAR_SEQ 348 430 Missing (in isoform PBX1b).
{ECO:0000303|PubMed:7913464}.
/FTId=VSP_002274.
STRAND 236 240 {ECO:0000244|PDB:1LFU}.
TURN 241 243 {ECO:0000244|PDB:1DU6}.
HELIX 244 254 {ECO:0000244|PDB:1DU6}.
TURN 255 257 {ECO:0000244|PDB:1DU6}.
HELIX 263 273 {ECO:0000244|PDB:1DU6}.
HELIX 277 287 {ECO:0000244|PDB:1DU6}.
TURN 288 290 {ECO:0000244|PDB:1DU6}.
HELIX 295 307 {ECO:0000244|PDB:1LFU}.
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


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