PBX2_MOUSE
ID PBX2_MOUSE Reviewed; 430 AA.
AC O35984;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Pre-B-cell leukemia transcription factor 2;
DE AltName: Full=Homeobox protein PBX2;
GN Name=Pbx2;
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].
RA Liu Y., MacDonald R.J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Lung;
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).
CC -!- FUNCTION: Transcriptional activator that binds the sequence 5'-
CC ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms heterodimers with MEIS1 and heterotrimers with MEIS1 and
CC HOXA9. Interacts with PBXIP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; AF020198; AAB71193.1; -; mRNA.
DR EMBL; AF030001; AAB82006.1; -; Genomic_DNA.
DR EMBL; BC010287; AAH10287.1; -; mRNA.
DR EMBL; BC062147; AAH62147.1; -; mRNA.
DR CCDS; CCDS28648.1; -.
DR PIR; T09061; T09061.
DR RefSeq; NP_059491.1; NM_017463.2.
DR AlphaFoldDB; O35984; -.
DR SMR; O35984; -.
DR BioGRID; 202038; 9.
DR IntAct; O35984; 9.
DR STRING; 10090.ENSMUSP00000040464; -.
DR iPTMnet; O35984; -.
DR PhosphoSitePlus; O35984; -.
DR jPOST; O35984; -.
DR PaxDb; O35984; -.
DR PeptideAtlas; O35984; -.
DR PRIDE; O35984; -.
DR ProteomicsDB; 287795; -.
DR Antibodypedia; 28518; 204 antibodies from 25 providers.
DR DNASU; 18515; -.
DR Ensembl; ENSMUST00000038149; ENSMUSP00000040464; ENSMUSG00000034673.
DR GeneID; 18515; -.
DR KEGG; mmu:18515; -.
DR UCSC; uc008ccv.1; mouse.
DR CTD; 5089; -.
DR MGI; MGI:1341793; Pbx2.
DR VEuPathDB; HostDB:ENSMUSG00000034673; -.
DR eggNOG; KOG0774; Eukaryota.
DR GeneTree; ENSGT00940000160293; -.
DR InParanoid; O35984; -.
DR OMA; HALHEPP; -.
DR OrthoDB; 804740at2759; -.
DR PhylomeDB; O35984; -.
DR TreeFam; TF314340; -.
DR BioGRID-ORCS; 18515; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Pbx2; mouse.
DR PRO; PR:O35984; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35984; protein.
DR Bgee; ENSMUSG00000034673; Expressed in undifferentiated genital tubercle and 274 other tissues.
DR ExpressionAtlas; O35984; baseline and differential.
DR Genevisible; O35984; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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.
DR PROSITE; PS51978; PBC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..430
FT /note="Pre-B-cell leukemia transcription factor 2"
FT /id="PRO_0000049238"
FT DOMAIN 48..243
FT /note="PBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT DNA_BIND 244..306
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..134
FT /note="PBC-A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT REGION 137..243
FT /note="PBC-B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40425"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40425"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40425"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 430 AA; 45809 MW; CB6B71A6FE207E8D CRC64;
MDERLLGPPP PGGGRGGLGL VGAEPGGPGE PPGGGDPGGG SGGVPGGRGK QDIGDILQQI
MTITDQSLDE AQAKKHALNC HRMKPALFSV LCEIKEKTGL SIRSSQEEEP VDPQLMRLDN
MLLAEGVAGP EKGGGSAAAA AAAAASGGGV SPDNSIEHSD YRSKLAQIRH IYHSELEKYE
QACNEFTTHV MNLLREQSRT RPVAPKEMER MVSIIHRKFS AIQMQLKQST CEAVMILRSR
FLDARRKRRN FSKQATEVLN EYFYSHLSNP YPSEEAKEEL AKKCGITVSQ VSNWFGNKRI
RYKKNIGKFQ EEANIYAVKT AVSVAQGGHS RTSSPTPPSS AGSGGSFNLS GSGDMFLGMP
GLNGDSYPAS QVESLRHSMG PGSYGDNIGG GQIYSPREIR ANGGWQEAVT PSSVTSPTEG
PGSVHSDTSN
