ID BBX_MOUSE Reviewed; 907 AA. AC Q8VBW5; B8JK46; B8JK47; B8JK48; B8JK49; Q3TZK1; Q6NXY8; Q6PEU3; Q8BQJ7; AC Q8C7E0; Q8CDQ0; Q8CDV1; Q8VI48; Q8VI49; Q8VI50; Q9CS94; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 2. DT 25-MAY-2022, entry version 136. DE RecName: Full=HMG box transcription factor BBX; DE AltName: Full=Bobby sox homolog; DE AltName: Full=HMG box-containing protein 2; GN Name=Bbx; Synonyms=Hbp2; 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 1). RA Lee C.-J., Chan W.-I., Appleby V.J., Orme A.T., Scotting P.J.; RT "BBX is expressed in developing CNS and in neuronal tumours."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS LEU-30 AND RP HIS-281. RC STRAIN=C3H/He, and NMRI; RC TISSUE=Mammary gland, Mammary tumor, and Mesenchymal stem cell; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-454, AND FUNCTION. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=11680820; DOI=10.1007/s002940100241; RA Sanchez-Diaz A., Blanco M.A., Jones N., Moreno S.; RT "HBP2: a new mammalian protein that complements the fission yeast MBF RT transcription complex."; RL Curr. Genet. 40:110-118(2001). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-476, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, 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 [8] RP STRUCTURE BY NMR OF 80-148. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the HMG-box domain of murine bobby sox homolog."; RL Submitted (AUG-2005) to the PDB data bank. CC -!- FUNCTION: Transcription factor that is necessary for cell cycle CC progression from G1 to S phase. {ECO:0000269|PubMed:11680820}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=BbxA; CC IsoId=Q8VBW5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VBW5-2; Sequence=VSP_018007, VSP_018008, VSP_018009; CC Name=3; CC IsoId=Q8VBW5-3; Sequence=VSP_018010; CC Name=4; CC IsoId=Q8VBW5-4; Sequence=VSP_018011, VSP_018012; CC -!- SEQUENCE CAUTION: CC Sequence=AAL68987.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAL68988.1; Type=Erroneous initiation; Evidence={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; AF454943; AAL58872.1; -; mRNA. DR EMBL; AF454944; AAL58873.1; -; mRNA. DR EMBL; AK017487; BAB30768.1; -; mRNA. DR EMBL; AK029532; BAC26500.2; -; mRNA. DR EMBL; AK029747; BAC26596.1; -; mRNA. DR EMBL; AK049516; BAC33788.1; -; mRNA. DR EMBL; AK050488; BAC34285.1; -; mRNA. DR EMBL; AK157813; BAE34207.1; -; mRNA. DR EMBL; AC109627; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CT571273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC057869; AAH57869.1; -; mRNA. DR EMBL; BC066821; AAH66821.1; -; mRNA. DR EMBL; AF276950; AAL68986.1; -; mRNA. DR EMBL; AF276951; AAL68987.1; ALT_SEQ; mRNA. DR EMBL; AF276952; AAL68988.1; ALT_INIT; mRNA. DR CCDS; CCDS37354.1; -. [Q8VBW5-1] DR CCDS; CCDS84241.1; -. [Q8VBW5-3] DR RefSeq; NP_001334169.1; NM_001347240.1. [Q8VBW5-3] DR RefSeq; NP_081720.2; NM_027444.3. [Q8VBW5-1] DR RefSeq; XP_011244310.1; XM_011246008.2. [Q8VBW5-1] DR RefSeq; XP_011244311.1; XM_011246009.1. [Q8VBW5-3] DR RefSeq; XP_017172619.1; XM_017317130.1. [Q8VBW5-1] DR PDB; 1WZ6; NMR; -; A=80-148. DR PDBsum; 1WZ6; -. DR AlphaFoldDB; Q8VBW5; -. DR SMR; Q8VBW5; -. DR BioGRID; 214101; 1. DR STRING; 10090.ENSMUSP00000119238; -. DR iPTMnet; Q8VBW5; -. DR PhosphoSitePlus; Q8VBW5; -. DR EPD; Q8VBW5; -. DR jPOST; Q8VBW5; -. DR MaxQB; Q8VBW5; -. DR PaxDb; Q8VBW5; -. DR PeptideAtlas; Q8VBW5; -. DR PRIDE; Q8VBW5; -. DR ProteomicsDB; 277183; -. [Q8VBW5-1] DR ProteomicsDB; 277184; -. [Q8VBW5-2] DR ProteomicsDB; 277185; -. [Q8VBW5-3] DR ProteomicsDB; 277186; -. [Q8VBW5-4] DR Antibodypedia; 32337; 113 antibodies from 24 providers. DR DNASU; 70508; -. DR Ensembl; ENSMUST00000066037; ENSMUSP00000066384; ENSMUSG00000022641. [Q8VBW5-2] DR Ensembl; ENSMUST00000089399; ENSMUSP00000086821; ENSMUSG00000022641. [Q8VBW5-4] DR Ensembl; ENSMUST00000089404; ENSMUSP00000086826; ENSMUSG00000022641. [Q8VBW5-3] DR Ensembl; ENSMUST00000114488; ENSMUSP00000110132; ENSMUSG00000022641. [Q8VBW5-1] DR Ensembl; ENSMUST00000138166; ENSMUSP00000119238; ENSMUSG00000022641. [Q8VBW5-1] DR GeneID; 70508; -. DR KEGG; mmu:70508; -. DR UCSC; uc007zkn.2; mouse. [Q8VBW5-1] DR UCSC; uc007zkp.2; mouse. [Q8VBW5-3] DR UCSC; uc007zkq.2; mouse. [Q8VBW5-2] DR UCSC; uc007zkr.2; mouse. [Q8VBW5-4] DR CTD; 56987; -. DR MGI; MGI:1917758; Bbx. DR VEuPathDB; HostDB:ENSMUSG00000022641; -. DR eggNOG; KOG2746; Eukaryota. DR GeneTree; ENSGT00940000158592; -. DR HOGENOM; CLU_017230_0_0_1; -. DR InParanoid; Q8VBW5; -. DR OMA; LAEAKMC; -. DR OrthoDB; 1641977at2759; -. DR PhylomeDB; Q8VBW5; -. DR TreeFam; TF106402; -. DR BioGRID-ORCS; 70508; 6 hits in 74 CRISPR screens. DR ChiTaRS; Bbx; mouse. DR EvolutionaryTrace; Q8VBW5; -. DR PRO; PR:Q8VBW5; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q8VBW5; protein. DR Bgee; ENSMUSG00000022641; Expressed in placenta and 295 other tissues. DR Genevisible; Q8VBW5; MM. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0060348; P:bone development; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 1.10.30.10; -; 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR019102; TF_HMG_box_BBX_DUF2028. DR Pfam; PF09667; DUF2028; 2. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; SSF47095; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..907 FT /note="HMG box transcription factor BBX" FT /id="PRO_0000232886" FT DNA_BIND 80..148 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 37..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 152..185 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 495..612 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 628..672 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..736 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 769..854 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 877..907 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..55 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 459..479 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 592..612 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 646..668 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 773..787 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 476 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 483 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT MOD_RES 701 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT MOD_RES 789 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT MOD_RES 811 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT CROSSLNK 384 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT CROSSLNK 571 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT CROSSLNK 693 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q8WY36" FT VAR_SEQ 55..135 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018007" FT VAR_SEQ 223..249 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018008" FT VAR_SEQ 730 FT /note="S -> SKGPFQSQKKNLFHKIVSKYKHKKEKPNVPE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018009" FT VAR_SEQ 732..751 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_018010" FT VAR_SEQ 733..750 FT /note="SGDKWSHKQFFLDAIHPT -> PFQSQKKNLFHKIVSKYK (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_018011" FT VAR_SEQ 751..907 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_018012" FT VARIANT 30 FT /note="P -> L (in strain: C3H/He)" FT /evidence="ECO:0000269|PubMed:15489334" FT VARIANT 281 FT /note="Q -> H (in strain: C3H/He)" FT /evidence="ECO:0000269|PubMed:15489334" FT CONFLICT 269 FT /note="L -> F (in Ref. 1; AAL58872/AAL58873 and 2; FT BAB30768)" FT /evidence="ECO:0000305" FT CONFLICT 450 FT /note="K -> R (in Ref. 2; BAC34285)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="N -> T (in Ref. 1; AAL58872/AAL58873)" FT /evidence="ECO:0000305" FT HELIX 86..101 FT /evidence="ECO:0007829|PDB:1WZ6" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:1WZ6" FT HELIX 109..119 FT /evidence="ECO:0007829|PDB:1WZ6" FT HELIX 123..140 FT /evidence="ECO:0007829|PDB:1WZ6" SQ SEQUENCE 907 AA; 100783 MW; 53E113D4B3DE4DAC CRC64; MKGSNRNKDH STEGEGDGKR PKRKCLQWHP LLAKKLLDFS EEEEEDEEEE DIDKVQLLEA DGLEQDVAET EDDESPEQRA RRPMNAFLLF CKRHRSLVRQ EHPRLDNRGA TKILADWWAV LDPKEKQKYT DMAKEYKDAF MKANPGYRWC PTTNKPVKSP TPTVNPRKKL WAFPPDSSRD LPTPKKAKTE VPQLNFGMAD PTQMGGLSML LLAGEHALGT PEASSGTCRP DISESPELRQ KSPLFQFAEI SSRTSHPDAP SKQCQASALF QFAEISSSTS QLGGTEPVKR CGNSALFQLA EMCLASEGVK MEDTKLIKSK ESDGGRIEEI EKGKEERGTE VEKTTETSFQ KEAEFGKSAK GNVRESKDLR DIEQLQMDNV MAIKVEDPKE IRKEPEDDQK YSHFPDFSYS ASSKIIISGV PSRKDHMCHP HGIMIIEDPT TLNKPEKIKK KKKKNKLDRH GNDKSTPKKT CKKRQSSESD IESVMYTIEA VAKGDWGVDK LGETPRKKVR PSSSGKGGIL DAKPPKKKVK SKEKKVSKEK CSDITKESRP PDFLSISASK SVPGEVPEGI KAEPLTPTED ALPPSLPGQA KPEDSDCHRK TETCGSRKSE RSCKGALYKT LVSEGMLTSL RANVDRGKRS SGKGNSSDHE GCWSEESWTF NQSGTSGSKK FKKKLREDSF LGSAKLDEEF EKKFNSLPQY SPITFDRKCV STPRKKKKTG NMSSESTKTS KGSGDKWSHK QFFLDAIHPT EAIFSEDKST TEPAFKVKNA LSIPNTPEPT TMQEPLVGSQ KRKARKTKIT HLVRTADGRV SPAGGTLDDK PKEQLQRSLP KVPGTYCGDN CSHSTVEEPR SSTPDMPAVS AFFSLAALAE VAAMENVHRG QRSTPLTHDG QPKEMPQAPV LISCADQ //