ID BBX_MOUSE Reviewed; 907 AA. AC Q8VBW5; B8JK46; B8JK47; B8JK48; B8JK49; Q3TZK1; Q6NXY8; Q6PEU3; AC Q8BQJ7; Q8C7E0; Q8CDQ0; Q8CDV1; Q8VI48; Q8VI49; Q8VI50; Q9CS94; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 2. DT 12-SEP-2018, entry version 116. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS RP LEU-30 AND 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 RT project: 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 RT 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 RT 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; CT571273; CAX15928.1; -; Genomic_DNA. DR EMBL; AC109627; CAX15928.1; JOINED; Genomic_DNA. DR EMBL; CT571273; CAX15929.1; -; Genomic_DNA. DR EMBL; AC109627; CAX15929.1; JOINED; Genomic_DNA. DR EMBL; CT571273; CAX15930.1; -; Genomic_DNA. DR EMBL; AC109627; CAX15930.1; JOINED; Genomic_DNA. DR EMBL; CT571273; CAX15931.1; -; Genomic_DNA. DR EMBL; AC109627; CAX15931.1; JOINED; 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 UniGene; Mm.28940; -. DR PDB; 1WZ6; NMR; -; A=80-148. DR PDBsum; 1WZ6; -. DR ProteinModelPortal; Q8VBW5; -. DR SMR; Q8VBW5; -. DR BioGrid; 214101; 1. DR iPTMnet; Q8VBW5; -. DR PhosphoSitePlus; Q8VBW5; -. DR EPD; Q8VBW5; -. DR PaxDb; Q8VBW5; -. DR PeptideAtlas; Q8VBW5; -. DR PRIDE; Q8VBW5; -. 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 eggNOG; ENOG410ITBH; Eukaryota. DR eggNOG; ENOG410Y941; LUCA. DR GeneTree; ENSGT00530000063757; -. DR HOVERGEN; HBG079777; -. DR InParanoid; Q8VBW5; -. DR KO; K21643; -. DR OMA; DPTQMGG; -. DR OrthoDB; EOG091G16LO; -. DR PhylomeDB; Q8VBW5; -. DR TreeFam; TF106402; -. DR EvolutionaryTrace; Q8VBW5; -. DR PRO; PR:Q8VBW5; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; ENSMUSG00000022641; Expressed in 274 organ(s), highest expression level in placenta. DR CleanEx; MM_BBX; -. DR ExpressionAtlas; Q8VBW5; baseline and differential. DR Genevisible; Q8VBW5; MM. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0060348; P:bone development; IMP:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. 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; 1. 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; Complete proteome; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1 907 HMG box transcription factor BBX. FT /FTId=PRO_0000232886. FT DNA_BIND 80 148 HMG box. {ECO:0000255|PROSITE- FT ProRule:PRU00267}. FT COMPBIAS 41 50 Poly-Glu. FT COMPBIAS 444 540 Lys-rich. FT COMPBIAS 715 718 Poly-Lys. FT MOD_RES 242 242 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 476 476 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 483 483 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8WY36}. FT MOD_RES 701 701 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8WY36}. FT MOD_RES 789 789 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8WY36}. FT MOD_RES 811 811 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8WY36}. FT CROSSLNK 384 384 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q8WY36}. FT CROSSLNK 571 571 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q8WY36}. FT CROSSLNK 693 693 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q8WY36}. FT VAR_SEQ 55 135 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_018007. FT VAR_SEQ 223 249 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_018008. FT VAR_SEQ 730 730 S -> SKGPFQSQKKNLFHKIVSKYKHKKEKPNVPE (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_018009. FT VAR_SEQ 732 751 Missing (in isoform 3). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_018010. FT VAR_SEQ 733 750 SGDKWSHKQFFLDAIHPT -> PFQSQKKNLFHKIVSKYK FT (in isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_018011. FT VAR_SEQ 751 907 Missing (in isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_018012. FT VARIANT 30 30 P -> L (in strain: C3H/He). FT {ECO:0000269|PubMed:15489334}. FT VARIANT 281 281 Q -> H (in strain: C3H/He). FT {ECO:0000269|PubMed:15489334}. FT CONFLICT 269 269 L -> F (in Ref. 1; AAL58872/AAL58873 and FT 2; BAB30768). {ECO:0000305}. FT CONFLICT 450 450 K -> R (in Ref. 2; BAC34285). FT {ECO:0000305}. FT CONFLICT 455 455 N -> T (in Ref. 1; AAL58872/AAL58873). FT {ECO:0000305}. FT HELIX 86 101 {ECO:0000244|PDB:1WZ6}. FT STRAND 103 105 {ECO:0000244|PDB:1WZ6}. FT HELIX 109 119 {ECO:0000244|PDB:1WZ6}. FT HELIX 123 140 {ECO:0000244|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 //