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   16-SEP-2015, entry version 100.
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; Sciurognathi;
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   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00267}.
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   RefSeq; NP_081720.2; NM_027444.3. [Q8VBW5-1]
DR   RefSeq; XP_006522626.1; XM_006522563.2. [Q8VBW5-3]
DR   RefSeq; XP_011244310.1; XM_011246008.1. [Q8VBW5-1]
DR   RefSeq; XP_011244311.1; XM_011246009.1. [Q8VBW5-3]
DR   UniGene; Mm.28940; -.
DR   PDB; 1WZ6; NMR; -; A=80-148.
DR   PDBsum; 1WZ6; -.
DR   ProteinModelPortal; Q8VBW5; -.
DR   SMR; Q8VBW5; 80-153.
DR   STRING; 10090.ENSMUSP00000110132; -.
DR   PhosphoSite; Q8VBW5; -.
DR   MaxQB; 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; NOG305473; -.
DR   GeneTree; ENSGT00530000063757; -.
DR   HOVERGEN; HBG079777; -.
DR   InParanoid; Q8VBW5; -.
DR   OMA; DPTQMGG; -.
DR   OrthoDB; EOG77DJ8X; -.
DR   PhylomeDB; Q8VBW5; -.
DR   TreeFam; TF106402; -.
DR   EvolutionaryTrace; Q8VBW5; -.
DR   NextBio; 331763; -.
DR   PRO; PR:Q8VBW5; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; Q8VBW5; -.
DR   CleanEx; MM_BBX; -.
DR   ExpressionAtlas; Q8VBW5; baseline and differential.
DR   Genevisible; Q8VBW5; MM.
DR   GO; GO:0005737; C:cytoplasm; 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; 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   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Transcription; Transcription regulation.
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   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
//