BBX_MOUSE
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 03-AUG-2022, entry version 137.
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};
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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; 118 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 labyrinth and 248 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
