HBP1_MOUSE
ID HBP1_MOUSE Reviewed; 516 AA.
AC Q8R316; Q3V0I4; Q8BUS3; Q8C199;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=HMG box-containing protein 1;
DE AltName: Full=HMG box transcription factor 1;
DE AltName: Full=High mobility group box transcription factor 1;
GN Name=Hbp1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Skin, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP INTERACTION WITH RB1, AND FUNCTION.
RX PubMed=9178770; DOI=10.1038/sj.onc.1201243;
RA Lavender P., Vandel L., Bannister A.J., Kouzarides T.;
RT "The HMG-box transcription factor HBP1 is targeted by the pocket proteins
RT and E1A.";
RL Oncogene 14:2721-2728(1997).
RN [4]
RP STRUCTURE BY NMR OF 208-345.
RX PubMed=14872137; DOI=10.1023/b:jnmr.0000015367.92295.0f;
RA de Chiara C., Kelly G., Frenkiel T.A., Pastore A.;
RT "Assignment of the 1H, 13C, and 15N resonances of the AXH domain of the
RT transcription factor HBP1.";
RL J. Biomol. NMR 28:411-412(2004).
RN [5]
RP STRUCTURE BY NMR OF 233-255, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-370
RP AND MET-373, AND INTERACTION WITH SIN3A.
RX PubMed=15235594; DOI=10.1038/nsmb798;
RA Swanson K.A., Knoepfler P.S., Huang K., Kang R.S., Cowley S.M.,
RA Laherty C.D., Eisenman R.N., Radhakrishnan I.;
RT "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with
RT opposite helical orientations.";
RL Nat. Struct. Mol. Biol. 11:738-746(2004).
CC -!- FUNCTION: Transcriptional repressor that binds to the promoter region
CC of target genes. Plays a role in the regulation of the cell cycle and
CC of the Wnt pathway. Binds preferentially to the sequence 5'-
CC TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by
CC interaction with RB1. Disrupts the interaction between DNA and TCF4 (By
CC similarity). {ECO:0000250|UniProtKB:O60381,
CC ECO:0000269|PubMed:9178770}.
CC -!- SUBUNIT: Binds TCF4 (By similarity). Binds RB1 (PubMed:9178770). Binds
CC the second PAH repeat of SIN3A (PubMed:15235594).
CC {ECO:0000250|UniProtKB:O60381, ECO:0000269|PubMed:15235594,
CC ECO:0000269|PubMed:9178770}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:15235594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R316-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R316-2; Sequence=VSP_014657;
CC -!- PTM: Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex,
CC leading to subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:O60381}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC026853; AAH26853.1; -; mRNA.
DR EMBL; AK028674; BAC26060.1; -; mRNA.
DR EMBL; AK082770; BAC38611.1; ALT_INIT; mRNA.
DR EMBL; AK133127; BAE21520.1; -; mRNA.
DR RefSeq; NP_694878.2; NM_153198.2.
DR RefSeq; NP_818774.2; NM_177993.3.
DR RefSeq; XP_017170701.1; XM_017315212.1.
DR PDB; 1S5R; NMR; -; A=358-380.
DR PDB; 1V06; NMR; -; A=208-345.
DR PDBsum; 1S5R; -.
DR PDBsum; 1V06; -.
DR AlphaFoldDB; Q8R316; -.
DR BMRB; Q8R316; -.
DR SMR; Q8R316; -.
DR BioGRID; 215977; 3.
DR STRING; 10090.ENSMUSP00000131158; -.
DR iPTMnet; Q8R316; -.
DR PhosphoSitePlus; Q8R316; -.
DR jPOST; Q8R316; -.
DR MaxQB; Q8R316; -.
DR PaxDb; Q8R316; -.
DR PRIDE; Q8R316; -.
DR ProteomicsDB; 269722; -. [Q8R316-1]
DR ProteomicsDB; 269723; -. [Q8R316-2]
DR DNASU; 73389; -.
DR GeneID; 73389; -.
DR KEGG; mmu:73389; -.
DR CTD; 26959; -.
DR MGI; MGI:894659; Hbp1.
DR eggNOG; ENOG502QR1P; Eukaryota.
DR InParanoid; Q8R316; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; Q8R316; -.
DR BioGRID-ORCS; 73389; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Hbp1; mouse.
DR EvolutionaryTrace; Q8R316; -.
DR PRO; PR:Q8R316; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R316; protein.
DR GO; GO:0016607; C:nuclear speck; 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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0032369; P:negative regulation of lipid transport; IDA:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR DisProt; DP01323; -.
DR Gene3D; 1.10.30.10; -; 1.
DR IDEAL; IID50097; -.
DR InterPro; IPR003652; Ataxin_AXH_dom.
DR InterPro; IPR036096; Ataxin_AXH_dom_sf.
DR InterPro; IPR039655; HBP1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR15499; PTHR15499; 1.
DR Pfam; PF08517; AXH; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00536; AXH; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF102031; SSF102031; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS51148; AXH; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..516
FT /note="HMG box-containing protein 1"
FT /id="PRO_0000048547"
FT DOMAIN 203..345
FT /note="AXH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496"
FT DNA_BIND 436..504
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 150..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 465..516
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014657"
FT MUTAGEN 370
FT /note="L->D: Strongly reduces Sin3A binding."
FT /evidence="ECO:0000269|PubMed:15235594"
FT MUTAGEN 373
FT /note="M->D: Strongly reduces Sin3A binding."
FT /evidence="ECO:0000269|PubMed:15235594"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1V06"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:1V06"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1V06"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:1V06"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1V06"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:1V06"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:1V06"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1S5R"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1S5R"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:1S5R"
SQ SEQUENCE 516 AA; 57645 MW; 2DC6D40FE41543B0 CRC64;
MVWEVKTNQM PNAVQKLLLV MDKRAPGMSD SLELLQCNEN LPSSPGYNSC DEHMELDDLP
ELQAVQSDPT QSAIYQLSSD VSHQEYPRSS WSQNTSDIPE NTHREDEVDW LTELANIATS
PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SGPAFPHDHW KEETPVRHER
ANSESESGIF CMSSLSDDDD LGWCNSWPST IWHCFLKGTR LCFHKESNKE WQDVEDFARA
ASCDNEEEIQ MGTHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH
PFYVKNKGWS SFYPSLTVVQ HGIPCCEIHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT
PMDSSAVYVL SSMARQRRAS LSCGGGPGTG QEFSGSEFSK SCGSPGSSQL SSSSLYAKAV
KSHSSGTVSA TSPNKCKRPM NAFMLFAKKY RVEYTQMYPG KDNRAISVIL GDRWKKMKNE
ERRMYTLEAK ALAEEQKRLN PDCWKRKRTN SGSQQH
