ID HBP1_RAT Reviewed; 513 AA.
AC Q62661; Q5BK86;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 08-NOV-2023, entry version 144.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7937077; DOI=10.1093/nar/22.18.3685;
RA Lesage F., Hugnot J.-P., Amri E.-Z., Grimaldi P., Barhanin J.,
RA Lazdunski M.;
RT "Expression cloning in K+ transport defective yeast and distribution of
RT HBP1, a new putative HMG transcriptional regulator.";
RL Nucleic Acids Res. 22:3685-3688(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBUNIT: Binds TCF4 (By similarity). Binds RB1. Binds the second PAH
CC repeat of SIN3A (By similarity). {ECO:0000250|UniProtKB:O60381,
CC ECO:0000250|UniProtKB:Q8R316}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, adipose tissue, lung,
CC brain, spleen, kidney, skeletal muscle and heart.
CC {ECO:0000269|PubMed:7937077}.
CC -!- DEVELOPMENTAL STAGE: Not detectable in undifferentiated preadipocytes
CC and myogenic cells. Accumulates at high levels during the terminal
CC stages of the differentiation process. {ECO:0000269|PubMed:7937077}.
CC -!- INDUCTION: Up-regulated by insulin in differentiated cultured
CC adipocytes. {ECO:0000269|PubMed:7937077}.
CC -!- PTM: Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex,
CC leading to subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:O60381}.
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; U09551; AAA53240.1; -; mRNA.
DR EMBL; BC091165; AAH91165.1; -; mRNA.
DR PIR; I58311; I58311.
DR RefSeq; NP_037353.2; NM_013221.2.
DR AlphaFoldDB; Q62661; -.
DR BMRB; Q62661; -.
DR SMR; Q62661; -.
DR STRING; 10116.ENSRNOP00000012004; -.
DR iPTMnet; Q62661; -.
DR PhosphoSitePlus; Q62661; -.
DR PaxDb; 10116-ENSRNOP00000012004; -.
DR GeneID; 27080; -.
DR KEGG; rno:27080; -.
DR AGR; RGD:620444; -.
DR CTD; 26959; -.
DR RGD; 620444; Hbp1.
DR eggNOG; ENOG502QR1P; Eukaryota.
DR InParanoid; Q62661; -.
DR OrthoDB; 2882425at2759; -.
DR PhylomeDB; Q62661; -.
DR TreeFam; TF105381; -.
DR PRO; PR:Q62661; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:NTNU_SB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0032369; P:negative regulation of lipid transport; ISO:RGD.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:RGD.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB.
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 CDD; cd21988; HMG-box_HBP1; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
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; HMG BOX-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR15499:SF3; HMG BOX-CONTAINING PROTEIN 1; 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; AXH domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51148; AXH; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..513
FT /note="HMG box-containing protein 1"
FT /id="PRO_0000048549"
FT DOMAIN 202..343
FT /note="AXH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496"
FT DNA_BIND 433..501
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 151..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 144
FT /note="K -> N (in Ref. 1; AAA53240)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> T (in Ref. 1; AAA53240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57430 MW; CC71A0918E793036 CRC64;
MVWEVKTNQR PHAVQRLLLV MDERATGVSD SLELLQCNEN VPSSPGYNSC DEHMELDDLP
ELQAVQSDPT QSAIYQLSSD VSHQEYPRPS WSQNTSDIPE NTHREDEVDW LTELANIATS
PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSAKS GPAFPHDHWK EETPVRHERA
NSESESGIFC MSSLSDDDDL GWCNSWPSTV WHCFLKGTRL CFHKESKKEW QDVEDFARAA
SCDEEEIQMG THKGYGSDGL KLLSHEESVS FGESVLKLTF DPGTVEDGLL TVECKLDHPF
YVKNKGWSSF YPSLTVVQHG IPCCEIHIGD VCLPPGHPDA INFDDSGVFD TFKSYDFTPM
DSSAVYVLSS MARQRRASLS CGGPGTGQEF AGSEFSKSCG SPGSSQLSSS SLYTKAVKSH
SSGTVSATSP NKCKRPMNAF MLFAKKYRVE YTQMYPGKDN RAISVILGDR WKKMKNEERR
MYTLEAKALA EEQKRLNPDC WKRKRTNSGS QQH
//
