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HBP1_RAT
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   25-MAY-2022, entry version 139.
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}.
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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; Q62661; -.
DR   PRIDE; Q62661; -.
DR   GeneID; 27080; -.
DR   KEGG; rno:27080; -.
DR   CTD; 26959; -.
DR   RGD; 620444; Hbp1.
DR   eggNOG; ENOG502QR1P; Eukaryota.
DR   InParanoid; Q62661; -.
DR   OrthoDB; 1641977at2759; -.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 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; 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   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
 
 
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