ID HBP1_HUMAN Reviewed; 514 AA. AC O60381; B3KVB7; Q8TBM1; Q8TE93; Q96AJ2; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 27-MAR-2024, entry version 177. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND INTERACTION WITH RB1. RC TISSUE=Brain; RX PubMed=10958660; DOI=10.1128/mcb.20.18.6627-6637.2000; RA Lemercier C., Duncliffe K., Boibessot I., Zhang H., Verdel A., Angelov D., RA Khochbin S.; RT "Involvement of retinoblastoma protein and HBP1 in histone H1(0) gene RT expression."; RL Mol. Cell. Biol. 20:6627-6637(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 9-514 (ISOFORM 2). RC TISSUE=Hepatoma, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Uterus; 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 [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10562551; DOI=10.1093/emboj/18.22.6396; RA Zhuma T., Tyrrell R., Sekkali B., Skavdis G., Saveliev A., Tolaini M., RA Roderick K., Norton T., Smerdon S., Sedgwick S., Festenstein R., RA Kioussis D.; RT "Human HMG box transcription factor HBP1: a role in hCD2 LCR function."; RL EMBO J. 18:6396-6406(1999). RN [7] RP FUNCTION, AND INTERACTION WITH TCF4. RX PubMed=11500377; DOI=10.1093/emboj/20.16.4500; RA Sampson E.M., Haque Z.K., Ku M.-C., Tevosian S.G., Albanese C., RA Pestell R.G., Paulson K.E., Yee A.S.; RT "Negative regulation of the Wnt-beta-catenin pathway by the transcriptional RT repressor HBP1."; RL EMBO J. 20:4500-4511(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP UBIQUITINATION, AND INTERACTION WITH SIN3A. RX PubMed=29911972; DOI=10.7554/elife.35528; RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N., RA Picotti P., Stoffel M., Peter M.; RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets RT the transcription factor Hbp1 for degradation."; RL Elife 7:0-0(2018). RN [12] RP STRUCTURE BY NMR OF 422-503. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the HMG box domain from human HMG-box transcription RT factor 1."; RL Submitted (JUL-2007) to the PDB data bank. 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. CC {ECO:0000269|PubMed:10562551, ECO:0000269|PubMed:10958660, CC ECO:0000269|PubMed:11500377}. CC -!- SUBUNIT: Binds the second PAH repeat of SIN3A (Probable). Binds TCF4 CC (PubMed:11500377). Binds RB1 (PubMed:10958660). CC {ECO:0000269|PubMed:10958660, ECO:0000269|PubMed:11500377, CC ECO:0000305|PubMed:29911972}. CC -!- INTERACTION: CC O60381; P06400: RB1; NbExp=2; IntAct=EBI-954175, EBI-491274; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, CC ECO:0000269|PubMed:10562551}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O60381-1; Sequence=Displayed; CC Name=2; CC IsoId=O60381-2; Sequence=VSP_014655; CC Name=3; CC IsoId=O60381-3; Sequence=VSP_014656; CC -!- PTM: Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex, CC leading to subsequent proteasomal degradation. CC {ECO:0000269|PubMed:29911972}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB85059.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40791/HBP1"; 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; AF182038; AAD56225.1; -; mRNA. DR EMBL; AK074353; BAB85059.1; ALT_INIT; mRNA. DR EMBL; AK122785; BAG53729.1; -; mRNA. DR EMBL; AC004492; AAC08317.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83392.1; -; Genomic_DNA. DR EMBL; BC017069; AAH17069.1; -; mRNA. DR EMBL; BC022329; AAH22329.1; -; mRNA. DR CCDS; CCDS5741.1; -. [O60381-1] DR RefSeq; NP_001231191.1; NM_001244262.1. DR RefSeq; NP_036389.2; NM_012257.3. [O60381-1] DR RefSeq; XP_005250323.1; XM_005250266.2. [O60381-1] DR RefSeq; XP_005250324.1; XM_005250267.2. DR RefSeq; XP_016867456.1; XM_017011967.1. [O60381-1] DR PDB; 2E6O; NMR; -; A=424-503. DR PDB; 3QVE; X-ray; 2.04 A; A/B/C=206-342. DR PDBsum; 2E6O; -. DR PDBsum; 3QVE; -. DR AlphaFoldDB; O60381; -. DR SMR; O60381; -. DR BioGRID; 117927; 120. DR IntAct; O60381; 12. DR MINT; O60381; -. DR STRING; 9606.ENSP00000222574; -. DR GlyCosmos; O60381; 1 site, 1 glycan. DR GlyGen; O60381; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O60381; -. DR PhosphoSitePlus; O60381; -. DR BioMuta; HBP1; -. DR EPD; O60381; -. DR jPOST; O60381; -. DR MassIVE; O60381; -. DR MaxQB; O60381; -. DR PaxDb; 9606-ENSP00000222574; -. DR PeptideAtlas; O60381; -. DR ProteomicsDB; 49383; -. [O60381-1] DR ProteomicsDB; 49384; -. [O60381-2] DR ProteomicsDB; 49385; -. [O60381-3] DR Antibodypedia; 17158; 334 antibodies from 30 providers. DR DNASU; 26959; -. DR Ensembl; ENST00000222574.9; ENSP00000222574.4; ENSG00000105856.14. [O60381-1] DR Ensembl; ENST00000468410.5; ENSP00000420500.1; ENSG00000105856.14. [O60381-1] DR Ensembl; ENST00000485846.5; ENSP00000418738.1; ENSG00000105856.14. [O60381-1] DR Ensembl; ENST00000638303.2; ENSP00000491311.1; ENSG00000283847.2. [O60381-1] DR Ensembl; ENST00000638893.1; ENSP00000492167.1; ENSG00000283847.2. [O60381-1] DR Ensembl; ENST00000640195.1; ENSP00000492343.1; ENSG00000283847.2. [O60381-1] DR GeneID; 26959; -. DR KEGG; hsa:26959; -. DR MANE-Select; ENST00000222574.9; ENSP00000222574.4; NM_012257.4; NP_036389.2. DR UCSC; uc003vdy.3; human. [O60381-1] DR AGR; HGNC:23200; -. DR CTD; 26959; -. DR DisGeNET; 26959; -. DR GeneCards; HBP1; -. DR HGNC; HGNC:23200; HBP1. DR HPA; ENSG00000105856; Low tissue specificity. DR neXtProt; NX_O60381; -. DR OpenTargets; ENSG00000105856; -. DR PharmGKB; PA134901346; -. DR VEuPathDB; HostDB:ENSG00000105856; -. DR eggNOG; ENOG502QR1P; Eukaryota. DR GeneTree; ENSGT00390000011239; -. DR HOGENOM; CLU_041151_0_0_1; -. DR InParanoid; O60381; -. DR OMA; CDDSTVF; -. DR OrthoDB; 2882425at2759; -. DR PhylomeDB; O60381; -. DR TreeFam; TF105381; -. DR PathwayCommons; O60381; -. DR SignaLink; O60381; -. DR SIGNOR; O60381; -. DR BioGRID-ORCS; 26959; 11 hits in 1178 CRISPR screens. DR ChiTaRS; HBP1; human. DR EvolutionaryTrace; O60381; -. DR GeneWiki; HBP1; -. DR GenomeRNAi; 26959; -. DR Pharos; O60381; Tbio. DR PRO; PR:O60381; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O60381; Protein. DR Bgee; ENSG00000105856; Expressed in calcaneal tendon and 122 other cell types or tissues. DR ExpressionAtlas; O60381; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA: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; IBA:GO_Central. DR GO; GO:0051726; P:regulation of cell cycle; 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. DR Genevisible; O60381; HS. 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..514 FT /note="HMG box-containing protein 1" FT /id="PRO_0000048546" FT DOMAIN 203..345 FT /note="AXH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496" FT DNA_BIND 434..502 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 164..182 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 463..514 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014655" FT VAR_SEQ 510..514 FT /note="GSQQH -> VCFNK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10958660" FT /id="VSP_014656" FT CONFLICT 127 FT /note="Q -> L (in Ref. 5; AAH22329)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="S -> P (in Ref. 5; AAH22329)" FT /evidence="ECO:0000305" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:3QVE" FT HELIX 234..240 FT /evidence="ECO:0007829|PDB:3QVE" FT TURN 253..260 FT /evidence="ECO:0007829|PDB:3QVE" FT STRAND 262..272 FT /evidence="ECO:0007829|PDB:3QVE" FT STRAND 275..283 FT /evidence="ECO:0007829|PDB:3QVE" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:3QVE" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:3QVE" FT STRAND 301..304 FT /evidence="ECO:0007829|PDB:3QVE" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:3QVE" FT STRAND 308..313 FT /evidence="ECO:0007829|PDB:3QVE" FT HELIX 314..321 FT /evidence="ECO:0007829|PDB:3QVE" FT HELIX 440..447 FT /evidence="ECO:0007829|PDB:2E6O" FT HELIX 449..455 FT /evidence="ECO:0007829|PDB:2E6O" FT HELIX 461..474 FT /evidence="ECO:0007829|PDB:2E6O" FT HELIX 477..497 FT /evidence="ECO:0007829|PDB:2E6O" SQ SEQUENCE 514 AA; 57645 MW; 2AFADC995F73A031 CRC64; MVWEVKTNQM PNAVQKLLLV MDKRASGMND SLELLQCNEN LPSSPGYNSC DEHMELDDLP ELQAVQSDPT QSGMYQLSSD VSHQEYPRSS WNQNTSDIPE TTYRENEVDW LTELANIATS PQSPLMQCSF YNRSSPVHII ATSKSLHSYA RPPPVSSSSK SEPAFPHHHW KEETPVRHER ANSESESGIF CMSSLSDDDD LGWCNSWPST VWHCFLKGTR LCFHKGSNKE WQDVEDFARA EGCDNEEDLQ MGIHKGYGSD GLKLLSHEES VSFGESVLKL TFDPGTVEDG LLTVECKLDH PFYVKNKGWS SFYPSLTVVQ HGIPCCEVHI GDVCLPPGHP DAINFDDSGV FDTFKSYDFT PMDSSAVYVL SSMARQRRAS LSCGGPGGQD FARSGFSKNC GSPGSSQLSS NSLYAKAVKN HSSGTVSATS PNKCKRPMNA FMLFAKKYRV EYTQMYPGKD NRAISVILGD RWKKMKNEER RMYTLEAKAL AEEQKRLNPD CWKRKRTNSG SQQH //