HBP1_HUMAN
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 03-AUG-2022, entry version 168.
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="http://atlasgeneticsoncology.org/Genes/HBP1ID40791ch7q22.html";
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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. [O60381-1]
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 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; O60381; -.
DR PeptideAtlas; O60381; -.
DR PRIDE; O60381; -.
DR ProteomicsDB; 49383; -. [O60381-1]
DR ProteomicsDB; 49384; -. [O60381-2]
DR ProteomicsDB; 49385; -. [O60381-3]
DR Antibodypedia; 17158; 304 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 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; SPNTNWL; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; O60381; -.
DR TreeFam; TF105381; -.
DR PathwayCommons; O60381; -.
DR SignaLink; O60381; -.
DR SIGNOR; O60381; -.
DR BioGRID-ORCS; 26959; 10 hits in 1100 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 120 other tissues.
DR ExpressionAtlas; O60381; baseline and differential.
DR Genevisible; O60381; HS.
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 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 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
