HSBP1_HUMAN
ID HSBP1_HUMAN Reviewed; 76 AA.
AC O75506; Q53XA8; Q7Z5Z3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Heat shock factor-binding protein 1;
DE AltName: Full=Nasopharyngeal carcinoma-associated antigen 13;
DE Short=NPC-A-13;
GN Name=HSBP1; Synonyms=HSF1BP;
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], AND MUTAGENESIS.
RX PubMed=9649501; DOI=10.1101/gad.12.13.1962;
RA Satyal S.H., Chen D., Fox S.G., Kramer J.M., Morimoto R.I.;
RT "Negative regulation of the heat shock transcriptional response by HSBP1.";
RL Genes Dev. 12:1962-1974(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shu J., Li G., He X.;
RT "Construction of cDNA expression library from nasopharyngeal carcinoma
RT tissue and screening of antigenic genes.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-53 OF MUTANT ILE-31 AND PRO-56,
RP AND SUBUNIT.
RX PubMed=18767159; DOI=10.1002/prot.22216;
RA Liu X., Xu L., Liu Y., Tong X., Zhu G., Zhang X.C., Li X., Rao Z.;
RT "Crystal structure of the hexamer of human heat shock factor binding
RT protein 1.";
RL Proteins 75:1-11(2009).
CC -!- FUNCTION: Negative regulator of the heat shock response. Negatively
CC affects HSF1 DNA-binding activity. May have a role in the suppression
CC of the activation of the stress response during the aging process.
CC -!- SUBUNIT: Homohexamer. Associates with heptad repeats of HSF1 trimers
CC and probably also HSF1 monomers, and with HSP70. Association with HSF1
CC trimers and HSP70 coincides with attenuation of heat shock response and
CC the conversion of HSF1 trimer to monomer.
CC {ECO:0000269|PubMed:18767159}.
CC -!- INTERACTION:
CC O75506; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-748664, EBI-465861;
CC O75506; Q8WUW1: BRK1; NbExp=6; IntAct=EBI-748664, EBI-2837444;
CC O75506; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-748664, EBI-10175300;
CC O75506; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-748664, EBI-3867333;
CC O75506; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-748664, EBI-739467;
CC O75506; O75506: HSBP1; NbExp=4; IntAct=EBI-748664, EBI-748664;
CC O75506; Q5T5P2-6: KIAA1217; NbExp=5; IntAct=EBI-748664, EBI-10188326;
CC O75506; Q9BVG8: KIFC3; NbExp=5; IntAct=EBI-748664, EBI-2125614;
CC O75506; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-748664, EBI-14069005;
CC O75506; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-748664, EBI-11959885;
CC O75506; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-748664, EBI-10172290;
CC O75506; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-748664, EBI-10172052;
CC O75506; Q8TBB1: LNX1; NbExp=10; IntAct=EBI-748664, EBI-739832;
CC O75506; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-748664, EBI-2514004;
CC O75506; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-748664, EBI-945833;
CC O75506; O00560: SDCBP; NbExp=8; IntAct=EBI-748664, EBI-727004;
CC O75506; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-748664, EBI-742426;
CC O75506; Q9Y3C0: WASHC3; NbExp=13; IntAct=EBI-748664, EBI-712969;
CC O75506; P24278: ZBTB25; NbExp=3; IntAct=EBI-748664, EBI-739899;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the HSBP1 family. {ECO:0000305}.
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DR EMBL; AF068754; AAC25186.1; -; mRNA.
DR EMBL; AY320409; AAP73809.1; -; mRNA.
DR EMBL; BX537440; CAD97682.1; -; mRNA.
DR EMBL; BC007515; AAH07515.1; -; mRNA.
DR CCDS; CCDS45534.1; -.
DR RefSeq; NP_001528.1; NM_001537.3.
DR PDB; 3CI9; X-ray; 1.80 A; A/B=6-53.
DR PDBsum; 3CI9; -.
DR AlphaFoldDB; O75506; -.
DR SMR; O75506; -.
DR BioGRID; 109515; 57.
DR IntAct; O75506; 31.
DR STRING; 9606.ENSP00000392896; -.
DR GlyGen; O75506; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O75506; -.
DR MetOSite; O75506; -.
DR PhosphoSitePlus; O75506; -.
DR BioMuta; HSBP1; -.
DR EPD; O75506; -.
DR jPOST; O75506; -.
DR MassIVE; O75506; -.
DR MaxQB; O75506; -.
DR PaxDb; O75506; -.
DR PeptideAtlas; O75506; -.
DR PRIDE; O75506; -.
DR ProteomicsDB; 50056; -.
DR TopDownProteomics; O75506; -.
DR Antibodypedia; 30517; 114 antibodies from 23 providers.
DR DNASU; 3281; -.
DR Ensembl; ENST00000433866.7; ENSP00000392896.2; ENSG00000230989.8.
DR Ensembl; ENST00000570259.1; ENSP00000458007.1; ENSG00000230989.8.
DR GeneID; 3281; -.
DR KEGG; hsa:3281; -.
DR MANE-Select; ENST00000433866.7; ENSP00000392896.2; NM_001537.4; NP_001528.1.
DR UCSC; uc002fgy.3; human.
DR CTD; 3281; -.
DR DisGeNET; 3281; -.
DR GeneCards; HSBP1; -.
DR HGNC; HGNC:5203; HSBP1.
DR HPA; ENSG00000230989; Low tissue specificity.
DR MIM; 604553; gene.
DR neXtProt; NX_O75506; -.
DR OpenTargets; ENSG00000230989; -.
DR PharmGKB; PA29475; -.
DR VEuPathDB; HostDB:ENSG00000230989; -.
DR eggNOG; KOG4117; Eukaryota.
DR GeneTree; ENSGT00390000006293; -.
DR HOGENOM; CLU_149552_2_0_1; -.
DR InParanoid; O75506; -.
DR OMA; VDPKNMQ; -.
DR OrthoDB; 1576489at2759; -.
DR PhylomeDB; O75506; -.
DR TreeFam; TF314005; -.
DR PathwayCommons; O75506; -.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR SignaLink; O75506; -.
DR SIGNOR; O75506; -.
DR BioGRID-ORCS; 3281; 103 hits in 1086 CRISPR screens.
DR ChiTaRS; HSBP1; human.
DR EvolutionaryTrace; O75506; -.
DR GenomeRNAi; 3281; -.
DR Pharos; O75506; Tbio.
DR PRO; PR:O75506; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75506; protein.
DR Bgee; ENSG00000230989; Expressed in oral cavity and 216 other tissues.
DR ExpressionAtlas; O75506; baseline and differential.
DR Genevisible; O75506; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:ARUK-UCL.
DR GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR DisProt; DP01643; -.
DR InterPro; IPR009643; HS1-bd.
DR PANTHER; PTHR19424; PTHR19424; 1.
DR Pfam; PF06825; HSBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome.
FT CHAIN 1..76
FT /note="Heat shock factor-binding protein 1"
FT /id="PRO_0000124805"
FT MUTAGEN 16
FT /note="V->K: Loss of interaction with HSF1; in association
FT with K-19."
FT /evidence="ECO:0000269|PubMed:9649501"
FT MUTAGEN 19
FT /note="L->K: Loss of interaction with HSF1; in association
FT with K-16."
FT /evidence="ECO:0000269|PubMed:9649501"
FT MUTAGEN 45
FT /note="I->K: Loss of interaction with HSF1; in association
FT with K-48."
FT /evidence="ECO:0000269|PubMed:9649501"
FT MUTAGEN 48
FT /note="L->K: Loss of interaction with HSF1; in association
FT with K-45."
FT /evidence="ECO:0000269|PubMed:9649501"
FT CONFLICT 31
FT /note="S -> A (in Ref. 2; AAP73809)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> V (in Ref. 2; AAP73809)"
FT /evidence="ECO:0000305"
FT HELIX 9..46
FT /evidence="ECO:0007829|PDB:3CI9"
SQ SEQUENCE 76 AA; 8544 MW; 9838423C86B2D402 CRC64;
MAETDPKTVQ DLTSVVQTLL QQMQDKFQTM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG
VEELESENKI PATQKS
