ID   HSBP1_MOUSE             Reviewed;          76 AA.
AC   Q9CQZ1; Q3UKN1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Heat shock factor-binding protein 1;
GN   Name=Hsbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Liver, Pancreas, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By
CC       similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HSBP1 family. {ECO:0000305}.
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; AK010939; BAB27281.1; -; mRNA.
DR   EMBL; AK018708; BAB31359.1; -; mRNA.
DR   EMBL; AK050550; BAC34319.1; -; mRNA.
DR   EMBL; AK078498; BAC37310.1; -; mRNA.
DR   EMBL; AK145940; BAE26770.1; -; mRNA.
DR   EMBL; BC002153; AAH02153.1; -; mRNA.
DR   CCDS; CCDS40492.1; -.
DR   RefSeq; NP_077181.1; NM_024219.1.
DR   AlphaFoldDB; Q9CQZ1; -.
DR   SMR; Q9CQZ1; -.
DR   BioGRID; 212721; 6.
DR   IntAct; Q9CQZ1; 1.
DR   STRING; 10090.ENSMUSP00000034300; -.
DR   iPTMnet; Q9CQZ1; -.
DR   PhosphoSitePlus; Q9CQZ1; -.
DR   EPD; Q9CQZ1; -.
DR   jPOST; Q9CQZ1; -.
DR   MaxQB; Q9CQZ1; -.
DR   PaxDb; Q9CQZ1; -.
DR   PeptideAtlas; Q9CQZ1; -.
DR   PRIDE; Q9CQZ1; -.
DR   ProteomicsDB; 267167; -.
DR   TopDownProteomics; Q9CQZ1; -.
DR   Antibodypedia; 30517; 114 antibodies from 23 providers.
DR   DNASU; 68196; -.
DR   Ensembl; ENSMUST00000034300; ENSMUSP00000034300; ENSMUSG00000031839.
DR   Ensembl; ENSMUST00000212468; ENSMUSP00000148390; ENSMUSG00000031839.
DR   GeneID; 68196; -.
DR   KEGG; mmu:68196; -.
DR   UCSC; uc009npm.1; mouse.
DR   CTD; 3281; -.
DR   MGI; MGI:1915446; Hsbp1.
DR   VEuPathDB; HostDB:ENSMUSG00000031839; -.
DR   eggNOG; KOG4117; Eukaryota.
DR   GeneTree; ENSGT00390000006293; -.
DR   HOGENOM; CLU_149552_2_0_1; -.
DR   InParanoid; Q9CQZ1; -.
DR   OMA; VDPKNMQ; -.
DR   OrthoDB; 1576489at2759; -.
DR   PhylomeDB; Q9CQZ1; -.
DR   TreeFam; TF314005; -.
DR   Reactome; R-MMU-3371568; Attenuation phase.
DR   Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR   BioGRID-ORCS; 68196; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Hsbp1; mouse.
DR   PRO; PR:Q9CQZ1; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9CQZ1; protein.
DR   Bgee; ENSMUSG00000031839; Expressed in seminiferous tubule of testis and 266 other tissues.
DR   Genevisible; Q9CQZ1; MM.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; ISO:MGI.
DR   GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR   GO; GO:0035987; P:endodermal cell differentiation; IMP:MGI.
DR   GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR   InterPro; IPR009643; HS1-bd.
DR   PANTHER; PTHR19424; PTHR19424; 1.
DR   Pfam; PF06825; HSBP1; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..76
FT                   /note="Heat shock factor-binding protein 1"
FT                   /id="PRO_0000124806"
SQ   SEQUENCE   76 AA;  8611 MW;  3E86CA4988E2CB56 CRC64;
     MAETDPKTMQ DITLVVETLL QQMQDKFQIM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG
     VEELDPENKI PTAQKS