ID DNJB1_MOUSE Reviewed; 340 AA.
AC Q9QYJ3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=DnaJ homolog subfamily B member 1;
DE AltName: Full=Heat shock 40 kDa protein 1;
DE Short=HSP40;
DE Short=Heat shock protein 40;
GN Name=Dnajb1; Synonyms=Hsp40, Hspf1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver, and Testis;
RX PubMed=11092732; DOI=10.3109/10425170009033235;
RA Hata M., Ohtsuka K.;
RT "Cloning and expression of murine Hsp40 gene: differences in initiation
RT sites between heat-induced and constitutive transcripts.";
RL DNA Seq. 11:213-223(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary 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, Brown adipose tissue, Kidney, Lung, Spleen, 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: Interacts with HSP70 and can stimulate its ATPase activity.
CC Stimulates the association between HSC70 and HIP. Negatively regulates
CC heat shock-induced HSF1 transcriptional activity during the attenuation
CC and recovery phase period of the heat shock response. Stimulates ATP
CC hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B
CC (in vitro). {ECO:0000250|UniProtKB:P25685}.
CC -!- SUBUNIT: Interacts with DNAJC3. Interacts with HSF1 (via
CC transactivation domain); this interaction results in the inhibition of
CC heat shock- and HSF1-induced transcriptional activity during the
CC attenuation and recovery phase period of the heat shock response.
CC {ECO:0000250|UniProtKB:P25685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25685}. Nucleus
CC {ECO:0000250|UniProtKB:P25685}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P25685}. Note=Translocates rapidly from the
CC cytoplasm to the nucleus, and especially to the nucleoli, upon heat
CC shock. {ECO:0000250|UniProtKB:P25685}.
CC -!- INDUCTION: By heat shock. {ECO:0000250}.
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; AB028272; BAA88083.1; -; mRNA.
DR EMBL; AB028273; BAA95672.1; -; Genomic_DNA.
DR EMBL; BC012962; AAH12962.1; -; mRNA.
DR CCDS; CCDS22456.1; -.
DR RefSeq; NP_061278.1; NM_018808.3.
DR AlphaFoldDB; Q9QYJ3; -.
DR SMR; Q9QYJ3; -.
DR BioGRID; 219875; 25.
DR IntAct; Q9QYJ3; 1.
DR STRING; 10090.ENSMUSP00000005620; -.
DR GlyGen; Q9QYJ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9QYJ3; -.
DR PhosphoSitePlus; Q9QYJ3; -.
DR EPD; Q9QYJ3; -.
DR MaxQB; Q9QYJ3; -.
DR PaxDb; 10090-ENSMUSP00000005620; -.
DR ProteomicsDB; 277478; -.
DR Pumba; Q9QYJ3; -.
DR Antibodypedia; 26735; 934 antibodies from 41 providers.
DR DNASU; 81489; -.
DR Ensembl; ENSMUST00000005620.10; ENSMUSP00000005620.9; ENSMUSG00000005483.11.
DR GeneID; 81489; -.
DR KEGG; mmu:81489; -.
DR UCSC; uc009mkp.2; mouse.
DR AGR; MGI:1931874; -.
DR CTD; 3337; -.
DR MGI; MGI:1931874; Dnajb1.
DR VEuPathDB; HostDB:ENSMUSG00000005483; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000160312; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q9QYJ3; -.
DR OMA; PRDIFAQ; -.
DR OrthoDB; 2785358at2759; -.
DR PhylomeDB; Q9QYJ3; -.
DR TreeFam; TF105141; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR BioGRID-ORCS; 81489; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Dnajb1; mouse.
DR PRO; PR:Q9QYJ3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9QYJ3; Protein.
DR Bgee; ENSMUSG00000005483; Expressed in seminiferous tubule of testis and 263 other cell types or tissues.
DR ExpressionAtlas; Q9QYJ3; baseline and differential.
DR Genevisible; Q9QYJ3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0061827; C:sperm head; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISO:MGI.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IGI:MGI.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR24078:SF568; DNAJ HOMOLOG SUBFAMILY B MEMBER 1; 1.
DR PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..340
FT /note="DnaJ homolog subfamily B member 1"
FT /id="PRO_0000071017"
FT DOMAIN 2..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25685"
SQ SEQUENCE 340 AA; 38167 MW; F775BFBA4A5D324E CRC64;
MGKDYYQTLG LARGASDDEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK
REIFDRYGEE GLKGGSPSGG SSGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN
GEEGMDIDDT FSSFPMGMGG FTNMNFGRSR PSQEPTRKKQ DPPVTHDLRV SLEEIYSGCT
KKMKISHKRL NPDGKSIRNE DKILTIEVKR GWKEGTKITF PKEGDQTSNN IPADIVFVLK
DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE
GLPLPKTPEK RGDLVIEFEV IFPERIPVSS RTILEQVLPI
//
