DNJB1_HUMAN
ID DNJB1_HUMAN Reviewed; 340 AA.
AC P25685; B4DX52;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=DnaJ homolog subfamily B member 1;
DE AltName: Full=DnaJ protein homolog 1;
DE AltName: Full=Heat shock 40 kDa protein 1;
DE Short=HSP40;
DE Short=Heat shock protein 40;
DE AltName: Full=Human DnaJ protein 1;
DE Short=hDj-1;
GN Name=DNAJB1; Synonyms=DNAJ1, HDJ1, HSPF1;
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 1).
RC TISSUE=Placenta;
RX PubMed=1754405; DOI=10.1093/nar/19.23.6645;
RA Raabe T., Manley J.L.;
RT "A human homologue of the Escherichia coli DnaJ heat-shock protein.";
RL Nucleic Acids Res. 19:6645-6645(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 2-48.
RC TISSUE=Placenta;
RX PubMed=8250930; DOI=10.1006/bbrc.1993.2466;
RA Ohtsuka K.;
RT "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of
RT bacterial DnaJ.";
RL Biochem. Biophys. Res. Commun. 197:235-240(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8975727; DOI=10.1006/geno.1996.0653;
RA Hata M., Okumura K., Seto M., Ohtsuka K.;
RT "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and
RT its chromosomal localization to 19p13.2.";
RL Genomics 38:446-449(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [7]
RP PROTEIN SEQUENCE OF 2-49, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1586970; DOI=10.1247/csf.17.77;
RA Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T.,
RA Tanabe K., Ohtsuka K.;
RT "Intracellular localization and partial amino acid sequence of a stress-
RT inducible 40-kDa protein in HeLa cells.";
RL Cell Struct. Funct. 17:77-86(1992).
RN [8]
RP FUNCTION, AND INTERACTION WITH HSF1.
RX PubMed=9499401; DOI=10.1101/gad.12.5.654;
RA Shi Y., Mosser D.D., Morimoto R.I.;
RT "Molecular chaperones as HSF1-specific transcriptional repressors.";
RL Genes Dev. 12:654-666(1998).
RN [9]
RP INTERACTION WITH DNAJC3.
RX PubMed=9920933; DOI=10.1074/jbc.274.6.3797;
RA Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.;
RT "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an
RT influenza virus-activated co-chaperone that modulates heat shock protein 70
RT activity.";
RL J. Biol. Chem. 274:3797-3803(1999).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP FUNCTION.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [14]
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 [15]
RP STRUCTURE BY NMR OF 1-76.
RX PubMed=8764402; DOI=10.1006/jmbi.1996.0394;
RA Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.;
RT "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1)
RT J-domain.";
RL J. Mol. Biol. 260:224-235(1996).
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 (PubMed:9499401).
CC Stimulates ATP hydrolysis and the folding of unfolded proteins mediated
CC by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877,
CC ECO:0000269|PubMed:9499401}.
CC -!- SUBUNIT: Interacts with DNAJC3 (PubMed:9920933). Interacts with HSF1
CC (via transactivation domain); this interaction results in the
CC inhibition of heat shock- and HSF1-induced transcriptional activity
CC during the attenuation and recovery phase period of the heat shock
CC response (PubMed:9499401). {ECO:0000269|PubMed:9499401,
CC ECO:0000269|PubMed:9920933}.
CC -!- INTERACTION:
CC P25685; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-357034, EBI-618189;
CC P25685; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-357034, EBI-9088619;
CC P25685; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-357034, EBI-9091052;
CC P25685; O60907-2: TBL1X; NbExp=3; IntAct=EBI-357034, EBI-15904933;
CC P25685; P54274: TERF1; NbExp=2; IntAct=EBI-357034, EBI-710997;
CC P25685; Q03403: TFF2; NbExp=3; IntAct=EBI-357034, EBI-4314702;
CC P25685; Q14166: TTLL12; NbExp=4; IntAct=EBI-357034, EBI-923010;
CC P25685; P13051-2: UNG; NbExp=3; IntAct=EBI-357034, EBI-25834258;
CC P25685; P19544-6: WT1; NbExp=3; IntAct=EBI-357034, EBI-11745701;
CC P25685; Q62392: Phlda1; Xeno; NbExp=2; IntAct=EBI-357034, EBI-309727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1586970}. Nucleus
CC {ECO:0000269|PubMed:1586970}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:1586970}. Note=Translocates rapidly from the
CC cytoplasm to the nucleus, and especially to the nucleoli, upon heat
CC shock.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25685-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25685-2; Sequence=VSP_056414;
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:1586970}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44287.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X62421; CAA44287.1; ALT_FRAME; mRNA.
DR EMBL; D49547; BAA08495.1; -; mRNA.
DR EMBL; D85429; BAA12819.1; -; Genomic_DNA.
DR EMBL; AK301817; BAG63264.1; -; mRNA.
DR EMBL; AC009004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002352; AAH02352.1; -; mRNA.
DR EMBL; BC019827; AAH19827.1; -; mRNA.
DR CCDS; CCDS12312.1; -. [P25685-1]
DR CCDS; CCDS74295.1; -. [P25685-2]
DR PIR; JN0912; JN0912.
DR PIR; S20062; S20062.
DR RefSeq; NP_001287843.1; NM_001300914.1. [P25685-2]
DR RefSeq; NP_001300893.1; NM_001313964.1. [P25685-2]
DR RefSeq; NP_006136.1; NM_006145.2. [P25685-1]
DR RefSeq; XP_006722796.1; XM_006722733.1. [P25685-2]
DR RefSeq; XP_006722797.1; XM_006722734.3. [P25685-2]
DR RefSeq; XP_011526258.1; XM_011527956.2. [P25685-2]
DR PDB; 1HDJ; NMR; -; A=1-76.
DR PDB; 2QLD; X-ray; 2.70 A; A=158-340.
DR PDB; 3AGX; X-ray; 1.85 A; A/B=161-340.
DR PDB; 3AGY; X-ray; 1.85 A; A/B=161-340.
DR PDB; 3AGZ; X-ray; 2.51 A; A/B=151-340.
DR PDB; 4WB7; X-ray; 1.90 A; A/B=2-70.
DR PDB; 6BYR; X-ray; 3.66 A; A/C=2-70.
DR PDB; 6WJF; EM; 7.50 A; A/B=2-70.
DR PDB; 6WJG; EM; 6.20 A; A/B=2-70.
DR PDB; 6Z5N; NMR; -; A=1-110.
DR PDB; 7NDX; X-ray; 2.54 A; A=157-340.
DR PDBsum; 1HDJ; -.
DR PDBsum; 2QLD; -.
DR PDBsum; 3AGX; -.
DR PDBsum; 3AGY; -.
DR PDBsum; 3AGZ; -.
DR PDBsum; 4WB7; -.
DR PDBsum; 6BYR; -.
DR PDBsum; 6WJF; -.
DR PDBsum; 6WJG; -.
DR PDBsum; 6Z5N; -.
DR PDBsum; 7NDX; -.
DR AlphaFoldDB; P25685; -.
DR SMR; P25685; -.
DR BioGRID; 109569; 231.
DR CORUM; P25685; -.
DR DIP; DIP-41180N; -.
DR IntAct; P25685; 105.
DR MINT; P25685; -.
DR STRING; 9606.ENSP00000254322; -.
DR GlyGen; P25685; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P25685; -.
DR PhosphoSitePlus; P25685; -.
DR BioMuta; DNAJB1; -.
DR DMDM; 1706473; -.
DR REPRODUCTION-2DPAGE; IPI00015947; -.
DR EPD; P25685; -.
DR jPOST; P25685; -.
DR MassIVE; P25685; -.
DR MaxQB; P25685; -.
DR PaxDb; P25685; -.
DR PeptideAtlas; P25685; -.
DR PRIDE; P25685; -.
DR ProteomicsDB; 5411; -.
DR ProteomicsDB; 54280; -. [P25685-1]
DR Antibodypedia; 26735; 864 antibodies from 41 providers.
DR DNASU; 3337; -.
DR Ensembl; ENST00000254322.3; ENSP00000254322.1; ENSG00000132002.9. [P25685-1]
DR Ensembl; ENST00000396969.8; ENSP00000444212.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000594099.6; ENSP00000470460.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000595992.6; ENSP00000470596.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000596075.2; ENSP00000471603.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000596853.6; ENSP00000470063.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000598235.2; ENSP00000471073.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000598692.2; ENSP00000472886.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000601533.6; ENSP00000471798.2; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000676515.1; ENSP00000504619.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000676982.1; ENSP00000504186.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000677204.1; ENSP00000503027.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000677762.1; ENSP00000503810.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000678009.1; ENSP00000504352.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000678098.1; ENSP00000503271.1; ENSG00000132002.9. [P25685-2]
DR Ensembl; ENST00000679223.1; ENSP00000504527.1; ENSG00000132002.9. [P25685-2]
DR GeneID; 3337; -.
DR KEGG; hsa:3337; -.
DR MANE-Select; ENST00000254322.3; ENSP00000254322.1; NM_006145.3; NP_006136.1.
DR UCSC; uc010xnr.2; human. [P25685-1]
DR CTD; 3337; -.
DR DisGeNET; 3337; -.
DR GeneCards; DNAJB1; -.
DR HGNC; HGNC:5270; DNAJB1.
DR HPA; ENSG00000132002; Tissue enhanced (brain).
DR MalaCards; DNAJB1; -.
DR MIM; 604572; gene.
DR neXtProt; NX_P25685; -.
DR OpenTargets; ENSG00000132002; -.
DR Orphanet; 401920; Fibrolamellar hepatocellular carcinoma.
DR PharmGKB; PA27412; -.
DR VEuPathDB; HostDB:ENSG00000132002; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000160312; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; P25685; -.
DR OMA; KNNDLHQ; -.
DR PhylomeDB; P25685; -.
DR TreeFam; TF105141; -.
DR PathwayCommons; P25685; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR SignaLink; P25685; -.
DR SIGNOR; P25685; -.
DR BioGRID-ORCS; 3337; 30 hits in 1043 CRISPR screens.
DR ChiTaRS; DNAJB1; human.
DR EvolutionaryTrace; P25685; -.
DR GeneWiki; DNAJB1; -.
DR GenomeRNAi; 3337; -.
DR Pharos; P25685; Tbio.
DR PRO; PR:P25685; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P25685; protein.
DR Bgee; ENSG00000132002; Expressed in lower esophagus mucosa and 207 other tissues.
DR ExpressionAtlas; P25685; baseline and differential.
DR Genevisible; P25685; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR IDEAL; IID00446; -.
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 Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1586970,
FT ECO:0000269|PubMed:8250930"
FT CHAIN 2..340
FT /note="DnaJ homolog subfamily B member 1"
FT /id="PRO_0000071016"
FT DOMAIN 2..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056414"
FT CONFLICT 68
FT /note="G -> L (in Ref. 1; CAA44287)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="R -> C (in Ref. 1; CAA44287)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="M -> T (in Ref. 1; CAA44287)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> A (in Ref. 1; CAA44287)"
FT /evidence="ECO:0000305"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:4WB7"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:4WB7"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4WB7"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:4WB7"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4WB7"
FT TURN 77..87
FT /evidence="ECO:0007829|PDB:6Z5N"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:6Z5N"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:3AGX"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 179..190
FT /evidence="ECO:0007829|PDB:3AGX"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2QLD"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:3AGX"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3AGX"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:3AGX"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:3AGX"
SQ SEQUENCE 340 AA; 38044 MW; 17545098B0C196DF CRC64;
MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK
REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN
GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT
KKMKISHKRL NPDGKSIRNE DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK
DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI
