Full text data of DNAJB1
DNAJB1
(DNAJ1, HDJ1, HSPF1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
DnaJ homolog subfamily B member 1 (DnaJ protein homolog 1; Heat shock 40 kDa protein 1; HSP40; Heat shock protein 40; Human DnaJ protein 1; hDj-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DnaJ homolog subfamily B member 1 (DnaJ protein homolog 1; Heat shock 40 kDa protein 1; HSP40; Heat shock protein 40; Human DnaJ protein 1; hDj-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P25685
ID DNJB1_HUMAN Reviewed; 340 AA.
AC P25685;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 147.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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], 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)
RT and its chromosomal localization to 19p13.2.";
RL Genomics 38:446-449(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-49, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1586970;
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
RT stress-inducible 40-kDa protein in HeLa cells.";
RL Cell Struct. Funct. 17:77-86(1992).
RN [6]
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.,
RA 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
RT protein 70 activity.";
RL J. Biol. Chem. 274:3797-3803(1999).
RN [7]
RP INTERACTION WITH SRPK1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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
RT (HDJ-1) J-domain.";
RL J. Mol. Biol. 260:224-235(1996).
CC -!- FUNCTION: Interacts with HSP70 and can stimulate its ATPase
CC activity. Stimulates the association between HSC70 and HIP.
CC -!- SUBUNIT: Interacts with DNAJC3. Interacts with SRPK1.
CC -!- INTERACTION:
CC Q62392:Phlda1 (xeno); NbExp=2; IntAct=EBI-357034, EBI-309727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Translocates rapidly from the cytoplasm to the nucleus, and
CC especially to the nucleoli, upon heat shock.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44287.1; Type=Frameshift; Positions=11, 28, 81, 136;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X62421; CAA44287.1; ALT_FRAME; mRNA.
DR EMBL; D49547; BAA08495.1; -; mRNA.
DR EMBL; D85429; BAA12819.1; -; Genomic_DNA.
DR EMBL; BC002352; AAH02352.1; -; mRNA.
DR EMBL; BC019827; AAH19827.1; -; mRNA.
DR PIR; JN0912; JN0912.
DR PIR; S20062; S20062.
DR RefSeq; NP_006136.1; NM_006145.1.
DR UniGene; Hs.515210; -.
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 PDBsum; 1HDJ; -.
DR PDBsum; 2QLD; -.
DR PDBsum; 3AGX; -.
DR PDBsum; 3AGY; -.
DR PDBsum; 3AGZ; -.
DR ProteinModelPortal; P25685; -.
DR SMR; P25685; 1-76, 156-340.
DR DIP; DIP-41180N; -.
DR IntAct; P25685; 24.
DR MINT; MINT-204558; -.
DR STRING; 9606.ENSP00000254322; -.
DR PhosphoSite; P25685; -.
DR DMDM; 1706473; -.
DR REPRODUCTION-2DPAGE; IPI00015947; -.
DR PaxDb; P25685; -.
DR PeptideAtlas; P25685; -.
DR PRIDE; P25685; -.
DR DNASU; 3337; -.
DR Ensembl; ENST00000254322; ENSP00000254322; ENSG00000132002.
DR GeneID; 3337; -.
DR KEGG; hsa:3337; -.
DR UCSC; uc002myz.1; human.
DR CTD; 3337; -.
DR GeneCards; GC19M014625; -.
DR H-InvDB; HIX0014838; -.
DR HGNC; HGNC:5270; DNAJB1.
DR HPA; CAB017450; -.
DR MIM; 604572; gene.
DR neXtProt; NX_P25685; -.
DR PharmGKB; PA27412; -.
DR eggNOG; COG2214; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; P25685; -.
DR KO; K09507; -.
DR OMA; HSIFKRD; -.
DR OrthoDB; EOG7TF79F; -.
DR PhylomeDB; P25685; -.
DR ChiTaRS; DNAJB1; human.
DR EvolutionaryTrace; P25685; -.
DR GeneWiki; DNAJB1; -.
DR GenomeRNAi; 3337; -.
DR NextBio; 13208; -.
DR PRO; PR:P25685; -.
DR ArrayExpress; P25685; -.
DR Bgee; P25685; -.
DR CleanEx; HS_DNAJB1; -.
DR Genevestigator; P25685; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 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; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 DnaJ homolog subfamily B member 1.
FT /FTId=PRO_0000071016.
FT DOMAIN 2 70 J.
FT CONFLICT 68 68 G -> L (in Ref. 1; CAA44287).
FT CONFLICT 150 150 R -> C (in Ref. 1; CAA44287).
FT CONFLICT 183 183 M -> T (in Ref. 1; CAA44287).
FT CONFLICT 320 320 V -> A (in Ref. 1; CAA44287).
FT HELIX 6 9
FT HELIX 17 29
FT TURN 33 35
FT HELIX 41 54
FT HELIX 58 66
FT HELIX 69 71
FT STRAND 166 170
FT HELIX 172 177
FT STRAND 179 190
FT TURN 191 193
FT STRAND 197 208
FT STRAND 217 220
FT STRAND 228 230
FT STRAND 235 241
FT STRAND 248 250
FT STRAND 253 261
FT HELIX 262 267
FT STRAND 269 274
FT STRAND 280 285
FT STRAND 294 297
FT STRAND 305 307
FT STRAND 314 321
FT HELIX 328 337
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
//
ID DNJB1_HUMAN Reviewed; 340 AA.
AC P25685;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 147.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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], 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)
RT and its chromosomal localization to 19p13.2.";
RL Genomics 38:446-449(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-49, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1586970;
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
RT stress-inducible 40-kDa protein in HeLa cells.";
RL Cell Struct. Funct. 17:77-86(1992).
RN [6]
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.,
RA 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
RT protein 70 activity.";
RL J. Biol. Chem. 274:3797-3803(1999).
RN [7]
RP INTERACTION WITH SRPK1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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
RT (HDJ-1) J-domain.";
RL J. Mol. Biol. 260:224-235(1996).
CC -!- FUNCTION: Interacts with HSP70 and can stimulate its ATPase
CC activity. Stimulates the association between HSC70 and HIP.
CC -!- SUBUNIT: Interacts with DNAJC3. Interacts with SRPK1.
CC -!- INTERACTION:
CC Q62392:Phlda1 (xeno); NbExp=2; IntAct=EBI-357034, EBI-309727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Translocates rapidly from the cytoplasm to the nucleus, and
CC especially to the nucleoli, upon heat shock.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44287.1; Type=Frameshift; Positions=11, 28, 81, 136;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X62421; CAA44287.1; ALT_FRAME; mRNA.
DR EMBL; D49547; BAA08495.1; -; mRNA.
DR EMBL; D85429; BAA12819.1; -; Genomic_DNA.
DR EMBL; BC002352; AAH02352.1; -; mRNA.
DR EMBL; BC019827; AAH19827.1; -; mRNA.
DR PIR; JN0912; JN0912.
DR PIR; S20062; S20062.
DR RefSeq; NP_006136.1; NM_006145.1.
DR UniGene; Hs.515210; -.
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 PDBsum; 1HDJ; -.
DR PDBsum; 2QLD; -.
DR PDBsum; 3AGX; -.
DR PDBsum; 3AGY; -.
DR PDBsum; 3AGZ; -.
DR ProteinModelPortal; P25685; -.
DR SMR; P25685; 1-76, 156-340.
DR DIP; DIP-41180N; -.
DR IntAct; P25685; 24.
DR MINT; MINT-204558; -.
DR STRING; 9606.ENSP00000254322; -.
DR PhosphoSite; P25685; -.
DR DMDM; 1706473; -.
DR REPRODUCTION-2DPAGE; IPI00015947; -.
DR PaxDb; P25685; -.
DR PeptideAtlas; P25685; -.
DR PRIDE; P25685; -.
DR DNASU; 3337; -.
DR Ensembl; ENST00000254322; ENSP00000254322; ENSG00000132002.
DR GeneID; 3337; -.
DR KEGG; hsa:3337; -.
DR UCSC; uc002myz.1; human.
DR CTD; 3337; -.
DR GeneCards; GC19M014625; -.
DR H-InvDB; HIX0014838; -.
DR HGNC; HGNC:5270; DNAJB1.
DR HPA; CAB017450; -.
DR MIM; 604572; gene.
DR neXtProt; NX_P25685; -.
DR PharmGKB; PA27412; -.
DR eggNOG; COG2214; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; P25685; -.
DR KO; K09507; -.
DR OMA; HSIFKRD; -.
DR OrthoDB; EOG7TF79F; -.
DR PhylomeDB; P25685; -.
DR ChiTaRS; DNAJB1; human.
DR EvolutionaryTrace; P25685; -.
DR GeneWiki; DNAJB1; -.
DR GenomeRNAi; 3337; -.
DR NextBio; 13208; -.
DR PRO; PR:P25685; -.
DR ArrayExpress; P25685; -.
DR Bgee; P25685; -.
DR CleanEx; HS_DNAJB1; -.
DR Genevestigator; P25685; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 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; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 DnaJ homolog subfamily B member 1.
FT /FTId=PRO_0000071016.
FT DOMAIN 2 70 J.
FT CONFLICT 68 68 G -> L (in Ref. 1; CAA44287).
FT CONFLICT 150 150 R -> C (in Ref. 1; CAA44287).
FT CONFLICT 183 183 M -> T (in Ref. 1; CAA44287).
FT CONFLICT 320 320 V -> A (in Ref. 1; CAA44287).
FT HELIX 6 9
FT HELIX 17 29
FT TURN 33 35
FT HELIX 41 54
FT HELIX 58 66
FT HELIX 69 71
FT STRAND 166 170
FT HELIX 172 177
FT STRAND 179 190
FT TURN 191 193
FT STRAND 197 208
FT STRAND 217 220
FT STRAND 228 230
FT STRAND 235 241
FT STRAND 248 250
FT STRAND 253 261
FT HELIX 262 267
FT STRAND 269 274
FT STRAND 280 285
FT STRAND 294 297
FT STRAND 305 307
FT STRAND 314 321
FT HELIX 328 337
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
//
MIM
604572
*RECORD*
*FIELD* NO
604572
*FIELD* TI
*604572 DNAJ/HSP40 HOMOLOG, SUBFAMILY B, MEMBER 1; DNAJB1
;;HEAT-SHOCK 40-KD PROTEIN 1; HSPF1;;
read moreHDJ1
*FIELD* TX
CLONING
The E. coli heat-shock protein DnaJ functions together with DnaK
(HSPA1A; 140550) and GrpE (GRPEL1; 606173) as a molecular chaperone,
involving them in assembly and disassembly of protein complexes, protein
folding, renaturation of denatured proteins, prevention of protein
aggregation, and protein export. By screening a human placenta cDNA
library with anti-Hsp40 antibody, Ohtsuka (1993) isolated a cDNA
encoding a 40-kD heat-shock protein designated HSPF1. The deduced
340-amino acid HSPF1 protein is 34% identical to E. coli DnaJ and 34%
and 36% identical to HSJ1 (604139) and HSJ2 (602837), respectively. By
Northern blot analysis, Hata and Ohtsuka (1998) showed that expression
of a major 2.4-kb and a minor 1.4-kb HSPF1 transcript is drastically
induced by heat shock.
GENE STRUCTURE
Hata et al. (1996) determined that the HSPF1 gene spans over 7 kb and
contains 3 exons and 2 introns. The 5-prime region of the gene is highly
GC rich, and there are multiple basal elements for transcription
factors, including typical heat-shock elements (HSEs).
GENE FUNCTION
Hata and Ohtsuka (1998) found by gel mobility supershift assays that
HSF1 (140580) but not HSF2 (140581) interacts with the 8 exonic HSEs of
HSPF1. An intronic HSE in HSPF1 is inactive.
Several dominant human neurodegenerative diseases involve the expansion
of a polyglutamine within the disease proteins. This expansion confers
toxicity on the proteins and is associated with nuclear inclusion
formation. Data indicate that molecular chaperones can modulate
polyglutamine pathogenesis. To elucidate the basis of polyglutamine
toxicity and the mechanism by which chaperones suppress
neurodegeneration, Chan et al. (2000) studied transgenic Drosophila
disease models of Machado-Joseph disease (109150) and Huntington disease
(143100). They demonstrated that Hsp70 (see 140559) and Hdj1, the
Drosophila homolog to human HSP40 (see 604139), showed substrate
specificity for polyglutamine proteins as well as synergy in suppression
of neurotoxicity, and altered the solubility properties of the mutant
polyglutamine protein.
Using a Drosophila model for Huntington disease and other polyglutamine
diseases to screen for genetic factors modifying the degeneration caused
by expression of polyglutamine in the eye, Kazemi-Esfarjani and Benzer
(2000) isolated several suppressor strains, 2 of which led to the
discovery of suppressor genes. The predicted product of one is TPR2
(601964), which is homologous to the human tetratricopeptide repeat
protein-2. That of the second is HDJ1. The suppression of polyglutamine
toxicity was verified in transgenic flies.
MAPPING
By FISH, Hata et al. (1996) mapped the HSPF1 gene to chromosome 19p13.2.
*FIELD* RF
1. Chan, H. Y. E.; Warrick, J. M.; Gray-Board, G. L.; Paulson, H.
L.; Bonini, N. M.: Mechanisms of chaperone suppression of polyglutamine
disease: selectivity, synergy and modulation of protein solubility
in Drosophila. Hum. Molec. Genet. 9: 2811-2820, 2000.
2. Hata, M.; Ohtsuka, K.: Characterization of HSE sequences in human
Hsp40 gene: structural and promoter analysis. Biochim. Biophys. Acta 1397:
43-55, 1998.
3. Hata, M.; Okumura, K.; Seto, M.; Ohtsuka, K.: Genomic cloning
of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal
localization to 19p13.2. Genomics 38: 446-449, 1996.
4. Kazemi-Esfarjani, P.; Benzer, S.: Genetic suppression of polyglutamine
toxicity in Drosophila. Science 287: 1837-1840, 2000.
5. Ohtsuka, K.: Cloning of a cDNA for heat-shock protein Hsp40, a
human homologue of bacterial DnaJ. Biochem. Biophys. Res. Commun. 197:
235-240, 1993.
*FIELD* CN
George E. Tiller - updated: 2/5/2001
*FIELD* CD
Paul J. Converse: 2/18/2000
*FIELD* ED
carol: 08/17/2007
alopez: 11/20/2001
mgross: 8/3/2001
carol: 3/13/2001
cwells: 2/5/2001
carol: 2/18/2000
*RECORD*
*FIELD* NO
604572
*FIELD* TI
*604572 DNAJ/HSP40 HOMOLOG, SUBFAMILY B, MEMBER 1; DNAJB1
;;HEAT-SHOCK 40-KD PROTEIN 1; HSPF1;;
read moreHDJ1
*FIELD* TX
CLONING
The E. coli heat-shock protein DnaJ functions together with DnaK
(HSPA1A; 140550) and GrpE (GRPEL1; 606173) as a molecular chaperone,
involving them in assembly and disassembly of protein complexes, protein
folding, renaturation of denatured proteins, prevention of protein
aggregation, and protein export. By screening a human placenta cDNA
library with anti-Hsp40 antibody, Ohtsuka (1993) isolated a cDNA
encoding a 40-kD heat-shock protein designated HSPF1. The deduced
340-amino acid HSPF1 protein is 34% identical to E. coli DnaJ and 34%
and 36% identical to HSJ1 (604139) and HSJ2 (602837), respectively. By
Northern blot analysis, Hata and Ohtsuka (1998) showed that expression
of a major 2.4-kb and a minor 1.4-kb HSPF1 transcript is drastically
induced by heat shock.
GENE STRUCTURE
Hata et al. (1996) determined that the HSPF1 gene spans over 7 kb and
contains 3 exons and 2 introns. The 5-prime region of the gene is highly
GC rich, and there are multiple basal elements for transcription
factors, including typical heat-shock elements (HSEs).
GENE FUNCTION
Hata and Ohtsuka (1998) found by gel mobility supershift assays that
HSF1 (140580) but not HSF2 (140581) interacts with the 8 exonic HSEs of
HSPF1. An intronic HSE in HSPF1 is inactive.
Several dominant human neurodegenerative diseases involve the expansion
of a polyglutamine within the disease proteins. This expansion confers
toxicity on the proteins and is associated with nuclear inclusion
formation. Data indicate that molecular chaperones can modulate
polyglutamine pathogenesis. To elucidate the basis of polyglutamine
toxicity and the mechanism by which chaperones suppress
neurodegeneration, Chan et al. (2000) studied transgenic Drosophila
disease models of Machado-Joseph disease (109150) and Huntington disease
(143100). They demonstrated that Hsp70 (see 140559) and Hdj1, the
Drosophila homolog to human HSP40 (see 604139), showed substrate
specificity for polyglutamine proteins as well as synergy in suppression
of neurotoxicity, and altered the solubility properties of the mutant
polyglutamine protein.
Using a Drosophila model for Huntington disease and other polyglutamine
diseases to screen for genetic factors modifying the degeneration caused
by expression of polyglutamine in the eye, Kazemi-Esfarjani and Benzer
(2000) isolated several suppressor strains, 2 of which led to the
discovery of suppressor genes. The predicted product of one is TPR2
(601964), which is homologous to the human tetratricopeptide repeat
protein-2. That of the second is HDJ1. The suppression of polyglutamine
toxicity was verified in transgenic flies.
MAPPING
By FISH, Hata et al. (1996) mapped the HSPF1 gene to chromosome 19p13.2.
*FIELD* RF
1. Chan, H. Y. E.; Warrick, J. M.; Gray-Board, G. L.; Paulson, H.
L.; Bonini, N. M.: Mechanisms of chaperone suppression of polyglutamine
disease: selectivity, synergy and modulation of protein solubility
in Drosophila. Hum. Molec. Genet. 9: 2811-2820, 2000.
2. Hata, M.; Ohtsuka, K.: Characterization of HSE sequences in human
Hsp40 gene: structural and promoter analysis. Biochim. Biophys. Acta 1397:
43-55, 1998.
3. Hata, M.; Okumura, K.; Seto, M.; Ohtsuka, K.: Genomic cloning
of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal
localization to 19p13.2. Genomics 38: 446-449, 1996.
4. Kazemi-Esfarjani, P.; Benzer, S.: Genetic suppression of polyglutamine
toxicity in Drosophila. Science 287: 1837-1840, 2000.
5. Ohtsuka, K.: Cloning of a cDNA for heat-shock protein Hsp40, a
human homologue of bacterial DnaJ. Biochem. Biophys. Res. Commun. 197:
235-240, 1993.
*FIELD* CN
George E. Tiller - updated: 2/5/2001
*FIELD* CD
Paul J. Converse: 2/18/2000
*FIELD* ED
carol: 08/17/2007
alopez: 11/20/2001
mgross: 8/3/2001
carol: 3/13/2001
cwells: 2/5/2001
carol: 2/18/2000