ID   DNJB1_HUMAN             Reviewed;         340 AA.
AC   P25685;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-JAN-2012, entry version 129.
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   MEDLINE=92093635; 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   MEDLINE=94071949; 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   MEDLINE=97131529; 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   MEDLINE=92266438; 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   MEDLINE=99121125; 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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
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   [10]
RP   STRUCTURE BY NMR OF 1-76.
RX   MEDLINE=96291433; 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   -!- 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   IPI; IPI00015947; -.
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, 117-340.
DR   DIP; DIP-41180N; -.
DR   IntAct; P25685; 16.
DR   MINT; MINT-204558; -.
DR   STRING; P25685; -.
DR   PhosphoSite; P25685; -.
DR   DMDM; 1706473; -.
DR   REPRODUCTION-2DPAGE; IPI00015947; -.
DR   PeptideAtlas; P25685; -.
DR   PRIDE; P25685; -.
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; HIX0202810; -.
DR   HGNC; HGNC:5270; DNAJB1.
DR   HPA; CAB017450; -.
DR   MIM; 604572; gene.
DR   neXtProt; NX_P25685; -.
DR   PharmGKB; PA27412; -.
DR   eggNOG; prNOG06818; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; P25685; -.
DR   OMA; GGFTNMN; -.
DR   OrthoDB; EOG4PVP00; -.
DR   PhylomeDB; P25685; -.
DR   NextBio; 13208; -.
DR   ArrayExpress; P25685; -.
DR   Bgee; P25685; -.
DR   CleanEx; HS_DNAJB1; -.
DR   Genevestigator; P25685; -.
DR   GermOnline; ENSG00000132002; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   KO; K09507; -.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; 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   MOD_RES      44     44       N6-acetyllysine.
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         5      8
FT   HELIX        16     28
FT   TURN         32     34
FT   HELIX        40     53
FT   HELIX        57     65
FT   HELIX        68     70
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
//