[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Placenta; DOI=10.1093/nar/19.23.6645; PubMed=1754405 [NCBI, ExPASy, EBI, Israel, Japan] Raabe T., Manley J.L.; "A human homologue of the Escherichia coli DnaJ heat-shock protein."; Nucleic Acids Res. 19:6645-6645(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-48. TISSUE=Placenta; DOI=10.1006/bbrc.1993.2466; PubMed=8250930 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Placenta; DOI=10.1006/geno.1996.0653; PubMed=8975727 [NCBI, ExPASy, EBI, Israel, Japan] 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]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain, and Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 2-49, INDUCTION, AND SUBCELLULAR LOCATION. PubMed=1586970 [NCBI, ExPASy, EBI, Israel, Japan] Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.; "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."; Cell Struct. Funct. 17:77-86(1992).
[6]	INTERACTION WITH DNAJC3. DOI=10.1074/jbc.274.6.3797; PubMed=9920933 [NCBI, ExPASy, EBI, Israel, Japan] Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.; "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity."; J. Biol. Chem. 274:3797-3803(1999).
[7]	STRUCTURE BY NMR OF 1-76. DOI=10.1006/jmbi.1996.0394; PubMed=8764402 [NCBI, ExPASy, EBI, Israel, Japan] Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.; "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain."; J. Mol. Biol. 260:224-235(1996).

Comments

FUNCTION: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.
SUBUNIT: Interacts with DNAJC3.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.
INDUCTION: By heat shock.
SIMILARITY: Contains 1 J domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X62421; CAA44287.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D49547; BAA08495.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D85429; BAA12819.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002352; AAH02352.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019827; AAH19827.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0912; JN0912.
S20062; S20062.

RefSeq

NP_006136.1; -.

UniGene

Hs.515210

3D structure databases

PDB

1HDJ; NMR; -; A=1-76.

[ExPASy / RCSB / EBI]

1HDJ; -.

P25685; 1-76.

Protein-protein interaction databases

IntAct

P25685; -.

PTM databases

PhosphoSite

P25685; -.

2D gel databases

REPRODUCTION-2DPAGE

IPI00015947; -.

Organism-specific databases

HIX0014838; -.

HGNC:5270; DNAJB1.

CAB017450; -.

604572; gene. [NCBI / EBI]

PharmGKB

PA27412; -.

GeneCards

P25685.

Gene expression databases

ArrayExpress

P25685; -.

CleanEx

HS_DNAJB1; -.

GermOnline

ENSG00000132002; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0031072;	Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0051082;	Molecular function: unfolded protein binding (inferred from electronic annotation from InterPro).
GO:0006986;	Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002939; DnaJ_C.
IPR001623; DnaJ_N.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.287.110; DnaJ_N; 1.

PANTHER

PTHR11821; Hsp40/DnaJ_Rel; 1.

Pfam

PF00226; DnaJ; 1.
PF01556; DnaJ_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00625; DNAJPROTEIN.

SMART

SM00271; DnaJ; 1.
SMART graphical view of domain structure.

PROSITE

PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

P25685; -.

Genome annotation databases

Ensembl

ENSG00000132002; Homo sapiens. [Contig view]

GeneID

3337; -.

KEGG

hsa:3337; -.

Phylogenomic databases

HOGENOM

P25685; -.

HOVERGEN

P25685; -.

Other

LinkHub

P25685; -.

NextBio

13208; -.

SOURCE

DNAJB1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; Nucleus; Stress response.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 340`	`339`	`DnaJ homolog subfamily B member 1.`	`PRO_0000071016`
`DOMAIN`	`2 70`	`69`	`J.`
`CONFLICT`	`11 11`		`L -> Q (in Ref. 1).`
`CONFLICT`	`13 28`		`RGASDEEIKRAYRRQA -> AALGRGDQAGLPPPG (in Ref. 1).`
`CONFLICT`	`68 68`		`G -> L (in Ref. 1; CAA44287).`
`CONFLICT`	`81 136`		`SGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRN` `GEEGMDIDDPFSGFPM -> TAEEPMVPLSATHSMETLMPCLLSSSVAEIPLTPFLGSGT` `GRKAWTLMTHSLASLW (in Ref. 1).`
`CONFLICT`	`150 150`		`R -> C (in Ref. 1; CAA44287).`
`CONFLICT`	`183 183`		`M -> T (in Ref. 1; CAA44287).`
`CONFLICT`	`320 320`		`V -> A (in Ref. 1; CAA44287).`
`HELIX`	`5 8`	`4`
`HELIX`	`16 28`	`13`
`TURN`	`32 34`	`3`
`HELIX`	`40 53`	`14`
`HELIX`	`57 65`	`9`
`HELIX`	`68 70`	`3`

Sequence information

Length: 340 AA [This is the length of the unprocessed precursor]

Molecular weight: 38044 Da [This is the MW of the unprocessed precursor]

CRC64: 17545098B0C196DF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK 

        70         80         90        100        110        120 
REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN 

       130        140        150        160        170        180 
GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT 

       190        200        210        220        230        240 
KKMKISHKRL NPDGKSIRNE DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK 

       250        260        270        280        290        300 
DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE 

       310        320        330        340 
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI

P25685 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools