Reviewed, UniProtKB/Swiss-Prot P25685 (DNJB1_HUMAN)

Names and origin

Protein names

Recommended name:
    DnaJ homolog subfamily B member 1
Alternative name(s):
    Heat shock 40 kDa protein 1
      Short name=Heat shock protein 40
      Short name=HSP40
    DnaJ protein homolog 1
    HDJ-1

Gene names

Name:	DNAJB1
Synonyms:	DNAJ1, HDJ1, HSPF1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.
Subunit structure	Interacts with DNAJC3. Ref.6
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleolus. Note: Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock. Ref.5
Induction	By heat shock. Ref.5
Sequence similarities	Contains 1 J domain.
Sequence caution	The sequence CAA44287.1 differs from that shown. Reason: Frameshift at positions 11, 28, 81 and 136.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Nucleus
Molecular function	Chaperone
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to unfolded protein Ref.3 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heat shock protein binding Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.2

Chain

2 – 340

339

DnaJ homolog subfamily B member 1

PRO_0000071016

Regions

Domain

2 – 70

69

J

Amino acid modifications

Modified residue

44

1

N6-acetyllysine Ref.8

Experimental info

Sequence conflict

68

1

G → L in CAA44287. Ref.1

Sequence conflict

150

1

R → C in CAA44287. Ref.1

Sequence conflict

183

1

M → T in CAA44287. Ref.1

Sequence conflict

320

1

V → A in CAA44287. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

340

Helix Strand Turn

Details...

Helix

5 – 8

4

Helix

16 – 28

13

Turn

32 – 34

3

Helix

40 – 53

14

Helix

57 – 65

9

Helix

68 – 70

3

Sequences

	Sequence		Length	Mass (Da)
	P25685-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 17545098B0C196DF	FASTA	340	38,044
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human homologue of the Escherichia coli DnaJ heat-shock protein." Raabe T., Manley J.L. Nucleic Acids Res. 19:6645-6645(1991) [PubMed: 1754405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ." Ohtsuka K. Biochem. Biophys. Res. Commun. 197:235-240(1993) [PubMed: 8250930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-48. Tissue: Placenta.
[3]	"Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2." Hata M., Okumura K., Seto M., Ohtsuka K. Genomics 38:446-449(1996) [PubMed: 8975727] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lung.
[5]	"Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells." Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K. Cell Struct. Funct. 17:77-86(1992) [PubMed: 1586970] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-49, INDUCTION, SUBCELLULAR LOCATION.
[6]	"The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity." Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G. J. Biol. Chem. 274:3797-3803(1999) [PubMed: 9920933] [Abstract] Cited for: INTERACTION WITH DNAJC3.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, MASS SPECTROMETRY.
[9]	"Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain." Qian Y.Q., Patel D., Hartl F.-U., McColl D.J. J. Mol. Biol. 260:224-235(1996) [PubMed: 8764402] [Abstract] Cited for: STRUCTURE BY NMR OF 1-76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62421 mRNA. Translation: CAA44287.1. Frameshift.
D49547 mRNA. Translation: BAA08495.1.
D85429 Genomic DNA. Translation: BAA12819.1.
BC002352 mRNA. Translation: AAH02352.1.
BC019827 mRNA. Translation: AAH19827.1.

IPI

IPI00015947.

PIR

JN0912.
S20062.

RefSeq

NP_006136.1.

UniGene

Hs.515210

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HDJ	NMR	-	A	1-76	[»]
2QLD	X-ray	2.70	A	158-340	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41180N.

IntAct

P25685. 6 interactions.

STRING

P25685.

PTM databases

PhosphoSite

P25685.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00015947.

Proteomic databases

PeptideAtlas

P25685.

PRIDE

P25685.

Genome annotation databases

Ensembl

ENST00000254322; ENSP00000254322; ENSG00000132002; Homo sapiens. [Genome view]

GeneID

3337.

KEGG

hsa:3337.

UCSC

uc002myz.1. human.

Organism-specific databases

CTD

3337.

GeneCards

GC19M014486.

H-InvDB

HIX0014838.

HGNC

HGNC:5270. DNAJB1.

HPA

CAB017450.

MIM

604572. gene.

PharmGKB

PA27412.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06818.

HOGENOM

HBG635315.

HOVERGEN

P25685.

InParanoid

P25685.

OMA

GGFTNMN.

OrthoDB

EOG9NP9PN.

PhylomeDB

P25685.

Gene expression databases

ArrayExpress

P25685.

Bgee

P25685.

CleanEx

HS_DNAJB1.

Genevestigator

P25685.

GermOnline

ENSG00000132002. Homo sapiens.

Family and domain databases

InterPro

IPR002939. DnaJ_C.
IPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR015609. Hsp40/DnaJ_Rel.
IPR003095. Hsp_DnaJ.
[Graphical view]

Gene3D

G3DSA:1.10.287.110. DnaJ_N. 1 hit.

PANTHER

PTHR11821. Hsp40/DnaJ_Rel. 1 hit.

Pfam

PF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
[Graphical view]

PRINTS

PR00625. DNAJPROTEIN.

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

PROSITE

PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13208.

SOURCE

Search...

Entry information

Entry name

DNJB1_HUMAN

Accession

Primary (citable) accession number: P25685

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.