UniProt Accession

 DNJB1_HUMAN; P25685 

Genbank Protein ID

 X62421; D49547; D85429; BC002352; BC019827 

Genbank Nucleotide ID

 CAA44287.1; BAA08495.1; BAA12819.1; AAH02352.1; AAH19827.1 

Protein Name

 DnaJ homolog subfamily B member 1 

Protein Synonyms/Alias

 DnaJ protein homolog 1; Heat shock 40 kDa protein 1; HSP40; Heat shock protein 40; Human DnaJ protein 1; hDj-1 

Gene Name

 DNAJB1 

Gene Synonyms/Alias

 DNAJ1; HDJ1; HSPF1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MGKDYYQTLG	ubiquitination	[1]
21	GASDEEIKRAYRRQA	ubiquitination	[2, 3]
35	ALRYHPDKNKEPGAE	ubiquitination	[3]
44	KEPGAEEKFKEIAEA	acetylation	[4, 5]
46	PGAEEKFKEIAEAYD	ubiquitination	[1, 3]
158	SAQEPARKKQDPPVT	ubiquitination	[1]
159	AQEPARKKQDPPVTH	ubiquitination	[1]
181	EIYSGCTKKMKISHK	ubiquitination	[6]
195	KRLNPDGKSIRNEDK	ubiquitination	[1, 2]
286	RTIPVVFKDVIRPGM	ubiquitination	[1, 7, 8, 9]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. 

Sequence Annotation

 DOMAIN 2 70 J.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 340 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Compara.
 GO:0006986; P:response to unfolded protein; TAS:ProtInc. 

Interpro

 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd. 

Pfam

 PF00226; DnaJ
 PF01556; DnaJ_C 

SMART

 SM00271; DnaJ 

PROSITE

 PS00636; DNAJ_1
 PS50076; DNAJ_2 

PRINTS

 PR00625; JDOMAIN.