UniProt Accession

 DNJB6_HUMAN; O75190; A4D232; A8K7D8; O95806; Q53EN8; Q59EF2; Q6FIC8; Q75MA2; Q9UIK6 

Genbank Protein ID

 AF080569; AB015798; AB015799; AF060703; AB014888; AF075601; CR533498; AB209859; AK223601; AK291953; AL136707; AC079306; AC079306; CH236954; CH236954; CH471149; BC000177; BC002446 

Genbank Nucleotide ID

 AAD16010.1; BAA88769.1; BAA88770.1; AAF21257.1; BAA32209.1; AAD43194.1; CAG38529.1; BAD93096.1; BAD97321.1; BAF84642.1; CAB66642.1; AAS07392.1; AAS07393.1; EAL23923.1; EAL23924.1; EAX04570.1; AAH00177.1; AAH02446.1 

Protein Name

 DnaJ homolog subfamily B member 6 

Protein Synonyms/Alias

 HHDJ1; Heat shock protein J2; HSJ-2; MRJ; MSJ-1 

Gene Name

 DNAJB6 

Gene Synonyms/Alias

 HSJ2; MRJ; MSJ1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
20	HASPEDIKKAYRKLA	ubiquitination	[1]
29	AYRKLALKWHPDKNP	ubiquitination	[2]
34	ALKWHPDKNPENKEE	ubiquitination	[1]
39	PDKNPENKEEAERKF	ubiquitination	[1]
47	EEAERKFKQVAEAYE	ubiquitination	[1]
60	YEVLSDAKKRDIYDK	ubiquitination	[1]
67	KKRDIYDKYGKEGLN	ubiquitination	[1]
70	DIYDKYGKEGLNGGG	ubiquitination	[1]
196	KSISTSTKMVNGRKI	ubiquitination	[1, 2]
225	VEEDGQLKSLTINGK	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
232	KSLTINGKEQLLRLD	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] 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]
 [7] 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]
 [8] 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] 

Functional Description

 Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity. 

Sequence Annotation

 DOMAIN 2 69 J.
 REGION 2 146 Interaction with HSP70.
 REGION 119 242 Interaction with KRT18.
 MOD_RES 277 277 Phosphoserine.  

Keyword

 Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Limb-girdle muscular dystrophy; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 326 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
 GO:0051087; F:chaperone binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
 GO:0060710; P:chorio-allantoic fusion; IEA:Compara.
 GO:0045109; P:intermediate filament organization; IDA:UniProtKB.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0006457; P:protein folding; IDA:UniProtKB.
 GO:0034504; P:protein localization to nucleus; IEA:Compara.
 GO:0006986; P:response to unfolded protein; NAS:UniProtKB. 

Interpro

 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS. 

Pfam

 PF00226; DnaJ 

SMART

 SM00271; DnaJ 

PROSITE

 PS00636; DNAJ_1
 PS50076; DNAJ_2 

PRINTS

 PR00625; JDOMAIN.