DNJB6_HUMAN - dbPTM
DNJB6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJB6_HUMAN
UniProt AC O75190
Protein Name DnaJ homolog subfamily B member 6
Gene Name DNAJB6
Organism Homo sapiens (Human).
Sequence Length 326
Subcellular Localization Cytoplasm, perinuclear region . Nucleus . Cytoplasm, myofibril, sarcomere, Z line .
Protein 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..
Protein Sequence MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKKSTKGNH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MVDYYEVLGVQ
----CCCHHHHHCCC		7.0727642862
5Phosphorylation---MVDYYEVLGVQR
---CCCHHHHHCCCC		8.6329496907
15PhosphorylationLGVQRHASPEDIKKA
HCCCCCCCHHHHHHH		23.7730576142
18UbiquitinationQRHASPEDIKKAYRK
CCCCCHHHHHHHHHH		62.48-
20UbiquitinationHASPEDIKKAYRKLA
CCCHHHHHHHHHHHH		43.61-
202-HydroxyisobutyrylationHASPEDIKKAYRKLA
CCCHHHHHHHHHHHH		43.61-
20 (in isoform 2)Ubiquitination-43.61-
21UbiquitinationASPEDIKKAYRKLAL
CCHHHHHHHHHHHHH		51.49-
23PhosphorylationPEDIKKAYRKLALKW
HHHHHHHHHHHHHHC		19.7029496907
29UbiquitinationAYRKLALKWHPDKNP
HHHHHHHHCCCCCCC		37.5421890473
29UbiquitinationAYRKLALKWHPDKNP
HHHHHHHHCCCCCCC		37.5421890473
29 (in isoform 2)Ubiquitination-37.5421890473
29UbiquitinationAYRKLALKWHPDKNP
HHHHHHHHCCCCCCC		37.5421890473
29 (in isoform 3)Ubiquitination-37.5421890473
29 (in isoform 1)Ubiquitination-37.5421890473
34UbiquitinationALKWHPDKNPENKEE
HHHCCCCCCCCCHHH		78.01-
34 (in isoform 2)Ubiquitination-78.01-
39UbiquitinationPDKNPENKEEAERKF
CCCCCCCHHHHHHHH		56.10-
39 (in isoform 2)Ubiquitination-56.10-
47UbiquitinationEEAERKFKQVAEAYE
HHHHHHHHHHHHHHH		47.07-
47 (in isoform 2)Ubiquitination-47.07-
53PhosphorylationFKQVAEAYEVLSDAK
HHHHHHHHHHHHHHH		9.7020090780
57PhosphorylationAEAYEVLSDAKKRDI
HHHHHHHHHHHHCCH		40.47-
60 (in isoform 1)Ubiquitination-54.0221890473
60 (in isoform 3)Ubiquitination-54.0221890473
60 (in isoform 2)Ubiquitination-54.0221890473
60UbiquitinationYEVLSDAKKRDIYDK
HHHHHHHHHCCHHHH		54.0221906983
60UbiquitinationYEVLSDAKKRDIYDK
HHHHHHHHHCCHHHH		54.0221890473
61UbiquitinationEVLSDAKKRDIYDKY
HHHHHHHHCCHHHHH		57.96-
65PhosphorylationDAKKRDIYDKYGKEG
HHHHCCHHHHHCCCC		15.6329496907
67 (in isoform 2)Ubiquitination-38.6421890473
67UbiquitinationKKRDIYDKYGKEGLN
HHCCHHHHHCCCCCC		38.6421890473
67UbiquitinationKKRDIYDKYGKEGLN
HHCCHHHHHCCCCCC		38.6421890473
67UbiquitinationKKRDIYDKYGKEGLN
HHCCHHHHHCCCCCC		38.6421890473
67 (in isoform 1)Ubiquitination-38.6421890473
67 (in isoform 3)Ubiquitination-38.6421890473
68PhosphorylationKRDIYDKYGKEGLNG
HCCHHHHHCCCCCCC		30.4529496907
70UbiquitinationDIYDKYGKEGLNGGG
CHHHHHCCCCCCCCC		45.58-
70 (in isoform 2)Ubiquitination-45.58-
81PhosphorylationNGGGGGGSHFDSPFE
CCCCCCCCCCCCCCC		25.0230622161
85PhosphorylationGGGSHFDSPFEFGFT
CCCCCCCCCCCCCEE		30.4630622161
132PhosphorylationNRRGPRGSRSRGTGS
CCCCCCCCCCCCCCC		28.5020068231
134PhosphorylationRGPRGSRSRGTGSFF
CCCCCCCCCCCCCCH		36.4420068231
135MethylationGPRGSRSRGTGSFFS
CCCCCCCCCCCCCHH		45.65-
147UbiquitinationFFSAFSGFPSFGSGF
CHHHHCCCCCCCCCC		4.42-
176UbiquitinationHGGLTSFSSTSFGGS
CCCCCCCCCCCCCCC		32.26-
190PhosphorylationSGMGNFKSISTSTKM
CCCCCCCEEECCCCE		20.0322210691
196 (in isoform 3)Ubiquitination-40.3921890473
196 (in isoform 1)Ubiquitination-40.3921890473
196AcetylationKSISTSTKMVNGRKI
CEEECCCCEECCEEE		40.3925953088
196UbiquitinationKSISTSTKMVNGRKI
CEEECCCCEECCEEE		40.3921890473
196UbiquitinationKSISTSTKMVNGRKI
CEEECCCCEECCEEE		40.3921890473
196 (in isoform 2)Ubiquitination-40.3921890473
196UbiquitinationKSISTSTKMVNGRKI
CEEECCCCEECCEEE		40.3921890473
225 (in isoform 2)Ubiquitination-35.2221890473
225UbiquitinationVEEDGQLKSLTINGV
EECCCCEEEEEECCC		35.22-
226PhosphorylationEEDGQLKSLTINGVA
ECCCCEEEEEECCCC		39.06-
228PhosphorylationDGQLKSLTINGVADD
CCCEEEEEECCCCCC		21.3528555341
232 (in isoform 2)Ubiquitination-4.5821890473
253UbiquitinationGQNALPAQPAGLRPP
CCCCCCCCCCCCCCC		26.83-
257UbiquitinationLPAQPAGLRPPKPPR
CCCCCCCCCCCCCCC		8.91-
267PhosphorylationPKPPRPASLLRHAPH
CCCCCCHHHHHHCCC		30.5321406692
277PhosphorylationRHAPHCLSEEEGEQD
HHCCCCCCCCCCCCC		48.6429255136
297PhosphorylationGPWDPLASAAGLKEG
CCCCHHHHHHCHHHH		26.7430622161
302UbiquitinationLASAAGLKEGGKRKK
HHHHHCHHHHHHHHH		54.092190698
302AcetylationLASAAGLKEGGKRKK
HHHHHCHHHHHHHHH		54.0925953088
302 (in isoform 1)Ubiquitination-54.0921890473
306UbiquitinationAGLKEGGKRKKQKQR
HCHHHHHHHHHHHHH		72.41-
306AcetylationAGLKEGGKRKKQKQR
HCHHHHHHHHHHHHH		72.4125953088
312 (in isoform 3)Phosphorylation-56.3725849741
314 (in isoform 3)Phosphorylation-65.2225850435
315 (in isoform 3)Phosphorylation-70.7825849741
316PhosphorylationKQKQREESKKKKSTK
HHHHHHHHHHHHCCC		45.05-
321PhosphorylationEESKKKKSTKGNH--
HHHHHHHCCCCCC--		44.2026670566
322PhosphorylationESKKKKSTKGNH---
HHHHHHCCCCCC---		52.4226670566
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DNJB6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJB6_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DNJB6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C18_HUMANKRT18physical
10954706
HDAC4_HUMANHDAC4physical
20159555
HDAC6_HUMANHDAC6physical
20159555
SIR2_HUMANSIRT2physical
20159555
HDAC4_HUMANHDAC4physical
18163532
ALKB1_HUMANALKBH1physical
18163532
A4_HUMANAPPphysical
21832049
DNJB2_HUMANDNAJB2physical
26186194
CL045_HUMANC12orf45physical
26186194
BAG3_HUMANBAG3physical
22366786
HSPB8_HUMANHSPB8physical
22366786
CHIP_HUMANSTUB1physical
22366786
HSPB8_RATHspb8physical
22366786
CL045_HUMANC12orf45physical
28514442
DNJB2_HUMANDNAJB2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603511Limb-girdle muscular dystrophy 1E (LGMD1E)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJB6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.

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