DJC28_HUMAN - dbPTM
DJC28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJC28_HUMAN
UniProt AC Q9NX36
Protein Name DnaJ homolog subfamily C member 28
Gene Name DNAJC28
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization
Protein Description May have a role in protein folding or as a chaperone..
Protein Sequence MNTMYVMMAQILRSHLIKATVIPNRVKMLPYFGIIRNRMMSTHKSKKKIREYYRLLNVEEGCSADEVRESFHKLAKQYHPDSGSNTADSATFIRIEKAYRKVLSHVIEQTNASQSKGEEEEDVEKFKYKTPQHRHYLSFEGIGFGTPTQREKHYRQFRADRAAEQVMEYQKQKLQSQYFPDSVIVKNIRQSKQQKITQAIERLVEDLIQESMAKGDFDNLSGKGKPLKKFSDCSYIDPMTHNLNRILIDNGYQPEWILKQKEISDTIEQLREAILVSRKKLGNPMTPTEKKQWNHVCEQFQENIRKLNKRINDFNLIVPILTRQKVHFDAQKEIVRAQKIYETLIKTKEVTDRNPNNLDQGEGEKTPEIKKGFLNWMNLWKFIKIRSF
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
3Phosphorylation-----MNTMYVMMAQ
-----CCHHHHHHHH
14.4724043423
5Phosphorylation---MNTMYVMMAQIL
---CCHHHHHHHHHH
5.3324043423
14PhosphorylationMMAQILRSHLIKATV
HHHHHHHHHHCHHEE
21.1424043423
20PhosphorylationRSHLIKATVIPNRVK
HHHHCHHEECCCCCC
17.6124043423
31PhosphorylationNRVKMLPYFGIIRNR
CCCCCHHHHHHHHHH
15.5222817900
76AcetylationESFHKLAKQYHPDSG
HHHHHHHHHHCCCCC
62.9219821069
84PhosphorylationQYHPDSGSNTADSAT
HHCCCCCCCCCCCHH
34.65-
97AcetylationATFIRIEKAYRKVLS
HHHHHHHHHHHHHHH
48.6319821077
128PhosphorylationEDVEKFKYKTPQHRH
HHHHHHCCCCCCCCC
24.1924719451
130PhosphorylationVEKFKYKTPQHRHYL
HHHHCCCCCCCCCEE
25.7024719451
169PhosphorylationAAEQVMEYQKQKLQS
HHHHHHHHHHHHHHH
11.6927642862
223UbiquitinationDFDNLSGKGKPLKKF
CHHHCCCCCCCCCCC
61.4622817900
225UbiquitinationDNLSGKGKPLKKFSD
HHCCCCCCCCCCCCC
51.1422817900
228UbiquitinationSGKGKPLKKFSDCSY
CCCCCCCCCCCCCCC
61.3722817900
229UbiquitinationGKGKPLKKFSDCSYI
CCCCCCCCCCCCCCC
58.7622817900
252PhosphorylationRILIDNGYQPEWILK
HHEECCCCCCHHHHC
27.4427174698
286PhosphorylationKKLGNPMTPTEKKQW
HHHCCCCCCCHHHHH
28.4623403867
288PhosphorylationLGNPMTPTEKKQWNH
HCCCCCCCHHHHHHH
51.8026657352
341PhosphorylationIVRAQKIYETLIKTK
HHHHHHHHHHHHHHH
15.1920049867
347PhosphorylationIYETLIKTKEVTDRN
HHHHHHHHHCCCCCC
25.9917693683

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 DJC28_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DJC28_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 DJC28_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRC46_HUMANLRRC46physical
26186194
ATPB_HUMANATP5Bphysical
28514442
LRC46_HUMANLRRC46physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DJC28_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-347, AND MASSSPECTROMETRY.

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