| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MNTMYVMMAQ -----CCHHHHHHHH | 14.47 | 24043423 | |
| 5 | Phosphorylation | ---MNTMYVMMAQIL ---CCHHHHHHHHHH | 5.33 | 24043423 | |
| 14 | Phosphorylation | MMAQILRSHLIKATV HHHHHHHHHHCHHEE | 21.14 | 24043423 | |
| 20 | Phosphorylation | RSHLIKATVIPNRVK HHHHCHHEECCCCCC | 17.61 | 24043423 | |
| 31 | Phosphorylation | NRVKMLPYFGIIRNR CCCCCHHHHHHHHHH | 15.52 | 22817900 | |
| 76 | Acetylation | ESFHKLAKQYHPDSG HHHHHHHHHHCCCCC | 62.92 | 19821069 | |
| 84 | Phosphorylation | QYHPDSGSNTADSAT HHCCCCCCCCCCCHH | 34.65 | - | |
| 97 | Acetylation | ATFIRIEKAYRKVLS HHHHHHHHHHHHHHH | 48.63 | 19821077 | |
| 128 | Phosphorylation | EDVEKFKYKTPQHRH HHHHHHCCCCCCCCC | 24.19 | 24719451 | |
| 130 | Phosphorylation | VEKFKYKTPQHRHYL HHHHCCCCCCCCCEE | 25.70 | 24719451 | |
| 169 | Phosphorylation | AAEQVMEYQKQKLQS HHHHHHHHHHHHHHH | 11.69 | 27642862 | |
| 223 | Ubiquitination | DFDNLSGKGKPLKKF CHHHCCCCCCCCCCC | 61.46 | 22817900 | |
| 225 | Ubiquitination | DNLSGKGKPLKKFSD HHCCCCCCCCCCCCC | 51.14 | 22817900 | |
| 228 | Ubiquitination | SGKGKPLKKFSDCSY CCCCCCCCCCCCCCC | 61.37 | 22817900 | |
| 229 | Ubiquitination | GKGKPLKKFSDCSYI CCCCCCCCCCCCCCC | 58.76 | 22817900 | |
| 252 | Phosphorylation | RILIDNGYQPEWILK HHEECCCCCCHHHHC | 27.44 | 27174698 | |
| 286 | Phosphorylation | KKLGNPMTPTEKKQW HHHCCCCCCCHHHHH | 28.46 | 23403867 | |
| 288 | Phosphorylation | LGNPMTPTEKKQWNH HCCCCCCCHHHHHHH | 51.80 | 26657352 | |
| 341 | Phosphorylation | IVRAQKIYETLIKTK HHHHHHHHHHHHHHH | 15.19 | 20049867 | |
| 347 | Phosphorylation | IYETLIKTKEVTDRN HHHHHHHHHCCCCCC | 25.99 | 17693683 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DJC28_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LRC46_HUMAN | LRRC46 | physical | 26186194 | |
| ATPB_HUMAN | ATP5B | physical | 28514442 | |
| LRC46_HUMAN | LRRC46 | physical | 28514442 |
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |