| UniProt ID | DNJC2_MOUSE | |
|---|---|---|
| UniProt AC | P54103 | |
| Protein Name | DnaJ homolog subfamily C member 2 | |
| Gene Name | Dnajc2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 621 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytosol . | |
| Protein Description | Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity). Specifically binds DNA sequence 5'-GTCAAGC-3'.. | |
| Protein Sequence | MLLLPSAAEGQGTAITHALTSASSVCQVEPVGRWFEAFVKRRNRNASTSFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCDRLELASLQGLNEILASSTREVGKAALEKQIEEVNEQMRREKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVISKAKSLQKLDPHQKDDINKKAFDKFKKEHGVASQADSAAPSERFEGPCIDSTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MLLLPSAA -------CCCCCCCC | 5.55 | - | |
| 47 | Phosphorylation | KRRNRNASTSFQELE HHHCCCCCCCHHHHH | 28.29 | 27087446 | |
| 48 | Phosphorylation | RRNRNASTSFQELED HHCCCCCCCHHHHHH | 31.02 | 25521595 | |
| 49 | Phosphorylation | RNRNASTSFQELEDK HCCCCCCCHHHHHHH | 23.57 | 25521595 | |
| 60 | Phosphorylation | LEDKKELSEESEDEE HHHHHHHCCCCCCCC | 40.17 | 24925903 | |
| 63 | Phosphorylation | KKELSEESEDEELQL HHHHCCCCCCCCCCH | 46.42 | 27087446 | |
| 90 | Phosphorylation | DWKNQDHYAVLGLGH HHCCCCCEEEEECCC | 13.49 | 29514104 | |
| 137 | Phosphorylation | IKEGDNDYFTCITKA CCCCCCCHHHHHHHH | 13.67 | 20531401 | |
| 139 | Phosphorylation | EGDNDYFTCITKAYE CCCCCHHHHHHHHHH | 9.21 | 20531401 | |
| 183 | Phosphorylation | DNFFQVFSPVFERNS CCCHHHCHHHHHHCC | 22.69 | 26824392 | |
| 276 | Glutathionylation | LVDNAYSCDPRIKKF HHHHHHCCCHHHHHH | 5.63 | 24333276 | |
| 362 | Phosphorylation | KLRNSCKSWNHFSDN HHHHHHHHCCCCCCC | 37.12 | 25338131 | |
| 413 | Ubiquitination | VGKAALEKQIEEVNE HHHHHHHHHHHHHHH | 58.38 | 22790023 | |
| 443 | Phosphorylation | ASKNAEKSTGGSGSG HHHHHHHHCCCCCCC | 24.64 | 21149613 | |
| 444 | Phosphorylation | SKNAEKSTGGSGSGS HHHHHHHCCCCCCCC | 57.54 | 21149613 | |
| 447 | Phosphorylation | AEKSTGGSGSGSKNW HHHHCCCCCCCCCCC | 31.00 | 21149613 | |
| 449 | Phosphorylation | KSTGGSGSGSKNWSE HHCCCCCCCCCCCCH | 41.41 | 21149613 | |
| 451 | Phosphorylation | TGGSGSGSKNWSEDD CCCCCCCCCCCCHHH | 25.23 | 21149613 | |
| 455 | Phosphorylation | GSGSKNWSEDDLQLL CCCCCCCCHHHHHHH | 40.31 | 21149613 | |
| 548 | Glutathionylation | SERFEGPCIDSTPWT CHHCCCCCCCCCCCC | 8.74 | 24333276 | |
| 617 | Phosphorylation | QEQVLNASRARK--- HHHHHHHHHHCC--- | 25.96 | 28066266 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNJC2_MOUSE !! | ||||||
* 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 DNJC2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DNJC2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY. | |
| "A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-48; SER-49;SER-60 AND SER-63, AND MASS SPECTROMETRY. | |