UniProt ID | DNJC9_HUMAN | |
---|---|---|
UniProt AC | Q8WXX5 | |
Protein Name | DnaJ homolog subfamily C member 9 | |
Gene Name | DNAJC9 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 260 | |
Subcellular Localization | Nucleus . Cytoplasm . Cell membrane . Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock. | |
Protein Description | May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8.. | |
Protein Sequence | MGLLDLCEEVFGTADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDFKGDMDQIMESVLCVQYTEEPRIRNIIQQAIDAGEVPSYNAFVKESKQKMNARKRRAQEEAKEAEMSRKELGLDEGVDSLKAAIQSRQKDRQKEMDNFLAQMEAKYCKSSKGGGKKSALKKEKK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
37 | Ubiquitination | EVRRGYHKVSLQVHP CEECCEEEEEEEECC | 25.65 | - | |
39 | Phosphorylation | RRGYHKVSLQVHPDR ECCEEEEEEEECCCC | 20.21 | 22985185 | |
46 | Methylation | SLQVHPDRVGEGDKE EEEECCCCCCCCCHH | 42.67 | - | |
72 | Methylation | VYSVLSDREQRAVYD HHHHCCCHHHHHHHC | 38.27 | - | |
88 | Phosphorylation | QGTVDEDSPVLTQDR CCCCCCCCCCCCCCC | 18.17 | 26714015 | |
92 | Phosphorylation | DEDSPVLTQDRDWEA CCCCCCCCCCCCHHH | 28.76 | - | |
95 | Methylation | SPVLTQDRDWEAYWR CCCCCCCCCHHHHHH | 40.92 | - | |
107 | Ubiquitination | YWRLLFKKISLEDIQ HHHHHHHCCCHHHHH | 30.14 | - | |
109 | Phosphorylation | RLLFKKISLEDIQAF HHHHHCCCHHHHHHH | 34.29 | 23927012 | |
118 | Ubiquitination | EDIQAFEKTYKGSEE HHHHHHHHHHCCCHH | 51.18 | - | |
121 | Ubiquitination | QAFEKTYKGSEEELA HHHHHHHCCCHHHHH | 62.28 | - | |
121 | Ubiquitination | QAFEKTYKGSEEELA HHHHHHHCCCHHHHH | 62.28 | - | |
131 | Ubiquitination | EEELADIKQAYLDFK HHHHHHHHHHHHHCC | 29.44 | - | |
180 | Ubiquitination | PSYNAFVKESKQKMN CCHHHHHHHHHHHHH | 50.22 | - | |
183 | Ubiquitination | NAFVKESKQKMNARK HHHHHHHHHHHHHHH | 55.84 | - | |
205 | Ubiquitination | KEAEMSRKELGLDEG HHHHHHHHHHCCCHH | 50.40 | - | |
205 | Ubiquitination | KEAEMSRKELGLDEG HHHHHHHHHHCCCHH | 50.40 | - | |
205 | Acetylation | KEAEMSRKELGLDEG HHHHHHHHHHCCCHH | 50.40 | 30588283 | |
215 | Phosphorylation | GLDEGVDSLKAAIQS CCCHHHHHHHHHHHH | 29.39 | 17287340 | |
217 | Ubiquitination | DEGVDSLKAAIQSRQ CHHHHHHHHHHHHHH | 39.46 | 21906983 | |
217 | Ubiquitination | DEGVDSLKAAIQSRQ CHHHHHHHHHHHHHH | 39.46 | - | |
217 | Methylation | DEGVDSLKAAIQSRQ CHHHHHHHHHHHHHH | 39.46 | - | |
229 | Ubiquitination | SRQKDRQKEMDNFLA HHHHHHHHHHHHHHH | 56.77 | - | |
241 | Ubiquitination | FLAQMEAKYCKSSKG HHHHHHHHHHHHCCC | 37.56 | - | |
253 | Phosphorylation | SKGGGKKSALKKEKK CCCCCCHHHCHHCCC | 42.17 | - |
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 DNJC9_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNJC9_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 DNJC9_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
FCL_HUMAN | TSTA3 | physical | 22939629 | |
HYOU1_HUMAN | HYOU1 | physical | 26344197 | |
KIF3A_HUMAN | KIF3A | physical | 27173435 |
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 phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, 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-109, AND MASSSPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY. |