UniProt ID | DUS5_HUMAN | |
---|---|---|
UniProt AC | Q16690 | |
Protein Name | Dual specificity protein phosphatase 5 | |
Gene Name | DUSP5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 384 | |
Subcellular Localization | Nucleus . | |
Protein Description | Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.. | |
Protein Sequence | MKVTSLDGRQLRKMLRKEAAARCVVLDCRPYLAFAASNVRGSLNVNLNSVVLRRARGGAVSARYVLPDEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLPAGPRVYFLKGGYETFYSEYPECCVDVKPISQEKIESERALISQCGKPVVNVSYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACATHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREKGGKVLVHCEAGISRSPTICMAYLMKTKQFRLKEAFDYIKQRRSMVSPNFGFMGQLLQYESEILPSTPNPQPPSCQGEAAGSSLIGHLQTLSPDMQGAYCTFPASVLAPVPTHSTVSELSRSPVATATSC | |
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 |
---|---|---|---|---|---|
2 | Ubiquitination | ------MKVTSLDGR ------CCCCCCCHH | 54.97 | - | |
49 | Phosphorylation | SLNVNLNSVVLRRAR EEECCCCHHHHHHHC | 19.44 | - | |
64 | Phosphorylation | GGAVSARYVLPDEAA CCCCEEEEECCCHHH | 13.17 | 28152594 | |
110 | Phosphorylation | SAARVVLTSLLACLP HHHHHHHHHHHHHCC | 13.01 | - | |
144 | Ubiquitination | PECCVDVKPISQEKI CCCEEECCCCCHHHH | 31.97 | 21906983 | |
258 | Ubiquitination | CVREKGGKVLVHCEA HHHHCCCEEEEECCC | 40.85 | - | |
277 | Phosphorylation | SPTICMAYLMKTKQF CHHHHHHHHHHCCCH | 4.77 | - | |
287 | Ubiquitination | KTKQFRLKEAFDYIK HCCCHHHHHHHHHHH | 42.62 | 29967540 | |
294 | Ubiquitination | KEAFDYIKQRRSMVS HHHHHHHHHHHHHCC | 31.36 | 22817900 | |
321 | Phosphorylation | ESEILPSTPNPQPPS HHHCCCCCCCCCCCC | 25.75 | 19666109 | |
346 | Phosphorylation | IGHLQTLSPDMQGAY HHHHHHCCCCCCCCC | 23.42 | 19666109 | |
376 | Phosphorylation | TVSELSRSPVATATS CHHHHHCCCCCCCCC | 21.98 | 19666109 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
321 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
321 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
346 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
346 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
376 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
376 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DUS5_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 DUS5_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MK03_HUMAN | MAPK3 | physical | 7836374 | |
IPO7_HUMAN | IPO7 | physical | 27880917 | |
TEX10_HUMAN | TEX10 | physical | 27880917 | |
COIL_HUMAN | COIL | physical | 27880917 | |
DUS5_HUMAN | DUSP5 | physical | 27432908 | |
RL32_HUMAN | RPL32 | physical | 27432908 | |
LZTS2_HUMAN | LZTS2 | physical | 27432908 | |
RS15_HUMAN | RPS15 | physical | 27432908 | |
FBX11_HUMAN | FBXO11 | physical | 27432908 | |
RT35_HUMAN | MRPS35 | physical | 27432908 | |
SPB1_HUMAN | FTSJ3 | physical | 27432908 | |
DENR_HUMAN | DENR | physical | 27432908 | |
RL5_HUMAN | RPL5 | physical | 27432908 | |
RL36_HUMAN | RPL36 | physical | 27432908 | |
AP3S1_HUMAN | AP3S1 | physical | 27432908 |
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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