UniProt ID | BORG1_HUMAN | |
---|---|---|
UniProt AC | O14613 | |
Protein Name | Cdc42 effector protein 2 | |
Gene Name | CDC42EP2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 210 | |
Subcellular Localization |
Endomembrane system Peripheral membrane protein . Cytoplasm, cytoskeleton . |
|
Protein Description | Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner.. | |
Protein Sequence | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTMVEGPEEDGTFDLPFQFTRTATVCGRELPDGPSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLETPQPSPQEGGSVDIWRIPETGSPNSGLTPESGAEEPFLSNASSLLSLHVDLGPSILDDVLQIMDQDLDSMQIPT | |
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 | Phosphorylation | ------MSTKVPIYL ------CCCCCCEEE | 36.61 | 22167270 | |
2 | Acetylation | ------MSTKVPIYL ------CCCCCCEEE | 36.61 | 22814378 | |
3 | Phosphorylation | -----MSTKVPIYLK -----CCCCCCEEEC | 34.46 | 22167270 | |
8 | Phosphorylation | MSTKVPIYLKRGSRK CCCCCCEEECCCCCC | 10.49 | 29978859 | |
26 | Phosphorylation | EKLRDLLSSDMISPP HHHHHHHCCCCCCCC | 31.43 | 29396449 | |
27 | Phosphorylation | KLRDLLSSDMISPPL HHHHHHCCCCCCCCC | 31.03 | 29396449 | |
31 | Phosphorylation | LLSSDMISPPLGDFR HHCCCCCCCCCCCCC | 17.52 | 25159151 | |
45 | Phosphorylation | RHTIHIGSGGGSDMF CEEEEECCCCCCCCC | 33.39 | 28555341 | |
49 | Phosphorylation | HIGSGGGSDMFGDIS EECCCCCCCCCCCHH | 29.22 | 29214152 | |
56 | Phosphorylation | SDMFGDISFLQGKFH CCCCCCHHHHCCCEE | 25.33 | 28555341 | |
88 | Phosphorylation | LPFQFTRTATVCGRE CCEEEEEEEEECCCC | 24.50 | 22817900 | |
90 | Phosphorylation | FQFTRTATVCGRELP EEEEEEEEECCCCCC | 18.73 | 22817900 | |
101 | Phosphorylation | RELPDGPSPLLKNAI CCCCCCCCHHHHCCC | 33.44 | 29255136 | |
109 | Phosphorylation | PLLKNAISLPVIGGP HHHHCCCCCCCCCCC | 24.98 | 29255136 | |
120 | Phosphorylation | IGGPQALTLPTAQAP CCCCCCEECCCCCCC | 33.44 | 23312004 | |
123 | Phosphorylation | PQALTLPTAQAPPKP CCCEECCCCCCCCCC | 34.22 | 23312004 | |
137 | Phosphorylation | PPRLHLETPQPSPQE CCCEEEECCCCCCCC | 33.32 | 30266825 | |
141 | Phosphorylation | HLETPQPSPQEGGSV EEECCCCCCCCCCCE | 33.69 | 30266825 | |
147 | Phosphorylation | PSPQEGGSVDIWRIP CCCCCCCCEEEEECC | 27.72 | 23927012 |
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 BORG1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BORG1_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 BORG1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SEPT7_HUMAN | SEPT7 | physical | 11584266 | |
SEPT6_HUMAN | SEPT6 | physical | 11584266 | |
RHOQ_HUMAN | RHOQ | physical | 10490598 | |
CDC42_HUMAN | CDC42 | physical | 10490598 | |
RHG26_HUMAN | ARHGAP26 | physical | 25416956 | |
NDK7_HUMAN | NME7 | physical | 25416956 | |
RHG26_HUMAN | ARHGAP26 | physical | 21516116 |
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 |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-101 AND SER-141,AND MASS SPECTROMETRY. |