| UniProt ID | BRK1_HUMAN | |
|---|---|---|
| UniProt AC | Q8WUW1 | |
| Protein Name | Protein BRICK1 | |
| Gene Name | BRK1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 75 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. | |
| Protein Description | Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity).. | |
| Protein Sequence | MAGQEDPVQREIHQDWANREYIEIITSSIKKIADFLNSFDMSCRSRLATLNEKLTALERRIEYIEARVTKGETLT | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAGQEDPVQ ------CCCCCCHHH | 28.51 | 22814378 | |
| 21 | Phosphorylation | QDWANREYIEIITSS HHHHHHHHHHHHHHH | 10.70 | 30243723 | |
| 21 (in isoform 2) | Phosphorylation | - | 10.70 | 27642862 | |
| 26 | Phosphorylation | REYIEIITSSIKKIA HHHHHHHHHHHHHHH | 23.29 | 30243723 | |
| 27 | Phosphorylation | EYIEIITSSIKKIAD HHHHHHHHHHHHHHH | 21.47 | 30243723 | |
| 28 | Phosphorylation | YIEIITSSIKKIADF HHHHHHHHHHHHHHH | 29.76 | 30243723 | |
| 30 | Ubiquitination | EIITSSIKKIADFLN HHHHHHHHHHHHHHH | 39.82 | 21890473 | |
| 30 (in isoform 1) | Ubiquitination | - | 39.82 | 21890473 | |
| 30 | Ubiquitination | EIITSSIKKIADFLN HHHHHHHHHHHHHHH | 39.82 | 21890473 | |
| 30 (in isoform 2) | Ubiquitination | - | 39.82 | 21890473 | |
| 31 (in isoform 2) | Ubiquitination | - | 41.26 | - | |
| 31 | Ubiquitination | IITSSIKKIADFLNS HHHHHHHHHHHHHHH | 41.26 | 23000965 | |
| 41 | Sulfoxidation | DFLNSFDMSCRSRLA HHHHHCCHHHHHHHH | 3.72 | 21406390 | |
| 46 | Methylation | FDMSCRSRLATLNEK CCHHHHHHHHHHHHH | 14.69 | - | |
| 53 (in isoform 2) | Ubiquitination | - | 50.49 | 21890473 | |
| 53 | Ubiquitination | RLATLNEKLTALERR HHHHHHHHHHHHHHH | 50.49 | 23000965 | |
| 53 | 2-Hydroxyisobutyrylation | RLATLNEKLTALERR HHHHHHHHHHHHHHH | 50.49 | - | |
| 53 | Ubiquitination | RLATLNEKLTALERR HHHHHHHHHHHHHHH | 50.49 | 21890473 | |
| 53 (in isoform 1) | Ubiquitination | - | 50.49 | 21890473 | |
| 63 (in isoform 2) | Phosphorylation | - | 11.16 | 27642862 | |
| 63 | Phosphorylation | ALERRIEYIEARVTK HHHHHHHHHHHHHCC | 11.16 | 25884760 | |
| 70 | Ubiquitination | YIEARVTKGETLT-- HHHHHHCCCCCCC-- | 52.47 | 33845483 | |
| 70 (in isoform 2) | Ubiquitination | - | 52.47 | - | |
| 70 (in isoform 1) | Ubiquitination | - | 52.47 | 21890473 | |
| 75 | Phosphorylation | VTKGETLT------- HCCCCCCC------- | 43.94 | 25332170 |
| 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 BRK1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRK1_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 BRK1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DTBP1_HUMAN | DTNBP1 | physical | 25416956 |
| 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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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, AND MASSSPECTROMETRY. | |