UniProt ID | VINC_DROME | |
---|---|---|
UniProt AC | O46037 | |
Protein Name | Vinculin | |
Gene Name | Vinc | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 961 | |
Subcellular Localization |
Cytoplasm, cytoskeleton . Cell junction, adherens junction . Cell membrane Peripheral membrane protein Cytoplasmic side . Cell junction . Cytoplasmic face of adhesion plaques. |
|
Protein Description | Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane.. | |
Protein Sequence | MPVFHTKTIESILDPVAQQVSRLVILHEEAEDGNAMPDLSRPVQVVSAAVANLVKVGRDTINSSDDKILRQDMPSALHRVEGASQLLEEASDMLRSDPYSGPARKKLIEGSRGILQGTSSLLLCFDESEVRKIIQECKRVLDYLAVAEVINTMEQLVQFLKDLSPCLSKVHREVGAREKELTHQVHSEILVRCLEQVKTLAPILICSMKVYIHIVEQQGRGAEEAAENRNYLAARMSDELQEIIRVLQLTTYDEDTSELDNLTVLKKLSNAISNKMEQANEWLSNPYALRGGVGEKALRQVIDNATEISERCLPQDSYPIRKLADEVTAMANTLCELRQEGKGQSPQAESLVRGIRDRMGELKSLVHQAVLGVDKAGVQQTAHTIQGRLEQAVKWLQHPEINDGGLGERAINLIVEEGRKVAEGCPGHQKAEIQQLCDEVERLKRQAAGSGPAAKQAAKQLTQKLYELKAAIQNALVNRIVQDFMDVSTPLKQFTEAVLQPEGTPGREQNFNQKSNNLQAFSDRASKTSRMVAAGGACGNKKIAEILLSSAAQVDSLTPQLISAGRIRMNYPGSKAADEHLQNLKQQYADTVLRMRTLCDQATDPADFIKTSEEHMQVYAKLCEDAIHARQPQKMVDNTSNIARLINRVLLVAKQEADNSEDPVFTERLNAAANRLERSLPAMVGDAKLVATNIADPAAAAAWKNSFQRLLGDVREVRDAIAPPQPPPLPTSLPPPIPELSALHLSNQNAERAPPRPPLPREGLAPVRPPPPETDDEDEGVFRTMPHANQPILIAARGLHQEVRQWSSKDNEIIAAAKRMAILMARLSELVLSDSRGSKRELIATAKKIAEASEDVTRLAKELARQCTDRRIRTNLLQVCERIPTIGTQLKILSTVKATMLGAQGSDEDREATEMLVGNAQNLMQSVKETVRAAEGASIKIRSDQTSNRLQWVRRQPWYQY | |
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 |
---|---|---|---|---|---|
106 | Acetylation | YSGPARKKLIEGSRG CCCHHHHHHHHCCCH | 49.49 | 21791702 | |
571 | Phosphorylation | AGRIRMNYPGSKAAD HCCCCCCCCCCHHHH | 10.30 | 22817900 | |
574 | Phosphorylation | IRMNYPGSKAADEHL CCCCCCCCHHHHHHH | 18.02 | 22817900 | |
774 | Phosphorylation | VRPPPPETDDEDEGV CCCCCCCCCCCCCCC | 55.30 | 19429919 | |
784 | Phosphorylation | EDEGVFRTMPHANQP CCCCCCCCCCCCCCC | 24.48 | 21082442 |
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 VINC_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VINC_DROME !! |
* 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 VINC_DROME !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-774, AND MASSSPECTROMETRY. |