UniProt ID | TIG_DROME | |
---|---|---|
UniProt AC | Q9VMD9 | |
Protein Name | Tiggrin {ECO:0000312|EMBL:AAF52380.2} | |
Gene Name | Tig {ECO:0000312|EMBL:AAF52380.2, ECO:0000312|FlyBase:FBgn0011722} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 2188 | |
Subcellular Localization | Secreted, extracellular space, extracellular matrix . Localizes to the basal surface of the dorsoventral cell layer interface during pupal wing development. | |
Protein Description | Functions as a ligand for integrin alpha-PS2/beta-PS. Required in larvae for proper muscle structure and function. Involved in the regulation of cell adhesion during wing development.. | |
Protein Sequence | MRALGGITLLLAVAICQGYETYQRSSFRSSSSSSYGGGQTVPQLNSFASAHFNEVRELANQLKQKFNVLSQGSTNFAYTSPWSASILDLSGKSTLQLDQLSSEISRQLVQDMREGITNYHTIAQPNFFEAKAAELLERYSGAESASLQQTVGLGPYQPVDLSGFDEVKNYAYPAEVKVIDGKTYVVHRNCTEATKLSDYGSSGQLNSGFLGHQQTSLPLSSTTTTITRKKTIHDWVRENMEPSVVGYNSVVKLDGQLRNSALNQMVPLSPGSNVVIHRFNKTITTNPDGTSSVGGSEWQQRWQDGKLVYDHQQPFGQSTIPRDEQWKREERERLFWYLTTPQRLDDWQQQQEERLLGVVQRYQVSLPVLKEFHRRELARYEALLGQYQSRVQDTSSWQRQERGRLDWLIHQNGFTVQDIERWQNENARKLAEAARQHGISQNQLQQFQREELQRLYVHFNQVNESLAPQVPSVPQTTYNYQSSSSLTEDNTKEQQRLEELIRQHNATIAALQNSIKTDQQRLKNLSIKYQGDMQSQTQWLRGEVARIGDLIKEQNEQVSKITAWQSSERSRLENILLQHRGSVEEVQQRINMDRNYLQNLATKYQVSVEELEKWQKEELERLQVRGQQQLEEHIKDWQISVSSNLRDIATQNKLTIDEFQNYIINDRSHLEEMARLYKVKVEEIEQWIKSELKKFQSEGLLKGVEQELIQWQQKERERLQAIVQQNSLTVEQLEVRIKNDQDHFFKLADKYKINVEDIQDWLKKELLRLQSEGLVKAETLKEWQQQERAQISLLVQQNKYSLDEFERKMLADRARLQELSNTYNVKVSEIEQWIKSEGDRLQHEGQLRMESQLNNWQKIERQRLLDLINKNNLSIEEIESKISKDQTHLYSLAQQHQVRVEEIEQWIRQQIQKLQDQGLIEMQKLKNWQLEWRGNLTNMVQDRDFTVEEFHKWLLKDREQLQSLAMQHNVQIEEIEQFVKKEEQRFIGMGLLKPSEKLTNWQEVERLHLKNLAQQQYKSTEQLEARLRQDRELLERLARQYSVQVEEIESWMKQELARMRDEGQLQIDNLTSWQLAERERLEALIKQNKQWSAEELRAELEKDREHMQTMAFQYHTSVEEIEKWLQSEIERLKQQGKLNIEQLTAWQRTEQQRILSLLQQHSNITLEQFQAKVHNDRRFLMNLAEQHHVHIEEVDNYVKQVIEDLRKNGQFEIEQLQTWQRVERDYIKSLISEYKNSLSTAEYEEKLLADRAHLKHLADQYRINVEQIEEWMIAELKRLRGSTEETLKSLSAWQVSELERLQNLVKQQNHLTFVEFEMELNQERDRLQKLANQYSVNVVEIEEWLRQQLINLRTTGQAKVENLSKWQVEEQQRLIEMLLKKQQEMPYEQVERELTQDHARLQSLSQTHHVDIDHVDHWLREELRRLQSSGLVQIEQQTQWQQKISNGFNNWLEQQRNGASYQDFVDFLKRDKQRMDGIATDYHVTVEQVEKWVQKEAARLSLIGVIERPENNLKYEDISNIWVGDQTDSWKNELVTRLRSVTRQRPFTRQEFESYLIRNKPIFEQIARQYHVTIEDIHLWLDQSAKNEGLVTTEWQAKERLHIDNLINQQLRKQQRWTIEELELRLNNDQKHLQDAVAQYHVTVEELKVWYKDELNRLLEQRRIDRGSGISWQNIESQRIYLAIVNNPGISRQALENRLFRDVHVRASQYQITVEELRQFILSQLRRFSDMGLIVDNGRQANNWHDQERKRLREVVKGVVITEQELLDFISQDTSFQTQLAQSYQVGLEQLAPVQRIFIGNLAREQLLEQRRLNHLTTWQQRERDRLYEFIGNQNMTQTELKTWQIQDSKLLAEFAKRYEISVQQLSDWQKKELARINQLARYYGMSQSDLQQFREGELRQLAYINHRQLLSAAEAQKWEKRHQWTLSRLQSRYGKFGQELVAWRRTLYLLSQGLIDLPADSGSNGGYVVDAGSTNATAVYKPIFSKDRGDQPPHTYDESFVEGDEPGLEGETARPRPPNPAPIVSTPKPPLPYSRGGPSGGFEYRRQDYTFNVPVGSASASASGGPTGSSASASASLGKWNRASGDEPLQQEVDLGQQQQIEELGWNEKLEDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVEATSEPSFWEKLKEKLG | |
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 |
---|---|---|---|---|---|
269 | Phosphorylation | LNQMVPLSPGSNVVI HHCCCCCCCCCCEEE | 22817900 |
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 TIG_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TIG_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 TIG_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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