UniProt ID | KRI1_DROME | |
---|---|---|
UniProt AC | Q9VTU0 | |
Protein Name | Protein KRI1 homolog | |
Gene Name | CG5645 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 855 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MNNNLFEGSDDDGEDLQLSTNKDYAKTYNILRKKELLQKYKDRGLDVSESEFDSDSSSSEEDEVDPKFDQDFFKTLSSLKSKDPCIYDKGTKFFSESSGDEDDKDGEAPKKKKKAKPVTLKDYERKVILEHNGKFESSDEEQQEKEHEELQRAQSPSAVEEERRLKAEFRKVMNKEDDSEDEEFGGIFKKRSKTKEQTAAEEADFAKWLAGKQAEIQETDKKQLEPLKQYWSSNKLTQGESFLRDYILNKGYANTDESAIPTYDEIVGEAAPLSEDEQELEKQAEFEHKYNFRFEEPDADFIKRYPRTIEQSLRRTDDKRKEKRKELKERKDQEKQQKMKELELVKEMKRKEIDEKIRKLKAVTGNDELGFRDEELEEDFDPAAHDRRMQELFDDEYYNVDEGEEKPECPSDIDELVLEDWDNYDPRQHANGGGEDYEGHCEDDDFNMDCDYDPSTAKEQLQQELIENTRGRKGRKGRRNRFMEMIQAEKPAFNPEDEKTYSEYIDEYYQMDCEDIIGDQPCRFKYVETTPNDFGLTIEEILLAKNKELNQWASLKKAVQNRPEHVEKKEQRLYKMKAKNEDLKRKIFKSLYGEGSDDEEQPAEEKPEVTPAEATAPAENGQVSTEGLSKSKRKRLKRKAAAAAASAPKVLKEESDSKDPKEADGSTEDVQAESSKKKVDTPSKKGKDDANQETKNSPQSTEKTKNNNALKNNKKEPKNVQNGFQKPQNQANKSAKTKSNQPFKTTESAPAKAEKSNGNNPFNKPQSKSQQRQELPPIHKNQGGNKKGPRNANGTNPFKKSNQKPSAPFPAKKTNNFKAKNKQNNNSGITDDRLKAYGINPRKFHKREKYGKKDN | |
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 |
---|---|---|---|---|---|
9 | Phosphorylation | NNNLFEGSDDDGEDL CCCCCCCCCCCCCCC | 30.57 | 19429919 | |
95 | Phosphorylation | DKGTKFFSESSGDED CCCCCEECCCCCCCC | 39.44 | 19429919 | |
97 | Phosphorylation | GTKFFSESSGDEDDK CCCEECCCCCCCCCC | 38.12 | 19429919 | |
98 | Phosphorylation | TKFFSESSGDEDDKD CCEECCCCCCCCCCC | 46.33 | 19429919 | |
137 | Phosphorylation | EHNGKFESSDEEQQE HCCCCCCCCHHHHHH | 46.34 | 19429919 | |
138 | Phosphorylation | HNGKFESSDEEQQEK CCCCCCCCHHHHHHH | 41.67 | 19429919 | |
155 | Phosphorylation | EELQRAQSPSAVEEE HHHHHCCCHHHHHHH | 21.60 | 19429919 | |
157 | Phosphorylation | LQRAQSPSAVEEERR HHHCCCHHHHHHHHH | 50.63 | 19429919 | |
179 | Phosphorylation | VMNKEDDSEDEEFGG HHCCCCCCCCCCCCH | 60.30 | 21082442 | |
252 | Phosphorylation | DYILNKGYANTDESA HHHHHCCCCCCCCCC | 9.78 | 23607784 | |
255 | Phosphorylation | LNKGYANTDESAIPT HHCCCCCCCCCCCCC | 32.73 | 23607784 | |
258 | Phosphorylation | GYANTDESAIPTYDE CCCCCCCCCCCCHHH | 34.02 | 23607784 | |
262 | Phosphorylation | TDESAIPTYDEIVGE CCCCCCCCHHHHHCC | 37.18 | 23607784 | |
263 | Phosphorylation | DESAIPTYDEIVGEA CCCCCCCHHHHHCCC | 13.26 | 23607784 | |
274 | Phosphorylation | VGEAAPLSEDEQELE HCCCCCCCCCHHHHH | 41.78 | 19429919 | |
590 | Phosphorylation | LKRKIFKSLYGEGSD HHHHHHHHHHCCCCC | 18.97 | 27794539 | |
596 | Phosphorylation | KSLYGEGSDDEEQPA HHHHCCCCCCCCCCC | 37.27 | 19429919 | |
697 | Phosphorylation | ANQETKNSPQSTEKT CCHHCCCCCCHHHHH | 26.35 | 21082442 | |
795 | Phosphorylation | GPRNANGTNPFKKSN CCCCCCCCCCCCCCC | 39.25 | 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 KRI1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KRI1_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 KRI1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-97; SER-98;SER-137 AND SER-138, AND MASS SPECTROMETRY. | |
"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 SER-179, AND MASSSPECTROMETRY. |