| UniProt ID | LRRF2_MOUSE | |
|---|---|---|
| UniProt AC | Q91WK0 | |
| Protein Name | Leucine-rich repeat flightless-interacting protein 2 | |
| Gene Name | Lrrfip2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 415 | |
| Subcellular Localization | ||
| Protein Description | May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity).. | |
| Protein Sequence | MGTPGSGRKRTPVKDRFSAEDEALSNIAREAEARLAAKRAARAEARDIRMRELERQQREGVEDTLSLRSLGSHRLDEKSDKQYAENYTRPSSRNSASATTPLSGQSSRRGSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ | |
| 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 |
|---|---|---|---|---|---|
| 11 | Phosphorylation | PGSGRKRTPVKDRFS CCCCCCCCCCCCCCC | 35.15 | - | |
| 18 | Phosphorylation | TPVKDRFSAEDEALS CCCCCCCCHHHHHHH | 31.48 | 26824392 | |
| 68 (in isoform 2) | Phosphorylation | - | 26.85 | 29514104 | |
| 79 | Phosphorylation | SHRLDEKSDKQYAEN CCCCCHHHHHHHHHH | 48.25 | 25777480 | |
| 83 | Phosphorylation | DEKSDKQYAENYTRP CHHHHHHHHHHCCCC | 22.94 | 25777480 | |
| 87 | Phosphorylation | DKQYAENYTRPSSRN HHHHHHHCCCCCCCC | 8.81 | 25777480 | |
| 88 | Phosphorylation | KQYAENYTRPSSRNS HHHHHHCCCCCCCCC | 47.92 | 24899341 | |
| 91 | Phosphorylation | AENYTRPSSRNSASA HHHCCCCCCCCCCCC | 38.34 | 25266776 | |
| 92 | Phosphorylation | ENYTRPSSRNSASAT HHCCCCCCCCCCCCC | 37.86 | 27742792 | |
| 95 | Phosphorylation | TRPSSRNSASATTPL CCCCCCCCCCCCCCC | 23.61 | 21183079 | |
| 100 | Phosphorylation | RNSASATTPLSGQSS CCCCCCCCCCCCCCC | 23.19 | - | |
| 103 | Phosphorylation | ASATTPLSGQSSRRG CCCCCCCCCCCCCCC | 35.67 | - | |
| 106 | Phosphorylation | TTPLSGQSSRRGSGD CCCCCCCCCCCCCCC | 29.36 | - | |
| 107 | Phosphorylation | TPLSGQSSRRGSGDT CCCCCCCCCCCCCCH | 20.36 | - | |
| 111 | Phosphorylation | GQSSRRGSGDTSSLI CCCCCCCCCCHHHCC | 31.51 | 24925903 | |
| 114 | Phosphorylation | SRRGSGDTSSLIDPD CCCCCCCHHHCCCCC | 24.60 | 24925903 | |
| 115 | Phosphorylation | RRGSGDTSSLIDPDT CCCCCCHHHCCCCCC | 28.08 | 24925903 | |
| 116 | Phosphorylation | RGSGDTSSLIDPDTS CCCCCHHHCCCCCCC | 31.28 | 24925903 | |
| 122 | Phosphorylation | SSLIDPDTSLSELRE HHCCCCCCCHHHHHH | 36.63 | 25619855 | |
| 123 | Phosphorylation | SLIDPDTSLSELRES HCCCCCCCHHHHHHH | 36.96 | 25619855 | |
| 125 | Phosphorylation | IDPDTSLSELRESLS CCCCCCHHHHHHHHH | 34.06 | 25619855 | |
| 299 | Phosphorylation | CSRNDGMSGDLAGLQ HHCCCCCCHHCCCCC | 34.38 | 22802335 | |
| 375 | Acetylation | ELKAERRKLQRELRT HHHHHHHHHHHHHHH | 56.01 | 8440431 |
| 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 LRRF2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LRRF2_MOUSE !! | ||||||
* 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 LRRF2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of LRRF2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114 AND SER-116, ANDMASS SPECTROMETRY. | |