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 | ||
* 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 | ||||||
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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. |