UniProt ID | LFG3_HUMAN | |
---|---|---|
UniProt AC | Q969X1 | |
Protein Name | Protein lifeguard 3 | |
Gene Name | TMBIM1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 311 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. Lysosome membrane . Endosome membrane . |
|
Protein Description | Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling.. | |
Protein Sequence | MSNPSAPPPYEDRNPLYPGPPPPGGYGQPSVLPGGYPAYPGYPQPGYGHPAGYPQPMPPTHPMPMNYGPGHGYDGEERAVSDSFGPGEWDDRKVRHTFIRKVYSIISVQLLITVAIIAIFTFVEPVSAFVRRNVAVYYVSYAVFVVTYLILACCQGPRRRFPWNIILLTLFTFAMGFMTGTISSMYQTKAVIIAMIITAVVSISVTIFCFQTKVDFTSCTGLFCVLGIVLLVTGIVTSIVLYFQYVYWLHMLYAALGAICFTLFLAYDTQLVLGNRKHTISPEDYITGALQIYTDIIYIFTFVLQLMGDRN | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSNPSAPPP ------CCCCCCCCC | 58.40 | 29255136 | |
5 | Phosphorylation | ---MSNPSAPPPYED ---CCCCCCCCCCCC | 58.62 | 29255136 | |
67 | Phosphorylation | THPMPMNYGPGHGYD CCCCCCCCCCCCCCC | 20.60 | 21253578 | |
73 | Phosphorylation | NYGPGHGYDGEERAV CCCCCCCCCCCCCCC | 18.33 | 19534553 | |
81 | Phosphorylation | DGEERAVSDSFGPGE CCCCCCCCCCCCCCC | 26.93 | 22167270 | |
83 | Phosphorylation | EERAVSDSFGPGEWD CCCCCCCCCCCCCCC | 25.29 | 23401153 | |
127 | Phosphorylation | FTFVEPVSAFVRRNV HHCCCCHHHHHHHHH | 27.06 | - |
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 LFG3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LFG3_HUMAN !! |
* 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 LFG3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LFG3_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASSSPECTROMETRY. | |
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-73, AND MASSSPECTROMETRY. |