UniProt ID | LEMD2_MOUSE | |
---|---|---|
UniProt AC | Q6DVA0 | |
Protein Name | LEM domain-containing protein 2 | |
Gene Name | Lemd2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 511 | |
Subcellular Localization |
Nucleus inner membrane Multi-pass membrane protein . Lamina-associated protein residing in the inner nuclear membrane (INM). Localized exclusively to the nuclear envelope, giving rise to a typical rim-like staining of the nuclear periphery. |
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Protein Description | Involved in nuclear structure organization. [PubMed: 16339967 Required for maintaining the integrity of the nuclear envelope (By similarity; Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT] | |
Protein Sequence | MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPLRARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPDRHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANVTSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER | |
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 | Acetylation | ------MAGLSDLEL ------CCCCCHHHH | 27.86 | - | |
5 | Phosphorylation | ---MAGLSDLELRRE ---CCCCCHHHHHHH | 38.95 | 30352176 | |
87 | Phosphorylation | LRARPAASVLRSEPW CCCCCHHHHHHCCCC | 24.64 | 29176673 | |
99 | Phosphorylation | EPWPLSPSPPAPSAA CCCCCCCCCCCCCCC | 39.89 | - | |
113 | Phosphorylation | ASDASGPYGNFGASA CCCCCCCCCCCCCCC | 28.38 | - | |
130 | Phosphorylation | WAASRGLSYPPHAGP HHHHCCCCCCCCCCC | 38.12 | 28833060 | |
131 | Phosphorylation | AASRGLSYPPHAGPG HHHCCCCCCCCCCCC | 26.31 | 28833060 | |
145 | Phosphorylation | GPLRRRASVRGSSED CCCCCCCCCCCCCCC | 15.55 | 25521595 | |
149 | Phosphorylation | RRASVRGSSEDDEDT CCCCCCCCCCCCCCC | 21.71 | 25521595 | |
150 | Phosphorylation | RASVRGSSEDDEDTR CCCCCCCCCCCCCCC | 48.12 | 25521595 | |
156 | Phosphorylation | SSEDDEDTRTPDRHA CCCCCCCCCCCCCCC | 34.10 | 27087446 | |
158 | Phosphorylation | EDDEDTRTPDRHAPG CCCCCCCCCCCCCCC | 31.47 | 25159016 | |
182 | Phosphorylation | SASARPHSALLGADA CCCCCCCHHHCCCCC | 24.24 | 26824392 | |
196 | Phosphorylation | ARPGLKGSRTGSAGA CCCCCCCCCCCCCCC | 25.69 | 26824392 | |
366 | Phosphorylation | DKVVCLESARPRMGI CEEEEHHCCCCCCCC | 19.34 | - | |
444 | Phosphorylation | WEQDMERYPYVGILH HHHHHHHCCEEEEEE | 5.89 | - | |
501 | Phosphorylation | DMLVWRWTKPSSFSD CEEEEEECCCCCCCC | 25.22 | 25619855 | |
504 | Phosphorylation | VWRWTKPSSFSDSER EEEECCCCCCCCCCC | 45.64 | 27742792 | |
505 | Phosphorylation | WRWTKPSSFSDSER- EEECCCCCCCCCCC- | 36.98 | 27742792 | |
507 | Phosphorylation | WTKPSSFSDSER--- ECCCCCCCCCCC--- | 42.02 | 26824392 | |
509 | Phosphorylation | KPSSFSDSER----- CCCCCCCCCC----- | 33.79 | 27742792 |
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 LEMD2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LEMD2_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 LEMD2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LEMD2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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