UniProt ID | LEGL_HUMAN | |
---|---|---|
UniProt AC | Q3ZCW2 | |
Protein Name | Galectin-related protein | |
Gene Name | LGALSL | |
Organism | Homo sapiens (Human). | |
Sequence Length | 172 | |
Subcellular Localization | ||
Protein Description | Does not bind lactose, and may not bind carbohydrates.. | |
Protein Sequence | MAGSVADSDAVVKLDDGHLNNSLSSPVQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG | |
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 | ------MAGSVADSD ------CCCCCCCCC | 20.97 | 19413330 | |
4 | Phosphorylation | ----MAGSVADSDAV ----CCCCCCCCCCE | 12.47 | 27732954 | |
8 | Phosphorylation | MAGSVADSDAVVKLD CCCCCCCCCCEEECC | 20.10 | 28450419 | |
22 | Phosphorylation | DDGHLNNSLSSPVQA CCCCCCCCCCCCCCC | 28.67 | 30266825 | |
24 | Phosphorylation | GHLNNSLSSPVQADV CCCCCCCCCCCCCCE | 32.20 | 30266825 | |
25 | Phosphorylation | HLNNSLSSPVQADVY CCCCCCCCCCCCCEE | 34.09 | 29255136 | |
32 | Phosphorylation | SPVQADVYFPRLIVP CCCCCCEEECCEECC | 14.38 | 22199227 |
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 LEGL_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LEGL_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 LEGL_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LEGL_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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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-25, AND MASSSPECTROMETRY. |