UniProt ID | ICOSL_HUMAN | |
---|---|---|
UniProt AC | O75144 | |
Protein Name | ICOS ligand | |
Gene Name | ICOSLG | |
Organism | Homo sapiens (Human). | |
Sequence Length | 302 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function (By similarity).. | |
Protein Sequence | MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | LLFLLFSSLRADTQE HHHHHHHHHCCCCCH | 17.97 | 24719451 | |
56 | Phosphorylation | DVYVYWQTSESKTVV CEEEEEECCCCCEEE | 21.95 | - | |
70 | N-linked_Glycosylation | VTYHIPQNSSLENVD EEEECCCCCCCCCCC | 28.36 | 16335952 | |
102 | N-linked_Glycosylation | DFSLRLFNVTPQDEQ CEEEEEECCCCCCCH | 41.15 | 16335952 | |
137 | N-linked_Glycosylation | VTLHVAANFSVPVVS EEEEEECCCCCEEEE | 21.71 | UniProtKB CARBOHYD | |
173 | N-linked_Glycosylation | RPNVYWINKTDNSLL CCCEEEEECCCCCHH | 27.33 | UniProtKB CARBOHYD | |
186 | N-linked_Glycosylation | LLDQALQNDTVFLNM HHHHHHHCCEEEEEC | 48.01 | 16335952 | |
225 | N-linked_Glycosylation | ENVLLQQNLTVGSQT ECCHHHCCCEECCCC | 25.39 | UniProtKB CARBOHYD | |
249 | Phosphorylation | ITENPVSTGEKNAAT CCCCCCCCCCHHHHH | 49.98 | 29759185 | |
285 | Phosphorylation | RDRCLQHSYAGAWAV HHHHHCCCCCCEEEE | 12.06 | 28387310 | |
293 | Phosphorylation | YAGAWAVSPETELTG CCCEEEECCCCCCCC | 14.85 | - | |
299 | Phosphorylation | VSPETELTGHV---- ECCCCCCCCCC---- | 21.00 | 28387310 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
285 | S | Phosphorylation | Kinase | PKCA | P17252 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ICOSL_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 ICOSL_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ICOS_HUMAN | ICOS | physical | 11956294 | |
ZDHC6_HUMAN | ZDHHC6 | physical | 28514442 | |
PTPRD_HUMAN | PTPRD | physical | 28514442 | |
LEG1_HUMAN | LGALS1 | physical | 28514442 | |
C2C2L_HUMAN | C2CD2L | physical | 28514442 | |
PREB_HUMAN | PREB | physical | 28514442 | |
UPK3L_HUMAN | UPK3BL | physical | 28514442 |
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. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-102 AND ASN-186,AND MASS SPECTROMETRY. |