ICOSL_HUMAN - dbPTM
ICOSL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
15PhosphorylationLLFLLFSSLRADTQE
HHHHHHHHHCCCCCH
17.9724719451
56PhosphorylationDVYVYWQTSESKTVV
CEEEEEECCCCCEEE
21.95-
70N-linked_GlycosylationVTYHIPQNSSLENVD
EEEECCCCCCCCCCC
28.3616335952
102N-linked_GlycosylationDFSLRLFNVTPQDEQ
CEEEEEECCCCCCCH
41.1516335952
137N-linked_GlycosylationVTLHVAANFSVPVVS
EEEEEECCCCCEEEE
21.71UniProtKB CARBOHYD
173N-linked_GlycosylationRPNVYWINKTDNSLL
CCCEEEEECCCCCHH
27.33UniProtKB CARBOHYD
186N-linked_GlycosylationLLDQALQNDTVFLNM
HHHHHHHCCEEEEEC
48.0116335952
225N-linked_GlycosylationENVLLQQNLTVGSQT
ECCHHHCCCEECCCC
25.39UniProtKB CARBOHYD
249PhosphorylationITENPVSTGEKNAAT
CCCCCCCCCCHHHHH
49.9829759185
285PhosphorylationRDRCLQHSYAGAWAV
HHHHHCCCCCCEEEE
12.0628387310
293PhosphorylationYAGAWAVSPETELTG
CCCEEEECCCCCCCC
14.85-
299PhosphorylationVSPETELTGHV----
ECCCCCCCCCC----
21.0028387310

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
285SPhosphorylationKinasePKCAP17252
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ICOSL_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ICOS_HUMANICOSphysical
11956294
ZDHC6_HUMANZDHHC6physical
28514442
PTPRD_HUMANPTPRDphysical
28514442
LEG1_HUMANLGALS1physical
28514442
C2C2L_HUMANC2CD2Lphysical
28514442
PREB_HUMANPREBphysical
28514442
UPK3L_HUMANUPK3BLphysical
28514442

Drug and Disease Associations
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.
Regulatory Network of ICOSL_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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