UniProt ID | GILT_HUMAN | |
---|---|---|
UniProt AC | P13284 | |
Protein Name | Gamma-interferon-inducible lysosomal thiol reductase | |
Gene Name | IFI30 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 250 | |
Subcellular Localization | Secreted . Lysosome . | |
Protein Description | Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity).. | |
Protein Sequence | MTLSPLLLFLPPLLLLLDVPTAAVQASPLQALDFFGNGPPVNYKTGNLYLRGPLKKSNAPLVNVTLYYEALCGGCRAFLIRELFPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACVLDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDRGMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGKKPDVCPSSTSSLRSVCFK | |
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 |
---|---|---|---|---|---|
45 | Phosphorylation | GPPVNYKTGNLYLRG CCCCCCCCCCEEEEC | 22.42 | 18187866 | |
63 | N-linked_Glycosylation | KSNAPLVNVTLYYEA CCCCCCEEEEHHHHH | 28.83 | UniProtKB CARBOHYD | |
95 | N-linked_Glycosylation | LLVMEILNVTLVPYG HHHHHHHCCEEEECC | 30.32 | UniProtKB CARBOHYD | |
108 | N-linked_Glycosylation | YGNAQEQNVSGRWEF CCCCCCCCCCCCEEE | 29.21 | UniProtKB CARBOHYD | |
116 | Acetylation | VSGRWEFKCQHGEEE CCCCEEEEECCCCCC | 22.82 | 27178108 |
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 GILT_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GILT_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 GILT_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. |
loading...
Phosphorylation | |
Reference | PubMed |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND MASSSPECTROMETRY. |