UniProt ID | TSN4_HUMAN | |
---|---|---|
UniProt AC | O14817 | |
Protein Name | Tetraspanin-4 | |
Gene Name | TSPAN4 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 238 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | ||
Protein Sequence | MARACLQAVKYLMFAFNLLFWLGGCGVLGVGIWLAATQGSFATLSSSFPSLSAANLLIITGAFVMAIGFVGCLGAIKENKCLLLTFFLLLLLVFLLEATIAILFFAYTDKIDRYAQQDLKKGLHLYGTQGNVGLTNAWSIIQTDFRCCGVSNYTDWFEVYNATRVPDSCCLEFSESCGLHAPGTWWKAPCYETVKVWLQENLLAVGIFGLCTALVQILGLTFAMTMYCQVVKADTYCA | |
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 |
---|---|---|---|---|---|
120 | Acetylation | RYAQQDLKKGLHLYG HHHHHHHHHCCEEEE | 53.75 | 27452117 | |
128 | Phosphorylation | KGLHLYGTQGNVGLT HCCEEEECCCCCCCC | 21.53 | 22210691 | |
135 | Phosphorylation | TQGNVGLTNAWSIIQ CCCCCCCCCCHHHHH | 19.57 | 22210691 | |
143 | Phosphorylation | NAWSIIQTDFRCCGV CCHHHHHCCCCCCCC | 27.05 | 22210691 | |
152 | N-linked_Glycosylation | FRCCGVSNYTDWFEV CCCCCCCCCCCHHHH | 41.12 | UniProtKB CARBOHYD | |
161 | N-linked_Glycosylation | TDWFEVYNATRVPDS CCHHHHHCCCCCCCC | 39.76 | 19159218 | |
168 | Phosphorylation | NATRVPDSCCLEFSE CCCCCCCCEEEEEHH | 10.72 | 26307563 | |
174 | Phosphorylation | DSCCLEFSESCGLHA CCEEEEEHHHCCCCC | 21.16 | 26307563 | |
176 | Phosphorylation | CCLEFSESCGLHAPG EEEEEHHHCCCCCCC | 16.58 | 26307563 | |
184 | Phosphorylation | CGLHAPGTWWKAPCY CCCCCCCCCCCCCCH | 27.39 | 26307563 | |
191 | Phosphorylation | TWWKAPCYETVKVWL CCCCCCCHHHHHHHH | 17.36 | 26307563 | |
193 | Phosphorylation | WKAPCYETVKVWLQE CCCCCHHHHHHHHHH | 10.11 | 26307563 | |
228 | S-palmitoylation | TFAMTMYCQVVKADT HHHHHHHHHHHCCCC | 1.39 | 29575903 |
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 TSN4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSN4_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 TSN4_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CD9_HUMAN | CD9 | physical | 9360996 | |
CD81_HUMAN | CD81 | physical | 9360996 | |
ITA3_HUMAN | ITGA3 | physical | 9360996 | |
ITA6_HUMAN | ITGA6 | physical | 9360996 | |
ITB1_HUMAN | ITGB1 | physical | 9360996 | |
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 |
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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161, AND MASSSPECTROMETRY. |