UniProt ID | TSN1_HUMAN | |
---|---|---|
UniProt AC | O60635 | |
Protein Name | Tetraspanin-1 | |
Gene Name | TSPAN1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 241 | |
Subcellular Localization |
Lysosome membrane Multi-pass membrane protein . |
|
Protein Description | ||
Protein Sequence | MQCFSFIKTMMILFNLLIFLCGAALLAVGIWVSIDGASFLKIFGPLSSSAMQFVNVGYFLIAAGVVVFALGFLGCYGAKTESKCALVTFFFILLLIFIAEVAAAVVALVYTTMAEHFLTLLVVPAIKKDYGSQEDFTQVWNTTMKGLKCCGFTNYTDFEDSPYFKENSAFPPFCCNDNVTNTANETCTKQKAHDQKVEGCFNQLLYDIRTNAVTVGGVAAGIGGLELAAMIVSMYLYCNLQ | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MQCFSFIKTMMI ---CCHHHHHHHHHH | 33.42 | 24719451 | |
38 | Phosphorylation | WVSIDGASFLKIFGP HHEECCCHHHHHHCC | 36.32 | 24961811 | |
141 | N-linked_Glycosylation | EDFTQVWNTTMKGLK HHHHHHHHHHCCCCE | 27.15 | 19508227 | |
141 | N-linked_Glycosylation | EDFTQVWNTTMKGLK HHHHHHHHHHCCCCE | 27.15 | 19508227 | |
154 | N-linked_Glycosylation | LKCCGFTNYTDFEDS CEECCCCCCCCCCCC | 35.13 | 19508227 | |
154 | N-linked_Glycosylation | LKCCGFTNYTDFEDS CEECCCCCCCCCCCC | 35.13 | 19508227 | |
155 | Phosphorylation | KCCGFTNYTDFEDSP EECCCCCCCCCCCCC | 12.48 | - | |
156 | Phosphorylation | CCGFTNYTDFEDSPY ECCCCCCCCCCCCCC | 35.96 | - | |
178 | N-linked_Glycosylation | PPFCCNDNVTNTANE CCCCCCCCCCCCCCH | 28.64 | 19508227 | |
178 | N-linked_Glycosylation | PPFCCNDNVTNTANE CCCCCCCCCCCCCCH | 28.64 | 19508227 | |
184 | N-linked_Glycosylation | DNVTNTANETCTKQK CCCCCCCCHHHHCHH | 42.97 | 19508227 | |
184 | N-linked_Glycosylation | DNVTNTANETCTKQK CCCCCCCCHHHHCHH | 42.97 | 19508227 | |
196 | Ubiquitination | KQKAHDQKVEGCFNQ CHHHHHHHHHHHHHH | 48.59 | 29901268 | |
210 | Phosphorylation | QLLYDIRTNAVTVGG HHHHHHHCCCEEECH | 28.06 | 27174698 | |
214 | Phosphorylation | DIRTNAVTVGGVAAG HHHCCCEEECHHHHC | 15.83 | 27174698 |
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 TSN1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSN1_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 TSN1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of TSN1_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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N-linked Glycosylation | |
Reference | PubMed |
"Glycosylation of tetraspanin Tspan-1 at four distinct sites promotesits transition through the endoplasmic reticulum."; Scholz C.-J., Sauer G., Deissler H.; Protein Pept. Lett. 16:1244-1248(2009). Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-141; ASN-154; ASN-178 ANDASN-184, AND MUTAGENESIS OF ASN-141; ASN-154; ASN-178 AND ASN-184. |