| UniProt ID | SEPP1_HUMAN | |
|---|---|---|
| UniProt AC | P49908 | |
| Protein Name | Selenoprotein P {ECO:0000303|PubMed:27645994} | |
| Gene Name | SELENOP {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:10751} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 381 | |
| Subcellular Localization | Secreted . Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium. | |
| Protein Description | Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.. | |
| Protein Sequence | MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASUYLCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSUCCHCRHLIFEKTGSAITUQCKENLPSLCSUQGLRAEENITESCQURLPPAAUQISQQLIPTEASASURUKNQAKKUEUPSN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 46 | N-linked_Glycosylation | QDPMLNSNGSVTVVA CCCCCCCCCCEEHHH | 45.76 | UniProtKB CARBOHYD | |
| 81 | Phosphorylation | VKLKKEGYSNISYIV HHHHHCCCCCEEEEE | 10.31 | 29759185 | |
| 82 | Phosphorylation | KLKKEGYSNISYIVV HHHHCCCCCEEEEEE | 38.25 | 29759185 | |
| 83 | N-linked_Glycosylation | LKKEGYSNISYIVVN HHHCCCCCEEEEEEC | 20.81 | 18638581 | |
| 85 | Phosphorylation | KEGYSNISYIVVNHQ HCCCCCEEEEEECCC | 17.04 | 29759185 | |
| 86 | Phosphorylation | EGYSNISYIVVNHQG CCCCCEEEEEECCCC | 8.24 | 29759185 | |
| 96 | Phosphorylation | VNHQGISSRLKYTHL ECCCCHHHHHHHHHH | 39.45 | 29759185 | |
| 119 | N-linked_Glycosylation | PVYQQEENQTDVWTL CCEECCCCCCCHHHH | 49.66 | 16335952 | |
| 128 | N-linked_Glycosylation | TDVWTLLNGSKDDFL CCHHHHHCCCCCCEE | 56.66 | 16335952 | |
| 174 | N-linked_Glycosylation | YCEKKCGNCSLTTLK HCCCCCCCCCCCCCC | 22.98 | UniProtKB CARBOHYD | |
| 190 | Phosphorylation | EDFCKRVSLATVDKT HHHHHCCEEEEECCC | 19.13 | - | |
| 193 | O-linked_Glycosylation | CKRVSLATVDKTVET HHCCEEEEECCCCCC | 34.23 | OGP | |
| 236 | O-linked_Glycosylation | PGAPNAPTHPAPPGL CCCCCCCCCCCCCCC | 37.77 | OGP | |
| 266 | Phosphorylation | ENRDMPASEDLQDLQ CCCCCCCCHHHHHHH | 26.27 | 23911959 | |
| 291 | Phosphorylation | QLLCKLPTDSELAPR HHHHCCCCCCCCCCC | 63.69 | 26270265 | |
| 291 | O-linked_Glycosylation | QLLCKLPTDSELAPR HHHHCCCCCCCCCCC | 63.69 | OGP | |
| 293 | Phosphorylation | LCKLPTDSELAPRSU HHCCCCCCCCCCCCC | 36.67 | 28857561 | |
| 293 | O-linked_Glycosylation | LCKLPTDSELAPRSU HHCCCCCCCCCCCCC | 36.67 | OGP | |
| 296 | Phosphorylation | LPTDSELAPRSUCCH CCCCCCCCCCCCCCC | 8.07 | 24719451 | |
| 338 | N-linked_Glycosylation | QGLRAEENITESCQU CCCCCHHHCCHHHCC | 37.68 | UniProtKB CARBOHYD |
| 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 SEPP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEPP1_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 SEPP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SEPP1_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 |
| "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-83 AND ASN-119, AND MASSSPECTROMETRY. | |
| "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-83; ASN-119 AND ASN-128,AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "An initial characterization of the serum phosphoproteome."; Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III; J. Proteome Res. 8:5523-5531(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, TISSUE SPECIFICITY,AND MASS SPECTROMETRY. | |
