| UniProt ID | C1S_HUMAN | |
|---|---|---|
| UniProt AC | P09871 | |
| Protein Name | Complement C1s subcomponent | |
| Gene Name | C1S | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 688 | |
| Subcellular Localization | ||
| Protein Description | C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.. | |
| Protein Sequence | MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED | |
| 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 |
|---|---|---|---|---|---|
| 115 | Phosphorylation | VIFKSDFSNEERFTG EEECCCCCCCCCCCE | 48.61 | 24505115 | |
| 149 | Hydroxylation | PCSHFCNNFIGGYFC CHHHHCCCCCCCCCC | 30.97 | 2141278 | |
| 174 | N-linked_Glycosylation | DMKNCGVNCSGDVFT HHHHCCCCCCHHHHH | 10.26 | 1533159 | |
| 174 | N-linked_Glycosylation | DMKNCGVNCSGDVFT HHHHCCCCCCHHHHH | 10.26 | 2141278 | |
| 320 | Phosphorylation | FRDVVQITCLDGFEV EECEEEEEEECCEEE | 7.02 | 22210691 | |
| 343 | Phosphorylation | SFYSTCQSNGKWSNS CHHHHHHHCCCCCCC | 50.09 | 22210691 | |
| 406 | N-linked_Glycosylation | GEYHCAGNGSWVNEV CCEECCCCCCCCCCC | 23.85 | 19159218 | |
| 442 | Phosphorylation | KQRIIGGSDADIKNF HCCCCCCCCCCCCCC | 25.14 | - | |
| 486 | Phosphorylation | GNREPTMYVGSTSVQ CCCCCEEEECCCCCC | 12.25 | - | |
| 575 | Acetylation | SGWGRTEKRDRAVRL CCCCCCCCHHHHHHH | 60.01 | 20167786 | |
| 648 | Phosphorylation | PNDKTKFYAAGLVSW CCCCCCEEEEEEEEE | 9.33 | - | |
| 662 | Phosphorylation | WGPQCGTYGLYTRVK ECCCCCCCCHHHHHH | 7.16 | - | |
| 683 | Phosphorylation | MKTMQENSTPRED-- HHHHHHCCCCCCC-- | 38.75 | 29496963 |
| 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 C1S_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C1S_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 C1S_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| C1R_HUMAN | C1R | physical | 10092586 | |
| C1R_HUMAN | C1R | physical | 10878362 | |
| C1R_HUMAN | C1R | physical | 28514442 | |
| CCDC6_HUMAN | CCDC6 | physical | 28514442 | |
| PP4R1_HUMAN | PPP4R1 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 613783 | Complement component C1s deficiency (C1SD) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Hydroxylation | |
| Reference | PubMed |
| "Chemical and functional characterization of a fragment of C1-scontaining the epidermal growth factor homology region."; Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.; Biochemistry 29:3570-3578(1990). Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATIONAT ASN-149. | |
| N-linked Glycosylation | |
| Reference | PubMed |
| "X-ray structure of the Ca2+-binding interaction domain of C1s.Insights into the assembly of the C1 complex of complement."; Gregory L.A., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C.,Gaboriaud C.; J. Biol. Chem. 278:32157-32164(2003). Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDINGSITES, AND GLYCOSYLATION AT ASN-406. | |
| "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-174 AND ASN-406, 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-406, AND MASSSPECTROMETRY. | |
| "Chemical and functional characterization of a fragment of C1-scontaining the epidermal growth factor homology region."; Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.; Biochemistry 29:3570-3578(1990). Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATIONAT ASN-149. | |
