| UniProt ID | C4BPA_HUMAN | |
|---|---|---|
| UniProt AC | P04003 | |
| Protein Name | C4b-binding protein alpha chain | |
| Gene Name | C4BPA | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 597 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.. | |
| Protein Sequence | MHPPKTPSGALHRKRKMAAWPFSRLWKVSDPILFQMTLIAALLPAVLGNCGPPPTLSFAAPMDITLTETRFKTGTTLKYTCLPGYVRSHSTQTLTCNSDGEWVYNTFCIYKRCRHPGELRNGQVEIKTDLSFGSQIEFSCSEGFFLIGSTTSRCEVQDRGVGWSHPLPQCEIVKCKPPPDIRNGRHSGEENFYAYGFSVTYSCDPRFSLLGHASISCTVENETIGVWRPSPPTCEKITCRKPDVSHGEMVSGFGPIYNYKDTIVFKCQKGFVLRGSSVIHCDADSKWNPSPPACEPNSCINLPDIPHASWETYPRPTKEDVYVVGTVLRYRCHPGYKPTTDEPTTVICQKNLRWTPYQGCEALCCPEPKLNNGEITQHRKSRPANHCVYFYGDEISFSCHETSRFSAICQGDGTWSPRTPSCGDICNFPPKIAHGHYKQSSSYSFFKEEIIYECDKGYILVGQAKLSCSYSHWSAPAPQCKALCRKPELVNGRLSVDKDQYVEPENVTIQCDSGYGVVGPQSITCSGNRTWYPEVPKCEWETPEGCEQVLTGKRLMQCLPNPEDVKMALEVYKLSLEIEQLELQRDSARQSTLDKEL | |
| 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 |
|---|---|---|---|---|---|
| 55 | O-linked_Glycosylation | GNCGPPPTLSFAAPM CCCCCCCCCCCCCCC | 40.59 | OGP | |
| 57 | O-linked_Glycosylation | CGPPPTLSFAAPMDI CCCCCCCCCCCCCEE | 18.47 | OGP | |
| 187 | Phosphorylation | DIRNGRHSGEENFYA CCCCCCCCCCCCEEE | 46.68 | 27130503 | |
| 193 | Phosphorylation | HSGEENFYAYGFSVT CCCCCCEEEEEEEEE | 15.53 | 28270605 | |
| 195 | Phosphorylation | GEENFYAYGFSVTYS CCCCEEEEEEEEEEE | 13.81 | 28270605 | |
| 221 | N-linked_Glycosylation | SISCTVENETIGVWR EEEEEEECCEEEEEC | 47.58 | 16335952 | |
| 221 | N-linked_Glycosylation | SISCTVENETIGVWR EEEEEEECCEEEEEC | 47.58 | 17623646 | |
| 230 | O-linked_Glycosylation | TIGVWRPSPPTCEKI EEEEECCCCCCCCEE | 34.63 | OGP | |
| 317 | O-linked_Glycosylation | WETYPRPTKEDVYVV CCCCCCCCCCCEEEE | 48.63 | OGP | |
| 340 | O-linked_Glycosylation | HPGYKPTTDEPTTVI CCCCCCCCCCCCEEE | 47.06 | OGP | |
| 416 | Phosphorylation | CQGDGTWSPRTPSCG ECCCCCCCCCCCCCC | 12.35 | 24719451 | |
| 469 | Phosphorylation | GQAKLSCSYSHWSAP EEEEEEECCCCCCCC | 26.71 | - | |
| 470 | Phosphorylation | QAKLSCSYSHWSAPA EEEEEECCCCCCCCC | 14.64 | - | |
| 471 | Phosphorylation | AKLSCSYSHWSAPAP EEEEECCCCCCCCCH | 11.37 | - | |
| 474 | Phosphorylation | SCSYSHWSAPAPQCK EECCCCCCCCCHHHH | 20.96 | - | |
| 495 | Phosphorylation | ELVNGRLSVDKDQYV CCCCCEECCCHHHCC | 27.23 | - | |
| 506 | N-linked_Glycosylation | DQYVEPENVTIQCDS HHCCCCCCEEEEECC | 47.12 | 3840370 | |
| 506 | N-linked_Glycosylation | DQYVEPENVTIQCDS HHCCCCCCEEEEECC | 47.12 | 16335952 | |
| 528 | N-linked_Glycosylation | QSITCSGNRTWYPEV CEEEECCCCEECCCC | 23.16 | 3840370 | |
| 528 | N-linked_Glycosylation | QSITCSGNRTWYPEV CEEEECCCCEECCCC | 23.16 | 14760718 |
| 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 C4BPA_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C4BPA_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 C4BPA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SAMP_HUMAN | APCS | physical | 7592941 | |
| SAMP_HUMAN | APCS | physical | 12100475 | |
| FXYD6_HUMAN | FXYD6 | physical | 21988832 | |
| GTF2I_HUMAN | GTF2I | physical | 21988832 | |
| LBP_HUMAN | LBP | physical | 21988832 | |
| SMRD1_HUMAN | SMARCD1 | physical | 21988832 | |
| GIT2_HUMAN | GIT2 | physical | 21988832 |
| 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-221 AND ASN-506, 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-221 AND ASN-506, AND MASSSPECTROMETRY. | |
| "Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-506 AND ASN-528, AND MASSSPECTROMETRY. | |
| "Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of thehuman complement system."; Chung L.P., Bentley D.R., Reid K.B.M.; Biochem. J. 230:133-141(1985). Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-597. | |
