UniProt ID | C1QA_MOUSE | |
---|---|---|
UniProt AC | P98086 | |
Protein Name | Complement C1q subcomponent subunit A | |
Gene Name | C1qa | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 245 | |
Subcellular Localization | Secreted. | |
Protein Description | C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.. | |
Protein Sequence | METSQGWLVACVLTMTLVWTVAEDVCRAPNGKDGAPGNPGRPGRPGLKGERGEPGAAGIRTGIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGPQGLKGVKGNPGNIRDQPRPAFSAIRQNPMTLGNVVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVISKWDLCLFIKSSSGGQPRDSLSFSNTNNKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLIFPSA | |
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 |
---|---|---|---|---|---|
20 | Phosphorylation | LTMTLVWTVAEDVCR HHHHHHHHHHHHHHC | 11.45 | 20139300 | |
39 | Hydroxylation | KDGAPGNPGRPGRPG CCCCCCCCCCCCCCC | 46.19 | - | |
45 | Hydroxylation | NPGRPGRPGLKGERG CCCCCCCCCCCCCCC | 59.38 | - | |
48 | Hydroxylation | RPGRPGLKGERGEPG CCCCCCCCCCCCCCC | 65.72 | - | |
48 | O-linked_Glycosylation | RPGRPGLKGERGEPG CCCCCCCCCCCCCCC | 65.72 | - | |
54 | Hydroxylation | LKGERGEPGAAGIRT CCCCCCCCCCCCHHC | 40.31 | - | |
67 | Hydroxylation | RTGIRGFKGDPGESG HCCCCCCCCCCCCCC | 66.29 | - | |
67 | O-linked_Glycosylation | RTGIRGFKGDPGESG HCCCCCCCCCCCCCC | 66.29 | - | |
79 | Hydroxylation | ESGPPGKPGNVGLPG CCCCCCCCCCCCCCC | 45.57 | - | |
85 | Hydroxylation | KPGNVGLPGPSGPLG CCCCCCCCCCCCCCC | 46.88 | - | |
100 | Hydroxylation | DSGPQGLKGVKGNPG CCCCCCCCCCCCCCC | 69.36 | - | |
100 | O-linked_Glycosylation | DSGPQGLKGVKGNPG CCCCCCCCCCCCCCC | 69.36 | - | |
146 | N-linked_Glycosylation | NQESPYQNHTGRFIC CCCCCCCCCCCCEEE | 28.92 | 16944957 |
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 C1QA_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C1QA_MOUSE !! |
* 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 C1QA_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of C1QA_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146, AND MASSSPECTROMETRY. |