UniProt ID | FCN1_HUMAN | |
---|---|---|
UniProt AC | O00602 | |
Protein Name | Ficolin-1 | |
Gene Name | FCN1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 326 | |
Subcellular Localization |
Secreted . Cell membrane Peripheral membrane protein Extracellular side . Found on the monocyte and granulocyte surface (PubMed:20400674). |
|
Protein Description | Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. [PubMed: 21037097 Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage.] | |
Protein Sequence | MELSGATMARGLAVLLVLFLHIKNLPAQAADTCPEVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQSQSCATGPRNCKDLLDRGYFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNIHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSEMKVRPA | |
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 |
---|---|---|---|---|---|
110 | Phosphorylation | GDAGQSQSCATGPRN CCCCCCCCCCCCCCC | 15.80 | 29083192 | |
113 | Phosphorylation | GQSQSCATGPRNCKD CCCCCCCCCCCCHHH | 52.63 | 29083192 | |
197 | Phosphorylation | NDNIHALTAQGSSEL CCCEEEEECCCCCEE | 20.09 | 24043423 | |
201 | Phosphorylation | HALTAQGSSELRVDL EEEECCCCCEEEEEE | 14.46 | 24043423 | |
202 | Phosphorylation | ALTAQGSSELRVDLV EEECCCCCEEEEEEE | 47.69 | 24043423 | |
305 | N-linked_Glycosylation | ESYANGINWSAAKGY HHHCCCCCHHHCCCC | 28.22 | UniProtKB CARBOHYD | |
312 | Phosphorylation | NWSAAKGYKYSYKVS CHHHCCCCCEEEEEE | 13.17 | 24719451 | |
319 | Phosphorylation | YKYSYKVSEMKVRPA CCEEEEEEEEEEECC | 28.02 | 24719451 |
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 FCN1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FCN1_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 FCN1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ELN_HUMAN | ELN | physical | 8947836 | |
K319L_HUMAN | KIAA0319L | physical | 26186194 | |
DJC13_HUMAN | DNAJC13 | physical | 26186194 | |
PTPRA_HUMAN | PTPRA | physical | 26186194 | |
POTEF_HUMAN | POTEF | physical | 26186194 | |
GT252_HUMAN | COLGALT2 | physical | 26186194 | |
PTPRG_HUMAN | PTPRG | physical | 26186194 | |
PODXL_HUMAN | PODXL | physical | 26186194 | |
FCN2_HUMAN | FCN2 | physical | 26186194 | |
SUSD5_HUMAN | SUSD5 | physical | 26186194 | |
FBLN1_HUMAN | FBLN1 | physical | 26186194 | |
SE6L2_HUMAN | SEZ6L2 | physical | 26186194 | |
K1549_HUMAN | KIAA1549 | physical | 26186194 | |
FCN2_HUMAN | FCN2 | physical | 28514442 | |
SUSD5_HUMAN | SUSD5 | physical | 28514442 | |
SE6L2_HUMAN | SEZ6L2 | physical | 28514442 | |
PODXL_HUMAN | PODXL | physical | 28514442 | |
DJC13_HUMAN | DNAJC13 | physical | 28514442 | |
K319L_HUMAN | KIAA0319L | physical | 28514442 | |
PTPRA_HUMAN | PTPRA | physical | 28514442 | |
PTPRG_HUMAN | PTPRG | physical | 28514442 | |
K1549_HUMAN | KIAA1549 | physical | 28514442 | |
POTEF_HUMAN | POTEF | physical | 28514442 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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