| UniProt ID | FHR1_HUMAN | |
|---|---|---|
| UniProt AC | Q03591 | |
| Protein Name | Complement factor H-related protein 1 | |
| Gene Name | CFHR1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 330 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. Can associate with lipoproteins and may play a role in lipid metabolism.. | |
| Protein Sequence | MWLLVSVILISRISSVGGEATFCDFPKINHGILYDEEKYKPFSQVPTGEVFYYSCEYNFVSPSKSFWTRITCTEEGWSPTPKCLRLCFFPFVENGHSESSGQTHLEGDTVQIICNTGYRLQNNENNISCVERGWSTPPKCRSTDTSCVNPPTVQNAHILSRQMSKYPSGERVRYECRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYLRTGESAEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR | |
| 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 |
|---|---|---|---|---|---|
| 126 | N-linked_Glycosylation | RLQNNENNISCVERG EECCCCCCEEEECCC | 22.75 | 18638581 | |
| 126 | N-linked_Glycosylation | RLQNNENNISCVERG EECCCCCCEEEECCC | 22.75 | 16335952 | |
| 194 | N-linked_Glycosylation | EVMCLNGNWTEPPQC EEEEECCCCCCCCCC | 41.23 | 16335952 | |
| 269 | Phosphorylation | CLHPCVISREIMENY CCCCEEECHHHHHHC | 11.94 | 27130503 | |
| 295 | Phosphorylation | LYLRTGESAEFVCKR EEECCCCCCEEEECC | 34.15 | 24505115 | |
| 304 | Phosphorylation | EFVCKRGYRLSSRSH EEEECCCCEECCCCC | 16.65 | 29759185 | |
| 307 | Phosphorylation | CKRGYRLSSRSHTLR ECCCCEECCCCCEEE | 18.08 | 29759185 | |
| 308 | Phosphorylation | KRGYRLSSRSHTLRT CCCCEECCCCCEEEE | 42.25 | 29759185 |
| 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 FHR1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FHR1_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 FHR1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PRDX4_HUMAN | PRDX4 | 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. | ||||||
loading...
| N-linked Glycosylation | |
| Reference | PubMed |
| "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-126 AND ASN-194, AND MASSSPECTROMETRY. | |
