| UniProt ID | MFAP4_HUMAN | |
|---|---|---|
| UniProt AC | P55083 | |
| Protein Name | Microfibril-associated glycoprotein 4 | |
| Gene Name | MFAP4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 255 | |
| Subcellular Localization | Secreted, extracellular space, extracellular matrix . | |
| Protein Description | Could be involved in calcium-dependent cell adhesion or intercellular interactions. May contribute to the elastic fiber assembly and/or maintenance. [PubMed: 26601954] | |
| Protein Sequence | MKALLALPLLLLLSTPPCAPQVSGIRGDALERFCLQQPLDCDDIYAQGYQSDGVYLIYPSGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWNDYKLGFGRADGEYWLGLQNMHLLTLKQKYELRVDLEDFENNTAYAKYADFSISPNAVSAEEDGYTLFVAGFEDGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA | |
| 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 |
|---|---|---|---|---|---|
| 87 | N-linked_Glycosylation | TVFQKRFNGSVSFFR EEEEEEECCCEEEEE | 45.95 | 19159218 | |
| 91 | Phosphorylation | KRFNGSVSFFRGWND EEECCCEEEEECCEE | 21.99 | 24719451 | |
| 100 | Acetylation | FRGWNDYKLGFGRAD EECCEECCEEECCCC | 45.02 | 30590399 | |
| 137 | N-linked_Glycosylation | VDLEDFENNTAYAKY CCHHHHCCCEEEEEE | 51.66 | 16335952 | |
| 244 | Phosphorylation | QWKGFYYSLKRTEMK HHHCHHHHHHHHHCC | 18.94 | 24719451 | |
| 246 | Acetylation | KGFYYSLKRTEMKIR HCHHHHHHHHHCCEE | 51.86 | 30590393 |
| 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 MFAP4_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MFAP4_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 MFAP4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MFAP4_HUMAN !! | ||||
| 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 |
| "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-87 AND ASN-137, 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-137, AND MASSSPECTROMETRY. | |
