UniProt ID | FBLN3_HUMAN | |
---|---|---|
UniProt AC | Q12805 | |
Protein Name | EGF-containing fibulin-like extracellular matrix protein 1 | |
Gene Name | EFEMP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 493 | |
Subcellular Localization | Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. Localizes to the lamina propria underneath the olfactory epithelium.. | |
Protein Description | Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.. | |
Protein Sequence | MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETQPAEGTSGATTGVVAASSMATSGVLPGGGFVASAAAVAGPEMQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQCPPGYQKRGEQCVDIDECTIPPYCHQRCVNTPGSFYCQCSPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPRNPCQDPYILTPENRCVCPVSNAMCRELPQSIVYKYMSIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLSGPREHIVDLEMLTVSSIGTFRTSSVLRLTIIVGPFSF | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MLKALFLTMLTLALV CHHHHHHHHHHHHHH | 11.64 | 26074081 | |
11 | Phosphorylation | ALFLTMLTLALVKSQ HHHHHHHHHHHHHCC | 10.12 | 26074081 | |
33 | Phosphorylation | YTQCTDGYEWDPVRQ EEECCCCCCCCHHHH | 19.36 | - | |
88 | O-linked_Glycosylation | NEQPQQETQPAEGTS CCCCCCCCCCCCCCC | 35.20 | OGP | |
98 | O-linked_Glycosylation | AEGTSGATTGVVAAS CCCCCCCCHHHEEEE | 27.84 | OGP | |
105 | O-linked_Glycosylation | TTGVVAASSMATSGV CHHHEEEECCCCCCC | 15.77 | OGP | |
106 | O-linked_Glycosylation | TGVVAASSMATSGVL HHHEEEECCCCCCCC | 14.01 | OGP | |
109 | O-linked_Glycosylation | VAASSMATSGVLPGG EEEECCCCCCCCCCC | 19.85 | OGP | |
110 | O-linked_Glycosylation | AASSMATSGVLPGGG EEECCCCCCCCCCCC | 19.84 | OGP | |
121 | O-linked_Glycosylation | PGGGFVASAAAVAGP CCCCHHHCCHHHHCC | 17.09 | OGP | |
149 | Ubiquitination | NPADPQRIPSNPSHR CCCCCCCCCCCHHHC | 3.55 | - | |
151 | Phosphorylation | ADPQRIPSNPSHRIQ CCCCCCCCCHHHCCC | 60.03 | - | |
207 | Ubiquitination | QCPPGYQKRGEQCVD CCCCCCCCCCCCCCC | 54.62 | - | |
249 | N-linked_Glycosylation | GFQLAANNYTCVDIN CCEEECCCEEEEEHH | 28.85 | UniProtKB CARBOHYD | |
397 | Phosphorylation | PQSIVYKYMSIRSDR CHHHHHHHHCCCCCC | 4.38 | - | |
408 | Phosphorylation | RSDRSVPSDIFQIQA CCCCCCCCCCEEEEE | 40.98 | - | |
425 | Phosphorylation | IYANTINTFRIKSGN EECCCCEEEEEECCC | 15.50 | - | |
442 | Phosphorylation | GEFYLRQTSPVSAML CCEEEEECCCCCEEE | 28.67 | 22210691 | |
454 | Phosphorylation | AMLVLVKSLSGPREH EEEEHHHHCCCCHHH | 21.93 | 27135362 | |
456 | Phosphorylation | LVLVKSLSGPREHIV EEHHHHCCCCHHHEE | 54.57 | 23312004 | |
472 | Phosphorylation | LEMLTVSSIGTFRTS EEEEEECCCCCCCCC | 22.24 | 22210691 | |
475 | Phosphorylation | LTVSSIGTFRTSSVL EEECCCCCCCCCCEE | 14.31 | 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 FBLN3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FBLN3_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 FBLN3_HUMAN !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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