UniProt ID | UPAR_HUMAN | |
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UniProt AC | Q03405 | |
Protein Name | Urokinase plasminogen activator surface receptor | |
Gene Name | PLAUR | |
Organism | Homo sapiens (Human). | |
Sequence Length | 335 | |
Subcellular Localization |
Cell membrane . Cell projection, invadopodium membrane . Colocalized with FAP (seprase) preferentially at the cell surface of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin-dependent manner. Isoform 1: Cell membrane Lipid-ancho |
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Protein Description | Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.. | |
Protein Sequence | MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
30 | Phosphorylation | LRCMQCKTNGDCRVE CCCCCCCCCCCCCEE | 52.65 | - | |
74 | N-linked_Glycosylation | CTHSEKTNRTLSYRT CCCCHHHCCEEEEHH | 46.11 | 15861141 | |
79 | Nitration | KTNRTLSYRTGLKIT HHCCEEEEHHCCCCC | 18.46 | - | |
109 | Nitration | NSGRAVTYSRSRYLE CCCCCEEEECCCEEE | 8.76 | - | |
114 | Nitration | VTYSRSRYLECISCG EEEECCCEEEEEECC | 14.22 | - | |
171 | Nitration | RHLRGCGYLPGCPGS CCCCCCCCCCCCCCC | 17.50 | - | |
184 | N-linked_Glycosylation | GSNGFHNNDTFHFLK CCCCCCCCCCEEEEE | 40.92 | 15861141 | |
194 | N-linked_Glycosylation | FHFLKCCNTTKCNEG EEEEEECCCCCCCCC | 61.32 | 15861141 | |
217 | Phosphorylation | PQNGRQCYSCKGNST CCCCCCCEECCCCCC | 14.57 | - | |
217 | Nitration | PQNGRQCYSCKGNST CCCCCCCEECCCCCC | 14.57 | - | |
222 | N-linked_Glycosylation | QCYSCKGNSTHGCSS CCEECCCCCCCCCCC | 29.27 | 22285761 | |
254 | Ubiquitination | ATGTHEPKNQSYMVR EECCCCCCCCCEEEE | 65.71 | - | |
255 | N-linked_Glycosylation | TGTHEPKNQSYMVRG ECCCCCCCCCEEEEC | 46.90 | 15861141 | |
258 | Nitration | HEPKNQSYMVRGCAT CCCCCCCEEEECCCC | 7.00 | - | |
305 | GPI-anchor | LDVQYRSGAAPQPGP CCHHEECCCCCCCCC | 19.43 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of UPAR_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of UPAR_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 UPAR_HUMAN !! |
Kegg Disease | ||||||
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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. |
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N-linked Glycosylation | |
Reference | PubMed |
"Structure of human urokinase plasminogen activator in complex withits receptor."; Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J.,Li Y., Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B.,Huang M.; Science 311:656-659(2006). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-297 IN COMPLEX WITH PLAU,GLYCOSYLATION AT ASN-74 AND ASN-194, AND DISULFIDE BONDS. | |
"Crystal structure of the human urokinase plasminogen activatorreceptor bound to an antagonist peptide."; Llinas P., Le Du M.H., Gaardsvoll H., Danoe K., Ploug M., Gilquin B.,Stura E.A., Menez A.; EMBO J. 24:1655-1663(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 23-335 OF MUTANT GLN-222 INCOMPLEX WITH PEPTIDE ANTAGONIST, GLYCOSYLATION AT ASN-74; ASN-184;ASN-194 AND ASN-255, AND DISULFIDE BONDS. |