Protein:PLAUR |
Protein Summary |
 Gene summary |
| Gene name: PLAUR | ASpdb.0 ID: 5329 | Gene | Gene symbol | PLAUR | Gene ID | 5329 |
| Gene name | plasminogen activator, urokinase receptor |
| Synonyms | CD87|U-PAR|UPAR|URKR |
| Cytomap | 19q13.31 |
| Type of gene | protein-coding |
| Description | urokinase plasminogen activator surface receptormonocyte activation antigen Mo3u-plasminogen activator receptor form 2urokinase-type plasminogen activator (uPA) receptor |
| Modification date | 20240403 |
| UniProtAcc | Q03405 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | PLAUR | GO:0005886 | plasma membrane | 12665524 |
| Gene | PLAUR | GO:0009986 | cell surface | 15922359 |
| Gene | PLAUR | GO:0030155 | regulation of cell adhesion | 10722842 |
| Gene | PLAUR | GO:0043388 | positive regulation of DNA binding | 22984561 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q03405-1 | Q03405-1_3u74_U.pdb | 3U74 | X-ray | 2.39 | U | 23 | 305 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q03405 | PLAUR | Q03405-1 | Q03405-2 | 335 | 281 | 253 | 335 | Substitution | PKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT | RSLWGSWLPCKSTTALRPPCCEEAQATHV | 253 | 281 |
| Q03405 | PLAUR | Q03405-1 | Q03405-3 | 335 | 290 | 158 | 202 | Deletion | none | none | 157 | 157 |
| Q03405 | PLAUR | Q03405-1 | Q03405-3 | 335 | 290 | 203 | 203 | Substitution | I | V | 158 | 158 |
| Multiple sequence alignment of our canonical and alternatively spliced PLAUR |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of PLAUR |
| UniProt-id | ENSG | ENST | ENSP |
| Q03405-1 | ENSG00000011422.12 | ENST00000340093.8 | ENSP00000339328.3 |
| Q03405-2 | ENSG00000011422.12 | ENST00000339082.7 | ENSP00000342049.2 |
| Q03405-3 | ENSG00000011422.12 | ENST00000221264.8 | ENSP00000221264.3 |
| UniProt-id | NM ID | NP ID |
| Q03405-1 | NM_002659.3 | NP_002650.1 |
| Q03405-2 | NM_001005376.2 | NP_001005376.1 |
| Q03405-3 | NM_001005377.2 | NP_001005377.1 |
| Amino acid sequences of our canonical and alternatively spliced PLAUR |
| accession_id | Protein sequence |
| Q03405-1 | MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTE VVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNG FHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQ |
| Q03405-2 | MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTE VVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNG FHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHERSLWGSWLPCKSTTALRP |
| Q03405-3 | MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTE VVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEVLELENLPQNGRQCYSCKGNSTH GCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHL |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| PLAUR (go to UniProt):Q03405 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q03405 | Domain | 115 | 213 | Note=UPAR/Ly6 2 | Type=Deletion;Start=158;End=202 |
| Q03405 | Domain | 115 | 213 | Note=UPAR/Ly6 2 | Type=Substitution;Start=203;End=203 |
| Q03405 | Domain | 214 | 305 | Note=UPAR/Ly6 3 | Type=Substitution;Start=253;End=335 |
Gene Isoform Structures and Expression Levels for PLAUR |
| Gene structures of our canonical and alternative spliced genes of PLAUR * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
 |
| Expression levels of gene isoforms across TCGA. |
 |
Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q03405-1 |
| 3D view using mol* of Q03405-2 |
| 3D view using mol* of Q03405-3 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q03405-1 |
 |
| pLDDT distribution across the protein length of Q03405-2 |
 |
| pLDDT distribution across the protein length of Q03405-3 |
 |
Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q03405-1 |
 |
| Ramachandran plot of Q03405-2 |
 |
| Ramachandran plot of Q03405-3 |
 |
Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q03405-1 | 1.036 | 279 | 1.021 | 867.447 | 0.523 | 0.751 | 0.963 | 0.66 | 1.133 | 0.582 | 0.637 | 49,75,76,77,88,89,90,147,148,149,150,151,152,153,1 54,155,156,157,158,159,160,161,162,163,164,166,172 ,173,179,185,188,189,190,220,222,251,252,253,254,2 56,257,258,268,273,276,277,278,279 |
| Q03405-2 | 1.024 | 547 | 1.038 | 1409.73 | 0.509 | 0.735 | 0.959 | 0.645 | 1.053 | 0.613 | 0.951 | 30,47,49,50,51,53,62,63,64,68,69,71,72,75,76,77,79 ,84,86,88,89,90,122,123,125,128,147,148,149,150,15 1,153,154,155,156,157,158,159,160,161,162,163,164, 165,166,172,173,174,179,181,183,186,188,189,190,22 0,245,247,248,249,250,251,252,256,257,258,266,267, 268,269,270,271,272,273,274,275,276,277,278,279,28 0,281 |
| Q03405-3 | 1.062 | 102 | 1.111 | 655.473 | 0.694 | 0.725 | 0.849 | 0.93 | 0.811 | 1.147 | 0.584 | 148,149,150,151,152,157,158,161,162,164,166,173,17 4,175,190,191,192,193,196,200,215,216,217,218,219, 223,229,232,233 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
 |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q03405-1_Q03405-1_3u74_U.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q03405-1_3u74_U_Q03405-2.pdb |
| 3D view using mol* of Q03405-1_3u74_U_Q03405-3.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q03405-1_Q03405-2.pdb |
| 3D view using mol* of Q03405-1_Q03405-3.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q03405-1_vs_Q03405-2.png |
 < |
| ./stats/secondary_structure/figure/Q03405-1_vs_Q03405-3.png |
 < |
| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q03405-1_vs_Q03405-2.png |
 < |
| ./stats/relative_asa/Q03405-1_vs_Q03405-3.png |
 < |
Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to PLAUR |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q03405 | PLAUR | DB00013 | Urokinase | approved, investigational, withdrawn | inducer, modulator |
| Q03405 | PLAUR | DB05476 | WX-UK1 | investigational | |
| Q03405 | PLAUR | DB06245 | Lanoteplase | investigational | |
| Q03405 | PLAUR | DB00031 | Tenecteplase | approved |
Related Diseases to PLAUR |
| Previous studies relating to the alternative splicing of PLAUR and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| PLAUR | 20635136 | Overexpression of the urokinase receptor mRNA splice variant uPAR-del4/5 affects tumor-associated processes of breast cancer cells in vitro and in vivo. | uPAR, the three-domain membrane receptor of the serine protease urokinase, plays a crucial role in tumor growth and metastasis. Several mRNA splice variants of this receptor have been reported. One of these, uPAR-del4/5, lacking exons 4 and 5, and thus encoding a uPAR form lacking domain DII, is specifically overexpressed in breast cancer and represents a statistically independent prognostic factor for distant metastasis-free survival in breast cancer patients. The aim of the present study was to examine the molecular and cellular properties of the encoded uPAR-del4/5 protein. To investigate the impact of the uPAR-del4/5 overexpression on in vitro and in vivo aspects of tumor progression (e.g., proliferation, adhesion, invasion, metastatic seeding, and/or metastatic growth), we combined the analysis of transfected cancer cell lines with a murine xenograft tumor model. Increased expression of uPAR-del4/5 in human cancer cells led to reduced adhesion to several extracellular matrix proteins and decreased invasion through Matrigel, while cell proliferation was not affected in vitro. Moreover, invasion of uPAR-del4/5 overexpressing cells was not altered by addition of urokinase, while that of uPAR-wild-type overexpressing cells was drastically increased. Accordingly, we observed that, in contrast to uPAR-wild-type, uPAR-del4/5 does not interact with urokinase. On the other hand, when overexpressed in human breast cancer cells, uPAR-del4/5 distinctly impaired metastatic dissemination and growth in vivo. We demonstrate that the uPAR-del4/5 mRNA splice variant mediates tumor-relevant biological processes in vitro and in vivo. Our results thus illustrate how tumor-specific alternative splicing can distinctly impact the biology of the tumor. | D001943 | Breast Neoplasms |
| PLAUR | 20635136 | Overexpression of the urokinase receptor mRNA splice variant uPAR-del4/5 affects tumor-associated processes of breast cancer cells in vitro and in vivo. | uPAR, the three-domain membrane receptor of the serine protease urokinase, plays a crucial role in tumor growth and metastasis. Several mRNA splice variants of this receptor have been reported. One of these, uPAR-del4/5, lacking exons 4 and 5, and thus encoding a uPAR form lacking domain DII, is specifically overexpressed in breast cancer and represents a statistically independent prognostic factor for distant metastasis-free survival in breast cancer patients. The aim of the present study was to examine the molecular and cellular properties of the encoded uPAR-del4/5 protein. To investigate the impact of the uPAR-del4/5 overexpression on in vitro and in vivo aspects of tumor progression (e.g., proliferation, adhesion, invasion, metastatic seeding, and/or metastatic growth), we combined the analysis of transfected cancer cell lines with a murine xenograft tumor model. Increased expression of uPAR-del4/5 in human cancer cells led to reduced adhesion to several extracellular matrix proteins and decreased invasion through Matrigel, while cell proliferation was not affected in vitro. Moreover, invasion of uPAR-del4/5 overexpressing cells was not altered by addition of urokinase, while that of uPAR-wild-type overexpressing cells was drastically increased. Accordingly, we observed that, in contrast to uPAR-wild-type, uPAR-del4/5 does not interact with urokinase. On the other hand, when overexpressed in human breast cancer cells, uPAR-del4/5 distinctly impaired metastatic dissemination and growth in vivo. We demonstrate that the uPAR-del4/5 mRNA splice variant mediates tumor-relevant biological processes in vitro and in vivo. Our results thus illustrate how tumor-specific alternative splicing can distinctly impact the biology of the tumor. | D009361 | Neoplasm Invasiveness |
| PLAUR | 20635136 | Overexpression of the urokinase receptor mRNA splice variant uPAR-del4/5 affects tumor-associated processes of breast cancer cells in vitro and in vivo. | uPAR, the three-domain membrane receptor of the serine protease urokinase, plays a crucial role in tumor growth and metastasis. Several mRNA splice variants of this receptor have been reported. One of these, uPAR-del4/5, lacking exons 4 and 5, and thus encoding a uPAR form lacking domain DII, is specifically overexpressed in breast cancer and represents a statistically independent prognostic factor for distant metastasis-free survival in breast cancer patients. The aim of the present study was to examine the molecular and cellular properties of the encoded uPAR-del4/5 protein. To investigate the impact of the uPAR-del4/5 overexpression on in vitro and in vivo aspects of tumor progression (e.g., proliferation, adhesion, invasion, metastatic seeding, and/or metastatic growth), we combined the analysis of transfected cancer cell lines with a murine xenograft tumor model. Increased expression of uPAR-del4/5 in human cancer cells led to reduced adhesion to several extracellular matrix proteins and decreased invasion through Matrigel, while cell proliferation was not affected in vitro. Moreover, invasion of uPAR-del4/5 overexpressing cells was not altered by addition of urokinase, while that of uPAR-wild-type overexpressing cells was drastically increased. Accordingly, we observed that, in contrast to uPAR-wild-type, uPAR-del4/5 does not interact with urokinase. On the other hand, when overexpressed in human breast cancer cells, uPAR-del4/5 distinctly impaired metastatic dissemination and growth in vivo. We demonstrate that the uPAR-del4/5 mRNA splice variant mediates tumor-relevant biological processes in vitro and in vivo. Our results thus illustrate how tumor-specific alternative splicing can distinctly impact the biology of the tumor. | D009362 | Neoplasm Metastasis |
Clinically important variants in PLAUR |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
Copyright 2024-PresentThe University of Texas Health Science Center at Houston (UTHealth Houston) Web File Viewing | Emergency Information |