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Urokinase plasminogen activator surface receptor (U-PAR) (uPAR) (Monocyte activation antigen Mo3) (CD antigen CD87)

 UPAR_HUMAN              Reviewed;         335 AA.
Q03405; A8K409; Q12876; Q15845; Q16887; Q6IB52; Q9BWT0; Q9NYC8;
Q9UD69; Q9UEA6; Q9UM92; Q9UMV0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 187.
RecName: Full=Urokinase plasminogen activator surface receptor;
Short=U-PAR;
Short=uPAR;
AltName: Full=Monocyte activation antigen Mo3;
AltName: CD_antigen=CD87;
Flags: Precursor;
Name=PLAUR; Synonyms=MO3, UPAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-33.
PubMed=1689240;
Roldan A.L., Cubellis M.V., Masucci M.T., Behrendt N., Lund L.R.,
Danoe K., Appella E., Blasi F.;
"Cloning and expression of the receptor for human urokinase
plasminogen activator, a central molecule in cell surface, plasmin
dependent proteolysis.";
EMBO J. 9:467-474(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1316922;
Min H.Y., Semnani R., Mizukami I.F., Watt K., Todd R.F. III, Liu D.Y.;
"cDNA for Mo3, a monocyte activation antigen, encodes the human
receptor for urokinase plasminogen activator.";
J. Immunol. 148:3636-3642(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=8131971; DOI=10.1042/bst021395s;
Bayraktutan U., Jones P.;
"A novel urokinase receptor on monocyte-like macrophage cell line.";
Biochem. Soc. Trans. 21:395-395(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8392005; DOI=10.1016/0014-5793(93)81763-P;
Pyke C., Eriksen J., Solberg H., Schnack Nielsen B., Kristensen P.,
Lund L.R., Danoe K.;
"An alternatively spliced variant of mRNA for the human receptor for
urokinase plasminogen activator.";
FEBS Lett. 326:69-74(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
TISSUE=Placenta;
PubMed=8049431;
Casey J.R., Petranka J.G., Kottra J., Fleenor D.E., Rosse W.F.;
"The structure of the urokinase-type plasminogen activator receptor
gene.";
Blood 84:1151-1156(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-55; ALA-86;
GLN-105; ARG-220; LYS-281 AND PRO-317.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-322 (ISOFORM 1).
TISSUE=Lung cancer;
PubMed=11051819;
Zhu F., Jia S., He F.;
"cDNA cloning and sequencing of human urokinase receptor.";
Sheng Wu Gong Cheng Xue Bao 16:461-463(2000).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-301 (ISOFORM 1).
Fu J., Bai X., Wang W., Xi X., Ruan C.;
"Experimental study of anti-metastatic effect of soluble receptor for
urokinase plasminogen activator on human breast cancer cells.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
PubMed=7605992;
Soravia E., Grebe A., De Luca P., Helin K., Suh T.T., Degen J.L.,
Blasi F.;
"A conserved TATA-less proximal promoter drives basal transcription
from the urokinase-type plasminogen activator receptor gene.";
Blood 86:624-635(1995).
[15]
PARTIAL PROTEIN SEQUENCE.
PubMed=2156852;
Behrendt N., Roenne E., Ploug M., Petri T., Loeber D., Nielsen L.S.,
Schleuning W.-D., Blasi F., Appella E., Danoe K.;
"The human receptor for urokinase plasminogen activator. NH2-terminal
amino acid sequence and glycosylation variants.";
J. Biol. Chem. 265:6453-6460(1990).
[16]
PROTEIN SEQUENCE OF 106-116, AND CLEAVAGE BY U-PA.
PubMed=9030717; DOI=10.1111/j.1432-1033.1997.0021a.x;
Hoeyer-Hansen G., Ploug M., Behrendt N., Roenne E., Danoe K.;
"Cell-surface acceleration of urokinase-catalyzed receptor cleavage.";
Eur. J. Biochem. 243:21-26(1997).
[17]
PROTEIN SEQUENCE OF 210-230 (ISOFORMS 1/2/3).
TISSUE=Serum;
PubMed=7539799; DOI=10.1074/jbc.270.23.14107;
Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.;
"A novel form of dipeptidylpeptidase IV found in human serum.
Isolation, characterization, and comparison with T lymphocyte membrane
dipeptidylpeptidase IV (CD26).";
J. Biol. Chem. 270:14107-14114(1995).
[18]
DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
PubMed=8394346;
Ploug M., Kjalke M., Roenne E., Weidle U., Hoeyer-Hansen G., Danoe K.;
"Localization of the disulfide bonds in the NH2-terminal domain of the
cellular receptor for human urokinase-type plasminogen activator. A
domain structure belonging to a novel superfamily of glycolipid-
anchored membrane proteins.";
J. Biol. Chem. 268:17539-17546(1993).
[19]
INTERACTION WITH MRC2.
PubMed=10636902; DOI=10.1074/jbc.275.3.1993;
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M.,
Danoe K.;
"A urokinase receptor-associated protein with specific collagen
binding properties.";
J. Biol. Chem. 275:1993-2002(2000).
[20]
INTERACTION WITH FAP, AND SUBCELLULAR LOCATION.
PubMed=12376466; DOI=10.1093/carcin/23.10.1593;
Artym V.V., Kindzelskii A.L., Chen W.T., Petty H.R.;
"Molecular proximity of seprase and the urokinase-type plasminogen
activator receptor on malignant melanoma cell membranes: dependence on
beta1 integrins and the cytoskeleton.";
Carcinogenesis 23:1593-1601(2002).
[21]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=14517339; DOI=10.1074/mcp.M300079-MCP200;
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,
Jensen O.N.;
"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane
proteins.";
Mol. Cell. Proteomics 2:1261-1270(2003).
[22]
INTERACTION WITH SORL1.
PubMed=14764453; DOI=10.1161/01.RES.0000120862.79154.0F;
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S.,
Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
"LR11, an LDL receptor gene family member, is a novel regulator of
smooth muscle cell migration.";
Circ. Res. 94:752-758(2004).
[23]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16602701; DOI=10.1021/pr050419u;
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
Brodbeck U., Peck S.C., Jensen O.N.;
"Modification-specific proteomics of plasma membrane proteins:
identification and characterization of glycosylphosphatidylinositol-
anchored proteins released upon phospholipase D treatment.";
J. Proteome Res. 5:935-943(2006).
[24]
INTERACTION WITH SRPX2.
PubMed=18718938; DOI=10.1093/hmg/ddn256;
Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C.,
Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A.,
Vincentelli R., Cau P., Szepetowski P.;
"Epileptic and developmental disorders of the speech cortex:
ligand/receptor interaction of wild-type and mutant SRPX2 with the
plasminogen activator receptor uPAR.";
Hum. Mol. Genet. 17:3617-3630(2008).
[25]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 23-335 OF MUTANT GLN-222 IN
COMPLEX WITH PEPTIDE ANTAGONIST, GLYCOSYLATION AT ASN-74; ASN-184;
ASN-194 AND ASN-255, AND DISULFIDE BONDS.
PubMed=15861141; DOI=10.1038/sj.emboj.7600635;
Llinas P., Le Du M.H., Gaardsvoll H., Danoe K., Ploug M., Gilquin B.,
Stura E.A., Menez A.;
"Crystal structure of the human urokinase plasminogen activator
receptor bound to an antagonist peptide.";
EMBO J. 24:1655-1663(2005).
[26]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-297 IN COMPLEX WITH PLAU,
GLYCOSYLATION AT ASN-74 AND ASN-194, AND DISULFIDE BONDS.
PubMed=16456079; DOI=10.1126/science.1121143;
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.;
"Structure of human urokinase plasminogen activator in complex with
its receptor.";
Science 311:656-659(2006).
[27]
X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 23-305 OF MUTANT CYS-69 AND
CYS-281 ALONE AND IN COMPLEX WITH PLAU, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-74 AND ASN-222.
PubMed=22285761; DOI=10.1016/j.jmb.2011.12.058;
Xu X., Gardsvoll H., Yuan C., Lin L., Ploug M., Huang M.;
"Crystal structure of the urokinase receptor in a ligand-free form.";
J. Mol. Biol. 416:629-641(2012).
-!- FUNCTION: 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.
-!- SUBUNIT: Monomer (Probable). Interacts with MRC2. Interacts (via
the UPAR/Ly6 domains) with SRPX2. Interacts with SORL1. Interacts
with FAP (seprase); the interaction occurs at the cell surface of
invadopodia membrane. {ECO:0000269|PubMed:10636902,
ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14764453,
ECO:0000269|PubMed:15861141, ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:18718938, ECO:0000269|PubMed:22285761,
ECO:0000305}.
-!- INTERACTION:
P03950:ANG; NbExp=5; IntAct=EBI-716505, EBI-525291;
P00749:PLAU; NbExp=2; IntAct=EBI-15695188, EBI-3905042;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12376466}.
Cell projection, invadopodium membrane
{ECO:0000269|PubMed:12376466}. Note=Colocalized with FAP (seprase)
preferentially at the cell surface of invadopodia membrane in a
cytoskeleton-, integrin- and vitronectin-dependent manner.
{ECO:0000269|PubMed:12376466}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P49616}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000250|UniProtKB:P49616}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=uPAR1, GPI-anchored;
IsoId=Q03405-1; Sequence=Displayed;
Name=2; Synonyms=uPAR2, Secreted;
IsoId=Q03405-2; Sequence=VSP_006715;
Name=3;
IsoId=Q03405-3; Sequence=VSP_046345, VSP_046346;
Note=Ref.3 (no nucleotide entry) sequence is in conflict in
position: 158:V->I. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in neurons of the rolandic area of
the brain (at protein level). Expressed in the brain.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/plaur/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PLAURID41741ch19q13.html";
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EMBL; X51675; CAA35981.1; -; mRNA.
EMBL; M83246; AAA59862.1; -; mRNA.
EMBL; X74039; CAA52191.1; -; mRNA.
EMBL; U09346; AAA17979.1; -; Genomic_DNA.
EMBL; U09347; AAA17978.1; -; mRNA.
EMBL; U08839; AAB60333.1; -; mRNA.
EMBL; U09937; AAB60690.1; -; Genomic_DNA.
EMBL; U09931; AAB60690.1; JOINED; Genomic_DNA.
EMBL; U09932; AAB60690.1; JOINED; Genomic_DNA.
EMBL; U09933; AAB60690.1; JOINED; Genomic_DNA.
EMBL; U09935; AAB60690.1; JOINED; Genomic_DNA.
EMBL; U09936; AAB60690.1; JOINED; Genomic_DNA.
EMBL; AY194849; AAN86351.1; -; Genomic_DNA.
EMBL; AK290774; BAF83463.1; -; mRNA.
EMBL; CR456952; CAG33233.1; -; mRNA.
EMBL; AC005525; AAC32739.1; -; Genomic_DNA.
EMBL; AC006953; AAD17387.1; -; Genomic_DNA.
EMBL; AC006953; AAD17388.1; -; Genomic_DNA.
EMBL; CH471126; EAW57220.1; -; Genomic_DNA.
EMBL; BC002788; AAH02788.1; -; mRNA.
EMBL; AF257789; AAF71751.1; -; mRNA.
EMBL; AY029180; AAK31795.1; -; mRNA.
EMBL; S78532; AAD14289.1; -; Genomic_DNA.
CCDS; CCDS12628.1; -. [Q03405-1]
CCDS; CCDS33041.1; -. [Q03405-2]
CCDS; CCDS33042.1; -. [Q03405-3]
PIR; I52614; I52614.
PIR; S12376; A39743.
PIR; S39495; S39495.
RefSeq; NP_001005376.1; NM_001005376.2. [Q03405-2]
RefSeq; NP_001005377.1; NM_001005377.2. [Q03405-3]
RefSeq; NP_001287966.1; NM_001301037.1.
RefSeq; NP_002650.1; NM_002659.3. [Q03405-1]
UniGene; Hs.466871; -.
PDB; 1YWH; X-ray; 2.70 A; A/C/E/G/I/K/M/O=23-335.
PDB; 2FD6; X-ray; 1.90 A; U=23-297.
PDB; 2I9B; X-ray; 2.80 A; E/F/G/H=23-299.
PDB; 3BT1; X-ray; 2.80 A; U=23-303.
PDB; 3BT2; X-ray; 2.50 A; U=23-303.
PDB; 3U73; X-ray; 3.19 A; U=23-305.
PDB; 3U74; X-ray; 2.39 A; U=23-305.
PDB; 4K24; X-ray; 4.50 A; U=23-303.
PDB; 4QTI; X-ray; 3.00 A; U=23-305.
PDBsum; 1YWH; -.
PDBsum; 2FD6; -.
PDBsum; 2I9B; -.
PDBsum; 3BT1; -.
PDBsum; 3BT2; -.
PDBsum; 3U73; -.
PDBsum; 3U74; -.
PDBsum; 4K24; -.
PDBsum; 4QTI; -.
ProteinModelPortal; Q03405; -.
SMR; Q03405; -.
BioGrid; 111345; 108.
CORUM; Q03405; -.
DIP; DIP-137N; -.
IntAct; Q03405; 10.
MINT; MINT-1370900; -.
STRING; 9606.ENSP00000339328; -.
BindingDB; Q03405; -.
ChEMBL; CHEMBL4883; -.
DrugBank; DB00009; Alteplase.
DrugBank; DB00029; Anistreplase.
DrugBank; DB00015; Reteplase.
DrugBank; DB00031; Tenecteplase.
DrugBank; DB00013; Urokinase.
DrugBank; DB05476; WX-UK1.
iPTMnet; Q03405; -.
PhosphoSitePlus; Q03405; -.
SwissPalm; Q03405; -.
BioMuta; PLAUR; -.
DMDM; 465003; -.
EPD; Q03405; -.
MaxQB; Q03405; -.
PaxDb; Q03405; -.
PeptideAtlas; Q03405; -.
PRIDE; Q03405; -.
DNASU; 5329; -.
Ensembl; ENST00000221264; ENSP00000221264; ENSG00000011422. [Q03405-3]
Ensembl; ENST00000339082; ENSP00000342049; ENSG00000011422. [Q03405-2]
Ensembl; ENST00000340093; ENSP00000339328; ENSG00000011422. [Q03405-1]
GeneID; 5329; -.
KEGG; hsa:5329; -.
UCSC; uc002oxd.3; human. [Q03405-1]
CTD; 5329; -.
DisGeNET; 5329; -.
EuPathDB; HostDB:ENSG00000011422.11; -.
GeneCards; PLAUR; -.
HGNC; HGNC:9053; PLAUR.
HPA; CAB073533; -.
HPA; HPA050843; -.
MIM; 173391; gene.
neXtProt; NX_Q03405; -.
OpenTargets; ENSG00000011422; -.
PharmGKB; PA33383; -.
eggNOG; ENOG410IJ50; Eukaryota.
eggNOG; ENOG410Z47S; LUCA.
GeneTree; ENSGT00510000049144; -.
HOVERGEN; HBG000245; -.
InParanoid; Q03405; -.
KO; K03985; -.
OMA; VERGCAH; -.
OrthoDB; EOG091G0FQ6; -.
PhylomeDB; Q03405; -.
TreeFam; TF338662; -.
Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
SIGNOR; Q03405; -.
EvolutionaryTrace; Q03405; -.
GeneWiki; Urokinase_receptor; -.
GenomeRNAi; 5329; -.
PMAP-CutDB; Q03405; -.
PRO; PR:Q03405; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000011422; -.
ExpressionAtlas; Q03405; baseline and differential.
Genevisible; Q03405; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:CAFA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0071438; C:invadopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:AgBase.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0005102; F:receptor binding; IPI:AgBase.
GO; GO:0030377; F:urokinase plasminogen activator receptor activity; IBA:GO_Central.
GO; GO:0016255; P:attachment of GPI anchor to protein; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
GO; GO:0006928; P:movement of cell or subcellular component; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:CACAO.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:CACAO.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:CACAO.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:CACAO.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:CACAO.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:CACAO.
GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; IBA:GO_Central.
InterPro; IPR018363; CD59_antigen_CS.
InterPro; IPR016054; LY6_UPA_recep-like.
InterPro; IPR033084; U-PAR.
PANTHER; PTHR10624:SF6; PTHR10624:SF6; 1.
Pfam; PF00021; UPAR_LY6; 2.
SMART; SM00134; LU; 3.
PROSITE; PS00983; LY6_UPAR; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:1689240}.
CHAIN 23 305 Urokinase plasminogen activator surface
receptor.
/FTId=PRO_0000036090.
PROPEP 306 335 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000036091.
DOMAIN 23 114 UPAR/Ly6 1.
DOMAIN 115 213 UPAR/Ly6 2.
DOMAIN 214 305 UPAR/Ly6 3.
SITE 105 106 Cleavage; by U-PA.
SITE 111 112 Cleavage; by U-PA.
LIPID 305 305 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15861141}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22285761}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15861141}.
DISULFID 25 46 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 28 34 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 39 67 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 93 98 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 117 144 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 120 127 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 137 169 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 175 192 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 193 198 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 216 244 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 219 227 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 237 263 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 269 287 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
DISULFID 288 293 {ECO:0000269|PubMed:15861141,
ECO:0000269|PubMed:16456079,
ECO:0000269|PubMed:22285761}.
VAR_SEQ 158 202 Missing (in isoform 3).
{ECO:0000303|PubMed:8049431,
ECO:0000303|PubMed:8131971}.
/FTId=VSP_046345.
VAR_SEQ 203 203 I -> V (in isoform 3).
{ECO:0000303|PubMed:8049431,
ECO:0000303|PubMed:8131971}.
/FTId=VSP_046346.
VAR_SEQ 253 335 PKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGC
NHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLW
T -> RSLWGSWLPCKSTTALRPPCCEEAQATHV (in
isoform 2). {ECO:0000303|PubMed:8392005,
ECO:0000303|Ref.7}.
/FTId=VSP_006715.
VARIANT 55 55 E -> G (in dbSNP:rs4251813).
{ECO:0000269|Ref.8}.
/FTId=VAR_016322.
VARIANT 86 86 T -> A (in dbSNP:rs399145).
{ECO:0000269|Ref.8}.
/FTId=VAR_016323.
VARIANT 105 105 R -> Q (in dbSNP:rs4251878).
{ECO:0000269|Ref.8}.
/FTId=VAR_016324.
VARIANT 220 220 K -> R (in dbSNP:rs2302524).
{ECO:0000269|Ref.8}.
/FTId=VAR_016325.
VARIANT 281 281 N -> K (in dbSNP:rs4251921).
{ECO:0000269|Ref.8}.
/FTId=VAR_016326.
VARIANT 297 297 D -> A (in dbSNP:rs16976608).
/FTId=VAR_052698.
VARIANT 317 317 L -> P (in dbSNP:rs4760).
{ECO:0000269|Ref.8}.
/FTId=VAR_014922.
CONFLICT 28 28 C -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 H -> P (in Ref. 13; AAK31795).
{ECO:0000305}.
CONFLICT 213 213 G -> E (in Ref. 17; AA sequence).
{ECO:0000305}.
CONFLICT 249 249 G -> D (in Ref. 12; AAF71751).
{ECO:0000305}.
CONFLICT 252 252 E -> G (in Ref. 12; AAF71751).
{ECO:0000305}.
STRAND 24 28 {ECO:0000244|PDB:2FD6}.
STRAND 34 38 {ECO:0000244|PDB:2FD6}.
STRAND 45 54 {ECO:0000244|PDB:2FD6}.
STRAND 60 68 {ECO:0000244|PDB:2FD6}.
STRAND 75 81 {ECO:0000244|PDB:2FD6}.
STRAND 84 93 {ECO:0000244|PDB:2FD6}.
TURN 96 99 {ECO:0000244|PDB:2FD6}.
STRAND 116 121 {ECO:0000244|PDB:2FD6}.
TURN 122 130 {ECO:0000244|PDB:2FD6}.
STRAND 133 136 {ECO:0000244|PDB:2FD6}.
STRAND 138 141 {ECO:0000244|PDB:2I9B}.
STRAND 143 150 {ECO:0000244|PDB:2FD6}.
STRAND 155 158 {ECO:0000244|PDB:3BT1}.
STRAND 164 171 {ECO:0000244|PDB:2FD6}.
STRAND 176 183 {ECO:0000244|PDB:2FD6}.
STRAND 186 193 {ECO:0000244|PDB:2FD6}.
TURN 196 199 {ECO:0000244|PDB:2FD6}.
HELIX 206 208 {ECO:0000244|PDB:2FD6}.
STRAND 211 222 {ECO:0000244|PDB:2FD6}.
TURN 223 225 {ECO:0000244|PDB:2FD6}.
STRAND 226 228 {ECO:0000244|PDB:2FD6}.
TURN 229 231 {ECO:0000244|PDB:2FD6}.
STRAND 233 238 {ECO:0000244|PDB:2FD6}.
STRAND 243 251 {ECO:0000244|PDB:2FD6}.
TURN 252 255 {ECO:0000244|PDB:2FD6}.
STRAND 256 264 {ECO:0000244|PDB:2FD6}.
HELIX 266 268 {ECO:0000244|PDB:2FD6}.
STRAND 270 273 {ECO:0000244|PDB:3BT1}.
HELIX 275 278 {ECO:0000244|PDB:2FD6}.
STRAND 284 288 {ECO:0000244|PDB:2FD6}.
TURN 291 294 {ECO:0000244|PDB:2FD6}.
HELIX 296 298 {ECO:0000244|PDB:3U74}.
SEQUENCE 335 AA; 36978 MW; AB1963EA3DC77171 CRC64;
MGHPPLLPLL LLLHTCVPAS WGLRCMQCKT NGDCRVEECA LGQDLCRTTI VRLWEEGEEL
ELVEKSCTHS EKTNRTLSYR TGLKITSLTE VVCGLDLCNQ GNSGRAVTYS RSRYLECISC
GSSDMSCERG RHQSLQCRSP EEQCLDVVTH WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG
FHNNDTFHFL KCCNTTKCNE GPILELENLP QNGRQCYSCK GNSTHGCSSE ETFLIDCRGP
MNQCLVATGT HEPKNQSYMV RGCATASMCQ HAHLGDAFSM NHIDVSCCTK SGCNHPDLDV
QYRSGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT


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