Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03405 (UPAR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urokinase plasminogen activator surface receptor

Short name=U-PAR
Short name=uPAR
Alternative name(s):
Monocyte activation antigen Mo3
CD_antigen=CD87
Gene names
Name:PLAUR
Synonyms:MO3, UPAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Monomer Probable. Interacts with MRC2. Interacts (via the UPAR/Ly6 domains) with SRPX2. Interacts with SORL1. Ref.19 Ref.21 Ref.23

Subcellular location

Isoform 1: Cell membrane; Lipid-anchorGPI-anchor.

Isoform 2: Secreted Probable.

Tissue specificity

Expressed in neurons of the rolandic area of the brain (at protein level). Expressed in the brain.

Sequence similarities

Contains 3 UPAR/Ly6 domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

attachment of GPI anchor to protein

Traceable author statement. Source: Reactome

blood coagulation

Non-traceable author statement Ref.4. Source: UniProtKB

cellular component movement

Non-traceable author statement Ref.1. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

chemotaxis

Traceable author statement PubMed 10749881. Source: ProtInc

fibrinolysis

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

regulation of proteolysis

Non-traceable author statement Ref.1. Source: UniProtKB

signal transduction

Traceable author statement PubMed 10749881. Source: ProtInc

urokinase plasminogen activator signaling pathway

Non-traceable author statement Ref.1Ref.4. Source: GOC

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of membrane

Traceable author statement Ref.5. Source: ProtInc

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 14688365. Source: UniProtKB

receptor activity

Non-traceable author statement Ref.1Ref.4. Source: UniProtKB

urokinase plasminogen activator receptor activity

Non-traceable author statement Ref.1Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03405-1)

Also known as: uPAR1; GPI-anchored;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q03405-2)

Also known as: uPAR2; Secreted;

The sequence of this isoform differs from the canonical sequence as follows:
     253-335: PKNQSYMVRG...RLWGGTLLWT → RSLWGSWLPCKSTTALRPPCCEEAQATHV
Isoform 3 (identifier: Q03405-3)

The sequence of this isoform differs from the canonical sequence as follows:
     158-202: Missing.
     203-203: I → V

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1
Chain23 – 305283Urokinase plasminogen activator surface receptor
PRO_0000036090
Propeptide306 – 33530Removed in mature form Probable
PRO_0000036091

Regions

Domain23 – 11492UPAR/Ly6 1
Domain115 – 21399UPAR/Ly6 2
Domain214 – 30592UPAR/Ly6 3

Sites

Site105 – 1062Cleavage; by U-PA
Site111 – 1122Cleavage; by U-PA

Amino acid modifications

Lipidation3051GPI-anchor amidated glycine Probable
Glycosylation741N-linked (GlcNAc...) Ref.24 Ref.25 Ref.26
Glycosylation1841N-linked (GlcNAc...) Ref.24
Glycosylation1941N-linked (GlcNAc...) Ref.24 Ref.25
Glycosylation2221N-linked (GlcNAc...) Ref.26
Glycosylation2551N-linked (GlcNAc...) Ref.24
Disulfide bond25 ↔ 46 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond28 ↔ 34 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond39 ↔ 67 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond93 ↔ 98 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond117 ↔ 144 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond120 ↔ 127 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond137 ↔ 169 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond175 ↔ 192 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond193 ↔ 198 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond216 ↔ 244 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond219 ↔ 227 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond237 ↔ 263 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond269 ↔ 287 Ref.18 Ref.24 Ref.25 Ref.26
Disulfide bond288 ↔ 293 Ref.18 Ref.24 Ref.25 Ref.26

Natural variations

Alternative sequence158 – 20245Missing in isoform 3.
VSP_046345
Alternative sequence2031I → V in isoform 3.
VSP_046346
Alternative sequence253 – 33583PKNQS…TLLWT → RSLWGSWLPCKSTTALRPPC CEEAQATHV in isoform 2.
VSP_006715
Natural variant551E → G. Ref.8
Corresponds to variant rs4251813 [ dbSNP | Ensembl ].
VAR_016322
Natural variant861T → A. Ref.8
Corresponds to variant rs399145 [ dbSNP | Ensembl ].
VAR_016323
Natural variant1051R → Q. Ref.8
Corresponds to variant rs4251878 [ dbSNP | Ensembl ].
VAR_016324
Natural variant2201K → R. Ref.8
Corresponds to variant rs2302524 [ dbSNP | Ensembl ].
VAR_016325
Natural variant2811N → K. Ref.8
Corresponds to variant rs4251921 [ dbSNP | Ensembl ].
VAR_016326
Natural variant2971D → A.
Corresponds to variant rs16976608 [ dbSNP | Ensembl ].
VAR_052698
Natural variant3171L → P. Ref.8
Corresponds to variant rs4760 [ dbSNP | Ensembl ].
VAR_014922

Experimental info

Sequence conflict281C → N AA sequence Ref.1
Sequence conflict1651H → P in AAK31795. Ref.13
Sequence conflict2131G → E AA sequence Ref.17
Sequence conflict2491G → D in AAF71751. Ref.12
Sequence conflict2521E → G in AAF71751. Ref.12
Isoform 3:
Sequence conflict1581V → I no nucleotide entry Ref.3

Secondary structure

........................................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (uPAR1) (GPI-anchored) [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: AB1963EA3DC77171

FASTA33536,978
        10         20         30         40         50         60 
MGHPPLLPLL LLLHTCVPAS WGLRCMQCKT NGDCRVEECA LGQDLCRTTI VRLWEEGEEL 

        70         80         90        100        110        120 
ELVEKSCTHS EKTNRTLSYR TGLKITSLTE VVCGLDLCNQ GNSGRAVTYS RSRYLECISC 

       130        140        150        160        170        180 
GSSDMSCERG RHQSLQCRSP EEQCLDVVTH WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG 

       190        200        210        220        230        240 
FHNNDTFHFL KCCNTTKCNE GPILELENLP QNGRQCYSCK GNSTHGCSSE ETFLIDCRGP 

       250        260        270        280        290        300 
MNQCLVATGT HEPKNQSYMV RGCATASMCQ HAHLGDAFSM NHIDVSCCTK SGCNHPDLDV 

       310        320        330 
QYRSGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT 

« Hide

Isoform 2 (uPAR2) (Secreted) [UniParc].

Checksum: E6C580F279FB0316
Show »

FASTA28131,263
Isoform 3 [UniParc].

Checksum: 60F14E2A2AFB67AC
Show »

FASTA29032,016

References

« Hide 'large scale' references
[1]"Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis."
Roldan A.L., Cubellis M.V., Masucci M.T., Behrendt N., Lund L.R., Danoe K., Appella E., Blasi F.
EMBO J. 9:467-474(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 23-33.
[2]"cDNA for Mo3, a monocyte activation antigen, encodes the human receptor for urokinase plasminogen activator."
Min H.Y., Semnani R., Mizukami I.F., Watt K., Todd R.F. III, Liu D.Y.
J. Immunol. 148:3636-3642(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"A novel urokinase receptor on monocyte-like macrophage cell line."
Bayraktutan U., Jones P.
Biochem. Soc. Trans. 21:395-395(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator."
Pyke C., Eriksen J., Solberg H., Schnack Nielsen B., Kristensen P., Lund L.R., Danoe K.
FEBS Lett. 326:69-74(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"The structure of the urokinase-type plasminogen activator receptor gene."
Casey J.R., Petranka J.G., Kottra J., Fleenor D.E., Rosse W.F.
Blood 84:1151-1156(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
Tissue: Placenta.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[8]SeattleSNPs variation discovery resource
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-55; ALA-86; GLN-105; ARG-220; LYS-281 AND PRO-317.
[9]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[12]"cDNA cloning and sequencing of human urokinase receptor."
Zhu F., Jia S., He F.
Sheng Wu Gong Cheng Xue Bao 16:461-463(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-322 (ISOFORM 1).
Tissue: Lung cancer.
[13]"Experimental study of anti-metastatic effect of soluble receptor for urokinase plasminogen activator on human breast cancer cells."
Fu J., Bai X., Wang W., Xi X., Ruan C.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-301 (ISOFORM 1).
[14]"A conserved TATA-less proximal promoter drives basal transcription from the urokinase-type plasminogen activator receptor gene."
Soravia E., Grebe A., De Luca P., Helin K., Suh T.T., Degen J.L., Blasi F.
Blood 86:624-635(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
[15]"The human receptor for urokinase plasminogen activator. NH2-terminal amino acid sequence and glycosylation variants."
Behrendt N., Roenne E., Ploug M., Petri T., Loeber D., Nielsen L.S., Schleuning W.-D., Blasi F., Appella E., Danoe K.
J. Biol. Chem. 265:6453-6460(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[16]"Cell-surface acceleration of urokinase-catalyzed receptor cleavage."
Hoeyer-Hansen G., Ploug M., Behrendt N., Roenne E., Danoe K.
Eur. J. Biochem. 243:21-26(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 106-116, CLEAVAGE BY U-PA.
[17]"A novel form of dipeptidylpeptidase IV found in human serum. Isolation, characterization, and comparison with T lymphocyte membrane dipeptidylpeptidase IV (CD26)."
Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.
J. Biol. Chem. 270:14107-14114(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 210-230 (ISOFORMS 1/2/3).
Tissue: Serum.
[18]"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."
Ploug M., Kjalke M., Roenne E., Weidle U., Hoeyer-Hansen G., Danoe K.
J. Biol. Chem. 268:17539-17546(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE.
[19]"A urokinase receptor-associated protein with specific collagen binding properties."
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.
J. Biol. Chem. 275:1993-2002(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRC2.
[20]"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration."
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.
Circ. Res. 94:752-758(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORL1.
[22]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR."
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.
Hum. Mol. Genet. 17:3617-3630(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRPX2.
[24]"Crystal structure of the human urokinase plasminogen activator receptor 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) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, DISULFIDE BONDS.
[25]"Structure of human urokinase plasminogen activator in complex with its 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) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-297 IN COMPLEX WITH PLAU, GLYCOSYLATION AT ASN-74 AND ASN-194, DISULFIDE BONDS.
[26]"Crystal structure of the urokinase receptor in a ligand-free form."
Xu X., Gardsvoll H., Yuan C., Lin L., Ploug M., Huang M.
J. Mol. Biol. 416:629-641(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 23-305 OF MUTANT CYS-69 AND CYS-281 ALONE AND IN COMPLEX WITH PLAU, DISULFIDE BONDS, GLYCOSYLATION AT ASN-74 AND ASN-222.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51675 mRNA. Translation: CAA35981.1.
M83246 mRNA. Translation: AAA59862.1.
X74039 mRNA. Translation: CAA52191.1.
U09346 Genomic DNA. Translation: AAA17979.1.
U09347 mRNA. Translation: AAA17978.1.
U08839 mRNA. Translation: AAB60333.1.
U09937 expand/collapse EMBL AC list , U09931, U09932, U09933, U09935, U09936 Genomic DNA. Translation: AAB60690.1.
AY194849 Genomic DNA. Translation: AAN86351.1.
AK290774 mRNA. Translation: BAF83463.1.
CR456952 mRNA. Translation: CAG33233.1.
AC005525 Genomic DNA. Translation: AAC32739.1.
AC006953 Genomic DNA. Translation: AAD17387.1.
AC006953 Genomic DNA. Translation: AAD17388.1.
CH471126 Genomic DNA. Translation: EAW57220.1.
BC002788 mRNA. Translation: AAH02788.1.
AF257789 mRNA. Translation: AAF71751.1.
AY029180 mRNA. Translation: AAK31795.1.
S78532 Genomic DNA. Translation: AAD14289.1.
PIRI52614.
A39743. S12376.
S39495.
RefSeqNP_001005376.1. NM_001005376.2.
NP_001005377.1. NM_001005377.2.
NP_002650.1. NM_002659.3.
UniGeneHs.466871.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YWHX-ray2.70A/C/E/G/I/K/M/O23-335[»]
2FD6X-ray1.90U23-297[»]
2I9BX-ray2.80E/F/G/H23-299[»]
3BT1X-ray2.80U23-303[»]
3BT2X-ray2.50U23-303[»]
3U73X-ray3.19U23-305[»]
3U74X-ray2.39U23-305[»]
4K24X-ray4.50U23-303[»]
ProteinModelPortalQ03405.
SMRQ03405. Positions 23-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111345. 27 interactions.
DIPDIP-137N.
IntActQ03405. 4 interactions.
MINTMINT-1370900.

Chemistry

BindingDBQ03405.
ChEMBLCHEMBL4883.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00086. Streptokinase.
DB00031. Tenecteplase.
DB00013. Urokinase.

Polymorphism databases

DMDM465003.

Proteomic databases

PaxDbQ03405.
PRIDEQ03405.

Protocols and materials databases

DNASU5329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221264; ENSP00000221264; ENSG00000011422. [Q03405-3]
ENST00000339082; ENSP00000342049; ENSG00000011422. [Q03405-2]
ENST00000340093; ENSP00000339328; ENSG00000011422. [Q03405-1]
GeneID5329.
KEGGhsa:5329.
UCSCuc002oxd.2. human. [Q03405-2]
uc002oxf.2. human. [Q03405-1]
uc002oxg.2. human. [Q03405-3]

Organism-specific databases

CTD5329.
GeneCardsGC19M044150.
HGNCHGNC:9053. PLAUR.
HPAHPA050843.
MIM173391. gene.
neXtProtNX_Q03405.
PharmGKBPA33383.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41870.
HOVERGENHBG000245.
InParanoidQ03405.
KOK03985.
OMATNRTMSY.
OrthoDBEOG7QRQVG.
PhylomeDBQ03405.
TreeFamTF338662.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ03405.
BgeeQ03405.
GenevestigatorQ03405.

Family and domain databases

InterProIPR018363. CD59_antigen_CS.
IPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]
PfamPF00021. UPAR_LY6. 3 hits.
[Graphical view]
SMARTSM00134. LU. 3 hits.
[Graphical view]
PROSITEPS00983. LY6_UPAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03405.
GeneWikiUrokinase_receptor.
GenomeRNAi5329.
NextBio20632.
PMAP-CutDBQ03405.
PROQ03405.
SOURCESearch...

Entry information

Entry nameUPAR_HUMAN
AccessionPrimary (citable) accession number: Q03405
Secondary accession number(s): A8K409 expand/collapse secondary AC list , Q12876, Q15845, Q16887, Q6IB52, Q9BWT0, Q9NYC8, Q9UD69, Q9UEA6, Q9UM92, Q9UMV0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries