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Q03405

- UPAR_HUMAN

UniProt

Q03405 - UPAR_HUMAN

Protein

Urokinase plasminogen activator surface receptor

Gene

PLAUR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei105 – 1062Cleavage; by U-PA
    Sitei111 – 1122Cleavage; by U-PA

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. receptor activity Source: UniProtKB
    4. urokinase plasminogen activator receptor activity Source: UniProtKB

    GO - Biological processi

    1. attachment of GPI anchor to protein Source: Reactome
    2. blood coagulation Source: UniProtKB
    3. cellular component movement Source: UniProtKB
    4. cellular protein metabolic process Source: Reactome
    5. chemotaxis Source: ProtInc
    6. C-terminal protein lipidation Source: Reactome
    7. fibrinolysis Source: Reactome
    8. post-translational protein modification Source: Reactome
    9. regulation of proteolysis Source: UniProtKB
    10. signal transduction Source: ProtInc
    11. urokinase plasminogen activator signaling pathway Source: GOC

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_1830. Attachment of GPI anchor to uPAR.
    REACT_641. Dissolution of Fibrin Clot.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urokinase plasminogen activator surface receptor
    Short name:
    U-PAR
    Short name:
    uPAR
    Alternative name(s):
    Monocyte activation antigen Mo3
    CD_antigen: CD87
    Gene namesi
    Name:PLAUR
    Synonyms:MO3, UPAR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9053. PLAUR.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. endoplasmic reticulum lumen Source: Reactome
    3. endoplasmic reticulum membrane Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. extrinsic component of membrane Source: ProtInc
    6. integral component of membrane Source: UniProtKB
    7. integral component of plasma membrane Source: Ensembl
    8. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33383.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 305283Urokinase plasminogen activator surface receptorPRO_0000036090Add
    BLAST
    Propeptidei306 – 33530Removed in mature formCuratedPRO_0000036091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi25 ↔ 46
    Disulfide bondi28 ↔ 34
    Disulfide bondi39 ↔ 67
    Glycosylationi74 – 741N-linked (GlcNAc...)3 Publications
    Disulfide bondi93 ↔ 98
    Disulfide bondi117 ↔ 144
    Disulfide bondi120 ↔ 127
    Disulfide bondi137 ↔ 169
    Disulfide bondi175 ↔ 192
    Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
    Disulfide bondi193 ↔ 198
    Glycosylationi194 – 1941N-linked (GlcNAc...)2 Publications
    Disulfide bondi216 ↔ 244
    Disulfide bondi219 ↔ 227
    Glycosylationi222 – 2221N-linked (GlcNAc...)1 Publication
    Disulfide bondi237 ↔ 263
    Glycosylationi255 – 2551N-linked (GlcNAc...)1 Publication
    Disulfide bondi269 ↔ 287
    Disulfide bondi288 ↔ 293
    Lipidationi305 – 3051GPI-anchor amidated glycineCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ03405.
    PaxDbiQ03405.
    PRIDEiQ03405.

    Miscellaneous databases

    PMAP-CutDBQ03405.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ03405.
    BgeeiQ03405.
    GenevestigatoriQ03405.

    Organism-specific databases

    HPAiHPA050843.

    Interactioni

    Subunit structurei

    Monomer Probable. Interacts with MRC2. Interacts (via the UPAR/Ly6 domains) with SRPX2. Interacts with SORL1.6 PublicationsCurated

    Protein-protein interaction databases

    BioGridi111345. 27 interactions.
    DIPiDIP-137N.
    IntActiQ03405. 4 interactions.
    MINTiMINT-1370900.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 285
    Beta strandi34 – 385
    Beta strandi45 – 5410
    Beta strandi60 – 689
    Beta strandi75 – 817
    Beta strandi84 – 9310
    Turni96 – 994
    Beta strandi116 – 1216
    Turni122 – 1309
    Beta strandi133 – 1364
    Beta strandi138 – 1414
    Beta strandi143 – 1508
    Beta strandi155 – 1584
    Beta strandi164 – 1718
    Beta strandi176 – 1838
    Beta strandi186 – 1938
    Turni196 – 1994
    Helixi206 – 2083
    Beta strandi211 – 22212
    Turni223 – 2253
    Beta strandi226 – 2283
    Turni229 – 2313
    Beta strandi233 – 2386
    Beta strandi243 – 2519
    Turni252 – 2554
    Beta strandi256 – 2649
    Helixi266 – 2683
    Beta strandi270 – 2734
    Helixi275 – 2784
    Beta strandi284 – 2885
    Turni291 – 2944
    Helixi296 – 2983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ03405.
    SMRiQ03405. Positions 23-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03405.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11492UPAR/Ly6 1Add
    BLAST
    Domaini115 – 21399UPAR/Ly6 2Add
    BLAST
    Domaini214 – 30592UPAR/Ly6 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 UPAR/Ly6 domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG41870.
    HOVERGENiHBG000245.
    InParanoidiQ03405.
    KOiK03985.
    OMAiTNRTMSY.
    OrthoDBiEOG7QRQVG.
    PhylomeDBiQ03405.
    TreeFamiTF338662.

    Family and domain databases

    InterProiIPR018363. CD59_antigen_CS.
    IPR016054. LY6_UPA_recep-like.
    IPR001526. LY6_UPAR.
    [Graphical view]
    PfamiPF00021. UPAR_LY6. 3 hits.
    [Graphical view]
    SMARTiSM00134. LU. 3 hits.
    [Graphical view]
    PROSITEiPS00983. LY6_UPAR. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q03405-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGHPPLLPLL LLLHTCVPAS WGLRCMQCKT NGDCRVEECA LGQDLCRTTI    50
    VRLWEEGEEL ELVEKSCTHS EKTNRTLSYR TGLKITSLTE VVCGLDLCNQ 100
    GNSGRAVTYS RSRYLECISC GSSDMSCERG RHQSLQCRSP EEQCLDVVTH 150
    WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG FHNNDTFHFL KCCNTTKCNE 200
    GPILELENLP QNGRQCYSCK GNSTHGCSSE ETFLIDCRGP MNQCLVATGT 250
    HEPKNQSYMV RGCATASMCQ HAHLGDAFSM NHIDVSCCTK SGCNHPDLDV 300
    QYRSGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT 335
    Length:335
    Mass (Da):36,978
    Last modified:February 1, 1994 - v1
    Checksum:iAB1963EA3DC77171
    GO
    Isoform 2 (identifier: Q03405-2) [UniParc]FASTAAdd to Basket

    Also known as: uPAR2, Secreted

    The sequence of this isoform differs from the canonical sequence as follows:
         253-335: PKNQSYMVRG...RLWGGTLLWT → RSLWGSWLPCKSTTALRPPCCEEAQATHV

    Show »
    Length:281
    Mass (Da):31,263
    Checksum:iE6C580F279FB0316
    GO
    Isoform 3 (identifier: Q03405-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:290
    Mass (Da):32,016
    Checksum:i60F14E2A2AFB67AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281C → N AA sequence (PubMed:1689240)Curated
    Sequence conflicti165 – 1651H → P in AAK31795. 1 PublicationCurated
    Sequence conflicti213 – 2131G → E AA sequence (PubMed:7539799)Curated
    Sequence conflicti249 – 2491G → D in AAF71751. (PubMed:11051819)Curated
    Sequence conflicti252 – 2521E → G in AAF71751. (PubMed:11051819)Curated
    Isoform 3 (identifier: Q03405-3)
    Sequence conflicti158 – 1581V → I no nucleotide entry (PubMed:8131971)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551E → G.1 Publication
    Corresponds to variant rs4251813 [ dbSNP | Ensembl ].
    VAR_016322
    Natural varianti86 – 861T → A.1 Publication
    Corresponds to variant rs399145 [ dbSNP | Ensembl ].
    VAR_016323
    Natural varianti105 – 1051R → Q.1 Publication
    Corresponds to variant rs4251878 [ dbSNP | Ensembl ].
    VAR_016324
    Natural varianti220 – 2201K → R.1 Publication
    Corresponds to variant rs2302524 [ dbSNP | Ensembl ].
    VAR_016325
    Natural varianti281 – 2811N → K.1 Publication
    Corresponds to variant rs4251921 [ dbSNP | Ensembl ].
    VAR_016326
    Natural varianti297 – 2971D → A.
    Corresponds to variant rs16976608 [ dbSNP | Ensembl ].
    VAR_052698
    Natural varianti317 – 3171L → P.1 Publication
    Corresponds to variant rs4760 [ dbSNP | Ensembl ].
    VAR_014922

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei158 – 20245Missing in isoform 3. 2 PublicationsVSP_046345Add
    BLAST
    Alternative sequencei203 – 2031I → V in isoform 3. 2 PublicationsVSP_046346
    Alternative sequencei253 – 33583PKNQS…TLLWT → RSLWGSWLPCKSTTALRPPC CEEAQATHV in isoform 2. 2 PublicationsVSP_006715Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS12628.1. [Q03405-1]
    CCDS33041.1. [Q03405-2]
    CCDS33042.1. [Q03405-3]
    PIRiI52614.
    S12376. A39743.
    S39495.
    RefSeqiNP_001005376.1. NM_001005376.2. [Q03405-2]
    NP_001005377.1. NM_001005377.2. [Q03405-3]
    NP_002650.1. NM_002659.3. [Q03405-1]
    UniGeneiHs.466871.

    Genome annotation databases

    EnsembliENST00000221264; ENSP00000221264; ENSG00000011422. [Q03405-3]
    ENST00000339082; ENSP00000342049; ENSG00000011422. [Q03405-2]
    ENST00000340093; ENSP00000339328; ENSG00000011422. [Q03405-1]
    GeneIDi5329.
    KEGGihsa:5329.
    UCSCiuc002oxd.2. human. [Q03405-2]
    uc002oxf.2. human. [Q03405-1]
    uc002oxg.2. human. [Q03405-3]

    Polymorphism databases

    DMDMi465003.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS12628.1. [Q03405-1 ]
    CCDS33041.1. [Q03405-2 ]
    CCDS33042.1. [Q03405-3 ]
    PIRi I52614.
    S12376. A39743.
    S39495.
    RefSeqi NP_001005376.1. NM_001005376.2. [Q03405-2 ]
    NP_001005377.1. NM_001005377.2. [Q03405-3 ]
    NP_002650.1. NM_002659.3. [Q03405-1 ]
    UniGenei Hs.466871.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YWH X-ray 2.70 A/C/E/G/I/K/M/O 23-335 [» ]
    2FD6 X-ray 1.90 U 23-297 [» ]
    2I9B X-ray 2.80 E/F/G/H 23-299 [» ]
    3BT1 X-ray 2.80 U 23-303 [» ]
    3BT2 X-ray 2.50 U 23-303 [» ]
    3U73 X-ray 3.19 U 23-305 [» ]
    3U74 X-ray 2.39 U 23-305 [» ]
    4K24 X-ray 4.50 U 23-303 [» ]
    ProteinModelPortali Q03405.
    SMRi Q03405. Positions 23-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111345. 27 interactions.
    DIPi DIP-137N.
    IntActi Q03405. 4 interactions.
    MINTi MINT-1370900.

    Chemistry

    BindingDBi Q03405.
    ChEMBLi CHEMBL4883.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00086. Streptokinase.
    DB00031. Tenecteplase.
    DB00013. Urokinase.

    Polymorphism databases

    DMDMi 465003.

    Proteomic databases

    MaxQBi Q03405.
    PaxDbi Q03405.
    PRIDEi Q03405.

    Protocols and materials databases

    DNASUi 5329.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221264 ; ENSP00000221264 ; ENSG00000011422 . [Q03405-3 ]
    ENST00000339082 ; ENSP00000342049 ; ENSG00000011422 . [Q03405-2 ]
    ENST00000340093 ; ENSP00000339328 ; ENSG00000011422 . [Q03405-1 ]
    GeneIDi 5329.
    KEGGi hsa:5329.
    UCSCi uc002oxd.2. human. [Q03405-2 ]
    uc002oxf.2. human. [Q03405-1 ]
    uc002oxg.2. human. [Q03405-3 ]

    Organism-specific databases

    CTDi 5329.
    GeneCardsi GC19M044150.
    HGNCi HGNC:9053. PLAUR.
    HPAi HPA050843.
    MIMi 173391. gene.
    neXtProti NX_Q03405.
    PharmGKBi PA33383.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41870.
    HOVERGENi HBG000245.
    InParanoidi Q03405.
    KOi K03985.
    OMAi TNRTMSY.
    OrthoDBi EOG7QRQVG.
    PhylomeDBi Q03405.
    TreeFami TF338662.

    Enzyme and pathway databases

    Reactomei REACT_1830. Attachment of GPI anchor to uPAR.
    REACT_641. Dissolution of Fibrin Clot.

    Miscellaneous databases

    EvolutionaryTracei Q03405.
    GeneWikii Urokinase_receptor.
    GenomeRNAii 5329.
    NextBioi 20632.
    PMAP-CutDB Q03405.
    PROi Q03405.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03405.
    Bgeei Q03405.
    Genevestigatori Q03405.

    Family and domain databases

    InterProi IPR018363. CD59_antigen_CS.
    IPR016054. LY6_UPA_recep-like.
    IPR001526. LY6_UPAR.
    [Graphical view ]
    Pfami PF00021. UPAR_LY6. 3 hits.
    [Graphical view ]
    SMARTi SM00134. LU. 3 hits.
    [Graphical view ]
    PROSITEi PS00983. LY6_UPAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiUPAR_HUMAN
    AccessioniPrimary (citable) accession number: Q03405
    Secondary accession number(s): A8K409
    , Q12876, Q15845, Q16887, Q6IB52, Q9BWT0, Q9NYC8, Q9UD69, Q9UEA6, Q9UM92, Q9UMV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 157 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3