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P00749

- UROK_HUMAN

UniProt

P00749 - UROK_HUMAN

Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 194 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

    Catalytic activityi

    Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

    Enzyme regulationi

    Inhibited by SERPINA5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei177 – 1782Cleavage; during zymogen activation
    Active sitei224 – 2241Charge relay system
    Active sitei275 – 2751Charge relay system
    Active sitei376 – 3761Charge relay system

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase activity Source: Reactome

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. chemotaxis Source: ProtInc
    3. fibrinolysis Source: Reactome
    4. proteolysis Source: ProtInc
    5. regulation of cell adhesion mediated by integrin Source: BHF-UCL
    6. regulation of cell proliferation Source: Ensembl
    7. regulation of receptor activity Source: BHF-UCL
    8. regulation of smooth muscle cell-matrix adhesion Source: BHF-UCL
    9. regulation of smooth muscle cell migration Source: BHF-UCL
    10. regulation of wound healing Source: BHF-UCL
    11. response to hypoxia Source: Ensembl
    12. signal transduction Source: ProtInc
    13. smooth muscle cell migration Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Fibrinolysis, Hemostasis, Plasminogen activation

    Enzyme and pathway databases

    ReactomeiREACT_641. Dissolution of Fibrin Clot.
    SABIO-RKP00749.

    Protein family/group databases

    MEROPSiS01.231.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urokinase-type plasminogen activator (EC:3.4.21.73)
    Short name:
    U-plasminogen activator
    Short name:
    uPA
    Cleaved into the following 3 chains:
    Gene namesi
    Name:PLAU
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9052. PLAU.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Quebec platelet disorder (QPD) [MIM:601709]: An autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Pharmaceutical usei

    Available under the name Abbokinase (Abbott). Used in Pulmonary Embolism (PE) to initiate fibrinolysis. Clinically used for therapy of thrombolytic disorders.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi158 – 1581S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. 1 Publication
    Mutagenesisi323 – 3231S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. 1 Publication

    Organism-specific databases

    MIMi601709. phenotype.
    Orphaneti220436. Quebec platelet disorder.
    PharmGKBiPA33382.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 431411Urokinase-type plasminogen activatorPRO_0000028318Add
    BLAST
    Chaini21 – 177157Urokinase-type plasminogen activator long chain APRO_0000028319Add
    BLAST
    Chaini156 – 17722Urokinase-type plasminogen activator short chain APRO_0000028320Add
    BLAST
    Chaini179 – 431253Urokinase-type plasminogen activator chain BPRO_0000028321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 39
    Disulfide bondi33 ↔ 51
    Glycosylationi38 – 381O-linked (Fuc)1 Publication
    Disulfide bondi53 ↔ 62
    Disulfide bondi70 ↔ 151
    Disulfide bondi91 ↔ 133
    Disulfide bondi122 ↔ 146
    Modified residuei158 – 1581Phosphoserine1 Publication
    Disulfide bondi168 ↔ 299Interchain (between A and B chains)
    Disulfide bondi209 ↔ 225
    Disulfide bondi217 ↔ 288
    Disulfide bondi313 ↔ 382
    Glycosylationi322 – 3221N-linked (GlcNAc...)CAR_000026
    Modified residuei323 – 3231Phosphoserine1 Publication
    Disulfide bondi345 ↔ 361
    Disulfide bondi372 ↔ 400

    Post-translational modificationi

    Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP00749.
    PaxDbiP00749.
    PRIDEiP00749.

    PTM databases

    PhosphoSiteiP00749.
    UniCarbKBiP00749.

    Miscellaneous databases

    PMAP-CutDBQ53XS3.

    Expressioni

    Tissue specificityi

    Expressed in the prostate gland and prostate cancers.1 Publication

    Gene expression databases

    ArrayExpressiP00749.
    BgeeiP00749.
    CleanExiHS_PLAU.
    GenevestigatoriP00749.

    Organism-specific databases

    HPAiHPA008719.

    Interactioni

    Subunit structurei

    Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR.3 Publications

    Protein-protein interaction databases

    BioGridi111344. 19 interactions.
    DIPiDIP-46387N.
    IntActiP00749. 4 interactions.
    STRINGi9606.ENSP00000361850.

    Structurei

    Secondary structure

    1
    431
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 363
    Beta strandi38 – 414
    Turni43 – 475
    Beta strandi49 – 524
    Beta strandi57 – 593
    Beta strandi64 – 674
    Beta strandi73 – 775
    Beta strandi86 – 894
    Beta strandi94 – 963
    Helixi99 – 1013
    Beta strandi102 – 1043
    Beta strandi106 – 1083
    Helixi111 – 1144
    Beta strandi117 – 1193
    Beta strandi132 – 1376
    Beta strandi140 – 1478
    Helixi162 – 1654
    Beta strandi180 – 1845
    Helixi187 – 1893
    Beta strandi193 – 1997
    Turni201 – 2033
    Beta strandi205 – 21511
    Beta strandi218 – 2214
    Helixi223 – 2253
    Turni226 – 2283
    Helixi232 – 2343
    Beta strandi235 – 2406
    Beta strandi243 – 2464
    Beta strandi252 – 26110
    Beta strandi269 – 2713
    Beta strandi272 – 2743
    Beta strandi277 – 2826
    Beta strandi293 – 2953
    Beta strandi312 – 3187
    Beta strandi329 – 3313
    Beta strandi333 – 3408
    Helixi342 – 3454
    Turni348 – 3514
    Helixi352 – 3543
    Turni356 – 3583
    Beta strandi359 – 3635
    Beta strandi365 – 3673
    Beta strandi379 – 3846
    Beta strandi387 – 39610
    Beta strandi398 – 4025
    Beta strandi407 – 4115
    Helixi412 – 4143
    Helixi416 – 4227

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C5WX-ray1.94A156-178[»]
    B179-431[»]
    1C5XX-ray1.75A156-178[»]
    B179-431[»]
    1C5YX-ray1.65A156-178[»]
    B179-431[»]
    1C5ZX-ray1.85A156-178[»]
    B179-431[»]
    1EJNX-ray1.80A179-431[»]
    1F5KX-ray1.80U179-431[»]
    1F5LX-ray2.10A179-431[»]
    1F92X-ray2.60A179-431[»]
    1FV9X-ray3.00A179-423[»]
    1GI7X-ray1.79A156-178[»]
    B179-423[»]
    1GI8X-ray1.75A156-178[»]
    B179-423[»]
    1GI9X-ray1.80A156-178[»]
    B179-423[»]
    1GJ7X-ray1.50A156-178[»]
    B179-431[»]
    1GJ8X-ray1.64A156-178[»]
    B179-431[»]
    1GJ9X-ray1.80A156-178[»]
    B179-431[»]
    1GJAX-ray1.56A156-178[»]
    B179-431[»]
    1GJBX-ray1.90A156-178[»]
    B179-431[»]
    1GJCX-ray1.73A156-178[»]
    B179-431[»]
    1GJDX-ray1.75A156-178[»]
    B179-431[»]
    1KDUNMR-A69-153[»]
    1LMWX-ray2.50A/C156-178[»]
    B/D179-431[»]
    1O3PX-ray1.81A156-178[»]
    B179-431[»]
    1O5AX-ray1.68A156-178[»]
    B179-431[»]
    1O5BX-ray1.85A156-178[»]
    B179-431[»]
    1O5CX-ray1.63A156-178[»]
    B179-431[»]
    1OWDX-ray2.32A179-423[»]
    1OWEX-ray1.60A179-423[»]
    1OWHX-ray1.61A179-410[»]
    1OWIX-ray2.93A179-423[»]
    1OWJX-ray3.10A179-423[»]
    1OWKX-ray2.80A179-423[»]
    1SC8X-ray2.40U164-425[»]
    1SQAX-ray2.00A179-423[»]
    1SQOX-ray1.84A179-423[»]
    1SQTX-ray1.90A179-423[»]
    1U6QX-ray2.02A179-423[»]
    1URKNMR-A26-155[»]
    1VJ9X-ray2.40U164-425[»]
    1VJAX-ray2.00U164-425[»]
    1W0ZX-ray1.90U179-425[»]
    1W10X-ray2.00U179-425[»]
    1W11X-ray2.00U179-425[»]
    1W12X-ray2.40U179-425[»]
    1W13X-ray2.00U179-425[»]
    1W14X-ray2.20U179-425[»]
    2FD6X-ray1.90A31-152[»]
    2I9AX-ray1.90A/B/C/D21-163[»]
    2I9BX-ray2.80A/B/C/D21-163[»]
    2NWNX-ray2.15A179-431[»]
    2O8TX-ray1.45A179-431[»]
    2O8UX-ray1.70A179-431[»]
    2O8WX-ray1.86A179-431[»]
    2R2WX-ray2.01U179-431[»]
    2VINX-ray1.90A179-431[»]
    2VIOX-ray1.80A179-431[»]
    2VIPX-ray1.72A179-431[»]
    2VIQX-ray2.00A179-431[»]
    2VIVX-ray1.72A179-431[»]
    2VIWX-ray2.05A179-431[»]
    2VNTX-ray2.20A/B/C/D/E/F156-431[»]
    3BT1X-ray2.80A21-153[»]
    3BT2X-ray2.50A21-153[»]
    3IG6X-ray1.83A/C156-178[»]
    B/D179-431[»]
    3KGPX-ray2.35A179-431[»]
    3KHVX-ray2.35A179-431[»]
    3KIDX-ray2.71U179-431[»]
    3M61X-ray1.68U179-431[»]
    3MHWX-ray1.45U179-425[»]
    3MWIX-ray2.03U179-424[»]
    3OX7X-ray1.58U179-431[»]
    3OY5X-ray2.31U179-431[»]
    3OY6X-ray2.31U179-431[»]
    3PB1X-ray2.30E179-431[»]
    3QN7X-ray1.90A179-431[»]
    3U73X-ray3.19A21-152[»]
    4DVAX-ray1.94U179-424[»]
    4DW2X-ray2.97U179-424[»]
    4FU7X-ray2.00A179-424[»]
    4FU8X-ray2.20A179-424[»]
    4FU9X-ray1.60A179-424[»]
    4FUBX-ray1.90A179-424[»]
    4FUCX-ray1.72A179-424[»]
    4FUDX-ray2.00A179-424[»]
    4FUEX-ray2.00A179-424[»]
    4FUFX-ray2.00A179-424[»]
    4FUGX-ray1.80A179-424[»]
    4FUHX-ray1.60A179-424[»]
    4FUIX-ray2.00A179-424[»]
    4FUJX-ray2.05A179-424[»]
    4GLYX-ray1.52A179-423[»]
    4H42X-ray2.01U179-426[»]
    4JK5X-ray1.55A179-423[»]
    4JK6X-ray2.20A179-423[»]
    4JNIX-ray1.17U179-425[»]
    4JNLX-ray2.00U179-425[»]
    4K24X-ray4.50A21-153[»]
    4MNVX-ray1.80A179-423[»]
    4MNWX-ray1.49A179-423[»]
    4MNXX-ray1.85A179-423[»]
    4MNYX-ray1.70A/B179-423[»]
    ProteinModelPortaliP00749.
    SMRiP00749. Positions 26-152, 179-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00749.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 6337EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 15182KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini179 – 424246Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 5724Binds urokinase plasminogen activator surface receptorBy similarityAdd
    BLAST
    Regioni152 – 17726Connecting peptideAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Kringle, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG008633.
    InParanoidiP00749.
    KOiK01348.
    OrthoDBiEOG75B84T.
    PhylomeDBiP00749.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 1 hit.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00181. EGF. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00749-1) [UniParc]FASTAAdd to Basket

    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

    MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW    50
    CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL 100
    QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD 150
    CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH 200
    RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG 250
    EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL 300
    PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY 350
    YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC 400
    ALKDKPGVYT RVSHFLPWIR SHTKEENGLA L 431
    Length:431
    Mass (Da):48,507
    Last modified:July 28, 2009 - v2
    Checksum:i62C72400BC23115F
    GO
    Isoform 2 (identifier: P00749-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MRALLARLLLCVLVVSDSKGSNELHQVPS → MVFHLRTRYEQA

    Show »
    Length:414
    Mass (Da):46,908
    Checksum:iFB35DBE360D7E1CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501D → G in BAG60754. (PubMed:14702039)Curated
    Sequence conflicti151 – 1511C → W in CAA26535. (PubMed:3888571)Curated
    Sequence conflicti386 – 3861G → C in CAA26535. (PubMed:3888571)Curated
    Sequence conflicti430 – 4301A → V in CAA26535. (PubMed:3888571)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151V → L.1 Publication
    Corresponds to variant rs2227580 [ dbSNP | Ensembl ].
    VAR_038730
    Natural varianti141 – 1411P → L.6 Publications
    Corresponds to variant rs2227564 [ dbSNP | Ensembl ].
    VAR_006722
    Natural varianti214 – 2141I → M.2 Publications
    VAR_013102
    Natural varianti231 – 2311K → Q.1 Publication
    Corresponds to variant rs2227567 [ dbSNP | Ensembl ].
    VAR_038731

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929MRALL…HQVPS → MVFHLRTRYEQA in isoform 2. 1 PublicationVSP_038368Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15476 mRNA. Translation: AAA61253.1.
    X02760 mRNA. Translation: CAA26535.1.
    D00244 mRNA. Translation: BAA00175.1.
    K03226 mRNA. Translation: AAC97138.1.
    X02419 Genomic DNA. Translation: CAA26268.1.
    AF377330 Genomic DNA. Translation: AAK53822.1.
    BT007391 mRNA. Translation: AAP36055.1.
    AK298560 mRNA. Translation: BAG60754.1.
    AL596247 Genomic DNA. Translation: CAI13969.1.
    CH471083 Genomic DNA. Translation: EAW54544.1.
    BC013575 mRNA. Translation: AAH13575.1.
    D11143 mRNA. Translation: BAA01919.1.
    K02286 Genomic DNA. Translation: AAA61252.1.
    CCDSiCCDS44442.1. [P00749-2]
    CCDS7339.1. [P00749-1]
    PIRiA00931. UKHU.
    RefSeqiNP_001138503.1. NM_001145031.1. [P00749-2]
    NP_002649.1. NM_002658.3. [P00749-1]
    UniGeneiHs.77274.

    Genome annotation databases

    EnsembliENST00000372764; ENSP00000361850; ENSG00000122861.
    ENST00000496777; ENSP00000431795; ENSG00000122861.
    GeneIDi5328.
    KEGGihsa:5328.
    UCSCiuc001jwa.3. human. [P00749-1]
    uc010qkw.2. human. [P00749-2]

    Polymorphism databases

    DMDMi254763341.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Urokinase entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15476 mRNA. Translation: AAA61253.1 .
    X02760 mRNA. Translation: CAA26535.1 .
    D00244 mRNA. Translation: BAA00175.1 .
    K03226 mRNA. Translation: AAC97138.1 .
    X02419 Genomic DNA. Translation: CAA26268.1 .
    AF377330 Genomic DNA. Translation: AAK53822.1 .
    BT007391 mRNA. Translation: AAP36055.1 .
    AK298560 mRNA. Translation: BAG60754.1 .
    AL596247 Genomic DNA. Translation: CAI13969.1 .
    CH471083 Genomic DNA. Translation: EAW54544.1 .
    BC013575 mRNA. Translation: AAH13575.1 .
    D11143 mRNA. Translation: BAA01919.1 .
    K02286 Genomic DNA. Translation: AAA61252.1 .
    CCDSi CCDS44442.1. [P00749-2 ]
    CCDS7339.1. [P00749-1 ]
    PIRi A00931. UKHU.
    RefSeqi NP_001138503.1. NM_001145031.1. [P00749-2 ]
    NP_002649.1. NM_002658.3. [P00749-1 ]
    UniGenei Hs.77274.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C5W X-ray 1.94 A 156-178 [» ]
    B 179-431 [» ]
    1C5X X-ray 1.75 A 156-178 [» ]
    B 179-431 [» ]
    1C5Y X-ray 1.65 A 156-178 [» ]
    B 179-431 [» ]
    1C5Z X-ray 1.85 A 156-178 [» ]
    B 179-431 [» ]
    1EJN X-ray 1.80 A 179-431 [» ]
    1F5K X-ray 1.80 U 179-431 [» ]
    1F5L X-ray 2.10 A 179-431 [» ]
    1F92 X-ray 2.60 A 179-431 [» ]
    1FV9 X-ray 3.00 A 179-423 [» ]
    1GI7 X-ray 1.79 A 156-178 [» ]
    B 179-423 [» ]
    1GI8 X-ray 1.75 A 156-178 [» ]
    B 179-423 [» ]
    1GI9 X-ray 1.80 A 156-178 [» ]
    B 179-423 [» ]
    1GJ7 X-ray 1.50 A 156-178 [» ]
    B 179-431 [» ]
    1GJ8 X-ray 1.64 A 156-178 [» ]
    B 179-431 [» ]
    1GJ9 X-ray 1.80 A 156-178 [» ]
    B 179-431 [» ]
    1GJA X-ray 1.56 A 156-178 [» ]
    B 179-431 [» ]
    1GJB X-ray 1.90 A 156-178 [» ]
    B 179-431 [» ]
    1GJC X-ray 1.73 A 156-178 [» ]
    B 179-431 [» ]
    1GJD X-ray 1.75 A 156-178 [» ]
    B 179-431 [» ]
    1KDU NMR - A 69-153 [» ]
    1LMW X-ray 2.50 A/C 156-178 [» ]
    B/D 179-431 [» ]
    1O3P X-ray 1.81 A 156-178 [» ]
    B 179-431 [» ]
    1O5A X-ray 1.68 A 156-178 [» ]
    B 179-431 [» ]
    1O5B X-ray 1.85 A 156-178 [» ]
    B 179-431 [» ]
    1O5C X-ray 1.63 A 156-178 [» ]
    B 179-431 [» ]
    1OWD X-ray 2.32 A 179-423 [» ]
    1OWE X-ray 1.60 A 179-423 [» ]
    1OWH X-ray 1.61 A 179-410 [» ]
    1OWI X-ray 2.93 A 179-423 [» ]
    1OWJ X-ray 3.10 A 179-423 [» ]
    1OWK X-ray 2.80 A 179-423 [» ]
    1SC8 X-ray 2.40 U 164-425 [» ]
    1SQA X-ray 2.00 A 179-423 [» ]
    1SQO X-ray 1.84 A 179-423 [» ]
    1SQT X-ray 1.90 A 179-423 [» ]
    1U6Q X-ray 2.02 A 179-423 [» ]
    1URK NMR - A 26-155 [» ]
    1VJ9 X-ray 2.40 U 164-425 [» ]
    1VJA X-ray 2.00 U 164-425 [» ]
    1W0Z X-ray 1.90 U 179-425 [» ]
    1W10 X-ray 2.00 U 179-425 [» ]
    1W11 X-ray 2.00 U 179-425 [» ]
    1W12 X-ray 2.40 U 179-425 [» ]
    1W13 X-ray 2.00 U 179-425 [» ]
    1W14 X-ray 2.20 U 179-425 [» ]
    2FD6 X-ray 1.90 A 31-152 [» ]
    2I9A X-ray 1.90 A/B/C/D 21-163 [» ]
    2I9B X-ray 2.80 A/B/C/D 21-163 [» ]
    2NWN X-ray 2.15 A 179-431 [» ]
    2O8T X-ray 1.45 A 179-431 [» ]
    2O8U X-ray 1.70 A 179-431 [» ]
    2O8W X-ray 1.86 A 179-431 [» ]
    2R2W X-ray 2.01 U 179-431 [» ]
    2VIN X-ray 1.90 A 179-431 [» ]
    2VIO X-ray 1.80 A 179-431 [» ]
    2VIP X-ray 1.72 A 179-431 [» ]
    2VIQ X-ray 2.00 A 179-431 [» ]
    2VIV X-ray 1.72 A 179-431 [» ]
    2VIW X-ray 2.05 A 179-431 [» ]
    2VNT X-ray 2.20 A/B/C/D/E/F 156-431 [» ]
    3BT1 X-ray 2.80 A 21-153 [» ]
    3BT2 X-ray 2.50 A 21-153 [» ]
    3IG6 X-ray 1.83 A/C 156-178 [» ]
    B/D 179-431 [» ]
    3KGP X-ray 2.35 A 179-431 [» ]
    3KHV X-ray 2.35 A 179-431 [» ]
    3KID X-ray 2.71 U 179-431 [» ]
    3M61 X-ray 1.68 U 179-431 [» ]
    3MHW X-ray 1.45 U 179-425 [» ]
    3MWI X-ray 2.03 U 179-424 [» ]
    3OX7 X-ray 1.58 U 179-431 [» ]
    3OY5 X-ray 2.31 U 179-431 [» ]
    3OY6 X-ray 2.31 U 179-431 [» ]
    3PB1 X-ray 2.30 E 179-431 [» ]
    3QN7 X-ray 1.90 A 179-431 [» ]
    3U73 X-ray 3.19 A 21-152 [» ]
    4DVA X-ray 1.94 U 179-424 [» ]
    4DW2 X-ray 2.97 U 179-424 [» ]
    4FU7 X-ray 2.00 A 179-424 [» ]
    4FU8 X-ray 2.20 A 179-424 [» ]
    4FU9 X-ray 1.60 A 179-424 [» ]
    4FUB X-ray 1.90 A 179-424 [» ]
    4FUC X-ray 1.72 A 179-424 [» ]
    4FUD X-ray 2.00 A 179-424 [» ]
    4FUE X-ray 2.00 A 179-424 [» ]
    4FUF X-ray 2.00 A 179-424 [» ]
    4FUG X-ray 1.80 A 179-424 [» ]
    4FUH X-ray 1.60 A 179-424 [» ]
    4FUI X-ray 2.00 A 179-424 [» ]
    4FUJ X-ray 2.05 A 179-424 [» ]
    4GLY X-ray 1.52 A 179-423 [» ]
    4H42 X-ray 2.01 U 179-426 [» ]
    4JK5 X-ray 1.55 A 179-423 [» ]
    4JK6 X-ray 2.20 A 179-423 [» ]
    4JNI X-ray 1.17 U 179-425 [» ]
    4JNL X-ray 2.00 U 179-425 [» ]
    4K24 X-ray 4.50 A 21-153 [» ]
    4MNV X-ray 1.80 A 179-423 [» ]
    4MNW X-ray 1.49 A 179-423 [» ]
    4MNX X-ray 1.85 A 179-423 [» ]
    4MNY X-ray 1.70 A/B 179-423 [» ]
    ProteinModelPortali P00749.
    SMRi P00749. Positions 26-152, 179-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111344. 19 interactions.
    DIPi DIP-46387N.
    IntActi P00749. 4 interactions.
    STRINGi 9606.ENSP00000361850.

    Chemistry

    BindingDBi P00749.
    ChEMBLi CHEMBL2111379.
    DrugBanki DB00594. Amiloride.
    DB00013. Urokinase.
    GuidetoPHARMACOLOGYi 2393.

    Protein family/group databases

    MEROPSi S01.231.

    PTM databases

    PhosphoSitei P00749.
    UniCarbKBi P00749.

    Polymorphism databases

    DMDMi 254763341.

    Proteomic databases

    MaxQBi P00749.
    PaxDbi P00749.
    PRIDEi P00749.

    Protocols and materials databases

    DNASUi 5328.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372764 ; ENSP00000361850 ; ENSG00000122861 .
    ENST00000496777 ; ENSP00000431795 ; ENSG00000122861 .
    GeneIDi 5328.
    KEGGi hsa:5328.
    UCSCi uc001jwa.3. human. [P00749-1 ]
    uc010qkw.2. human. [P00749-2 ]

    Organism-specific databases

    CTDi 5328.
    GeneCardsi GC10P075668.
    HGNCi HGNC:9052. PLAU.
    HPAi HPA008719.
    MIMi 191840. gene.
    601709. phenotype.
    neXtProti NX_P00749.
    Orphaneti 220436. Quebec platelet disorder.
    PharmGKBi PA33382.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG008633.
    InParanoidi P00749.
    KOi K01348.
    OrthoDBi EOG75B84T.
    PhylomeDBi P00749.
    TreeFami TF329901.

    Enzyme and pathway databases

    Reactomei REACT_641. Dissolution of Fibrin Clot.
    SABIO-RK P00749.

    Miscellaneous databases

    EvolutionaryTracei P00749.
    GeneWikii PLAU.
    GenomeRNAii 5328.
    NextBioi 20628.
    PMAP-CutDB Q53XS3.
    PROi P00749.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00749.
    Bgeei P00749.
    CleanExi HS_PLAU.
    Genevestigatori P00749.

    Family and domain databases

    Gene3Di 2.40.20.10. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00181. EGF. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the gene for pro-urokinase in Escherichia coli."
      Holmes W.E., Pennica D., Blaber M., Rey M.W., Guenzler W.A., Steffens G.J., Heyneker H.L.
      Biotechnology (N.Y.) 3:923-929(1985)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning, sequencing, and expression in Escherichia coli of human preprourokinase cDNA."
      Jacobs P., Cravador A., Loriau R., Brockly F., Colau B., Chuchana P., van Elsen A., Herzog A., Bollen A.
      DNA 4:139-146(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Molecular cloning of cDNA coding for human preprourokinase."
      Nagai M., Hiramatsu R., Kaneda T., Hayasuke N., Arimura H., Nishida M., Suyama T.
      Gene 36:183-188(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The human urokinase-plasminogen activator gene and its promoter."
      Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F.
      Nucleic Acids Res. 13:2759-2771(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-214.
    5. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 2).
      Tissue: Mesangial cell.
    7. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-15; LEU-141 AND GLN-231.
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-141.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Lung.
    11. "Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure."
      Yoshimoto M., Ushiyama Y., Sakai M., Tamaki S., Hara H., Takahashi K., Sawasaki Y., Hanada K.
      Biochim. Biophys. Acta 1293:83-89(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-431, VARIANT LEU-141.
    12. "Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator."
      Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R., Sarin V.K.
      Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA."
      Verde P., Stoppelli M.P., Galeffi P., di Nocera P., Blasi F.
      Proc. Natl. Acad. Sci. U.S.A. 81:4727-4731(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431, VARIANT MET-214.
    14. "The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain."
      Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E., Flohe L.
      Hoppe-Seyler's Z. Physiol. Chem. 363:1155-1165(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-177.
    15. "Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains."
      Schaller J., Nick H., Rickli E.E., Gillessen D., Lergier W., Studer R.O.
      Eur. J. Biochem. 125:251-257(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 156-176 AND 179-224.
    16. "The complete amino acid sequence of low molecular mass urokinase from human urine."
      Steffens G.J., Gunzler W.A., Otting F., Frankus E., Flohe L.
      Hoppe-Seyler's Z. Physiol. Chem. 363:1043-1058(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 158-410.
    17. "Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for identity of PCI and plasminogen activator inhibitor 3."
      Stief T.W., Radtke K.P., Heimburger N.
      Biol. Chem. Hoppe-Seyler 368:1427-1433(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
    18. "Phosphorylation of human pro-urokinase on Ser138/303 impairs its receptor-dependent ability to promote myelomonocytic adherence and motility."
      Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C., Mastronicola M.R., Nolli M.L., Stoppelli M.P.
      J. Cell Biol. 137:779-791(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-158 AND SER-323, MUTAGENESIS OF SER-158 AND SER-323.
    19. "Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility."
      He S., Lin Y.L., Liu Y.X.
      Mol. Hum. Reprod. 5:513-519(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMER WITH SERPINA5.
    20. "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.
    21. "The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
      Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
      J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP1B.
    22. "Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma."
      Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.
      Int. J. Cancer 108:516-523(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
    23. "Platelet-derived growth factor D is activated by urokinase plasminogen activator in prostate carcinoma cells."
      Ustach C.V., Kim H.-R.C.
      Mol. Cell. Biol. 25:6279-6288(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    24. "Persons with Quebec platelet disorder have a tandem duplication of PLAU, the urokinase plasminogen activator gene."
      Paterson A.D., Rommens J.M., Bharaj B., Blavignac J., Wong I., Diamandis M., Waye J.S., Rivard G.E., Hayward C.P.
      Blood 115:1264-1266(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN QPD.
    25. "Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR."
      Oswald R.E., Bogusky M.J., Bamberger M., Smith R.A.G., Dobson C.M.
      Nature 337:579-582(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    26. "Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase."
      Li X., Smith R.A.G., Dobson C.M.
      Biochemistry 31:9562-9571(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 67-155.
    27. "Solution structure of the kringle domain from urokinase-type plasminogen activator."
      Li X., Bokman A.M., Llinas M., Smith R.A.G., Dobson C.M.
      J. Mol. Biol. 235:1548-1559(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 67-155.
    28. "The crystal structure of the catalytic domain of human urokinase-type plasminogen activator."
      Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D., Dobson C.M., Stuart D.I., Jones E.Y.
      Structure 3:681-691(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    29. "(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase."
      Sperl S., Jacob U., Arroyo de Prada N., Sturzebecher J., Wilhelm O.G., Bode W., Magdolen V., Huber R., Moroder L.
      Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
    30. "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 31-152 IN COMPLEX WITH PLAUR.
    31. "Detection of polymorphisms in the human urokinase-type plasminogen activator gene."
      Conne B., Berczy M., Belin D.
      Thromb. Haemost. 77:434-435(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-141.
    32. Erratum
      Conne B., Berczy M., Belin D.
      Thromb. Haemost. 78:973-973(1997)
    33. "Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer."
      Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.
      Electrophoresis 18:686-689(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-141.
    34. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-141.

    Entry informationi

    Entry nameiUROK_HUMAN
    AccessioniPrimary (citable) accession number: P00749
    Secondary accession number(s): B4DPZ2
    , Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 194 of the entry and version 2 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, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3