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

P00749 (UROK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 189. 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-type plasminogen activator

Short name=U-plasminogen activator
Short name=uPA
EC=3.4.21.73
Gene names
Name:PLAU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Inhibited by SERPINA5. Ref.17 Ref.22

Subunit structure

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. Ref.20 Ref.21

Subcellular location

Secreted.

Tissue specificity

Expressed in the prostate gland and prostate cancers. Ref.23

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Pharmaceutical use

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

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 EGF-like domain.

Contains 1 kringle domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Hemostasis
Plasminogen activation
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Kringle
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

chemotaxis

Traceable author statement PubMed 10749881. Source: ProtInc

fibrinolysis

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement Ref.13. Source: ProtInc

regulation of cell adhesion mediated by integrin

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of receptor activity

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

regulation of smooth muscle cell migration

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

regulation of smooth muscle cell-matrix adhesion

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

regulation of wound healing

Inferred by curator PubMed 8837777. Source: BHF-UCL

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 10749881. Source: ProtInc

smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionserine-type endopeptidase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00749-1)

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: P00749-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.12 Ref.14
Chain21 – 431411Urokinase-type plasminogen activator
PRO_0000028318
Chain21 – 177157Urokinase-type plasminogen activator long chain A
PRO_0000028319
Chain156 – 17722Urokinase-type plasminogen activator short chain A
PRO_0000028320
Chain179 – 431253Urokinase-type plasminogen activator chain B
PRO_0000028321

Regions

Domain27 – 6337EGF-like
Domain70 – 15182Kringle
Domain179 – 424246Peptidase S1
Region34 – 5724Binds urokinase plasminogen activator surface receptor By similarity
Region152 – 17726Connecting peptide

Sites

Active site2241Charge relay system
Active site2751Charge relay system
Active site3761Charge relay system
Site177 – 1782Cleavage; during zymogen activation

Amino acid modifications

Modified residue1581Phosphoserine Ref.18
Modified residue3231Phosphoserine Ref.18
Glycosylation381O-linked (Fuc) Ref.12
Glycosylation3221N-linked (GlcNAc...)
CAR_000026
Disulfide bond31 ↔ 39
Disulfide bond33 ↔ 51
Disulfide bond53 ↔ 62
Disulfide bond70 ↔ 151
Disulfide bond91 ↔ 133
Disulfide bond122 ↔ 146
Disulfide bond168 ↔ 299Interchain (between A and B chains)
Disulfide bond209 ↔ 225
Disulfide bond217 ↔ 288
Disulfide bond313 ↔ 382
Disulfide bond345 ↔ 361
Disulfide bond372 ↔ 400

Natural variations

Alternative sequence1 – 2929MRALL…HQVPS → MVFHLRTRYEQA in isoform 2.
VSP_038368
Natural variant151V → L. Ref.7
Corresponds to variant rs2227580 [ dbSNP | Ensembl ].
VAR_038730
Natural variant1411P → L. Ref.7 Ref.8 Ref.11 Ref.31 Ref.33 Ref.34
Corresponds to variant rs2227564 [ dbSNP | Ensembl ].
VAR_006722
Natural variant2141I → M. Ref.4 Ref.13
VAR_013102
Natural variant2311K → Q. Ref.7
Corresponds to variant rs2227567 [ dbSNP | Ensembl ].
VAR_038731

Experimental info

Mutagenesis1581S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. Ref.18
Mutagenesis3231S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. Ref.18
Sequence conflict1501D → G in BAG60754. Ref.6
Sequence conflict1511C → W in CAA26535. Ref.2
Sequence conflict3861G → C in CAA26535. Ref.2
Sequence conflict4301A → V in CAA26535. Ref.2

Secondary structure

........................................................................................... 431
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 62C72400BC23115F

FASTA43148,507
        10         20         30         40         50         60 
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ 

        70         80         90        100        110        120 
HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL QQTYHAHRSD ALQLGLGKHN 

       130        140        150        160        170        180 
YCRNPDNRRR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKII 

       190        200        210        220        230        240 
GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG 

       250        260        270        280        290        300 
RSRLNSNTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL 

       310        320        330        340        350        360 
PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML 

       370        380        390        400        410        420 
CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSHFLPWIR 

       430 
SHTKEENGLA L 

« Hide

Isoform 2 [UniParc].

Checksum: FB35DBE360D7E1CC
Show »

FASTA41446,908

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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]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].
[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]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-141.
+Additional computationally mapped references.

Web resources

Wikipedia

Urokinase entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUKHU. A00931.
RefSeqNP_001138503.1. NM_001145031.1.
NP_002649.1. NM_002658.3.
UniGeneHs.77274.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray1.61A179-423[»]
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/F156-428[»]
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[»]
4K24X-ray4.50A21-153[»]
4MNVX-ray1.80A179-423[»]
4MNWX-ray1.49A179-423[»]
4MNXX-ray1.85A179-423[»]
4MNYX-ray1.70A/B179-423[»]
ProteinModelPortalP00749.
SMRP00749. Positions 26-152, 179-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111344. 16 interactions.
DIPDIP-46387N.
IntActP00749. 4 interactions.
STRING9606.ENSP00000361850.

Chemistry

BindingDBP00749.
ChEMBLCHEMBL2111379.
DrugBankDB00594. Amiloride.
DB00013. Urokinase.
GuidetoPHARMACOLOGY2393.

Protein family/group databases

MEROPSS01.231.

PTM databases

PhosphoSiteP00749.
UniCarbKBP00749.

Polymorphism databases

DMDM254763341.

Proteomic databases

PaxDbP00749.
PRIDEP00749.

Protocols and materials databases

DNASU5328.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372764; ENSP00000361850; ENSG00000122861.
ENST00000496777; ENSP00000431795; ENSG00000122861.
GeneID5328.
KEGGhsa:5328.
UCSCuc001jwa.3. human. [P00749-1]
uc010qkw.2. human. [P00749-2]

Organism-specific databases

CTD5328.
GeneCardsGC10P075668.
HGNCHGNC:9052. PLAU.
HPAHPA008719.
MIM191840. gene.
601709. phenotype.
neXtProtNX_P00749.
Orphanet220436. Quebec platelet disorder.
PharmGKBPA33382.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG008633.
InParanoidP00749.
KOK01348.
OrthoDBEOG75B84T.
PhylomeDBP00749.
TreeFamTF329901.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SABIO-RKP00749.

Gene expression databases

ArrayExpressP00749.
BgeeP00749.
CleanExHS_PLAU.
GenevestigatorP00749.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
InterProIPR000742. 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]
PfamPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP00749.
GeneWikiPLAU.
GenomeRNAi5328.
NextBio20628.
PMAP-CutDBQ53XS3.
PROP00749.
SOURCESearch...

Entry information

Entry nameUROK_HUMAN
AccessionPrimary (citable) accession number: P00749
Secondary accession number(s): B4DPZ2 expand/collapse secondary AC list , Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 189 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

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 10

Human chromosome 10: entries, gene names and cross-references to MIM