Reviewed, UniProtKB/Swiss-Prot P00749 (UROK_HUMAN)

Names and origin

Protein names

Recommended name:
    Urokinase-type plasminogen activator
      Short name=U-plasminogen activator
      Short name=uPA
    EC=3.4.21.73
Cleaved into the following 3 chains:
    1- Recommended name:
            Urokinase-type plasminogen activator long chain A
    2- Recommended name:
            Urokinase-type plasminogen activator short chain A
    3- Recommended name:
            Urokinase-type plasminogen activator chain B

Gene names

Name:

PLAU

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Specifically cleave the zymogen plasminogen to form the active enzyme plasmin.
Catalytic activity	Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
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. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR. Ref.13 Ref.14
Subcellular location	Secreted.
Tissue specificity	Expressed in the prostate gland and prostate cancers. Ref.15
Post-translational modification	Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.
Pharmaceutical use	Available under the name Abbokinase (Abbott). Used in Pulmonary Embolism (PE) to initiates 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 process	Blood coagulation Fibrinolysis Plasminogen activation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Kringle Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW chemotaxis Traceable author statement. Source: ProtInc fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Ref.8 Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.7 Ref.9

Chain

21 – 431

411

Urokinase-type plasminogen activator

PRO_0000028318

Chain

21 – 177

157

Urokinase-type plasminogen activator long chain A

PRO_0000028319

Chain

156 – 177

22

Urokinase-type plasminogen activator short chain A

PRO_0000028320

Chain

179 – 431

253

Urokinase-type plasminogen activator chain B

PRO_0000028321

Regions

Domain

27 – 63

37

EGF-like

Domain

70 – 151

82

Kringle

Domain

179 – 424

246

Peptidase S1

Region

34 – 57

24

Binds urokinase plasminogen activator surface receptor By similarity

Region

152 – 177

26

Connecting peptide

Sites

Active site

224

1

Charge relay system

Active site

275

1

Charge relay system

Active site

376

1

Charge relay system

Site

177 – 178

2

Cleavage; during zymogen activation

Amino acid modifications

Modified residue

158

1

Phosphoserine Ref.12

Modified residue

323

1

Phosphoserine Ref.12

Glycosylation

38

1

O-linked (Fuc) Ref.7

Glycosylation

322

1

N-linked (GlcNAc...)

CAR_000026

Disulfide bond

31 ↔ 39

Disulfide bond

33 ↔ 51

Disulfide bond

53 ↔ 62

Disulfide bond

70 ↔ 151

Disulfide bond

91 ↔ 133

Disulfide bond

122 ↔ 146

Disulfide bond

168 ↔ 299

Interchain (between A and B chains)

Disulfide bond

209 ↔ 225

Disulfide bond

217 ↔ 288

Disulfide bond

313 ↔ 382

Disulfide bond

345 ↔ 361

Disulfide bond

372 ↔ 400

Natural variations

Natural variant

15

1

V → L Ref.5

VAR_038730

Natural variant

141

1

P → L Rare polymorphism; linked with a decrease in the affinity for fibrin-binding. Ref.5 Ref.22 Ref.23 Ref.25 Ref.26

VAR_006722

Natural variant

214

1

M → I

VAR_013102

Natural variant

231

1

K → Q Ref.5

VAR_038731

Experimental info

Mutagenesis

158

1

S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. Ref.12

Mutagenesis

323

1

S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. Ref.12

Sequence conflict

151

1

C → W in CAA26535. Ref.4

Sequence conflict

386

1

G → C in CAA26535. Ref.4

Sequence conflict

430

1

A → V in CAA26535. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

431

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Turn

43 – 47

5

Beta strand

49 – 52

4

Beta strand

57 – 59

3

Beta strand

64 – 67

4

Helix

99 – 101

3

Beta strand

106 – 108

3

Helix

109 – 112

4

Turn

113 – 115

3

Beta strand

117 – 119

3

Beta strand

132 – 135

4

Beta strand

137 – 140

4

Beta strand

142 – 147

6

Beta strand

180 – 184

5

Helix

187 – 189

3

Beta strand

193 – 197

5

Beta strand

207 – 215

9

Beta strand

218 – 221

4

Helix

223 – 225

3

Turn

226 – 228

3

Helix

232 – 234

3

Beta strand

236 – 240

5

Beta strand

243 – 246

4

Beta strand

252 – 261

10

Beta strand

277 – 282

6

Beta strand

312 – 318

7

Beta strand

333 – 340

8

Helix

342 – 345

4

Turn

348 – 351

4

Helix

352 – 354

3

Beta strand

359 – 363

5

Beta strand

379 – 383

5

Beta strand

385 – 396

12

Beta strand

398 – 402

5

Beta strand

407 – 411

5

Helix

412 – 414

3

Helix

416 – 422

7

Sequences

	Sequence		Length	Mass (Da)
	P00749-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: BAA9A6ACD2A353F1	FASTA	431	48,525
	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 GSLMSPCWVI 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 2987867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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].
[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: 2415429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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: 3888571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	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.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"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: 2023947] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, MASS SPECTROMETRY.
[8]	"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: 6589620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431.
[9]	"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: 6754569] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-177.
[10]	"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: 6749491] [Abstract] Cited for: PROTEIN SEQUENCE OF 156-176 AND 179-224.
[11]	"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: 6754572] [Abstract] Cited for: PROTEIN SEQUENCE OF 158-410.
[12]	"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: 9151681] [Abstract] Cited for: PHOSPHORYLATION AT SER-158 AND SER-323, MUTAGENESIS OF SER-158 AND SER-323.
[13]	"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: 10636902] [Abstract] Cited for: INTERACTION WITH MRC2.
[14]	"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: 11384978] [Abstract] Cited for: INTERACTION WITH LRP1B.
[15]	"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: 15988036] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"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: 2536903] [Abstract] Cited for: STRUCTURE BY NMR.
[17]	"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: 1327118] [Abstract] Cited for: STRUCTURE BY NMR OF 67-155.
[18]	"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: 8107091] [Abstract] Cited for: STRUCTURE BY NMR OF 67-155.
[19]	"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: 8591045] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[20]	"(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: 10805774] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
[21]	"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: 16456079] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-152 IN COMPLEX WITH PLAUR.
[22]	"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: 8652631] [Abstract] Cited for: VARIANT LEU-141.
[23]	"Detection of polymorphisms in the human urokinase-type plasminogen activator gene." Conne B., Berczy M., Belin D. Thromb. Haemost. 77:434-435(1997) [PubMed: 9065988] [Abstract] Cited for: VARIANT LEU-141.
[24]	Erratum Conne B., Berczy M., Belin D. Thromb. Haemost. 78:973-973(1997)
[25]	"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: 9194591] [Abstract] Cited for: VARIANT LEU-141.
[26]	"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. , 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: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-141.
+	Additional computationally mapped references.

Web resources

Wikipedia

Urokinase entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

X02419 Genomic DNA. Translation: CAA26268.1.
M15476 mRNA. Translation: AAA61253.1.
D00244 mRNA. Translation: BAA00175.1.
D11143 mRNA. Translation: BAA01919.1.
X02760 mRNA. Translation: CAA26535.1.
AF377330 Genomic DNA. Translation: AAK53822.1.
BC013575 mRNA. Translation: AAH13575.1.
K03226 mRNA. Translation: AAC97138.1.
K02286 Genomic DNA. Translation: AAA61252.1.
A21571 Unassigned DNA. Translation: CAA01559.1.
A18397 Unassigned RNA. Translation: CAA01390.1.

IPI

IPI00296180.

PIR

UKHU. A00931.

RefSeq

NP_002649.1.

UniGene

Hs.77274

3D structure databases

PDBPDBe

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	179-423	[»]
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	19-163	[»]
2I9B	X-ray	2.80	A/B/C/D	19-163	[»]
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	[»]
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	19-153	[»]
3BT2	X-ray	2.50	A	19-153	[»]

ModBase

Search...

PTM databases

GlycoSuiteDB

P00749.

PhosphoSite

P00749.

Proteomic databases

PRIDE

P00749.

Genome annotation databases

Ensembl

ENSG00000122861. Homo sapiens. [Contig view]

GeneID

5328.

KEGG

hsa:5328.

Organism-specific databases

GeneCards

GC10P075340.

HGNC

HGNC:9052. PLAU.

HPA

HPA008719.

MIM

191840. gene.

PharmGKB

PA33382.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P00749.

HOVERGEN

P00749.

Enzyme and pathway databases

BRENDA

3.4.21.73. 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
fgf_pathway. FGF signaling pathway.
avb3_opn_pathway. Osteopontin-mediated events.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00749.

Bgee

P00749.

CleanEx

HS_PLAU.

GermOnline

ENSG00000122861. Homo sapiens.

Family and domain databases

InterPro

IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Gene3D

G3DSA:2.40.20.10. Kringle. 1 hit.

Pfam

PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.

ProDom

PD000395. Kringle. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
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]

ProtoNet

Search...

Other Resources

BindingDB

P00749.

DrugBank

DB00594. Amiloride.
DB00013. Urokinase.

NextBio

20628.

PMAP-CutDB

P00749.

SOURCE

Search...

Entry information

Entry name

UROK_HUMAN

Accession

Primary (citable) accession number: P00749
Secondary accession number(s): Q15844, Q16618, Q969W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 20, 1987
Last modified:	June 16, 2009
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)