Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P00749 (UROK_HUMAN)

Entry version 245 (13 Nov 2019)
Sequence version 2 (28 Jul 2009)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin. EC:3.4.21.73

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by SERPINA5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei224Charge relay system1
Active sitei275Charge relay system1
Active sitei376Charge relay system1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Fibrinolysis, Hemostasis, Plasminogen activation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.73 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-6798695 Neutrophil degranulation
R-HSA-75205 Dissolution of Fibrin Clot

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00749

SIGNOR Signaling Network Open Resource

More...SIGNORi		P00749

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.231

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
Urokinase-type plasminogen activator long chain A
Urokinase-type plasminogen activator short chain A
Urokinase-type plasminogen activator chain B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PLAU
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9052 PLAU

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		191840 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P00749

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Quebec platelet disorder (QPD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
Related information in OMIM

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi158S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. 1 Publication1
Mutagenesisi323S → E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5328

MalaCards human disease database

More...MalaCardsi		PLAU
MIMi601709 phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		220436 Quebec platelet disorder

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33382

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P00749

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3286

Drug and drug target database

More...DrugBanki		DB07129 (2R)-1-(2,6-dimethylphenoxy)propan-2-amine
DB07122 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine
DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02287 2-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-Carboxamidine
DB03729 2-Amino-5-Hydroxy-Benzimidazole
DB01725 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide
DB08072 4-(2-AMINOETHOXY)-3,5-DICHLORO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE
DB07625 4-(2-aminoethoxy)-N-(2,5-diethoxyphenyl)-3,5-dimethylbenzamide
DB07626 4-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide
DB08697 4-(2-aminoethoxy)-N-(3-chloro-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide
DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine
DB01977 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine
DB07076 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE
DB03082 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide
DB02705 6-[N-(1-Isopropyl-1,2,3,4-Tetrahydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02473 6-[N-(1-Isopropyl-3,4-Dihydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02398 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02551 6-[N-(4-Ethyl-1,2,3,4-Tetrahydro-6-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine
DB06855 6-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidine
DB06856 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE
DB03046 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide
DB04059 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide
DB04172 [2,4,6-Triisopropyl-Phenylsulfonyl-L-[3-Amidino-Phenylalanine]]-Piperazine-N'-Beta-Alanine
DB00594 Amiloride
DB03127 Benzamidine
DB02526 CRA_10655
DB03159 CRA_8696
DB05254 Fibrinolysin
DB03782 N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea
DB06857 N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE
DB03876 Thieno[2,3-B]Pyridine-2-Carboxamidine
DB03476 Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine
DB00013 Urokinase

DrugCentral

More...DrugCentrali		P00749

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2393

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PLAU

Domain mapping of disease mutations (DMDM)

More...DMDMi		254763341

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 202 PublicationsAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002831821 – 431Urokinase-type plasminogen activatorAdd BLAST411
ChainiPRO_000002831921 – 177Urokinase-type plasminogen activator long chain AAdd BLAST157
ChainiPRO_0000028320156 – 177Urokinase-type plasminogen activator short chain AAdd BLAST22
ChainiPRO_0000028321179 – 431Urokinase-type plasminogen activator chain BAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi31 ↔ 39
Disulfide bondi33 ↔ 51
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi38O-linked (Fuc) threonine1 Publication1
Disulfide bondi53 ↔ 62
Disulfide bondi70 ↔ 151
Disulfide bondi91 ↔ 133
Disulfide bondi122 ↔ 146
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei158Phosphoserine1 Publication1
Disulfide bondi168 ↔ 299Interchain (between A and B chains)
Disulfide bondi209 ↔ 225
Disulfide bondi217 ↔ 288
Disulfide bondi313 ↔ 382
GlycosylationiCAR_000026322N-linked (GlcNAc...) asparagine1
Modified residuei323Phosphoserine1 Publication1
Disulfide bondi345 ↔ 361
Disulfide bondi372 ↔ 400

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei177 – 178Cleavage; during zymogen activation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P00749

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00749

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P00749

MaxQB - The MaxQuant DataBase

More...MaxQBi		P00749

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P00749

PeptideAtlas

More...PeptideAtlasi		P00749

PRoteomics IDEntifications database

More...PRIDEi		P00749

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51279 [P00749-1]
51280 [P00749-2]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		519
612

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P00749

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P00749

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P00749

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P00749

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the prostate gland and prostate cancers.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000122861 Expressed in 181 organ(s), highest expression level in epithelium of bronchus

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P00749 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P00749 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA008719

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. In complex with SERPINE1, interacts with PLAUR/uPAR (PubMed:15053742).

Interacts with SORL1 and LRP1, either alone or in complex with SERPINE1; these interactions are abolished in the presence of LRPAP1/RAP (PubMed:15053742). The ternary complex composed of PLAUR-PLAU-PAI1 also interacts with SORLA (PubMed:15053742).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Q03405-12EBI-3905042,EBI-15695188

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111344, 22 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-483 uPA-PAI-1 complex
CPX-487 uPA-uPAR complex
CPX-501 uPA-uPAR-vitronectin complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P00749

Database of interacting proteins

More...DIPi		DIP-46387N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P00749

Protein interaction database and analysis system

More...IntActi		P00749, 11 interactors

Molecular INTeraction database

More...MINTi		P00749

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361850

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00749

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P00749

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00749

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 63EGF-likePROSITE-ProRule annotationAdd BLAST37
Domaini70 – 151KringlePROSITE-ProRule annotationAdd BLAST82
Domaini179 – 424Peptidase S1PROSITE-ProRule annotationAdd BLAST246

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni34 – 57Binds urokinase plasminogen activator surface receptorBy similarityAdd BLAST24
Regioni152 – 177Connecting peptideAdd BLAST26

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IGFI Eukaryota
COG5640 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00749

KEGG Orthology (KO)

More...KOi		K01348

Database of Orthologous Groups

More...OrthoDBi		972218at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00749

TreeFam database of animal gene trees

More...TreeFami		TF329901

Family and domain databases

Conserved Domains Database

More...CDDi		cd00108 KR, 1 hit
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
IPR034814 Urokinase

The PANTHER Classification System

More...PANTHERi		PTHR24264:SF38 PTHR24264:SF38, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00130 KR, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW 
        60         70         80         90        100
CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL 
       110        120        130        140        150
QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD 
       160        170        180        190        200
CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH 
       210        220        230        240        250
RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG 
       260        270        280        290        300
EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL 
       310        320        330        340        350
PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY 
       360        370        380        390        400
YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC 
       410        420        430 
ALKDKPGVYT RVSHFLPWIR SHTKEENGLA L
Length:431
Mass (Da):48,507
Last modified:July 28, 2009 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ET40E7ET40_HUMAN
Urokinase-type plasminogen activato...
PLAU
414Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
S4R3G7S4R3G7_HUMAN
Urokinase-type plasminogen activato...
PLAU
106Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti150D → G in BAG60754 (PubMed:14702039).Curated1
Sequence conflicti151C → W in CAA26535 (PubMed:3888571).Curated1
Sequence conflicti386G → C in CAA26535 (PubMed:3888571).Curated1
Sequence conflicti430A → V in CAA26535 (PubMed:3888571).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03873015V → L1 PublicationCorresponds to variant dbSNP:rs2227580EnsemblClinVar.1
Natural variantiVAR_006722141P → L6 PublicationsCorresponds to variant dbSNP:rs2227564EnsemblClinVar.1
Natural variantiVAR_013102214I → M2 PublicationsCorresponds to variant dbSNP:rs1050120Ensembl.1
Natural variantiVAR_038731231K → Q1 PublicationCorresponds to variant dbSNP:rs2227567EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0383681 – 29MRALL…HQVPS → MVFHLRTRYEQA in isoform 2. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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 No translation available.
CH471083 Genomic DNA Translation: EAW54544.1
BC013575 mRNA Translation: AAH13575.1
D11143 mRNA Translation: BAA01919.1
K02286 Genomic DNA Translation: AAA61252.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44442.1 [P00749-2]
CCDS7339.1 [P00749-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A00931 UKHU

NCBI Reference Sequences

More...RefSeqi		NP_001138503.1, NM_001145031.2 [P00749-2]
NP_001306120.1, NM_001319191.1
NP_002649.1, NM_002658.4 [P00749-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000372764; ENSP00000361850; ENSG00000122861
ENST00000496777; ENSP00000431795; ENSG00000122861

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5328

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5328

UCSC genome browser

More...UCSCi		uc001jwa.4 human [P00749-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Urokinase entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
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_001145031.2 [P00749-2]
NP_001306120.1, NM_001319191.1
NP_002649.1, NM_002658.4 [P00749-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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/F156-431[»]
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[»]
4K24X-ray4.50A21-153[»]
4MNVX-ray1.80A179-423[»]
4MNWX-ray1.49A179-423[»]
4MNXX-ray1.85A179-423[»]
4MNYX-ray1.70A/B179-423[»]
4OS1X-ray2.20A179-423[»]
4OS2X-ray1.79A179-423[»]
4OS4X-ray2.00A179-423[»]
4OS5X-ray2.26A179-423[»]
4OS6X-ray1.75A179-423[»]
4OS7X-ray2.00A179-423[»]
4X0WX-ray2.10U179-425[»]
4X1NX-ray1.80U179-425[»]
4X1PX-ray1.60U179-425[»]
4X1QX-ray2.28U179-425[»]
4X1RX-ray2.10U179-425[»]
4X1SX-ray1.90U179-425[»]
4XSKX-ray1.50U179-424[»]
4ZHLX-ray2.06U179-425[»]
4ZHMX-ray1.90U179-425[»]
4ZKNX-ray1.36U179-425[»]
4ZKOX-ray1.29U179-425[»]
4ZKRX-ray1.36U179-425[»]
4ZKSX-ray1.85U179-425[»]
5HGGX-ray1.97A/B179-424[»]
5WXFX-ray1.46U179-431[»]
5WXOX-ray1.64U179-431[»]
5WXPX-ray1.75U179-431[»]
5WXQX-ray1.79U179-431[»]
5WXRX-ray1.75U179-431[»]
5WXSX-ray2.30U179-431[»]
5WXTX-ray2.10U179-431[»]
5XG4X-ray3.00U179-424[»]
5YC6X-ray1.18U179-424[»]
5YC7X-ray2.00U179-424[»]
5Z1CX-ray1.45U179-423[»]
5ZA7X-ray1.70U179-431[»]
5ZA8X-ray1.90U179-431[»]
5ZA9X-ray1.62U179-431[»]
5ZAEX-ray1.73U179-431[»]
5ZAFX-ray1.65U179-431[»]
5ZAGX-ray1.95U179-431[»]
5ZAHX-ray2.98U179-431[»]
5ZAJX-ray1.65U179-431[»]
5ZC5X-ray1.90U179-431[»]
6AG2X-ray1.77U179-431[»]
6AG3X-ray2.48U179-431[»]
6AG7X-ray1.90U179-423[»]
6AG9X-ray1.63U179-431[»]
6NMBX-ray2.30A/B/C/D162-431[»]
SMRiP00749
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111344, 22 interactors
ComplexPortaliCPX-483 uPA-PAI-1 complex
CPX-487 uPA-uPAR complex
CPX-501 uPA-uPAR-vitronectin complex
CORUMiP00749
DIPiDIP-46387N
ELMiP00749
IntActiP00749, 11 interactors
MINTiP00749
STRINGi9606.ENSP00000361850

Chemistry databases

BindingDBiP00749
ChEMBLiCHEMBL3286
DrugBankiDB07129 (2R)-1-(2,6-dimethylphenoxy)propan-2-amine
DB07122 1-[4-(2-oxo-2-phenylethyl)phenyl]guanidine
DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02287 2-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-Carboxamidine
DB03729 2-Amino-5-Hydroxy-Benzimidazole
DB01725 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide
DB08072 4-(2-AMINOETHOXY)-3,5-DICHLORO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE
DB07625 4-(2-aminoethoxy)-N-(2,5-diethoxyphenyl)-3,5-dimethylbenzamide
DB07626 4-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide
DB08697 4-(2-aminoethoxy)-N-(3-chloro-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide
DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine
DB01977 6-(N-Phenylcarbamyl)-2-Naphthalenecarboxamidine
DB07076 6-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDE
DB03082 6-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-Naphthamide
DB02705 6-[N-(1-Isopropyl-1,2,3,4-Tetrahydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02473 6-[N-(1-Isopropyl-3,4-Dihydro-7-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02398 6-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-Naphthalenecarboxamidine
DB02551 6-[N-(4-Ethyl-1,2,3,4-Tetrahydro-6-Isoquinolinyl)Carbamyl]-2-Naphthalenecarboxamidine
DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine
DB06855 6-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidine
DB06856 6-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINE
DB03046 7-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-Carboximidamide
DB04059 8-(Pyrimidin-2-Ylamino)Naphthalene-2-Carboximidamide
DB04172 [2,4,6-Triisopropyl-Phenylsulfonyl-L-[3-Amidino-Phenylalanine]]-Piperazine-N'-Beta-Alanine
DB00594 Amiloride
DB03127 Benzamidine
DB02526 CRA_10655
DB03159 CRA_8696
DB05254 Fibrinolysin
DB03782 N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)Urea
DB06857 N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDE
DB03876 Thieno[2,3-B]Pyridine-2-Carboxamidine
DB03476 Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-Carboxamidine
DB00013 Urokinase
DrugCentraliP00749
GuidetoPHARMACOLOGYi2393

Protein family/group databases

MEROPSiS01.231

PTM databases

GlyConnecti519
612
iPTMnetiP00749
PhosphoSitePlusiP00749
UniCarbKBiP00749

Polymorphism and mutation databases

BioMutaiPLAU
DMDMi254763341

Proteomic databases

EPDiP00749
jPOSTiP00749
MassIVEiP00749
MaxQBiP00749
PaxDbiP00749
PeptideAtlasiP00749
PRIDEiP00749
ProteomicsDBi51279 [P00749-1]
51280 [P00749-2]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P00749

The DNASU plasmid repository

More...DNASUi		5328

Genome annotation databases

EnsembliENST00000372764; ENSP00000361850; ENSG00000122861
ENST00000496777; ENSP00000431795; ENSG00000122861
GeneIDi5328
KEGGihsa:5328
UCSCiuc001jwa.4 human [P00749-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5328
DisGeNETi5328

GeneCards: human genes, protein and diseases

More...GeneCardsi		PLAU
HGNCiHGNC:9052 PLAU
HPAiHPA008719
MalaCardsiPLAU
MIMi191840 gene
601709 phenotype
neXtProtiNX_P00749
Orphaneti220436 Quebec platelet disorder
PharmGKBiPA33382

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IGFI Eukaryota
COG5640 LUCA
InParanoidiP00749
KOiK01348
OrthoDBi972218at2759
PhylomeDBiP00749
TreeFamiTF329901

Enzyme and pathway databases

BRENDAi3.4.21.73 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-75205 Dissolution of Fibrin Clot
SABIO-RKiP00749
SIGNORiP00749

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PLAU human
EvolutionaryTraceiP00749

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PLAU

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5328
PharosiP00749
PMAP-CutDBiP00749

Protein Ontology

More...PROi		PR:P00749

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000122861 Expressed in 181 organ(s), highest expression level in epithelium of bronchus
ExpressionAtlasiP00749 baseline and differential
GenevisibleiP00749 HS

Family and domain databases

CDDicd00108 KR, 1 hit
cd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 1 hit
InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
IPR034814 Urokinase
PANTHERiPTHR24264:SF38 PTHR24264:SF38, 1 hit
PfamiView protein in Pfam
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00130 KR, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUROK_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00749
Secondary accession number(s): B4DPZ2
, Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 28, 2009
Last modified: November 13, 2019
This is version 245 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again