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Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by SERPINA5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei224Charge relay system1
Active sitei275Charge relay system1
Active sitei376Charge relay system1

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • chemotaxis Source: ProtInc
  • fibrinolysis Source: Reactome
  • positive regulation of cell migration Source: MGI
  • proteolysis Source: ProtInc
  • regulation of cell adhesion mediated by integrin Source: BHF-UCL
  • regulation of cell proliferation Source: Ensembl
  • regulation of receptor activity Source: BHF-UCL
  • regulation of smooth muscle cell-matrix adhesion Source: BHF-UCL
  • regulation of smooth muscle cell migration Source: BHF-UCL
  • regulation of wound healing Source: BHF-UCL
  • response to hypoxia Source: Ensembl
  • signal transduction Source: ProtInc
  • smooth muscle cell migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Plasminogen activation

Enzyme and pathway databases

BioCyciZFISH:HS04608-MONOMER.
BRENDAi3.4.21.73. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-75205. Dissolution of Fibrin Clot.
SABIO-RKP00749.
SIGNORiP00749.

Protein family/group databases

MEROPSiS01.231.

Names & Taxonomyi

Protein namesi
Recommended name:
Urokinase-type plasminogen activator (EC:3.4.21.73)
Short name:
U-plasminogen activator
Short name:
uPA
Cleaved into the following 3 chains:
Gene namesi
Name:PLAU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9052. PLAU.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

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.
See also OMIM:601709

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
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

DisGeNETi5328.
MalaCardsiPLAU.
MIMi601709. phenotype.
Orphaneti220436. Quebec platelet disorder.
PharmGKBiPA33382.

Chemistry databases

ChEMBLiCHEMBL3286.
DrugBankiDB00594. Amiloride.
DB00013. Urokinase.
GuidetoPHARMACOLOGYi2393.

Polymorphism and mutation databases

BioMutaiPLAU.
DMDMi254763341.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
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
Disulfide bondi31 ↔ 39
Disulfide bondi33 ↔ 51
Glycosylationi38O-linked (Fuc)1 Publication1
Disulfide bondi53 ↔ 62
Disulfide bondi70 ↔ 151
Disulfide bondi91 ↔ 133
Disulfide bondi122 ↔ 146
Modified residuei158Phosphoserine1 Publication1
Disulfide bondi168 ↔ 299Interchain (between A and B chains)
Disulfide bondi209 ↔ 225
Disulfide bondi217 ↔ 288
Disulfide bondi313 ↔ 382
GlycosylationiCAR_000026322N-linked (GlcNAc...)1
Modified residuei323Phosphoserine1 Publication1
Disulfide bondi345 ↔ 361
Disulfide bondi372 ↔ 400

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei177 – 178Cleavage; during zymogen activation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDiP00749.
MaxQBiP00749.
PaxDbiP00749.
PeptideAtlasiP00749.
PRIDEiP00749.

PTM databases

iPTMnetiP00749.
PhosphoSitePlusiP00749.
UniCarbKBiP00749.

Miscellaneous databases

PMAP-CutDBQ53XS3.

Expressioni

Tissue specificityi

Expressed in the prostate gland and prostate cancers.1 Publication

Gene expression databases

BgeeiENSG00000122861.
CleanExiHS_PLAU.
ExpressionAtlasiP00749. baseline and differential.
GenevisibleiP00749. HS.

Organism-specific databases

HPAiHPA008719.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111344. 19 interactors.
DIPiDIP-46387N.
IntActiP00749. 8 interactors.
STRINGi9606.ENSP00000361850.

Chemistry databases

BindingDBiP00749.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Beta strandi38 – 41Combined sources4
Turni43 – 47Combined sources5
Beta strandi49 – 52Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi64 – 67Combined sources4
Beta strandi70 – 72Combined sources3
Beta strandi73 – 77Combined sources5
Beta strandi86 – 89Combined sources4
Beta strandi94 – 96Combined sources3
Helixi99 – 101Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi106 – 108Combined sources3
Helixi111 – 114Combined sources4
Beta strandi117 – 119Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi132 – 137Combined sources6
Beta strandi140 – 147Combined sources8
Helixi162 – 165Combined sources4
Beta strandi180 – 184Combined sources5
Helixi187 – 189Combined sources3
Beta strandi193 – 199Combined sources7
Beta strandi201 – 203Combined sources3
Beta strandi205 – 215Combined sources11
Beta strandi218 – 221Combined sources4
Helixi223 – 225Combined sources3
Turni226 – 228Combined sources3
Helixi232 – 234Combined sources3
Beta strandi235 – 240Combined sources6
Beta strandi243 – 246Combined sources4
Beta strandi252 – 261Combined sources10
Beta strandi268 – 271Combined sources4
Beta strandi272 – 274Combined sources3
Beta strandi277 – 282Combined sources6
Beta strandi293 – 295Combined sources3
Beta strandi312 – 318Combined sources7
Beta strandi329 – 331Combined sources3
Beta strandi333 – 340Combined sources8
Helixi342 – 345Combined sources4
Turni348 – 351Combined sources4
Helixi352 – 354Combined sources3
Turni356 – 358Combined sources3
Beta strandi359 – 363Combined sources5
Beta strandi365 – 367Combined sources3
Beta strandi379 – 384Combined sources6
Beta strandi387 – 396Combined sources10
Beta strandi398 – 402Combined sources5
Beta strandi407 – 411Combined sources5
Helixi412 – 414Combined sources3
Helixi416 – 422Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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-ray1.61A179-410[»]
1OWIX-ray2.93A179-423[»]
1OWJX-ray3.10A179-423[»]
1OWKX-ray2.80A179-423[»]
1SC8X-ray2.40U164-425[»]
1SQAX-ray2.00A179-423[»]
1SQOX-ray1.84A179-423[»]
1SQTX-ray1.90A179-423[»]
1U6QX-ray2.02A179-423[»]
1URKNMR-A26-155[»]
1VJ9X-ray2.40U164-425[»]
1VJAX-ray2.00U164-425[»]
1W0ZX-ray1.90U179-425[»]
1W10X-ray2.00U179-425[»]
1W11X-ray2.00U179-425[»]
1W12X-ray2.40U179-425[»]
1W13X-ray2.00U179-425[»]
1W14X-ray2.20U179-425[»]
2FD6X-ray1.90A31-152[»]
2I9AX-ray1.90A/B/C/D21-163[»]
2I9BX-ray2.80A/B/C/D21-163[»]
2NWNX-ray2.15A179-431[»]
2O8TX-ray1.45A179-431[»]
2O8UX-ray1.70A179-431[»]
2O8WX-ray1.86A179-431[»]
2R2WX-ray2.01U179-431[»]
2VINX-ray1.90A179-431[»]
2VIOX-ray1.80A179-431[»]
2VIPX-ray1.72A179-431[»]
2VIQX-ray2.00A179-431[»]
2VIVX-ray1.72A179-431[»]
2VIWX-ray2.05A179-431[»]
2VNTX-ray2.20A/B/C/D/E/F156-431[»]
3BT1X-ray2.80A21-153[»]
3BT2X-ray2.50A21-153[»]
3IG6X-ray1.83A/C156-178[»]
B/D179-431[»]
3KGPX-ray2.35A179-431[»]
3KHVX-ray2.35A179-431[»]
3KIDX-ray2.71U179-431[»]
3M61X-ray1.68U179-431[»]
3MHWX-ray1.45U179-425[»]
3MWIX-ray2.03U179-424[»]
3OX7X-ray1.58U179-431[»]
3OY5X-ray2.31U179-431[»]
3OY6X-ray2.31U179-431[»]
3PB1X-ray2.30E179-431[»]
3QN7X-ray1.90A179-431[»]
3U73X-ray3.19A21-152[»]
4DVAX-ray1.94U179-424[»]
4DW2X-ray2.97U179-424[»]
4FU7X-ray2.00A179-424[»]
4FU8X-ray2.20A179-424[»]
4FU9X-ray1.60A179-424[»]
4FUBX-ray1.90A179-424[»]
4FUCX-ray1.72A179-424[»]
4FUDX-ray2.00A179-424[»]
4FUEX-ray2.00A179-424[»]
4FUFX-ray2.00A179-424[»]
4FUGX-ray1.80A179-424[»]
4FUHX-ray1.60A179-424[»]
4FUIX-ray2.00A179-424[»]
4FUJX-ray2.05A179-424[»]
4GLYX-ray1.52A179-423[»]
4H42X-ray2.01U179-426[»]
4JK5X-ray1.55A179-423[»]
4JK6X-ray2.20A179-423[»]
4JNIX-ray1.17U179-425[»]
4JNLX-ray2.00U179-425[»]
4K24X-ray4.50A21-153[»]
4MNVX-ray1.80A179-423[»]
4MNWX-ray1.49A179-423[»]
4MNXX-ray1.85A179-423[»]
4MNYX-ray1.70A/B179-423[»]
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[»]
ProteinModelPortaliP00749.
SMRiP00749.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 63EGF-likePROSITE-ProRule annotationAdd BLAST37
Domaini70 – 151KringlePROSITE-ProRule annotationAdd BLAST82
Domaini179 – 424Peptidase S1PROSITE-ProRule annotationAdd BLAST246

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 57Binds urokinase plasminogen activator surface receptorBy similarityAdd BLAST24
Regioni152 – 177Connecting peptideAdd BLAST26

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

eggNOGiENOG410IGFI. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG008633.
InParanoidiP00749.
KOiK01348.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00749.
TreeFamiTF329901.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Checksum:i62C72400BC23115F
GO
Isoform 2 (identifier: P00749-2) [UniParc]FASTAAdd to basket

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Natural variantiVAR_03873015V → L.1 PublicationCorresponds to variant rs2227580dbSNPEnsembl.1
Natural variantiVAR_006722141P → L.6 PublicationsCorresponds to variant rs2227564dbSNPEnsembl.1
Natural variantiVAR_013102214I → M.2 Publications1
Natural variantiVAR_038731231K → Q.1 PublicationCorresponds to variant rs2227567dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0383681 – 29MRALL…HQVPS → MVFHLRTRYEQA in isoform 2. 1 PublicationAdd BLAST29

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. Translation: CAI13969.1.
CH471083 Genomic DNA. Translation: EAW54544.1.
BC013575 mRNA. Translation: AAH13575.1.
D11143 mRNA. Translation: BAA01919.1.
K02286 Genomic DNA. Translation: AAA61252.1.
CCDSiCCDS44442.1. [P00749-2]
CCDS7339.1. [P00749-1]
PIRiA00931. UKHU.
RefSeqiNP_001138503.1. NM_001145031.2. [P00749-2]
NP_001306120.1. NM_001319191.1.
NP_002649.1. NM_002658.4. [P00749-1]
UniGeneiHs.77274.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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. Translation: CAI13969.1.
CH471083 Genomic DNA. Translation: EAW54544.1.
BC013575 mRNA. Translation: AAH13575.1.
D11143 mRNA. Translation: BAA01919.1.
K02286 Genomic DNA. Translation: AAA61252.1.
CCDSiCCDS44442.1. [P00749-2]
CCDS7339.1. [P00749-1]
PIRiA00931. UKHU.
RefSeqiNP_001138503.1. NM_001145031.2. [P00749-2]
NP_001306120.1. NM_001319191.1.
NP_002649.1. NM_002658.4. [P00749-1]
UniGeneiHs.77274.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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-ray1.61A179-410[»]
1OWIX-ray2.93A179-423[»]
1OWJX-ray3.10A179-423[»]
1OWKX-ray2.80A179-423[»]
1SC8X-ray2.40U164-425[»]
1SQAX-ray2.00A179-423[»]
1SQOX-ray1.84A179-423[»]
1SQTX-ray1.90A179-423[»]
1U6QX-ray2.02A179-423[»]
1URKNMR-A26-155[»]
1VJ9X-ray2.40U164-425[»]
1VJAX-ray2.00U164-425[»]
1W0ZX-ray1.90U179-425[»]
1W10X-ray2.00U179-425[»]
1W11X-ray2.00U179-425[»]
1W12X-ray2.40U179-425[»]
1W13X-ray2.00U179-425[»]
1W14X-ray2.20U179-425[»]
2FD6X-ray1.90A31-152[»]
2I9AX-ray1.90A/B/C/D21-163[»]
2I9BX-ray2.80A/B/C/D21-163[»]
2NWNX-ray2.15A179-431[»]
2O8TX-ray1.45A179-431[»]
2O8UX-ray1.70A179-431[»]
2O8WX-ray1.86A179-431[»]
2R2WX-ray2.01U179-431[»]
2VINX-ray1.90A179-431[»]
2VIOX-ray1.80A179-431[»]
2VIPX-ray1.72A179-431[»]
2VIQX-ray2.00A179-431[»]
2VIVX-ray1.72A179-431[»]
2VIWX-ray2.05A179-431[»]
2VNTX-ray2.20A/B/C/D/E/F156-431[»]
3BT1X-ray2.80A21-153[»]
3BT2X-ray2.50A21-153[»]
3IG6X-ray1.83A/C156-178[»]
B/D179-431[»]
3KGPX-ray2.35A179-431[»]
3KHVX-ray2.35A179-431[»]
3KIDX-ray2.71U179-431[»]
3M61X-ray1.68U179-431[»]
3MHWX-ray1.45U179-425[»]
3MWIX-ray2.03U179-424[»]
3OX7X-ray1.58U179-431[»]
3OY5X-ray2.31U179-431[»]
3OY6X-ray2.31U179-431[»]
3PB1X-ray2.30E179-431[»]
3QN7X-ray1.90A179-431[»]
3U73X-ray3.19A21-152[»]
4DVAX-ray1.94U179-424[»]
4DW2X-ray2.97U179-424[»]
4FU7X-ray2.00A179-424[»]
4FU8X-ray2.20A179-424[»]
4FU9X-ray1.60A179-424[»]
4FUBX-ray1.90A179-424[»]
4FUCX-ray1.72A179-424[»]
4FUDX-ray2.00A179-424[»]
4FUEX-ray2.00A179-424[»]
4FUFX-ray2.00A179-424[»]
4FUGX-ray1.80A179-424[»]
4FUHX-ray1.60A179-424[»]
4FUIX-ray2.00A179-424[»]
4FUJX-ray2.05A179-424[»]
4GLYX-ray1.52A179-423[»]
4H42X-ray2.01U179-426[»]
4JK5X-ray1.55A179-423[»]
4JK6X-ray2.20A179-423[»]
4JNIX-ray1.17U179-425[»]
4JNLX-ray2.00U179-425[»]
4K24X-ray4.50A21-153[»]
4MNVX-ray1.80A179-423[»]
4MNWX-ray1.49A179-423[»]
4MNXX-ray1.85A179-423[»]
4MNYX-ray1.70A/B179-423[»]
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[»]
ProteinModelPortaliP00749.
SMRiP00749.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111344. 19 interactors.
DIPiDIP-46387N.
IntActiP00749. 8 interactors.
STRINGi9606.ENSP00000361850.

Chemistry databases

BindingDBiP00749.
ChEMBLiCHEMBL3286.
DrugBankiDB00594. Amiloride.
DB00013. Urokinase.
GuidetoPHARMACOLOGYi2393.

Protein family/group databases

MEROPSiS01.231.

PTM databases

iPTMnetiP00749.
PhosphoSitePlusiP00749.
UniCarbKBiP00749.

Polymorphism and mutation databases

BioMutaiPLAU.
DMDMi254763341.

Proteomic databases

EPDiP00749.
MaxQBiP00749.
PaxDbiP00749.
PeptideAtlasiP00749.
PRIDEiP00749.

Protocols and materials databases

DNASUi5328.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5328.
DisGeNETi5328.
GeneCardsiPLAU.
HGNCiHGNC:9052. PLAU.
HPAiHPA008719.
MalaCardsiPLAU.
MIMi191840. gene.
601709. phenotype.
neXtProtiNX_P00749.
Orphaneti220436. Quebec platelet disorder.
PharmGKBiPA33382.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGFI. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG008633.
InParanoidiP00749.
KOiK01348.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00749.
TreeFamiTF329901.

Enzyme and pathway databases

BioCyciZFISH:HS04608-MONOMER.
BRENDAi3.4.21.73. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-75205. Dissolution of Fibrin Clot.
SABIO-RKP00749.
SIGNORiP00749.

Miscellaneous databases

EvolutionaryTraceiP00749.
GeneWikiiPLAU.
GenomeRNAii5328.
PMAP-CutDBQ53XS3.
PROiP00749.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122861.
CleanExiHS_PLAU.
ExpressionAtlasiP00749. baseline and differential.
GenevisibleiP00749. HS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUROK_HUMAN
AccessioniPrimary (citable) accession number: P00749
Secondary accession number(s): B4DPZ2
, Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 28, 2009
Last modified: November 30, 2016
This is version 217 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.