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P00749

- UROK_HUMAN

UniProt

P00749 - UROK_HUMAN

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Protein

Urokinase-type plasminogen activator

Gene
PLAU
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei177 – 1782Cleavage; during zymogen activation
Active sitei224 – 2241Charge relay system
Active sitei275 – 2751Charge relay system
Active sitei376 – 3761Charge relay system

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Plasminogen activation

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.
SABIO-RKP00749.

Protein family/group databases

MEROPSiS01.231.

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:9052. PLAU.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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

Pharmaceutical usei

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

Mutagenesis

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

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP00749.
PaxDbiP00749.
PRIDEiP00749.

PTM databases

PhosphoSiteiP00749.
UniCarbKBiP00749.

Miscellaneous databases

PMAP-CutDBQ53XS3.

Expressioni

Tissue specificityi

Expressed in the prostate gland and prostate cancers.1 Publication

Gene expression databases

ArrayExpressiP00749.
BgeeiP00749.
CleanExiHS_PLAU.
GenevestigatoriP00749.

Organism-specific databases

HPAiHPA008719.

Interactioni

Subunit structurei

Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6337EGF-likeAdd
BLAST
Domaini70 – 15182KringleAdd
BLAST
Domaini179 – 424246Peptidase S1Add
BLAST

Region

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

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

« Hide

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

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

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MRALL…HQVPS → MVFHLRTRYEQA in isoform 2. VSP_038368Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501D → G in BAG60754. 1 Publication
Sequence conflicti151 – 1511C → W in CAA26535. 1 Publication
Sequence conflicti386 – 3861G → C in CAA26535. 1 Publication
Sequence conflicti430 – 4301A → V in CAA26535. 1 Publication

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi254763341.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Urokinase entry

SeattleSNPs

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

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

Protein family/group databases

MEROPSi S01.231.

PTM databases

PhosphoSitei P00749.
UniCarbKBi P00749.

Polymorphism databases

DMDMi 254763341.

Proteomic databases

MaxQBi P00749.
PaxDbi P00749.
PRIDEi P00749.

Protocols and materials databases

DNASUi 5328.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the gene for pro-urokinase in Escherichia coli."
    Holmes W.E., Pennica D., Blaber M., Rey M.W., Guenzler W.A., Steffens G.J., Heyneker H.L.
    Biotechnology (N.Y.) 3:923-929(1985)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning, sequencing, and expression in Escherichia coli of human preprourokinase cDNA."
    Jacobs P., Cravador A., Loriau R., Brockly F., Colau B., Chuchana P., van Elsen A., Herzog A., Bollen A.
    DNA 4:139-146(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Molecular cloning of cDNA coding for human preprourokinase."
    Nagai M., Hiramatsu R., Kaneda T., Hayasuke N., Arimura H., Nishida M., Suyama T.
    Gene 36:183-188(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The human urokinase-plasminogen activator gene and its promoter."
    Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F.
    Nucleic Acids Res. 13:2759-2771(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-214.
  5. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mesangial cell.
  7. SeattleSNPs variation discovery resource
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-15; LEU-141 AND GLN-231.
  8. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-141.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  11. "Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure."
    Yoshimoto M., Ushiyama Y., Sakai M., Tamaki S., Hara H., Takahashi K., Sawasaki Y., Hanada K.
    Biochim. Biophys. Acta 1293:83-89(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-431, VARIANT LEU-141.
  12. "Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator."
    Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R., Sarin V.K.
    Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA."
    Verde P., Stoppelli M.P., Galeffi P., di Nocera P., Blasi F.
    Proc. Natl. Acad. Sci. U.S.A. 81:4727-4731(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431, VARIANT MET-214.
  14. "The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain."
    Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E., Flohe L.
    Hoppe-Seyler's Z. Physiol. Chem. 363:1155-1165(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-177.
  15. "Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains."
    Schaller J., Nick H., Rickli E.E., Gillessen D., Lergier W., Studer R.O.
    Eur. J. Biochem. 125:251-257(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 156-176 AND 179-224.
  16. "The complete amino acid sequence of low molecular mass urokinase from human urine."
    Steffens G.J., Gunzler W.A., Otting F., Frankus E., Flohe L.
    Hoppe-Seyler's Z. Physiol. Chem. 363:1043-1058(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 158-410.
  17. "Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for identity of PCI and plasminogen activator inhibitor 3."
    Stief T.W., Radtke K.P., Heimburger N.
    Biol. Chem. Hoppe-Seyler 368:1427-1433(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
  18. "Phosphorylation of human pro-urokinase on Ser138/303 impairs its receptor-dependent ability to promote myelomonocytic adherence and motility."
    Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C., Mastronicola M.R., Nolli M.L., Stoppelli M.P.
    J. Cell Biol. 137:779-791(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-158 AND SER-323, MUTAGENESIS OF SER-158 AND SER-323.
  19. "Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility."
    He S., Lin Y.L., Liu Y.X.
    Mol. Hum. Reprod. 5:513-519(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: HETERODIMER WITH SERPINA5.
  20. "A urokinase receptor-associated protein with specific collagen binding properties."
    Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.
    J. Biol. Chem. 275:1993-2002(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MRC2.
  21. "The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
    Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
    J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP1B.
  22. "Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma."
    Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.
    Int. J. Cancer 108:516-523(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
  23. "Platelet-derived growth factor D is activated by urokinase plasminogen activator in prostate carcinoma cells."
    Ustach C.V., Kim H.-R.C.
    Mol. Cell. Biol. 25:6279-6288(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  24. "Persons with Quebec platelet disorder have a tandem duplication of PLAU, the urokinase plasminogen activator gene."
    Paterson A.D., Rommens J.M., Bharaj B., Blavignac J., Wong I., Diamandis M., Waye J.S., Rivard G.E., Hayward C.P.
    Blood 115:1264-1266(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN QPD.
  25. "Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR."
    Oswald R.E., Bogusky M.J., Bamberger M., Smith R.A.G., Dobson C.M.
    Nature 337:579-582(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  26. "Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase."
    Li X., Smith R.A.G., Dobson C.M.
    Biochemistry 31:9562-9571(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 67-155.
  27. "Solution structure of the kringle domain from urokinase-type plasminogen activator."
    Li X., Bokman A.M., Llinas M., Smith R.A.G., Dobson C.M.
    J. Mol. Biol. 235:1548-1559(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 67-155.
  28. "The crystal structure of the catalytic domain of human urokinase-type plasminogen activator."
    Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D., Dobson C.M., Stuart D.I., Jones E.Y.
    Structure 3:681-691(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  29. "(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase."
    Sperl S., Jacob U., Arroyo de Prada N., Sturzebecher J., Wilhelm O.G., Bode W., Magdolen V., Huber R., Moroder L.
    Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
  30. "Structure of human urokinase plasminogen activator in complex with its receptor."
    Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J., Li Y., Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B., Huang M.
    Science 311:656-659(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-152 IN COMPLEX WITH PLAUR.
  31. "Detection of polymorphisms in the human urokinase-type plasminogen activator gene."
    Conne B., Berczy M., Belin D.
    Thromb. Haemost. 77:434-435(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-141.
  32. Erratum
    Conne B., Berczy M., Belin D.
    Thromb. Haemost. 78:973-973(1997)
  33. "Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer."
    Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.
    Electrophoresis 18:686-689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-141.
  34. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-141.

Entry informationi

Entry nameiUROK_HUMAN
AccessioniPrimary (citable) accession number: P00749
Secondary accession number(s): B4DPZ2
, Q15844, Q16618, Q53XS3, Q5SWW9, Q969W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 28, 2009
Last modified: September 3, 2014
This is version 193 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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