Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Urokinase-type plasminogen activator  

UniProtKB / Swiss-Prot ID :  UROK_HUMAN

Gene Name (Synonyms) : 
PLAU  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  Specifically cleave the zymogen plasminogen to form the active enzyme plasmin. 

Protein Sequence MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTC...
Predicted Secondary Structure CHHHEEEHHHHHCCCCCCCCCHHCCCCCCCCCCCCCCEEEECCCCCCCEEEECCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
15V -> L (in dbSNP:rs2227580). VAR_038730
141P -> L (in dbSNP:rs2227564). VAR_006722
214I -> M. VAR_013102
231K -> Q (in dbSNP:rs2227567). VAR_038731
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
38O-linked (Fuc)LNGGTCVSN
CCCCEEEEC
15.90OGlycBase
Link-
38O-linked (Fuc).LNGGTCVSN
CCCCEEEEC
15.90UniProtKB
Link-
158PhosphoserineGKKPSSPPE
CCCCCCCCC
65.44Phosphositeplus
Link-
158Phosphoserine (PKC_alpha)GKKPSSPPE
CCCCCCCCC
65.44PhosphoELM
Link-
158Phosphoserine.GKKPSSPPE
CCCCCCCCC
65.44UniProtKB
Link-
178noneRPRFKIIGG
CCCCEEEEC
34.39HPRD
Link-
178noneRPRFKIIGG
CCCCEEEEC
34.39HPRD
Link-
322N-linked (GlcNAc...)./FTId=CAR_000026.FGKENSTDY
EEEECCCCC
54.41UniProtKB
Link-
323PhosphoserineGKENSTDYL
EEECCCCCC
24.60Phosphositeplus
Link-
323Phosphoserine (PKC_alpha)GKENSTDYL
EEECCCCCC
24.60PhosphoELM
Link-
323Phosphoserine.GKENSTDYL
EEECCCCCC
24.60UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NID1_HUMANin vitroHPRD:01883HPRD1499567
MPRI_HUMANin vitroHPRD:01883HPRD9566979
SPB6_HUMANin vitroHPRD:01883HPRD7548163
PLMN_HUMANin vitroHPRD:01883HPRD3920216
2829380
4226004
PAI1_HUMANin vitro
in vivo
HPRD:01883HPRD2161846
2544876
3090045
TPA_HUMANin vitroHPRD:01883HPRD7721771
PAI2_HUMANin vitro
in vivo
HPRD:01883HPRD2161846
8388810
2166055
UPAR_HUMANin vitro
in vivo
HPRD:01883HPRD3031025
11501527
3023326
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Disease Reference
Kegg disease
OMIM disease
601709Quebec platelet disorder (QPD)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Characterization of a posttranslational fucosylation in the growthfactor 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).
Cited for: PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation of human pro-urokinase on Ser138/303 impairs itsreceptor-dependent ability to promote myelomonocytic adherence andmotility.";
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).
Cited for: PHOSPHORYLATION AT SER-158 AND SER-323, AND MUTAGENESIS OF SER-158 ANDSER-323.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures