Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6AEX

Crystal structure of unoccupied murine uPAR

Functional Information from GO Data
ChainGOidnamespacecontents
U0001934biological_processpositive regulation of protein phosphorylation
U0005102molecular_functionsignaling receptor binding
U0005515molecular_functionprotein binding
U0005576cellular_componentextracellular region
U0005886cellular_componentplasma membrane
U0009897cellular_componentexternal side of plasma membrane
U0009986cellular_componentcell surface
U0010755biological_processregulation of plasminogen activation
U0019899molecular_functionenzyme binding
U0019904molecular_functionprotein domain specific binding
U0030155biological_processregulation of cell adhesion
U0030377molecular_functionurokinase plasminogen activator receptor activity
U0031639biological_processplasminogen activation
U0034112biological_processpositive regulation of homotypic cell-cell adhesion
U0034394biological_processprotein localization to cell surface
U0038195biological_processurokinase plasminogen activator signaling pathway
U0043066biological_processnegative regulation of apoptotic process
U0045742biological_processpositive regulation of epidermal growth factor receptor signaling pathway
U0048762biological_processmesenchymal cell differentiation
U0051917biological_processregulation of fibrinolysis
U0060742biological_processepithelial cell differentiation involved in prostate gland development
U0090200biological_processpositive regulation of release of cytochrome c from mitochondria
U0098552cellular_componentside of membrane
U0098637cellular_componentprotein complex involved in cell-matrix adhesion
U1905370cellular_componentserine-type endopeptidase complex
U2001243biological_processnegative regulation of intrinsic apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00983
Number of Residues44
DetailsLY6_UPAR Ly-6 / u-PAR domain signature. QCMqCesnqs...Clve.....ECAlgqdlCrttvlrewqddrelevvtrg....C
ChainResidueDetails
UGLN2-CYS45
UGLU95-CYS145
UGLN191-CYS245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20133942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

PDB statisticsPDBj update infoContact PDBjnumon