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

2P03

The structure of receptor-associated protein(RAP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0002091biological_processnegative regulation of receptor internalization
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005794cellular_componentGolgi apparatus
A0005796cellular_componentGolgi lumen
A0005801cellular_componentcis-Golgi network
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0008201molecular_functionheparin binding
A0009986cellular_componentcell surface
A0010916biological_processnegative regulation of very-low-density lipoprotein particle clearance
A0012505cellular_componentendomembrane system
A0031904cellular_componentendosome lumen
A0031982cellular_componentvesicle
A0035473molecular_functionlipase binding
A0048018molecular_functionreceptor ligand activity
A0048019molecular_functionreceptor antagonist activity
A0048237cellular_componentrough endoplasmic reticulum lumen
A0048259biological_processregulation of receptor-mediated endocytosis
A0050750molecular_functionlow-density lipoprotein particle receptor binding
A0070326molecular_functionvery-low-density lipoprotein particle receptor binding
A0150093biological_processamyloid-beta clearance by transcytosis
A1900116biological_processextracellular negative regulation of signal transduction
A1900222biological_processnegative regulation of amyloid-beta clearance
A1900223biological_processpositive regulation of amyloid-beta clearance
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. HNEL
ChainResidueDetails
AHIS320-LEU323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsRegion: {"description":"LDL receptor binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues91
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsMotif: {"description":"Prevents secretion from ER","evidences":[{"source":"PubMed","id":"7774585","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99068","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55302","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon