Gene Symbol | LRPAP1 |
Entrez ID | 4043 |
Uniprot ID | P30533 |
Description | LDL receptor related protein associated protein 1 |
Chromosomal Location | chr4: 3,506,376-3,532,559 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006457 |
protein folding |
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
TAS |
BP |
GO:0006898 |
receptor-mediated endocytosis |
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles. |
IEA |
BP |
GO:0010916 |
negative regulation of very-low-density lipoprotein particle clearance |
Any process that decreases the rate, frequency or extent of very-low-density lipoprotein particle clearance. Very-low-density lipoprotein particle clearance is the process in which a very-low-density lipoprotein particle is removed from the blood via receptor-mediated endocytosis and its constituent parts degraded. |
IDA |
BP |
GO:0016192 |
vesicle-mediated transport |
A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane. |
TAS |
BP |
GO:0032091 |
negative regulation of protein binding |
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding. |
IDA |
BP |
GO:1900116 |
extracellular negative regulation of signal transduction |
Any negative regulation of signal transduction that takes place in extracellular region. |
TAS |
BP |
GO:1900222 |
negative regulation of beta-amyloid clearance |
Any process that stops, prevents or reduces the frequency, rate or extent of beta-amyloid clearance. |
IGI |
CC |
GO:0005576 |
extracellular region |
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
TAS |
CC |
GO:0005783 |
endoplasmic reticulum |
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
IDA |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
IDA |
CC |
GO:0009986 |
cell surface |
The external part of the cell wall and/or plasma membrane. |
IEA |
CC |
GO:0016021 |
integral component of membrane |
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
TAS |
CC |
GO:0031982 |
vesicle |
Any small, fluid-filled, spherical organelle enclosed by membrane. |
IEA |
CC |
GO:0048237 |
rough endoplasmic reticulum lumen |
The volume enclosed by the membranes of the rough endoplasmic reticulum. |
IEA |
MF |
GO:0004873 |
asialoglycoprotein receptor activity |
Receiving an asialoglycoprotein, and delivering the asialoglycoprotein into the cell via endocytosis. An asialoglycoprotein is a plasma glycoproteins from which the terminal sialic acid residue on their complex carbohydrate groups has been removed. The asialoglycoprotein receptor recognizes the terminal galactose and N-acetylgalactosamine units of the asialoglycoprotein, the receptor-ligand complex is internalized and transported to a sorting organelle where disassociation occurs before the receptor is recycled to the cell membrane. |
TAS |
MF |
GO:0005102 |
receptor binding |
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
TAS |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0008201 |
heparin binding |
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues. |
IEA |
MF |
GO:0035473 |
lipase binding |
Interacting selectively and non-covalently with any lipase. |
IEA |
MF |
GO:0048019 |
receptor antagonist activity |
Interacts with receptors to reduce the action of another ligand, the agonist. |
IDA|TAS |
MF |
GO:0050750 |
low-density lipoprotein particle receptor binding |
Interacting selectively and non-covalently with a low-density lipoprotein receptor. |
IDA |
MF |
GO:0051082 |
unfolded protein binding |
Interacting selectively and non-covalently with an unfolded protein. |
TAS |
MF |
GO:0070326 |
very-low-density lipoprotein particle receptor binding |
Interacting selectively and non-covalently with a very-low-density lipoprotein receptor. |
IPI |
Domain ID | Description |
---|---|
IPR009066 |
Alpha-2-macroglobulin receptor-associated protein, domain 1 |
IPR010483 |
Alpha-2-macroglobulin RAP, C-terminal |
Tissue | Cell Type |
---|---|
caudate |
neuronal cells |
cerebellum |
cells in molecular layer |
cerebellum |
Purkinje cells |
cerebral cortex |
glial cells |
cerebral cortex |
neuronal cells |
epididymis |
glandular cells |
hippocampus |
neuronal cells |
kidney |
cells in tubules |
lung |
macrophages |
pancreas |
islets of Langerhans |
parathyroid gland |
glandular cells |
placenta |
decidual cells |
placenta |
trophoblastic cells |
testis |
cells in seminiferous ducts |
testis |
Leydig cells |
thyroid gland |
glandular cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
17148555 |
Wood et al. |
2007 |
Molecular Abnormalities in Oocytes from Women with Polycystic Ovary Syndrome Revealed by Microarray Analysis |
22951915 |
Haozi et al. |
2012 |
Altered gene expression profile in cumulus cells of mature MII oocytes from patients with polycystic ovary syndrome |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
MTOR |
2475 |
P42345 |
0.63 |
PPM1G |
5496 |
O15355 |
0.63 |
RAF1 |
5894 |
P04049 |
0.63 |
RALGDS |
5900 |
Q12967 |
0.63 |
RANBP2 |
5903 |
P49792 |
0.63 |
POLA2 |
23649 |
Q14181 |
0.63 |
ETV7 |
51513 |
Q9Y603 |
0.63 |
RTN4 |
57142 |
Q9NQC3 |
0.63 |
EIF4EBP1 |
1978 |
Q13541 |
0.72 |
SMAD2 |
4087 |
Q15796 |
0.49 |
TCTN3 |
26123 |
Q6NUS6 |
0.49 |
TCTN1 |
79600 |
Q2MV58 |
0.49 |
MAPK1 |
5594 |
P28482 |
0.52 |
MAPK3 |
5595 |
P27361 |
0.52 |
LRP1B |
53353 |
Q9NZR2 |
0.52 |
HDAC1 |
3065 |
Q13547 |
0.63 |
SUMO3 |
6612 |
P55854 |
0.63 |
SUMO2 |
6613 |
P61956 |
0.63 |
SUMO1 |
7341 |
P63165 |
0.63 |
RALA |
5898 |
P11233 |
0.75 |
LRP8 |
7804 |
Q14114 |
0.75 |
LDLR |
3949 |
P01130 |
0.76 |
LRP2 |
4036 |
P98164 |
0.87 |
SORT1 |
6272 |
Q99523 |
0.87 |
LRP1 |
4035 |
Q07954 |
0.90 |
SORL1 |
6653 |
Q92673 |
0.90 |
VLDLR |
7436 |
P98155 |
0.90 |