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ApoER2
3A7QIdentifiersAliases LRP8, APOER2, HSZ75190, LRP-8, MCI1, low density lipoprotein receptor-related protein 8, LDL receptor
LDL receptor
related protein 8External IDs MGI: 1340044 HomoloGene: 31250 GeneCards: LRP8 Gene
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Protein Data Bank
The Protein
Protein
Data Bank (PDB) is a crystallographic database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe,[1] PDBj,[2] and RCSB[3]). The PDB is overseen by an organization called the Worldwide Protein
Protein
Data Bank, wwPDB. The PDB is a key resource in areas of structural biology, such as structural genomics. Most major scientific journals, and some funding agencies, now require scientists to submit their structure data to the PDB
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PI3K
Phosphatidylinositol-4,5-bisphosphate 3-kinase (also called phosphatidylinositide 3-kinases, phosphatidylinositol-3-kinases, PI 3-kinases, PI(3)Ks, PI-3Ks or by the HUGO official stem symbol for the gene family, PI3K(s)) are a family of enzymes involved in cellular functions such as cell growth, proliferation, differentiation, motility, survival and intracellular trafficking, which in turn are involved in cancer. PI3Ks are a family of related intracellular signal transducer enzymes capable of phosphorylating the 3 position hydroxyl group of the inositol ring of phosphatidylinositol (PtdIns).[2] The pathway, with oncogene
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Proline
Proline
Proline
(symbol Pro or P;[4] encoded by the codons CCU, CCC, CCA, and CCG) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated NH2+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain pyrrolidine, classifying it as a nonpolar (at physiological pH), aliphatic amino acid
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Tyrosine
Tyrosine
Tyrosine
(symbol Tyr or Y[1]) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. Its codons are UAC and UAU. The word "tyrosine" is from the Greek tyros, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese.[2][3] It is called tyrosyl when referred to as a functional group or side chain
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Endocytosis
Endocytosis
Endocytosis
is a form of active transport in which a cell transports molecules (such as proteins) into the cell (endo- + cytosis) by engulfing them in an energy-using process
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LDL Receptor
1AJJ, 1D2J, 1F5Y, 1HJ7, 1HZ8, 1I0U, 1IJQ, 1LDL, 1LDR, 1N7D, 1XFE, 2FCW, 2KRI, 2LGP, 2W2M, 2W2N, 2W2O, 2W2P, 2W2Q, 3BPS, 3GCW, 3GCX, 3M0C, 3SO6, 2M7P, 2MG9, 3P5B, 3P5C, 4NE9IdentifiersAliases LDLR, FH, FHC, LDLCQ2, low density lipoprotein receptorExternal IDs OMIM: 606945 MGI: 96765 HomoloGene: 55469 GeneCards: LDLR Gene
Gene
location (Human)Chr. Chromosome
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PSD-95
1KEF, 3I4W, 3K82, 3ZRTIdentifiersAliases DLG4, PSD95, SAP-90, SAP90, Dlgh4, PSD-95, SAP90A, discs large homolog 4, discs large MAGUK scaffold protein 4External IDs MGI: 1277959 HomoloGene: 1047 GeneCards: DLG4 Gene
Gene
location (Human)Chr. Chromosome
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NMDA Receptor
The N-methyl-D-aspartate
N-methyl-D-aspartate
receptor (also known as the NMDA receptor
NMDA receptor
or NMDAR), is a glutamate receptor and ion channel protein found in nerve cells. The NMDA receptor
NMDA receptor
is one of three types of ionotropic glutamate receptors, the others being the AMPA
AMPA
and kainate receptors
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MAPK8IP2
NM_012324 NM_016431 NM_139124NM_021921RefSeq (protein)NP_036456NP_068740Location (UCSC) Chr 22: 50.6 – 50.61 Mb Chr 15: 89.45 – 89.46 MbPubMed search [3] [4]WikidataView/Edit Human View/Edit MouseC-jun-amino-terminal kinase-interacting protein 2 is a protein or the name of the gene that encodes it.[5][6] The gene is also known as Islet-Brain-2 (IB2). This protein is highly expressed in the brain and is almost always deleted in Phelan-McDermid syndrome (PMS). MAPK8IP2 appears to regulate the ratio of AMPA receptors to NMDA receptors at glutamate synapses,[7] and thus may be an important contributor to the intellectual dysfunction and related neurological manifestations characteristic of PMS. The protein encoded by this gene is closely related to MAPK8IP1/IB1/JIP-1, a scaffold protein that is involved in the c-Jun amino-terminal kinase signaling pathway. This protein is expressed in brain and pancreatic cells
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JNK
c-Jun N-terminal kinases (JNKs), were originally identified as kinases that bind and phosphorylate c-Jun on Ser-63 and Ser-73 within its transcriptional activation domain. They belong to the mitogen-activated protein kinase family, and are responsive to stress stimuli, such as cytokines, ultraviolet irradiation, heat shock, and osmotic shock. They also play a role in T cell
T cell
differentiation and the cellular apoptosis pathway. Activation occurs through a dual phosphorylation of threonine (Thr) and tyrosine (Tyr) residues within a Thr-Pro-Tyr motif located in kinase subdomain VIII
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Lipoprotein
A lipoprotein is a biochemical assembly whose purpose is to transport hydrophobic lipid (a.k.a. fat) molecules in water, as in blood or extracellular fluid. They have a single-layer phospholipid and cholesterol outer shell, with the hydrophilic portions oriented outward toward the surrounding water and lipophilic portions of each molecule oriented inwards toward the lipids molecules within the particles. Apolipoproteins are embedded in the membrane, both stabilising the complex and giving it functional identity determining its fate. Thus the complex serves to emulsify the fats. Many enzymes, transporters, structural proteins, antigens, adhesions, and toxins are lipoproteins. Examples include the plasma lipoprotein particles classified as HDL, LDL, IDL, VLDL and ULDL (a.k.a. chylomicrons) lipoproteins, according to density / size (an inverse relationship), compared with the surrounding plasma water
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Tyrosine Kinase
A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to a protein in a cell. It functions as an "on" or "off" switch in many cellular functions. Tyrosine
Tyrosine
kinases are a subclass of protein kinase. The phosphate group is attached to the amino acid tyrosine on the protein. Tyrosine
Tyrosine
kinases are a subgroup of the larger class of protein kinases that attach phosphate groups to other amino acids (serine and threonine). Phosphorylation
Phosphorylation
of proteins by kinases is an important mechanism in communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division. Protein
Protein
kinases can become mutated, stuck in the "on" position, and cause unregulated growth of the cell, which is a necessary step for the development of cancer
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Gene Nomenclature
Gene
Gene
nomenclature is the scientific naming of genes, the units of heredity in living organisms
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FYN
1A0N, 1AOT, 1AOU, 1AVZ, 1AZG, 1EFN, 1FYN, 1G83, 1M27, 1NYF, 1NYG, 1SHF, 1ZBJ, 2DQ7, 3H0F, 3H0H, 3H0I, 3UA6, 3UA7, 4D8D, 4EIK, 2MQI, 2MRJ, 2MRK, 4U17, 4U1P, 4ZNXIdentifiersAliases FYN, SLK, SYN, p59- FYN
FYN
proto-oncogene, Src family tyrosine kinaseExternal IDs MGI: 95602 HomoloGene: 48068 GeneCards: FYN Gene
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SRC (gene)
1A07, 1A08, 1A09, 1A1A, 1A1B, 1A1C, 1A1E, 1FMK, 1HCS, 1HCT, 1KSW, 1O41, 1O42, 1O43, 1O44, 1O45, 1O46, 1O47, 1O48, 1O49, 1O4A, 1O4B, 1O4C, 1O4D, 1O4E, 1O4F, 1O4G, 1O4H, 1O4I, 1O4J, 1O4K, 1O4L, 1O4M, 1O4N, 1O4O, 1O4P, 1O4Q, 1O4R, 1SHD, 1Y57, 1YI6, 1YOJ, 1YOL, 1YOM, 2BDF, 2H8H, 3VRO, 3ZMP, 3ZMQ, 4F59, 4F5A, 4F5B, 4HXJ, 4K11, 4MXO, 4MXX, 4MXY, 4MXZIdentifiersAliases SRC, ASV, SRC1, c-p60-Src, SRC proto-oncogene, non-receptor tyrosine kinase, THC6External IDs MGI: 98397 HomoloGene: 21120 GeneCards: SRC Gene
Gene
location (Human)Chr.
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