postsynaptic cytoskeleton / Acetylcholine regulates insulin secretion / epithelial cell maturation involved in salivary gland development / organelle / positive regulation of vascular wound healing / ATF6-mediated unfolded protein response / positive regulation of protein acetylation / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / outer dense fiber ...postsynaptic cytoskeleton / Acetylcholine regulates insulin secretion / epithelial cell maturation involved in salivary gland development / organelle / positive regulation of vascular wound healing / ATF6-mediated unfolded protein response / positive regulation of protein acetylation / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / outer dense fiber / negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / intracellular transport of virus / positive regulation of cell proliferation involved in heart morphogenesis / response to insulin-like growth factor stimulus / N-terminal peptidyl-glycine N-myristoylation / peptidyl-lysine N6-myristoyltransferase activity / positive regulation of skeletal muscle tissue growth / glandular epithelial cell maturation / positive regulation of lactation / sterol homeostasis / IRE1alpha activates chaperones / ATF6 (ATF6-alpha) activates chaperone genes / positive regulation of plasma cell differentiation / regulation of opsin-mediated signaling pathway / positive regulation of phospholipid biosynthetic process / cardiac ventricle development / negative regulation of myotube differentiation / positive regulation of ERAD pathway / intracellular triglyceride homeostasis / actin crosslink formation / ventricular cardiac muscle tissue development / bleb / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / cellular response to fructose stimulus / chromatoid body / cellular response to laminar fluid shear stress / regulation of modification of postsynaptic actin cytoskeleton / XBP1(S) activates chaperone genes / positive regulation of dendritic spine morphogenesis / heart trabecula morphogenesis / cellular response to nutrient / skeletal muscle tissue regeneration / positive regulation of hepatocyte proliferation / dendritic branch / cellular response to fluid shear stress / positive regulation of MHC class II biosynthetic process / negative regulation of endoplasmic reticulum unfolded protein response / exocrine pancreas development / positive regulation of vascular associated smooth muscle cell migration / germinal vesicle / ribosomal subunit / endothelial cell proliferation / protein localization to membrane / neural tube development / cellular response to peptide hormone stimulus / positive regulation of B cell differentiation / positive regulation of T cell differentiation / positive regulation of immunoglobulin production / muscle organ development / IRE1-mediated unfolded protein response / phosphatidylserine binding / cell-substrate adhesion / actin filament bundle / negative regulation of SMAD protein signal transduction / actin filament bundle assembly / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / cellular response to vascular endothelial growth factor stimulus / positive regulation of endothelial cell apoptotic process / positive regulation of TOR signaling / 90S preribosome / positive regulation of insulin receptor signaling pathway / adipose tissue development / fatty acid homeostasis / vascular endothelial growth factor receptor signaling pathway / positive regulation of fat cell differentiation / neuron development / phagocytic cup / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / endoplasmic reticulum unfolded protein response / cellular response to glucose starvation / cis-regulatory region sequence-specific DNA binding / presynaptic cytosol / ribosomal small subunit export from nucleus / positive regulation of vascular associated smooth muscle cell proliferation / rough endoplasmic reticulum / translation regulator activity / eNOS activation / gastrulation / ERAD pathway / neurogenesis / MDM2/MDM4 family protein binding / axon terminus / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / Membrane binding and targetting of GAG proteins / positive regulation of autophagy / cytosolic ribosome Similarity search - Function
Myristoylated alanine-rich C-kinase substrate MARCKS / MARCKS family / MARCKS family signature 1. / MARCKS family phosphorylation site domain. / : / Transcription factor BTF3 / Nascent polypeptide-associated complex NAC domain / Nascent polypeptide-associated complex subunit alpha / NAC A/B domain superfamily / NAC domain ...Myristoylated alanine-rich C-kinase substrate MARCKS / MARCKS family / MARCKS family signature 1. / MARCKS family phosphorylation site domain. / : / Transcription factor BTF3 / Nascent polypeptide-associated complex NAC domain / Nascent polypeptide-associated complex subunit alpha / NAC A/B domain superfamily / NAC domain / NAC A/B domain profile. / NAC / Nascent polypeptide-associated complex subunit alpha-like, UBA domain / HYPK UBA domain / Glycylpeptide N-tetradecanoyltransferase, conserved site / Myristoyl-CoA:protein N-myristoyltransferase signature 1. / Myristoyl-CoA:protein N-myristoyltransferase signature 2. / Glycylpeptide N-tetradecanoyltransferase / Glycylpeptide N-tetradecanoyltransferase, N-terminal / Glycylpeptide N-tetradecanoyltransferase, C-terminal / Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain / Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain / Basic region leucine zipper / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. / basic region leucin zipper / Basic-leucine zipper domain / Basic-leucine zipper domain superfamily / 60s Acidic ribosomal protein / 60S acidic ribosomal protein P0 / : / Ribosomal protein L6, N-terminal / Ribosomal protein L6, N-terminal domain / Ubiquitin-like protein FUBI / Ribosomal protein L30e / Ribosomal protein L28e / Ribosomal L15/L27a, N-terminal / 50S ribosomal protein L10, insertion domain superfamily / Ribosomal protein L23 / 60S ribosomal protein L10P, insertion domain / Insertion domain in 60S ribosomal protein L10P / Ribosomal protein L2, archaeal-type / Ribosomal L28e/Mak16 / Ribosomal L28e protein family / metallochaperone-like domain / TRASH domain / Ribosomal protein L41 / Ribosomal protein L41 / : / Ribosomal protein S12e signature. / Ribosomal protein S12e / Ribosomal protein L29e / Ribosomal L29e protein family / Ribosomal protein S19e, conserved site / Ribosomal protein S19e signature. / Ribosomal protein S5, eukaryotic/archaeal / Small (40S) ribosomal subunit Asc1/RACK1 / Ribosomal protein L27e, conserved site / Ribosomal protein L27e signature. / S27a-like superfamily / Ribosomal protein L10e, conserved site / Ribosomal protein L10e signature. / 40S Ribosomal protein S10 / : / Ribosomal protein S7e signature. / Ribosomal protein L10e / Ribosomal protein L24e, conserved site / : / Ribosomal protein L24e signature. / Ribosomal protein L44e signature. / Ribosomal protein L6e signature. / Plectin/S10, N-terminal / Plectin/S10 domain / Ribosomal protein S10, eukaryotic/archaeal / Ribosomal protein S30 / Ribosomal protein S17e, conserved site / Ribosomal protein S30 / Ribosomal protein S17e signature. / Ribosomal protein L34e, conserved site / Ribosomal protein L34e signature. / Ribosomal protein S3Ae, conserved site / Ribosomal protein S3Ae signature. / Ribosomal protein S25 / S25 ribosomal protein / Ribosomal protein S27a / Ribosomal protein S27a / Ribosomal protein S27a / : / Ribosomal protein L5 eukaryotic, C-terminal / Ribosomal L18 C-terminal region / Ribosomal protein L44e / Ribosomal protein L44 / Ribosomal protein L23/L25, N-terminal / Ribosomal protein L23, N-terminal domain / Ribosomal protein L30e signature 1. / Ribosomal L40e family / 40S ribosomal protein S29/30S ribosomal protein S14 type Z / Ribosomal protein L36e signature. / Ribosomal protein L35Ae, conserved site / : Similarity search - Domain/homology
Small ribosomal subunit protein eS32 / Small ribosomal subunit protein eS24 / Ribosomal protein L36a / Large ribosomal subunit protein uL30 / Small ribosomal subunit protein uS5 / 60S ribosomal protein L32 / Large ribosomal subunit protein uL16 / Small ribosomal subunit protein uS4 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein eL24 ...Small ribosomal subunit protein eS32 / Small ribosomal subunit protein eS24 / Ribosomal protein L36a / Large ribosomal subunit protein uL30 / Small ribosomal subunit protein uS5 / 60S ribosomal protein L32 / Large ribosomal subunit protein uL16 / Small ribosomal subunit protein uS4 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein eL24 / Large ribosomal subunit protein uL23 / Large ribosomal subunit protein eL33 / Small ribosomal subunit protein eS12 / Large ribosomal subunit protein eL29 / Small ribosomal subunit protein uS9 / Large ribosomal subunit protein eL31 / Large ribosomal subunit protein eL21 / Large ribosomal subunit protein uL29 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein RACK1 / Ubiquitin-ribosomal protein eS31 fusion protein / Large ribosomal subunit protein eL6 / Large ribosomal subunit protein uL11 / Large ribosomal subunit protein uL15 / Small ribosomal subunit protein uS15 / Large ribosomal subunit protein uL10 / Large ribosomal subunit protein uL24 / Small ribosomal subunit protein eS1 / Large ribosomal subunit protein eL8 / Small ribosomal subunit protein eS7 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL6 / Large ribosomal subunit protein eL43 / Large ribosomal subunit protein eL14 / Small ribosomal subunit protein uS12 / Large ribosomal subunit protein eL15 / Small ribosomal subunit protein uS11 / Large ribosomal subunit protein uL14 / Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein / Small ribosomal subunit protein eS25 / Large ribosomal subunit protein eL30 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein eS28 / Small ribosomal subunit protein eS4 / Large ribosomal subunit protein uL3 / Small ribosomal subunit protein eS6 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS17 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein eL39 / Large ribosomal subunit protein eL36 / Small ribosomal subunit protein eS17 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein eL27 / Large ribosomal subunit protein eL34 / Small ribosomal subunit protein eS27 / Small ribosomal subunit protein uS19 / Large ribosomal subunit protein eL28 / Small ribosomal subunit protein uS14 / Glycylpeptide N-tetradecanoyltransferase 2 / Ubiquitin-ribosomal protein eL40 fusion protein / X-box-binding protein 1 / Large ribosomal subunit protein uL18 / Transcription factor BTF3 / Myristoylated alanine-rich C-kinase substrate / Nascent polypeptide-associated complex subunit alpha / Large ribosomal subunit protein eL37 Similarity search - Component
Biological species
Oryctolagus cuniculus (rabbit) / Homo sapiens (human)
Method
single particle reconstruction / cryo EM / Resolution: 2.82 Å
Journal: EMBO J / Year: 2025 Title: NAC couples protein synthesis with nascent polypeptide myristoylation on the ribosome. Authors: Sara Zdancewicz / Emir Maldosevic / Kinga Malezyna / Ahmad Jomaa / Abstract: N-glycine myristoylation allows for reversible association of newly synthesized proteins with membranes to regulate essential functions such as cellular signaling and stress responses. This process ...N-glycine myristoylation allows for reversible association of newly synthesized proteins with membranes to regulate essential functions such as cellular signaling and stress responses. This process can be catalyzed during protein synthesis by N-myristoyltransferases (NMTs), and its dysregulation has been implicated both in cancer and heart disease. Although the nascent polypeptide-associated complex (NAC) orchestrates the binding of several co-translational processing factors on ribosomes, its role in facilitating nascent protein myristoylation by NMT2 remains unclear. Here, we show that NAC mediates binding of NMT2 to translating ribosomes, which together form an extended channel that guides the nascent chain as it emerges from the polypeptide exit tunnel to the catalytic site of NMT2. Furthermore, the ternary ribosome:NMT2:NAC complex is stabilized by a ribosomal RNA clamp that, together with NAC, orients NMT2 on the ribosomal surface for co-translational myristoylation of nascent chains. Our work uncovers the molecular mechanism coupling protein synthesis to nascent protein myristoylation and underscores the role of NAC as a master regulator of protein biogenesis on the ribosome.
Name: Myristoylated alanine-rich C-kinase substrate,X-box-binding protein 1, luminal form type: protein_or_peptide / ID: 87 Details: The listed sample sequence is not correct! Please update! The full sample sequence should be "GAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEDPVPYQPPFLCQWGRHQCAWKPLM" but the software ...Details: The listed sample sequence is not correct! Please update! The full sample sequence should be "GAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEDPVPYQPPFLCQWGRHQCAWKPLM" but the software will not properly align the first 9 residues and the final residues with such a large gap in between. I deleted 31 residues from the middle of the sequence to get the system to accept this,The listed sample sequence is not correct! Please update! The full sample sequence should be "GAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEDPVPYQPPFLCQWGRHQCAWKPLM" but the software will not properly align the first 9 residues and the final residues with such a large gap in between. I deleted 31 residues from the middle of the sequence to get the system to accept this Number of copies: 1 / Enantiomer: LEVO
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