- EMDB-8085: Sub-unit of the Inner ring of the Nuclear Pore complex -
+
Open data
ID or keywords:
Loading...
-
Basic information
Entry
Database: EMDB / ID: EMD-8085
Title
Sub-unit of the Inner ring of the Nuclear Pore complex
Map data
None
Sample
Complex: Inner ring of the Nuclear Pore complex
Function / homology
Function and homology information
centriole assembly / positive regulation of centriole replication / regulation of protein import into nucleus / regulation of Ras protein signal transduction / positive regulation of mitotic cytokinetic process / nuclear pore inner ring / nuclear envelope organization / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore complex assembly ...centriole assembly / positive regulation of centriole replication / regulation of protein import into nucleus / regulation of Ras protein signal transduction / positive regulation of mitotic cytokinetic process / nuclear pore inner ring / nuclear envelope organization / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore complex assembly / protein localization to nuclear inner membrane / nuclear pore organization / positive regulation of protein localization to centrosome / Nuclear Pore Complex (NPC) Disassembly / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of Ribonucleoproteins into the Host Nucleus / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / negative regulation of Ras protein signal transduction / mitotic centrosome separation / SUMOylation of SUMOylation proteins / structural constituent of nuclear pore / Flemming body / Transport of Mature mRNA Derived from an Intronless Transcript / NS1 Mediated Effects on Host Pathways / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / SUMOylation of RNA binding proteins / NEP/NS2 Interacts with the Cellular Export Machinery / RNA export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / NLS-bearing protein import into nucleus / centrosome cycle / nucleocytoplasmic transport / nuclear localization sequence binding / negative regulation of programmed cell death / Viral Messenger RNA Synthesis / poly(A)+ mRNA export from nucleus / PTB domain binding / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / negative regulation of epidermal growth factor receptor signaling pathway / SUMOylation of DNA replication proteins / positive regulation of SMAD protein signal transduction / regulation of signal transduction / nuclear pore / Regulation of HSF1-mediated heat shock response / mitotic metaphase chromosome alignment / mRNA transport / SUMOylation of DNA damage response and repair proteins / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of mitotic nuclear division / nuclear periphery / SH2 domain binding / Hsp70 protein binding / SUMOylation of chromatin organization proteins / regulation of mitotic spindle organization / HCMV Late Events / ubiquitin binding / protein import into nucleus / Hsp90 protein binding / phospholipid binding / ISG15 antiviral mechanism / mitotic spindle / spindle pole / HCMV Early Events / nuclear envelope / protein transport / nuclear membrane / signaling receptor complex adaptor activity / snRNP Assembly / positive regulation of canonical NF-kappaB signal transduction / cell surface receptor signaling pathway / negative regulation of cell population proliferation / ribonucleoprotein complex / centrosome / chromatin binding / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / protein-containing complex binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / nucleoplasm / membrane / identical protein binding / cytosol / cytoplasm Similarity search - Function
Journal: Science / Year: 2016 Title: Molecular architecture of the inner ring scaffold of the human nuclear pore complex. Authors: Jan Kosinski / Shyamal Mosalaganti / Alexander von Appen / Roman Teimer / Amanda L DiGuilio / William Wan / Khanh Huy Bui / Wim J H Hagen / John A G Briggs / Joseph S Glavy / Ed Hurt / Martin Beck / Abstract: Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these ...Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.
History
Deposition
Feb 22, 2016
-
Header (metadata) release
Apr 27, 2016
-
Map release
Apr 27, 2016
-
Update
Apr 11, 2018
-
Current status
Apr 11, 2018
Processing site: PDBe / Status: Released
-
Structure visualization
Movie
Surface view with section colored by density value
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi