[English] 日本語
Yorodumi- PDB-1a5r: STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER S... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1a5r | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES | ||||||
Components | SUMO-1SUMO1 | ||||||
Keywords | TARGETING PROTEIN / SUMO-1 / POST-TRANSLATIONAL PROTEIN MODIFICATION / UBIQUITIN-LIKE PROTEINS | ||||||
Function / homology | Function and homology information negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of action potential / small protein activating enzyme binding ...negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / nuclear stress granule / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / negative regulation of action potential / small protein activating enzyme binding / SUMOylation of DNA methylation proteins / SUMOylation of SUMOylation proteins / SUMOylation of immune response proteins / Maturation of nucleoprotein / SUMOylation of RNA binding proteins / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / negative regulation of protein import into nucleus / ubiquitin-specific protease binding / SUMOylation of ubiquitinylation proteins / roof of mouth development / negative regulation of DNA binding / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / transcription factor binding / SUMOylation of transcription factors / potassium channel regulator activity / SUMOylation of DNA damage response and repair proteins / nuclear pore / Regulation of IFNG signaling / cellular response to cadmium ion / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / positive regulation of protein-containing complex assembly / SUMOylation of intracellular receptors / PKR-mediated signaling / negative regulation of DNA-binding transcription factor activity / PML body / protein tag activity / Formation of Incision Complex in GG-NER / regulation of protein localization / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to heat / nuclear membrane / protein stabilization / nuclear body / nuclear speck / DNA repair / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / nucleolus / enzyme binding / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Bayer, P. / Arndt, A. / Metzger, S. / Mahajan, R. / Melchior, F. / Jaenicke, R. / Becker, J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: Structure determination of the small ubiquitin-related modifier SUMO-1. Authors: Bayer, P. / Arndt, A. / Metzger, S. / Mahajan, R. / Melchior, F. / Jaenicke, R. / Becker, J. #1: Journal: Cell(Cambridge,Mass.) / Year: 1997 Title: A Small Ubiquitin-Related Polypeptide Involved in Targeting Rangap1 to Nuclear Pore Complex Protein Ranbp2 Authors: Mahajan, R. / Delphin, C. / Guan, T. / Gerace, L. / Melchior, F. #2: Journal: J.Biol.Chem. / Year: 1997 Title: Preferential Modification of Nuclear Proteins by a Novel Ubiquitin-Like Molecule Authors: Kamitani, T. / Nguyen, H.P. / Yeh, E.T. #3: Journal: J.Cell Biol. / Year: 1996 Title: A Novel Ubiquitin-Like Modification Modulates the Partitioning of the Ran-Gtpase-Activating Protein Rangap1 between the Cytosol and the Nuclear Pore Complex Authors: Matunis, M.J. / Coutavas, E. / Blobel, G. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1a5r.cif.gz | 315.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1a5r.ent.gz | 274.3 KB | Display | PDB format |
PDBx/mmJSON format | 1a5r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a5/1a5r ftp://data.pdbj.org/pub/pdb/validation_reports/a5/1a5r | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 11719.133 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P63165 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: H2O |
---|---|
Sample conditions | Ionic strength: 100 mM / pH: 7.0 / Pressure: STANDARD / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
---|
-Processing
Software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| ||||||||||||||||
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY / Conformers calculated total number: 30 / Conformers submitted total number: 10 |