Prelamin-A/C
UniProt P02545 · gene LMNA · Homo sapiens · 664 residues
51evidence items
0mapped to a state
0states
7techniques
6sources
0conflicts
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | cryoem | nmr_structure | nmr_shifts | force_spectroscopy | af_prediction | md | Total |
|---|---|---|---|---|---|---|---|---|---|
| No states defined yet. | |||||||||
Unmapped evidence: 51 of 51 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 1 | 0 |
| DisProt | 1 | 0 |
| MDDB | 1 | 0 |
| RCSB PDB | 29 | 0 |
| SMASH-BIO | 18 | 0 |
Structure
No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.
States and transitions
No states defined.
| State | Basis | Parent | Description |
|---|
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-1IFR-1 RCSB PDB | xray | resolution: 1.4 Å | in vitro · pH 8 · ligands GOL Structure of Lamin A/C Globular Domain · Lamin A/C (chains A) | unmapped |
| EV-PDB-2YPT-2 RCSB PDB | xray | resolution: 3.8 Å | in vitro · -173.15 °C · pH 7 · ligands ZN Crystal structure of the human nuclear membrane zinc metalloprotease ZMPSTE24 mutant (E336A) in complex with a synthetic CSIM tetrapeptide from the C-terminus of prelamin A · PRELAMIN-A/C (chains F,G,H,I) | unmapped |
| EV-PDB-3GEF-1 RCSB PDB | xray | resolution: 1.5 Å | in vitro · -173.15 °C · pH 6.3 Crystal structure of the R482W mutant of lamin A/C · Lamin-A/C (chains A,B,C,D) | unmapped |
| EV-PDB-3V4Q-1 RCSB PDB | xray | resolution: 3.06 Å | in vitro · -100.15 °C · pH 5.5 Structure of R335W mutant of human Lamin · Prelamin-A/C (chains A) | unmapped |
| EV-PDB-3V5B-1 RCSB PDB | xray | resolution: 3 Å | in vitro · -100.15 °C · pH 7.5 Structure of Coil 2b of human lamin · Prelamin-A/C (chains A) | unmapped |
| EV-PDB-6GHD-3 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C · ligands EDO, SO4 Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases · Prelamin-A/C (chains B,F) | unmapped |
| EV-PDB-6JLB-1 RCSB PDB | xray | resolution: 3.205 Å | in vitro · -173.15 °C · pH 8.5 Crystal structure of lamin A/C fragment and assembly mechanisms of intermediate filaments · Lamin A/C (chains A,B,C,D) | unmapped |
| EV-PDB-6YF5-1 RCSB PDB | xray | resolution: 1.83 Å | in vitro · -173.15 °C · pH 4.9 Lamin A 17-70 coil1A dimer stabilized by C-terminal capping · Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains A,B,C,D) | unmapped |
| EV-PDB-6YJD-1 RCSB PDB | xray | resolution: 2.9 Å | in vitro · -173.15 °C · pH 8.2 · ligands CL, NI, TRS Lamin A coil2 dimer stabilized by N-terminal capping · Capsid assembly scaffolding protein,Prelamin-A/C (chains A) | unmapped |
| EV-PDB-6YSH-2 RCSB PDB | xray | resolution: 2.83 Å | in vitro · -173.15 °C · pH 6 Lamin A 1-70 coil1A dimer stabilized by C-terminal capping · Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains B) | unmapped |
| EV-PDB-6YSH-1 RCSB PDB | xray | resolution: 2.83 Å | in vitro · -173.15 °C · pH 6 Lamin A 1-70 coil1A dimer stabilized by C-terminal capping · Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains A) | unmapped |
| EV-PDB-7WZZ-3 RCSB PDB | xray | resolution: 1.305 Å | in vitro · -173.15 °C · pH 6.9 · ligands GOL Crystal structure of peptide KAGQVVTIW in complex with HLA-B5801 · LYS-ALA-GLY-GLN-VAL-VAL-THR-ILE-TRP (chains C) | unmapped |
| EV-PDB-7X1B-3 RCSB PDB | xray | resolution: 1.399 Å | in vitro · -173.15 °C · pH 6.9 · ligands GOL Crystal structure of peptide KAGQVVTI in complex with HLA-B5801 · LYS-ALA-GLY-GLN-VAL-VAL-THR-ILE (chains C) | unmapped |
| EV-PDB-7X5D-1 RCSB PDB | xray | resolution: 1.82 Å | in vitro · -173.15 °C Crystal Structure of the K316C mutant of Human Lamin A/C Coil 2 (residues 244-340) · Lamin-A/C (chains A,B) | unmapped |
| EV-PDB-7YVD-1 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C · pH 6.5 · ligands SEC The crystal structure of the progerin C-terminal peptide and the Ig-like domain of lamin A/C · Lamin-A/C (chains A,B,C) | unmapped |
| EV-PDB-9J8M-8 RCSB PDB | cryoem | resolution: 3.82 Å | in vitro Cryo-EM structure of BAF-Lamin A/C IgF-nucleosome complex (High mobility complex) · Lamin-A/C (chains M) | unmapped |
| EV-PDB-9J8N-8 RCSB PDB | cryoem | resolution: 7.14 Å | in vitro Cryo-EM structure of BAF-Lamin A/C IgF-nucleosome complex (Low mobility complex) · Lamin-A/C (chains M,P,m,p) | unmapped |
| EV-PDB-9J8O-8 RCSB PDB | cryoem | resolution: 4.05 Å | in vitro Cryo-EM structure of BAF-Lamin A/C IgF-H1-nucleosome complex · Lamin-A/C (chains M,m) | unmapped |
| EV-PDB-9UL6-1 RCSB PDB | xray | resolution: 2.5 Å | in vitro · -193.15 °C Crystal structure of Lamin A/C Ig-like domain mutant - R435C · Lamin-A/C (chains A,B,C) | unmapped |
| EV-PDB-8I33-1 RCSB PDB | xray | resolution: 1.62 Å | in vitro · -173.15 °C Coil 1a of lamin A (residue 25-65) · Prelamin-A/C (chains A,B,C,D) | unmapped |
| EV-PDB-7Z21-2 RCSB PDB | xray | resolution: 1.629 Å | in vitro · -173.15 °C · pH 9 · ligands CL BAF A12T bound to the lamin A/C Ig-fold domain · Lamin-A/C (chains E,F) | unmapped |
| EV-PDB-7D9N-1 RCSB PDB | xray | resolution: 3.7 Å | in vitro · 24.85 °C Crystal structure of a non-canonic progeria mutation S143F at lamin A/C and its structural implication to the premature aging · Lamin-A/C (chains A,B) | unmapped |
| EV-PDB-7CRG-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · 24.85 °C Beta-strand-mediated dimeric formation of the extended Ig-like domains of human lamin A/C · Prelamin-A/C (chains A,B,C) | unmapped |
| EV-PDB-6SNZ-1 RCSB PDB | xray | resolution: 2.6 Å | in vitro · -173.15 °C · ligands GOL Crystal structure of lamin A coil1b tetramer · Prelamin-A/C (chains A,B,C,D) | unmapped |
| EV-PDB-6RPR-1 RCSB PDB | xray | resolution: 2.26 Å | in vitro · 19.85 °C · ligands SO4 LEM domain of Emerin mutant T43I in complex with BAF dimer and the Igfold of the lamin A/C · Prelamin-A/C (chains B) | unmapped |
| EV-PDB-3V4W-1 RCSB PDB | xray | resolution: 3.7 Å | in vitro · -100.15 °C · pH 4.6 Structure of E347K mutant of Lamin · Prelamin-A/C (chains A) | unmapped |
| EV-PDB-2XV5-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 8.5 Human lamin A coil 2B fragment · LAMIN-A/C (chains A,B) | unmapped |
| EV-PDB-1X8Y-1 RCSB PDB | xray | resolution: 2.2 Å | in vitro · -173.15 °C · pH 7.5 Human lamin coil 2B · Lamin A/C (chains A) | unmapped |
| EV-PDB-1IVT-1 RCSB PDB | nmr_structure | structure | in vitro · 29.85 °C · pH 6.3 NMR structures of the C-terminal globular domain of human lamin A/C · Lamin A/C (chains A) | unmapped |
| EV-BMRB-5224 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C 1H, 13C and 15N Chemical shifts assignments for the C-terminal domain (region 428-547) of human lamin A/C · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-DISPROT-DP00716r002 DisProt | nmr_shifts | disorder_region: 98 residues | in vitro DisProt DP00716: disorder, residues 567-664 · residues 567-664; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-AFDB-AF-P02545-F1 AlphaFold DB | af_prediction | plddt: 76.38 pLDDT | in silico AlphaFold DB prediction AF-P02545-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-664 | unmapped |
| EV-MDDB-A00L3 MDDB | md | trajectory: 10 ns | in silico · 26.85 °C MoDEL 1IVT · start 1IVT; Amber Parm99 | unmapped |
| EV-SMASH-SMFS-000272 SMASH-BIO | force_spectroscopy | study_record | in vitro Single Cell Mechanics in Disease Progression. · Lamin A/C; magnetic tweezers; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-000362 SMASH-BIO | force_spectroscopy | study_record | in vitro A protein-DNA surface hydrogel mechanically reinforces the cell nucleus and protects the genome · Lamin A/C; optical tweezers; experiment class: nucleic_acid_protein_interaction, rheology_cell | unmapped |
| EV-SMASH-SMFS-000407 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.5 Co-translational ribosome pairing enables native assembly of misfolding-prone subunits. · Lamin A/C; optical tweezers; experiment class: translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000472 SMASH-BIO | force_spectroscopy | study_record | in cell Integrin Tension Represents the Directed Differentiation of Mesenchymal Stem Cells via Mechanoadaptation. · Lamin A/C; tension sensors; experiment class: nucleic_acid_protein_interaction, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-000788 SMASH-BIO | force_spectroscopy | study_record | in vitro Heterogeneous force response of chromatin in isolated nuclei. · Lamin A/C; optical tweezers; experiment class: chromatin_mechanics, rheology_cell | unmapped |
| EV-SMASH-SMFS-001084 SMASH-BIO | force_spectroscopy | study_record | in vitro Co-translational ribosome pairing enables native assembly of misfolding-prone subunits · Lamin A/C; force spectroscopy unspecified; experiment class: translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001815 SMASH-BIO | force_spectroscopy | study_record | in vitro Active microrheology using pulsed optical tweezers to probe viscoelasticity of Lamin A towards diagnosis of laminopathies · Lamin A/C; optical tweezers; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-001816 SMASH-BIO | force_spectroscopy | study_record | in vitro Active microrheology using pulsed optical tweezers to probe viscoelasticity of lamin A. · Lamin A/C; optical tweezers; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-001873 SMASH-BIO | force_spectroscopy | study_record | in vitro Depletion of HP1α alters the mechanical properties of MCF7 nuclei. · Lamin A/C; optical tweezers; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, rheology_cell, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-002656 SMASH-BIO | force_spectroscopy | study_record | in vitro Cell migration through three-dimensional confining pores: speed accelerations by deformation and recoil of the nucleus. · Lamin A/C; afm smfs; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, rheology_cell | unmapped |
| EV-SMASH-SMFS-002761 SMASH-BIO | force_spectroscopy | study_record | in vitro Intracellular manipulation and measurement with multipole magnetic tweezers. · Lamin A/C; magnetic tweezers; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-003581 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanics and Buckling of Biopolymeric Shells and Cell Nuclei. · Lamin A/C; force spectroscopy unspecified; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-003582 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanics and buckling of biopolymeric shells and cell nuclei · Lamin A/C; force spectroscopy unspecified; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-004041 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8.5 Significance of 1B and 2B domains in modulating elastic properties of lamin A. · Lamin A/C; afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-004122 SMASH-BIO | force_spectroscopy | study_record | in vitro AFM single-cell force spectroscopy links altered nuclear and cytoskeletal mechanics to defective cell adhesion in cardiac myocytes with a nuclear lamin mutation. · Lamin A/C; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-004415 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 6.5 The tethering of chromatin to the nuclear envelope supports nuclear mechanics. · Lamin A/C; optical tweezers; experiment class: chromatin_mechanics, membrane_mechanics, rheology_cell | unmapped |
| EV-SMASH-SMFS-004489 SMASH-BIO | force_spectroscopy | study_record | in vitro Characterization of unfolding mechanism of human lamin A Ig fold by single-molecule force spectroscopy-implications in EDMD. · Lamin A/C; afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004587 SMASH-BIO | force_spectroscopy | study_record | in vitro Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus. · Lamin A/C; magnetic tweezers; experiment class: chromatin_mechanics, receptor_ligand_adhesion, rheology_cell | unmapped |
Conflicts
No conflicts found among comparable evidence.
51 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.