Huntingtin
UniProt P42858 · gene HTT · Homo sapiens · 3142 residues
78evidence items
0mapped to a state
0states
10techniques
5sources
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 | saxs_sans | epr_deer | cd | ensemble_fret | force_spectroscopy | auc | Total |
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| No states defined yet. | ||||||||||||
Unmapped evidence: 78 of 78 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| BMRB | 3 | 0 |
| DisProt | 35 | 0 |
| RCSB PDB | 30 | 0 |
| SASBDB | 2 | 0 |
| SMASH-BIO | 8 | 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-2LD0-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 7.2 Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFE · Huntingtin (chains A) | unmapped |
| EV-PDB-2LD2-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 6 Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles · Huntingtin (chains A) | unmapped |
| EV-PDB-3IO4-1 RCSB PDB | xray | resolution: 3.63 Å | in vitro · -173.15 °C · pH 7.2 · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - Crystal C90 · Maltose-binding periplasmic protein,Huntingtin fusion protein (chains A,B,C) | unmapped |
| EV-PDB-3IOT-1 RCSB PDB | xray | resolution: 3.5 Å | in vitro · -173.15 °C · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C92-b · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-3IOV-1 RCSB PDB | xray | resolution: 3.7 Å | in vitro · -173.15 °C · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C99 · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-4FEB-1 RCSB PDB | xray | resolution: 2.8 Å | in vitro · -173.15 °C · pH 6.5 · ligands NA, ZN Crystal Structure of Htt36Q3H-EX1-X1-C2(Beta) · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-4FEC-1 RCSB PDB | xray | resolution: 3 Å | in vitro · -173.15 °C · pH 6.5 · ligands ZN Crystal Structure of Htt36Q3H · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-4RAV-3 RCSB PDB | xray | resolution: 2.5 Å | in vitro · -173.15 °C · pH 4.6 · ligands SO4 Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin · Huntingtin (chains E,F) | unmapped |
| EV-PDB-9YR6-1 RCSB PDB | cryoem | resolution: 2.3 Å | in vitro · ligands A1CYY Structure of HTTQ23-HAP40 complex bound to a small molecule ligand · Huntingtin (chains A) | unmapped |
| EV-PDB-9PN0-4 RCSB PDB | cryoem | resolution: 2.3 Å | in vitro Structure of HTTQ23-HAP40 complex bound to macrocycles HHD3, HD4 and HL2 · Huntingtin (chains A) | unmapped |
| EV-PDB-9PMW-4 RCSB PDB | cryoem | resolution: 2.1 Å | in vitro Structure of HTTQ23-HAP40 complex bound to macrocycles HHL1, HD4 and HL2 · Huntingtin (chains A) | unmapped |
| EV-PDB-8YAO-1 RCSB PDB | cryoem | resolution: 20.8 Å | in vitro Cryo-ET structure of huntingtin actin dimer complex · Huntingtin (chains A,a) | unmapped |
| EV-PDB-8YAE-1 RCSB PDB | cryoem | resolution: 10.08 Å | in vitro Cryo-ET structure of huntingtin actin complex · Huntingtin (chains A) | unmapped |
| EV-PDB-8W15-1 RCSB PDB | cryoem | resolution: 2.72 Å | in vitro HTT in complex with HAP40 in the apo state. · Huntingtin (chains A) | unmapped |
| EV-PDB-8VLX-1 RCSB PDB | cryoem | resolution: 2.6 Å | in vitro · ligands A1ACS HTT in complex with HAP40 and a small molecule. · Huntingtin (chains A) | unmapped |
| EV-PDB-8SAH-1 RCSB PDB | cryoem | resolution: 3.2 Å | in vitro Huntingtin C-HEAT domain in complex with HAP40 · Huntingtin (chains A) | unmapped |
| EV-PDB-7DXK-1 RCSB PDB | cryoem | resolution: 4.1 Å | in vitro Human 128QHuntingtin-HAP40 complex structure · Huntingtin (chains A) | unmapped |
| EV-PDB-7DXJ-1 RCSB PDB | cryoem | resolution: 3.6 Å | in vitro Human 46QHuntingtin-HAP40 complex structure · Huntingtin (chains A) | unmapped |
| EV-PDB-6YEJ-1 RCSB PDB | cryoem | resolution: 18.2 Å | in vitro Cryo-EM structure of the Full-length disease type human Huntingtin · Huntingtin (chains A) | unmapped |
| EV-PDB-6X9O-1 RCSB PDB | cryoem | resolution: 2.6 Å | in vitro High resolution cryoEM structure of huntingtin in complex with HAP40 · Huntingtin (chains A) | unmapped |
| EV-PDB-6RMH-1 RCSB PDB | cryoem | resolution: 9.6 Å | in vitro The Rigid-body refined model of the normal Huntingtin. · Huntingtin (chains A) | unmapped |
| EV-PDB-6N8C-1 RCSB PDB | nmr_structure | structure | in vitro · 4.85 °C · pH 6.5 Structure of the Huntingtin tetramer/dimer mixture determined by paramagnetic NMR · Huntingtin (chains A,B,C,D) | unmapped |
| EV-PDB-6EZ8-1 RCSB PDB | cryoem | resolution: 4 Å | in vitro Human Huntingtin-HAP40 complex structure · Huntingtin (chains A) | unmapped |
| EV-PDB-4FED-1 RCSB PDB | xray | resolution: 2.807 Å | in vitro · -173.15 °C · pH 6.5 · ligands CA, ZN Crystal Structure of Htt36Q3H · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-4FE8-1 RCSB PDB | xray | resolution: 3 Å | in vitro · -173.15 °C · pH 6.5 · ligands ZN Crystal Structure of Htt36Q3H-EX1-X1-C1(Alpha) · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-3LRH-2 RCSB PDB | xray | resolution: 2.6 Å | in vitro · -173.15 °C · pH 4.1 Structure of anti-huntingtin VL domain in complex with huntingtin peptide · Huntingtin (chains B,D,F,H,J,L,N,P) | unmapped |
| EV-PDB-3IOW-1 RCSB PDB | xray | resolution: 3.5 Å | in vitro · -173.15 °C · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C99-Hg · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-3IOU-1 RCSB PDB | xray | resolution: 3.7 Å | in vitro · -173.15 °C · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C94 · Maltose-binding periplasmic protein,Huntingtin (chains A,B,C) | unmapped |
| EV-PDB-3IOR-1 RCSB PDB | xray | resolution: 3.6 Å | in vitro · -173.15 °C · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C95 · Maltose-binding protein, huntingtin fusion protein (chains A,B,C) | unmapped |
| EV-PDB-3IO6-1 RCSB PDB | xray | resolution: 3.7 Å | in vitro · pH 7.2 · ligands CA, ZN Huntingtin amino-terminal region with 17 Gln residues - crystal C92-a · Maltose-binding periplasmic protein, HUNTINGTIN FUSION PROTEIN (chains A,B,C) | unmapped |
| EV-BMRB-17642 BMRB | nmr_shifts | chemical_shift | in vitro · -0.15 °C · pH 7.2 Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFE · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-17644 BMRB | nmr_shifts | chemical_shift | in vitro · -0.15 °C · pH 6 Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-30545 BMRB | nmr_shifts | chemical_shift | in vitro · 4.85 °C · pH 6.5 Structure of the Huttingtin tetramer/dimer mixture determined by paramagnetic NMR · BMRB data: 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-SASBDB-SASDQR8 SASBDB | saxs_sans | radius_of_gyration: 3.299 nm ± 0.019 | in vitro · 10 °C · pH 6.5 The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity. · Huntingtin | unmapped |
| EV-SASBDB-SASDQS8 SASBDB | saxs_sans | radius_of_gyration: 4.15 nm ± 0.042 | in vitro · 10 °C · pH 6.5 The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity. · Huntingtin | unmapped |
| EV-DISPROT-DP04129r001 DisProt | cd | disorder_region: 17 residues | in vitro DisProt DP04129: disorder, residues 1-17 · residues 1-17; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r002 DisProt | nmr_shifts | disorder_region: 17 residues | in vitro DisProt DP04129: disorder, residues 1-17 · residues 1-17; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r003 DisProt | xray | disorder_region: 11 residues | in vitro DisProt DP04129: disorder, residues 19-29 · residues 19-29; evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r004 DisProt | nmr_shifts | disorder_region: 34 residues | in vitro DisProt DP04129: disorder, residues 1-34 · residues 1-34; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r005 DisProt | cd | disorder_region: 17 residues | in vitro DisProt DP04129: disorder, residues 1-17 · residues 1-17; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r006 DisProt | ensemble_fret | disorder_region: 50 residues | in vitro DisProt DP04129: disorder, residues 39-88 · residues 39-88; evidence: fluorescence resonance energy transfer evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r007 DisProt | ensemble_fret | disorder_region: 38 residues | in vitro DisProt DP04129: disorder, residues 1-38 · residues 1-38; evidence: fluorescence resonance energy transfer evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r008 DisProt | nmr_shifts | disorder_region: 90 residues | in vitro DisProt DP04129: disorder, residues 1-90 · residues 1-90; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r010 DisProt | cd | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r011 DisProt | auc | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: analytical ultracentrifugation evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r012 DisProt | cd | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r014 DisProt | saxs_sans | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: small-angle X-ray scattering evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r015 DisProt | cd | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r016 DisProt | epr_deer | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r017 DisProt | nmr_shifts | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r018 DisProt | nmr_shifts | disorder_region: 88 residues | in vitro DisProt DP04129: disorder, residues 1-88 · residues 1-88; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r019 DisProt | saxs_sans | disorder_region: 88 residues | in vitro DisProt DP04129: disorder, residues 1-88 · residues 1-88; evidence: small-angle X-ray scattering evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r020 DisProt | nmr_shifts | disorder_region: 88 residues | in vitro DisProt DP04129: disorder, residues 1-88 · residues 1-88; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r021 DisProt | nmr_shifts | disorder_region: 87 residues | in vitro DisProt DP04129: disorder, residues 1-87 · residues 1-87; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP04129r022 DisProt | cryoem | disorder_region: 15 residues | in vitro DisProt DP04129: disorder, residues 1718-1732 · residues 1718-1732; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r024 DisProt | cryoem | disorder_region: 29 residues | in vitro DisProt DP04129: disorder, residues 2067-2095 · residues 2067-2095; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r028 DisProt | cryoem | disorder_region: 258 residues | in vitro DisProt DP04129: disorder, residues 407-664 · residues 407-664; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r031 DisProt | cryoem | disorder_region: 65 residues | in vitro DisProt DP04129: disorder, residues 1162-1226 · residues 1162-1226; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r032 DisProt | cryoem | disorder_region: 94 residues | in vitro DisProt DP04129: disorder, residues 1-94 · residues 1-94; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r033 DisProt | cryoem | disorder_region: 29 residues | in vitro DisProt DP04129: disorder, residues 1323-1351 · residues 1323-1351; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r034 DisProt | cryoem | disorder_region: 47 residues | in vitro DisProt DP04129: disorder, residues 1376-1422 · residues 1376-1422; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r035 DisProt | cryoem | disorder_region: 27 residues | in vitro DisProt DP04129: disorder, residues 1859-1885 · residues 1859-1885; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r036 DisProt | cryoem | disorder_region: 23 residues | in vitro DisProt DP04129: disorder, residues 2329-2351 · residues 2329-2351; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r037 DisProt | cryoem | disorder_region: 34 residues | in vitro DisProt DP04129: disorder, residues 2631-2664 · residues 2631-2664; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r038 DisProt | cryoem | disorder_region: 40 residues | in vitro DisProt DP04129: disorder, residues 3103-3142 · residues 3103-3142; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r041 DisProt | cryoem | disorder_region: 20 residues | in vitro DisProt DP04129: disorder, residues 327-346 · residues 327-346; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r042 DisProt | cryoem | disorder_region: 18 residues | in vitro DisProt DP04129: disorder, residues 964-981 · residues 964-981; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r043 DisProt | cryoem | disorder_region: 18 residues | in vitro DisProt DP04129: disorder, residues 1107-1124 · residues 1107-1124; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r044 DisProt | cryoem | disorder_region: 19 residues | in vitro DisProt DP04129: disorder, residues 2476-2494 · residues 2476-2494; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-DISPROT-DP04129r045 DisProt | cryoem | disorder_region: 19 residues | in vitro DisProt DP04129: disorder, residues 2930-2948 · residues 2930-2948; evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion | unmapped |
| EV-SMASH-SMFS-000299 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.5 Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65. · Huntingtin; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000622 SMASH-BIO | force_spectroscopy | study_record | in vitro Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilising Effects on the Scaffold PR65 · Huntingtin; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000956 SMASH-BIO | force_spectroscopy | study_record | in vitro Stick-slip unfolding favors self-association of expanded HTT mRNA · Huntingtin; afm smfs; experiment class: nucleic_acid_protein_interaction, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000957 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 6.5 Stick-slip unfolding favors self-association of expanded HTT mRNA. · Huntingtin; afm smfs; experiment class: nucleic_acid_protein_interaction, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001136 SMASH-BIO | force_spectroscopy | study_record | in vitro Elucidating the Influence of Lipid Composition on Bilayer Perturbations Induced by the N-terminal Region of the Huntingtin Protein. · Huntingtin; afm smfs; experiment class: membrane_mechanics, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001184 SMASH-BIO | force_spectroscopy | study_record | in vitro Huntingtin S421 phosphorylation increases kinesin and dynein engagement on early endosomes and lysosomes. · Huntingtin; optical tweezers; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001550 SMASH-BIO | force_spectroscopy | study_record | in vitro Huntingtin S421 phosphorylation increases kinesin and dynein engagement on early endosomes and lysosomes · Huntingtin; optical tweezers; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006179 SMASH-BIO | force_spectroscopy | study_record | in vitro Single homopolypeptide chains collapse into mechanically rigid conformations. · Huntingtin; force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
76 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.