Homo sapiens · seed P10636 · 758 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P10636 RCSB by accession PDBe-KB AlphaFold DB InterPro RCSB 9BXI PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
9BXI, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
63 distinct constructs across 242 entries. 236 polymer entities differ from the UniProt canonical sequence in some way, 2 carry a recognised expression tag and 0 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 85 | 441 | 1.86 | 7QKY | 2 internal deletions |
| 44 | 382 | 1.75 | 8Q98 | 3 internal deletions |
| 18 | 75 | 2.31 | 8UQ7 | residues 622-696 |
| 8 | 73 | 2.70 | 8FUG | residues 623-695 |
| 6 | 77 | 2.70 | 9BXI | residues 621-697 |
| 6 | 441 | 2.30 | 9EOE | 2 internal deletions; V654M |
| 6 | 758 | 2.29 | 9PGO | matches the canonical sequence |
| 2 | 31 | 1.80 | 6DC8 | residues 696-726 |
| 2 | 48 | 3.30 | 6QJM | residues 591-638 |
| 2 | 94 | 2.61 | 8P34 | residues 602-695; S602K, Q605K, C608I +5 more |
| 2 | 96 | 2.50 | 7YPG | residues 613-708; N613M |
| 2 | 107 | 3.10 | 10IJ | residues 590-696; S622I |
| 2 | 107 | 3.80 | 6VH7 | residues 591-697 |
| 2 | 194 | 4.10 | 7PQC | residues 519-712 |
| 2 | 202 | residues 515-716 | ||
| 2 | 352 | 2.48 | 9H5G | 4 internal deletions; T498D, S519D, T522D +9 more |
| 2 | 352 | 2.69 | 9CGZ | 4 internal deletions |
| 2 | 412 | 2.30 | 8ORG | 3 internal deletions |
| 2 | 430 | 3.40 | 29OU | 2 internal deletions |
| 2 | 441 | 2.50 | 9BBL | 2 internal deletions; S713E, S717E, T720E +1 more |
| 2 | 449 | 3.10 | 9O8E | His6; 2 internal deletions |
| 1 | 20 | 2.00 | 6DCW | residues 543-562 |
| 1 | 22 | 2.90 | 9S2B | residues 614-635 |
| 1 | 23 | 2.10 | 6BB4 | residues 703-725 |
| 1 | 24 | 1.95 | 6H0E | residues 698-721 |
Showing the 25 most-used of 63.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| hexameric | 6 | 97 | 40.1% |
| decameric | 10 | 35 | 14.5% |
| trimeric | 3 | 32 | 13.2% |
| pentameric | 5 | 20 | 8.3% |
| nonameric | 9 | 10 | 4.1% |
| octadecameric | 18 | 8 | 3.3% |
| 15-meric | 15 | 7 | 2.9% |
| monomeric | 1 | 6 | 2.5% |
140 entries have the depositor's assembly corroborated by PISA, 99 carry the depositor's word alone and 2 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run.
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| GDP | cofactor | Guanosine-5'-Diphosphate | 6 | 2.21 |
| MG | ion | Magnesium Ion | 6 | 2.21 |
| GTP | cofactor | Guanosine-5'-Triphosphate | 6 | 2.21 |
| GOL | cryoprotectant | Glycerol | 5 | 1.80 |
| PO4 | ion | Phosphate Ion | 4 | 1.80 |
| A1B91 | ligand | 7-Nitro-N-[2-(2-{[(3p)-3-(1h-Pyrrolo[2,3-C]pyridin-1-Yl)isoquino | 4 | 2.31 |
| GLY | buffer | Glycine | 2 | 3.30 |
| CL | ion | Chloride Ion | 2 | 1.92 |
| K | ion | Potassium Ion | 1 | 1.92 |
| KDH | ligand | (2r,3r)-5,7-Dihydroxy-2-(3,4,5-Trihydroxyphenyl)-3,4-Dihydro-2h- | 1 | 3.80 |
| S9C | ligand | 7-(6-Fluoranylpyridin-3-Yl)-5~{H}-Pyrido[4,3-B]indole | 1 | 2.60 |
| Y9H | ligand | (5s)-2-[4-(2-Fluoroethyl)piperidin-1-Yl]pyrimido[1,2-A]benzimida | 1 | 2.70 |
| X6R | ligand | 6-Fluoro-3-(1h-Pyrrolo[2,3-C]pyridin-1-Yl)isoquinolin-5-Amine | 1 | 2.31 |
| A1AHG | ligand | 4-Hydroxy-3-{(E)-[4-(6-Methyl-1,3-Benzothiazol-2-Yl)phenyl]diaze | 1 | 3.30 |
| EDT | ligand | {[-(Bis-Carboxymethyl-Amino)-Ethyl]-Carboxymethyl-Amino}-Acetic | 1 | 3.10 |
| TA1 | ligand | Taxol | 1 | 2.94 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 1 | 2.21 |
| PGE | cryoprotectant | Triethylene Glycol | 1 | 2.21 |
| P6G | cryoprotectant | Hexaethylene Glycol | 1 | 2.21 |
| 1PE | cryoprotectant | Pentaethylene Glycol | 1 | 2.21 |
Parsed from the free text 9 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 9
entries that recorded anything at all.
Median pH 7.0
(range 6.5 to 7.0).
239 entries carry a wwPDB validation report: 197 clean, 32 worth a check and 10 with something to explain. Median clashscore 1.49, median RSRZ outliers 1.55%, median R-free minus R-work 0.052. 239 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 236 | 1.75 | 16 | 100% |
| Mus musculus | 4 | 1.95 | 0 | 100% |
| synthetic construct | 1 | 2.21 | 1 | 3% |
| Homo | 1 | 2.90 | 0 | 10% |
| Mus | 1 | 3.40 | 0 | 100% |
758 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | The Pick fold in tau filaments from human MAPT mutants. Acta Neuropathol doi:10.1007/s00401-026-03049-8 |
| 2026 | Cryo-EM structure of pro-aggregant P301L/S320F double-mutant tau filaments formed in mouse brains following peripheral AAV delivery Biorxiv doi:10.64898/2026.01.19.700132 |
| 2026 | Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments. Elife doi:10.7554/eLife.104778 |
| 2026 | Repositioning of polyubiquitin alters the pathologic tau filament structure. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01879-4 |
| 2026 | Distinct tau filament folds in familial frontotemporal dementia due to the MAPT S305I mutation. Biorxiv doi:10.64898/2026.02.12.705620 |
| 2026 | Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils. Iscience doi:10.1016/j.isci.2026.115501 |
| 2026 | Dopamine-Induced Tau Modification Prevents Pathological Phosphorylation and Generates a Distinct Fibril Polymorph. J.Am.Chem.Soc. doi:10.1021/jacs.5c22156 |
| 2025 | Tau filaments with the Alzheimer fold in human MAPT mutants V337M and R406W. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01498-5 |
| 2025 | Serial amplification of tau filaments using Alzheimer's brain homogenates and C322A or C322S recombinant tau. Febs Lett. doi:10.1002/1873-3468.70141 |
| 2025 | Structures of Delta D421 Truncated Tau Fibrils. J.Mol.Biol. doi:10.1016/j.jmb.2025.169051 |
| 2025 | How short peptides disassemble tau fibrils in Alzheimer's disease. Nature doi:10.1038/s41586-025-09244-z |
| 2025 | Cryo-EM studies of amyloid-beta fibrils from human and murine brains carrying the Uppsala APP mutation ( Delta 690-695). Acta Neuropathol Commun doi:10.1186/s40478-025-02120-x |
| 2025 | Seeding biosensor cell line that reproduces the Alzheimer tau fold. J.Biol.Chem. doi:10.1016/j.jbc.2025.110952 |
| 2024 | Disease-specific tau filaments assemble via polymorphic intermediates. Nature doi:10.1038/s41586-023-06788-w |
| 2024 | The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization. Pnas Nexus doi:10.1093/pnasnexus/pgae487 |
| 2024 | Novel tau filament folds in individuals with MAPT mutations P301L and P301T. Biorxiv doi:10.1101/2024.08.15.608062 |
| 2024 | Tau filaments with the chronic traumatic encephalopathy fold in a case of vacuolar tauopathy with VCP mutation D395G. Acta Neuropathol doi:10.1007/s00401-024-02741-x |
| 2024 | Cryo-EM structure of Alzheimer's disease tau filaments with PET ligand MK-6240. Nat Commun doi:10.1038/s41467-024-52265-x |
| 2024 | Structures of AT8 and PHF1 phosphomimetic tau: Insights into the posttranslational modification code of tau aggregation. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2316175121 |
| 2024 | Milligram-scale assembly and NMR fingerprint of tau fibrils adopting the Alzheimer's disease fold. J.Biol.Chem. doi:10.1016/j.jbc.2024.107326 |
| 2024 | Alzheimer's disease seeded tau forms paired helical filaments yet lacks seeding potential. J.Biol.Chem. doi:10.1016/j.jbc.2024.107730 |
| 2024 | Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer's disease fold. Acta Neuropathol Commun doi:10.1186/s40478-024-01806-y |
| 2024 | Cryo-EM structures of amyloid-beta and tau filaments in Down syndrome. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01252-3 |
| 2024 | Cryo-EM structures of cotton wool plaques' amyloid beta and of tau filaments in dominantly inherited Alzheimer disease. Acta Neuropathol doi:10.1007/s00401-024-02786-y |
| 2024 | Post-Translational Modifications Control Phase Transitions of Tau. Biorxiv doi:10.1101/2024.03.08.583040 |
| 2024 | Cryo-EM structures reveal variant Tau amyloid fibrils between the rTg4510 mouse model and sporadic human tauopathies. Cell Discov doi:10.1038/s41421-023-00637-w |
| 2023 | Tau filaments from amyotrophic lateral sclerosis/parkinsonism-dementia complex adopt the CTE fold. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2306767120 |
| 2023 | Identical tau filaments in subacute sclerosing panencephalitis and chronic traumatic encephalopathy. Acta Neuropathol Commun doi:10.1186/s40478-023-01565-2 |
| 2023 | Cryo-EM structures of tau filaments from SH-SY5Y cells seeded with brain extracts from cases of Alzheimer's disease and corticobasal degeneration. Febs Open Bio doi:10.1002/2211-5463.13657 |
| 2023 | Cryo-EM Structures of Chronic Traumatic Encephalopathy Tau Filaments with PET Ligand Flortaucipir. J.Mol.Biol. doi:10.1016/j.jmb.2023.168025 |
| 2023 | Mutation ∆K281 in MAPT causes Pick's disease. Acta Neuropathol doi:10.1007/s00401-023-02598-6 |
| 2023 | Stacked binding of a PET ligand to Alzheimer's tau paired helical filaments. Nat Commun doi:10.1038/s41467-023-38537-y |
| 2023 | Cryo-EM structures of tau filaments from the brains of mice transgenic for human mutant P301S Tau. Acta Neuropathol Commun doi:10.1186/s40478-023-01658-y |
| 2023 | Abundant A beta fibrils in ultracentrifugal supernatants of aqueous extracts from Alzheimer's disease brains. Neuron doi:10.1016/j.neuron.2023.04.007 |
| 2023 | Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates. Nat Commun doi:10.1038/s41467-023-39314-7 |
| 2023 | Tau filaments are tethered within brain extracellular vesicles in Alzheimer's disease. Biorxiv doi:10.1101/2023.04.30.537820 |
| 2023 | Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat. Sci Adv doi:10.1126/sciadv.adh4731 |
| 2023 | Structure of the nonhelical filament of the Alzheimer's disease tau core. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2310067120 |
| 2022 | Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy. Elife doi:10.7554/eLife.76494 |
| 2022 | Subtle change of fibrillation condition leads to substantial alteration of recombinant Tau fibril structure. Iscience doi:10.1016/j.isci.2022.105645 |