Homo sapiens · seed P68133 · 377 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P68133 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.20.10 CATH 2.30.36.70 CATH 3.30.420.40 CATH 3.90.640.10 SCOP 8040506 SCOP 8043436 SCOP 8082531 SCOP 8044481 SCOP 8003798 SCOP 8037889 SCOP 8082549 SCOP 8043438 SCOP 8040509 SCOP 8092415 SCOP 8044482 SCOP 8092404 SCOP 8092422 SCOP 8037893 SCOP 8037891 RCSB 2FXU 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.
2FXU, 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.
144 distinct constructs across 749 entries. 418 polymer entities differ from the UniProt canonical sequence in some way, 13 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 |
|---|---|---|---|---|
| 160 | 375 | 1.35 | 2FXU | residues 3-377 |
| 155 | 377 | 1.15 | 7W4Z | matches the canonical sequence |
| 78 | 375 | 2.40 | 3U4L | matches the canonical sequence |
| 46 | 377 | 2.79 | 9ZBL | matches the canonical sequence |
| 32 | 418 | 2.00 | 1K8K | matches the canonical sequence |
| 29 | 394 | 2.00 | 1K8K | matches the canonical sequence |
| 26 | 429 | 2.40 | 8QR1 | matches the canonical sequence |
| 24 | 376 | 3.30 | 7Z8I | 2 internal deletions; W310F, S311G, R319D +25 more |
| 17 | 371 | 1.90 | 2GWJ | residues 7-377 |
| 16 | 376 | 1.29 | 4B1Y | residues 2-377 |
| 15 | 374 | 2.18 | 9QEW | residues 2-375; C272A |
| 12 | 373 | 1.53 | 5ZZA | residues 5-377 |
| 12 | 375 | 1.90 | 1YAG | matches the canonical sequence |
| 11 | 375 | 2.60 | 8K6V | matches the canonical sequence |
| 9 | 374 | 1.80 | 2HF3 | residues 3-376; A205E, P244K |
| 9 | 769 | 2.70 | 8OOP | residues 98-866 |
| 8 | 374 | 2.20 | 3UB5 | residues 2-375 |
| 7 | 378 | 1.22 | 6I4E | matches the canonical sequence |
| 6 | 373 | 4.60 | 6BNP | residues 1-373 |
| 6 | 427 | 2.70 | 8UXW | matches the canonical sequence |
| 5 | 390 | 2.70 | 8UXW | matches the canonical sequence |
| 4 | 370 | 1.72 | 36OQ | residues 7-376 |
| 4 | 370 | 3.02 | 8ZBN | residues 7-376 |
| 3 | 367 | 8.00 | 5NOL | residues 7-373; M301L, T360S |
| 3 | 371 | 3.08 | 8ZI9 | residues 7-377 |
Showing the 25 most-used of 144.
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 |
|---|---|---|---|
| dimeric | 2 | 150 | 20.0% |
| heptameric | 7 | 67 | 8.9% |
| tetrameric | 4 | 61 | 8.1% |
| pentameric | 5 | 60 | 8.0% |
| trimeric | 3 | 46 | 6.1% |
| decameric | 10 | 40 | 5.3% |
| octameric | 8 | 34 | 4.5% |
| monomeric | 1 | 33 | 4.4% |
353 entries have the depositor's assembly corroborated by PISA, 387 carry the depositor's word alone and 8 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 17 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1D4X, 1NLV, 1NM1, 1NMD, 1P8Z, 1YAG, 1YVN, 2A40, 2Q97, 2YJF, 3CI5, 3CIP, 3M6G, 4V0U, 6DEC, 6WK1, 6WK2.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| Severin | CATH 3.40.20.10 | 3–129 | 11 |
| Actin; Chain A, domain 2 | CATH 2.30.36.70 | 37–70 | 67 |
| ATPase, nucleotide binding domain | CATH 3.30.420.40 | 145–187 | 837 |
| ATPase, substrate binding domain, subdomain 4 | CATH 3.90.640.10 | 184–273 | 236 |
| Actin-like ATPases | SCOP2B 8040506 | 7–148 | 243 |
| Actin-like ATPases | SCOP2B 8043436 | 7–146 | 53 |
| Actin-like ATPases | SCOP2B 8082531 | 7–149 | 14 |
| Actin-like ATPases | SCOP2B 8044481 | 7–149 | 8 |
| Actin-like ATPases | SCOP2B 8003798 | 8–149 | 8 |
| Actin-like ATPases | SCOP2B 8037889 | 11–168 | 28 |
| Actin-like ATPases | SCOP2B 8082549 | 11–153 | 13 |
| Actin-like ATPases | SCOP2B 8043438 | 147–374 | 53 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| ADP | cofactor | Adenosine-5'-Diphosphate | 420 | 1.15 |
| MG | ion | Magnesium Ion | 418 | 1.15 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 247 | 1.24 |
| CA | ion | Calcium Ion | 211 | 1.15 |
| PO4 | ion | Phosphate Ion | 57 | 1.15 |
| EDO | cryoprotectant | 1,2-Ethanediol | 31 | 1.15 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 30 | 1.15 |
| LAB | ligand | Latrunculin B | 28 | 1.29 |
| ZN | ion | Zinc Ion | 28 | 3.20 |
| GOL | cryoprotectant | Glycerol | 24 | 1.29 |
| SO4 | ion | Sulfate Ion | 20 | 1.60 |
| LAR | ligand | Latrunculin A | 18 | 1.75 |
| 9UE | ligand | Jasplakinolide | 12 | 2.60 |
| SCN | ion | Thiocyanate Ion | 11 | 1.22 |
| GDP | cofactor | Guanosine-5'-Diphosphate | 10 | 3.10 |
| CL | ion | Chloride Ion | 9 | 1.24 |
| BEF | ion | Beryllium Trifluoride Ion | 8 | 2.17 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 8 | 1.22 |
| GTP | cofactor | Guanosine-5'-Triphosphate | 7 | 3.10 |
| AGS | cofactor | Phosphothiophosphoric Acid-Adenylate Ester | 7 | 2.75 |
Parsed from the free text 218 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 222
entries that recorded anything at all.
Median pH 6.6
(range 3.5 to 10.0).
736 entries carry a wwPDB validation report: 468 clean, 145 worth a check and 123 with something to explain. Median clashscore 6.13, median RSRZ outliers 2.95%, median R-free minus R-work 0.04. 712 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Oryctolagus cuniculus | 323 | 1.29 | 298 | 100% |
| Homo sapiens | 124 | 1.35 | 121 | 100% |
| Sus scrofa | 64 | 3.00 | 65 | 100% |
| Bos taurus | 41 | 2.00 | 60 | 100% |
| Gallus gallus | 58 | 1.15 | 56 | 100% |
| Mus musculus | 34 | 3.00 | 30 | 100% |
| Drosophila melanogaster | 13 | 1.80 | 14 | 100% |
| Plasmodium falciparum 3D7 | 13 | 1.22 | 13 | 99% |
| Dictyostelium discoideum | 13 | 1.60 | 13 | 100% |
| Thermochaetoides thermophila | 11 | 2.70 | 10 | 99% |
| Saccharomyces cerevisiae S288C | 8 | 2.80 | 7 | 99% |
| Limulus polyphemus | 1 | 9.50 | 0 | 97% |
377 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 | Mechanisms of disassembly at the actin filament pointed and barbed ends. Sci Adv doi:10.1126/sciadv.aee5882 |
| 2026 | Mechanism of actin thin filament pointed-end elongation by leiomodin. Nat Commun doi:10.1038/s41467-026-74810-6 |
| 2026 | Structural mechanisms of drebrin-mediated F-actin network modulation. Nat Commun doi:10.1038/s41467-026-74543-6 |
| 2026 | Molecular basis of host ATP level modulation by actin-dependent secreted bacterial ATPase and its metaeffector. Nat Commun doi:10.1038/s41467-026-74513-y |
| 2026 | Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase. Nat.Chem.Biol. doi:10.1038/s41589-025-01945-w |
| 2026 | Structural basis for BCL7B-mediated ncBAF-nucleosome engagement. Nucleic Acids Res. doi:10.1093/nar/gkag092 |
| 2026 | Evolutionarily conserved short linear motifs drive actin filament binding. Nat.Cell Biol. doi:10.1038/s41556-026-01979-9 |
| 2026 | Tonotopic specialization of MYO7A isoforms in auditory hair cells. Nat Commun doi:10.1038/s41467-026-73220-y |
| 2026 | Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation. J.Cell Biol. doi:10.1083/jcb.202409067 |
| 2026 | The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2. Mol.Cell doi:10.1016/j.molcel.2026.01.021 |
| 2026 | Structural basis of human gamma TuRC closure during CM1-activated microtubule nucleation. Nat Commun doi:10.1038/s41467-026-70773-w |
| 2026 | Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Sci Adv doi:10.1126/sciadv.aei7728 |
| 2026 | Roles of microtubules and LIS1 in dynein transport machinery assembly. Nature doi:10.1038/s41586-026-10153-y |
| 2026 | Leiomodin 2 is a processive pointed-end elongator of actin filaments. Nat Commun doi:10.1038/s41467-026-74809-z |
| 2026 | The structure of the native cardiac crossbridge in the rigor state. Sci Adv doi:10.1126/sciadv.aeg1209 |
| 2026 | Structural basis of complex assembly and nucleosome recognition by the chromatin remodeling ncBAF complex. J Mol Cell Biol doi:10.1093/jmcb/mjag020 |
| 2026 | Activation and regulation of the dynein-dynactin-NuMA complex. Nat.Chem.Biol. doi:10.1038/s41589-026-02156-7 |
| 2025 | Microscopic and structural observations of actin filament capping and severing by cytochalasin D. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2502164122 |
| 2025 | Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1. Cell doi:10.1016/j.cell.2025.09.016 |
| 2025 | Aglycone Polyether Ionophores Affecting Actin Filaments as Broad-Spectrum Antiviral Agents. Acs Pharmacol Transl Sci doi:10.1021/acsptsci.5c00144 |
| 2025 | Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 angstrom resolution. A comparison with vertebrate F-actin. Structure doi:10.1016/j.str.2024.12.008 |
| 2025 | Mechanism of actin filament severing and capping by gelsolin. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01412-5 |
| 2025 | The structure of an actin nucleus stabilized by villin. Sci Adv doi:10.1126/sciadv.adw6915 |
| 2025 | High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2415457122 |
| 2025 | Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments. J.Mol.Cell.Cardiol. doi:10.1016/j.yjmcc.2025.12.008 |
| 2025 | Dimerization of GAS2 mediates crosslinking of microtubules and F-actin. Embo J. doi:10.1038/s44318-025-00415-2 |
| 2025 | ncBAF recognizes the nucleosome through BCL7A in chromatin remodeling. Cell Discov doi:10.1038/s41421-025-00858-1 |
| 2025 | NPF binding to Arp2 is allosterically linked to the release of ArpC5's N-terminal tail and conformational changes in Arp2/3 complex. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2421557122 |
| 2025 | Biochemical and structural bases for talin ABSs-F-actin interactions. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2405922122 |
| 2025 | Fascin structural plasticity mediates flexible actin bundle construction. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01477-2 |
| 2025 | Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01665-8 |
| 2025 | Actin isoform-specific interactions revealed by Vibrio VopV actin-binding repeats. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2523856122 |
| 2025 | Harnessing the Evolution of Proteostasis Networks to Reverse Cognitive Dysfunction. Biorxiv doi:10.1101/2025.02.28.640897 |
| 2025 | Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms. Science doi:10.1126/science.adr3314 |
| 2025 | Structure of the F-tractin-F-actin complex. J.Cell Biol. doi:10.1083/jcb.202409192 |
| 2025 | Unveiling the structural proteome of an Alzheimer's disease rat brain model. Structure doi:10.1016/j.str.2024.11.004 |
| 2025 | Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01673-8 |
| 2025 | The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection. Cell Rep doi:10.1016/j.celrep.2025.115509 |
| 2025 | The hypertrophic cardiomyopathy-associated A331P actin variant enhances basal contractile activity and elicits resting muscle dysfunction. Iscience doi:10.1016/j.isci.2025.111816 |
| 2025 | Cryo-EM structure revealed a novel F-actin binding motif in a Legionella pneumophila lysine fatty-acyltransferase Elife doi:10.7554/elife.106975.1 |