Worked example — how one UniProtKB entry demultiplexes across the four axes
Using P25888 (ATP-dependent RNA helicase RhlE, Escherichia coli K12) to
illustrate how a single UniProtKB entry’s FT/CC annotations map onto the
trait axes and categories.
Note. This is an illustration of the demultiplexing model, not a set of
live records. Per-protein records like these are instance-level annotations,
not reusable trait classes, so they are not seeded standalone; instead a
real protein is attached as a canonical_example on the relevant class-level
trait (via fetch_uniprot_examples.py). The mapping below — FT type → axis /
category — is what the seeders and the README table encode.
← back to index · source entry
SEQUENCE (6 records)
| # |
Trait |
Category |
UniProt evidence |
| 1 |
Disordered C-terminal region, residues 373-454 |
SEQ_DISORDER |
FT REGION /note="Disordered" (MobiDB-lite) |
| 2 |
Gly-rich composition bias 393-406 |
SEQ_COMPOSITION |
FT COMPBIAS /note="Gly residues" |
| 3 |
Basic + acidic residues 424-434 |
SEQ_COMPOSITION |
FT COMPBIAS /note="Basic and acidic residues" |
| 4 |
Basic residues 443-454 |
SEQ_COMPOSITION |
FT COMPBIAS /note="Basic residues" |
| 5 |
Q motif 1-29 |
SEQ_MOTIF |
FT MOTIF /note="Q motif" (cross-refs PROSITE PS51195) |
| 6 |
DEAD box 156-159 |
SEQ_MOTIF |
FT MOTIF /note="DEAD box" (cross-refs PROSITE PS00039) |
STRUCTURE (3 records)
| # |
Trait |
Category |
UniProt evidence |
| 7 |
Helicase ATP-binding domain 32-208 |
STRUCT_DOMAIN |
FT DOMAIN /note="Helicase ATP-binding" |
| 8 |
Helicase C-terminal domain 219-381 |
STRUCT_DOMAIN |
FT DOMAIN /note="Helicase C-terminal" |
| 9 |
ATP binding site 45-52 |
STRUCT_BINDING_SITE |
FT BINDING /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
FUNCTION (11 records)
FUNC_ENZYMATIC_ACTIVITY (3)
| # |
Trait |
Source |
| 10 |
ATP + H₂O → ADP + phosphate + H⁺ (EC 3.6.4.13, Rhea:13065) |
CC CATALYTIC ACTIVITY |
| 11 |
ATP hydrolysis activity (GO:0016887) |
DR GO F: |
| 12 |
RNA helicase activity (GO:0003724) |
DR GO F: |
FUNC_BINDING_CAPACITY (2)
| # |
Trait |
Source |
| 13 |
ATP binding (GO:0005524) |
DR GO F: (complements the localised binding site #9) |
| 14 |
RNA binding (GO:0003723) |
DR GO F: |
FUNC_LOCALIZATION (2)
| # |
Trait |
Source |
| 15 |
Cytoplasm (with ribosome-associated note) |
CC SUBCELLULAR LOCATION |
| 16 |
Cytosol (GO:0005829) |
DR GO C: |
FUNC_ENVIRONMENTAL_RESPONSE (2)
| # |
Trait |
Source |
| 17 |
Response to cold shock (PubMed:14527658) |
CC INDUCTION — keyword scan matches “cold shock” |
| 18 |
Response to heat (GO:0009408) |
DR GO P: response to heat |
FUNC_INTERACTION_PARTNER (2)
| # |
Trait |
Source |
| 19 |
Interacts with PcnB (PubMed:10361280) |
CC SUBUNIT |
| 20 |
Interacts in vitro with RNase E (PubMed:15554979) |
CC SUBUNIT |
What’s captured, what’s still open
Captured automatically: identifiers, human-readable labels, cross-references to source ontologies, canonical exemplar (the source UniProt entry + NCBITaxon), evidence PMIDs where the flat file cites them.
Open for curator work:
- Deduplication where CC-derived and GO-derived records describe the same concept (e.g. records #15 + #16 both describe cytoplasmic localisation).
mapping_status: SEEDED → REVIEWED after curator sign-off.
causal_graphs — none of these 20 records carry a mechanism graph yet. A natural first graph on record #9 (ATP binding site) would model ATP → (binds) → helicase ATP-binding domain → (hydrolyses) → ADP + Pi → (couples to) → RNA unwinding → (leads to) → ribosome assembly, with each edge citing PubMed:15196029 / PubMed:18083833.
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