DHX36
registry:0252 · Q9H2U1
Experimental material and evidence scope
- Experimental material
- DHX36-derived RHAU53 peptide
- Material type
- Protein fragment
- Material identity
- Material qualified by source
- Source support
- No target-specific support
- Relationship to the registered name
- Archive source lead
- Research purpose
- RNA recognition
Author-processed binding-library tables are acquired and checked. The assayed material is the DHX36-derived RHAU53 peptide, not full-length DHX36.
Query and download access
PRJNA994088 Linked; not live-checked
Source context
GSE237159_RHAU53_enrichment_6mers_Rvalue_K.tsv.gz Linked; not live-checked
Author-processed results
GSE237159_RHAU53_enrichment_6mers_Rvalue_Li.tsv.gz Linked; not live-checked
Author-processed results
Counts and their scope
| Measure | Count | Scope or reason unavailable |
|---|---|---|
| Independent molecular targets | Undetermined | this registration Experimental identity unresolved |
| Processed source sequence rows | Undetermined | historical processed source labels; not public unique sequences Not yet verified |
| Retained candidate records | Undetermined | sum of distinct linked source-target groups; not globally unique sequences Not yet connected |
| Round records | Undetermined | sum of distinct linked source-target groups; not globally unique sequences Not yet connected |
| Sequence–round observations | Undetermined | sum of distinct linked source-target groups; not globally unique sequences Not yet connected |
| Target-specific read records | Undetermined | experiment material matched to this registration No target-specific count established |
Sources and supporting relationships
Archive source lead · PRJNA994088 · PRJNA994088
Transcriptomic RNA structure mapping unveils the structure dynamic induced by DHX36 binding (RBNS)
PRJNA994088 identifies an RHAU53 peptide RBNS source; it is not proof of acquisition or full-length DHX36 data.
Author-processed tables · GSE237159 · GSE237159
Author-processed binding-library tables are acquired and checked. The assayed material is the DHX36-derived RHAU53 peptide, not full-length DHX36.
Remaining evidence gaps
- Author tables have been acquired; source-qualified sequence integration is not complete.
- Author-processed binding-library tables are acquired and checked. The assayed material is the DHX36-derived RHAU53 peptide, not full-length DHX36.
- No explicit public retained-candidate target mapping is established in this matrix.