Q9P013: Spliceosome-associated protein CWC15 homolog (CWC15)

Spliceosome-associated protein CWC15 homolog (CWC15) is a 229-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9P013.

Gene
CWC15
Organism
Homo sapiens
Length
229 residues
Mean pLDDT
74.9
Model
AF-Q9P013-F1 v6
Model created
1 Aug 2025
PDB structures
33

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.9 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate30%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution24%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:28076346, PubMed:28502770). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)

Subunit structure

Identified in the spliceosome C complex (PubMed:28076346, PubMed:28502770). Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 (PubMed:20176811). Interacts directly with CTNNBL1 in the complex (PubMed:20176811). Component of the minor…

Subcellular location

Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
8C6JEM2.8 ÅP=1-229
6ID1EM2.86 ÅP=1-229
7DVQEM2.89 ÅP=1-229
6ID0EM2.9 ÅP=1-229
6ICZEM3.0 ÅP=1-229
8I0REM3.0 ÅP=1-229
8I0TEM3.0 ÅP=1-229
8I0VEM3.0 ÅP=1-229
7QTTEM3.1 ÅQ=1-229
6QDVEM3.3 ÅP=1-229
8I0UEM3.3 ÅP=1-229
9FMDEM3.3 ÅP=1-229
6ZYMEM3.4 ÅR=1-229
8I0PEM3.4 ÅP=1-229
8I0WEM3.4 ÅP=1-229
8RO2EM3.5 ÅP=1-229
5XJCEM3.6 ÅP=1-229
7W59EM3.6 ÅP=1-229
7W5AEM3.6 ÅP=1-229
7ABFEM3.9 ÅR=1-229

Showing 20 of 33 experimental structures (best resolution first).

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