ExonSkipAD: functional annotation of exon skipping event in human

Gene summary for CPM

Gene summary

Gene information	Gene symbol	CPM
	Gene ID	1368
	Gene name	carboxypeptidase M
	Synonyms	-
	Cytomap	12q15
	Type of gene	protein-coding
	Description	carboxypeptidase Mrenal carboxypeptidaseurinary carboxypeptidase B
	Modification date	20200313
	UniProtAcc	F8VR29, F8VU13, F8VVI6, F8W111, H0YHG6, H0YHN7, P14384,
	Context

Gene ontology of each this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Gene

GO ID

GO term

PubMed ID

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Gene structures and expression levels for CPM

Skipped exons in the ROSMAP, MSBB, and Mayo based on Ensembl gene isoform structure.
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

ENSG00000135678

Differentially expressed gene analysis across multiple brain tissues between AD and control.

Tissue type

DEG direction

Base mean exp.

log2FC(AD/control)

P-value

Adj. p-value

Differentially expressed isoform analysis across multiple brain tissues between AD and control.

Tissue type	DEG direction	ENST	Transcript info.	Base mean exp.	log2FC(AD/control)	P-value	Adjc. p-value
PG	UP	ENST00000546373.5	CPM-202:protein_coding:CPM	8.598593e+01	9.638316e-01	5.671745e-15	2.624086e-11
PG	UP	ENST00000551568.6	CPM-211:protein_coding:CPM	2.045893e+02	8.005687e-01	1.303094e-07	1.871235e-05
PG	UP	ENST00000546556.1	CPM-203:nonsense_mediated_decay:CPM	1.089595e+01	1.052027e+00	1.701326e-04	4.045047e-03
PG	UP	ENST00000546912.1	CPM-204:retained_intron:CPM	3.313878e+00	1.440163e+00	4.656927e-03	4.347057e-02
CB	UP	ENST00000546373.5	CPM-202:protein_coding:CPM	1.071124e+01	1.182202e+00	8.632839e-03	3.081353e-02
TC	UP	ENST00000548954.5	CPM-208:protein_coding:CPM	8.082487e+00	9.939635e-01	4.177601e-04	4.994820e-03
TC	UP	ENST00000549781.1	CPM-210:protein_coding:CPM	1.957430e+00	1.242260e+00	8.792828e-04	8.946052e-03

Landscape of isoform expressions across multiple brain tissues between AD and control.

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Exon skipping events with PSIs in ROSMAP, MSBB, and Mayo for CPM

Landscape of individual exon skipping event across AD tissues and controls (PSI heatmap).

All exon skipping events in AD cohorts.

Exon skip ID	chr	Exons involved in exon skipping	Skipped exon
exon_skip_101169	chr12	68871806:68871956:68885792:68885885:68932678:68932840	68885792:68885885
exon_skip_107053	chr12	68871806:68871956:68885792:68885889:68932678:68932840	68885792:68885889
exon_skip_139775	chr12	68858923:68859071:68866896:68867048:68869325:68869495	68866896:68867048
exon_skip_296478	chr12	68869375:68869495:68870215:68870399:68871784:68871956	68870215:68870399

Differentially expressed PSI values of individual exon skipping events in multiple brain tissues between AD and control.

Exon skipping information

Tissue type

Avg(PSIs) in AD

Avg(PSIs) in control

Difference (PSI)

Adj. p-value

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Open reading frame (ORF) annotation in the exon skipping event for CPM

Open reading frame (ORF) of individual exon skipping events in ROSMAP based on the Ensembl gene structure combined from isoforms.

ENST	Start of skipped exon	End of skipped exon	ORF
ENST00000338356	68870215	68870399	Frame-shift
ENST00000546373	68870215	68870399	Frame-shift
ENST00000551568	68870215	68870399	Frame-shift
ENST00000338356	68885792	68885889	Frame-shift
ENST00000546373	68885792	68885889	Frame-shift
ENST00000551568	68885792	68885889	Frame-shift
ENST00000338356	68866896	68867048	In-frame
ENST00000546373	68866896	68867048	In-frame
ENST00000551568	68866896	68867048	In-frame

Open reading frame (ORF) of individual exon skipping events in MSBB based on the Ensembl gene structure combined from isoforms.

ENST	Start of skipped exon	End of skipped exon	ORF
ENST00000338356	68870215	68870399	Frame-shift
ENST00000546373	68870215	68870399	Frame-shift
ENST00000551568	68870215	68870399	Frame-shift
ENST00000338356	68885792	68885889	Frame-shift
ENST00000546373	68885792	68885889	Frame-shift
ENST00000551568	68885792	68885889	Frame-shift

Open reading frame (ORF) of individual exon skipping events in Mayo based on the Ensembl gene structure combined from isoforms.

ENST	Start of skipped exon	End of skipped exon	ORF
ENST00000338356	68870215	68870399	Frame-shift
ENST00000546373	68870215	68870399	Frame-shift
ENST00000551568	68870215	68870399	Frame-shift
ENST00000338356	68885792	68885889	Frame-shift
ENST00000546373	68885792	68885889	Frame-shift
ENST00000551568	68885792	68885889	Frame-shift
ENST00000338356	68866896	68867048	In-frame
ENST00000546373	68866896	68867048	In-frame
ENST00000551568	68866896	68867048	In-frame

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Infer the effects of exon skipping event on protein functional features for CPM

p-ENSG00000135678_img4.png
boxplot

Loci of skipped exons in ROSMAP across genomic, transcript, and protein sequence levels of In-frame cases.

ENST	Length of mRNA	Length of AA seq.	Genomic start	Genomic end	mRNA start	mRNA end	AA start	AA end
ENST00000338356	6653	443	68866896	68867048	835	986	262	313
ENST00000546373	2133	443	68866896	68867048	892	1043	262	313
ENST00000551568	6672	443	68866896	68867048	849	1000	262	313

Loci of skipped exons in MSBB across genomic, transcript, and protein sequence levels of In-frame cases.

ENST

Length of mRNA

Length of AA seq.

Genomic start

Genomic end

mRNA start

mRNA end

AA start

AA end

Loci of skipped exons in Mayo across genomic, transcript, and protein sequence levels of In-frame cases.

ENST	Length of mRNA	Length of AA seq.	Genomic start	Genomic end	mRNA start	mRNA end	AA start	AA end
ENST00000338356	6653	443	68866896	68867048	835	986	262	313
ENST00000546373	2133	443	68866896	68867048	892	1043	262	313
ENST00000551568	6672	443	68866896	68867048	849	1000	262	313

Lost protein functional features of individual exon skipping events in ROSMAP.

UniProt acc.	Start of exon skipping (AA)	End of exon skipping (AA)	Protein feature start (AA)	Protein feature end (AA)	Category of protein feature	Description of feature
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462

Lost protein functional features of individual exon skipping events in MSBB.

UniProt acc.

Start of exon skipping (AA)

End of exon skipping (AA)

Protein feature start (AA)

Protein feature end (AA)

Category of protein feature

Description of feature

Lost protein functional features of individual exon skipping events in Mayo.

UniProt acc.	Start of exon skipping (AA)	End of exon skipping (AA)	Protein feature start (AA)	Protein feature end (AA)	Category of protein feature	Description of feature
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Active site	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	279	287	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	18	423	Chain	ID=PRO_0000004391;Note=Carboxypeptidase M
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	138	285	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	242	284	Disulfide bond	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244\|PDB:1UWY,ECO:0000269\|PubMed:15066430;Dbxref=PMID:15066430
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	265	271	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	290	292	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	293	298	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	301	308	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	309	312	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UWY
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Mutagenesis	Note=2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	281	281	Mutagenesis	Note=Abolishes enzyme activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462
P14384	262	313	277	277	Site	Note=Probable structural role;Ontology_term=ECO:0000305;evidence=ECO:0000305\|PubMed:12457462;Dbxref=PMID:12457462

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3'-UTR located exon skipping events that lost miRNA binding sites in CPM

3'-UTR exon skipping evnets lost miRNA binding.

Tissue type

ENST

Exon skip start

Exon skip end

microRNA

Binding site by TargetScan

Binding type by TargetScan

Bdinding site by miRanda

Score of miRanda

Energy by miRanda

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SNVs in the skipped exons for CPM

- Differential PSIs between mutated versus non-mutated samples.

- Depth of Coverage in the skipped exon of the mutated samples.

- Sashimi plot in the skipped exon of the mutated samples.

- Non-synonymous mutations located in the skipped exons.

Cancer type

Sample

ESID

Skipped exon start

Skipped exon end

Mutation start

Mutation end

Mutation type

Reference seq

Mutation seq

AAchange

- Non-synonymous mutations located in the skipped exons in CCLE.

Sample

Skipped exon start

Skipped exon end

Mutation start

Mutation end

Mutation type

Reference seq

Mutation seq

AAchange

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AD stage-associated exon skippint events for CPM

Associated exon skipping events with Braak staging or Clinical Dementia Rating (CDR).

AD stage info

Cohort

Tissue

SE id

Coefficient

P-value

Chromosome

Strand

E1 start

E1 end

Skipped start

Skipped end

E2 start

E2 end

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Splicing Quantitative Trait Loci (sQTL) in the exon skipping event for CPM

sQTL information located at the skipped exons.

Tissue type

Exon skip ID

SNP id

Location

P-value

FDR

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Correlation with RNA binding proteins (RBPs) for CPM

Correlated RBP and related information.

Tissue type	RBP name	Exon skip ID	Correlation coeifficient	P-value
IFG	BOLL	exon_skip_107053	-4.720395e-01	3.560497e-02

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RelatedDrugs for CPM

Approved drugs targeting this gene.
(DrugBank Version 5.1.0 2018-04-02)

UniProtAcc

DrugBank ID

Drug name

Drug activity

Drug type

Drug status

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RelatedDiseases for CPM

Diseases associated with this gene.
(DisGeNet 4.0)

Gene

Disease ID

Disease name

# pubmeds

Source

	Gene summary
	Gene structures and expression levels
	Exon skipping events with PSIs in RPSMAP, MSBB, and Mayo
	Open reading frame (ORF) annotation in the exon skipping event
	Exon skipping events in the canonical protein sequence
	3'-UTR located exon skipping events lost miRNA binding sites
	SNVs in the skipped exons with depth of coverage
	AD stage-associated exon skipping events
	Splicing Quantitative Trait Loci (sQTLs) in the skipped exons
	Correlation with RNA binding proteins (RBPs)
	Related drugs with this gene
	Related diseases with this gene

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Gene summary for CPM

Gene structures and expression levels for CPM

Exon skipping events with PSIs in ROSMAP, MSBB, and Mayo for CPM

Open reading frame (ORF) annotation in the exon skipping event for CPM

Infer the effects of exon skipping event on protein functional features for CPM

3'-UTR located exon skipping events that lost miRNA binding sites in CPM

SNVs in the skipped exons for CPM

AD stage-associated exon skippint events for CPM

Splicing Quantitative Trait Loci (sQTL) in the exon skipping event for CPM

Correlation with RNA binding proteins (RBPs) for CPM

RelatedDrugs for CPM

RelatedDiseases for CPM