ExonSkipAD: functional annotation of exon skipping event in human

Gene summary for AKT1

Gene summary

Gene information	Gene symbol	AKT1
	Gene ID	207
	Gene name	AKT serine/threonine kinase 1
	Synonyms	AKT\|CWS6\|PKB\|PKB-ALPHA\|PRKBA\|RAC\|RAC-ALPHA
	Cytomap	14q32.33
	Type of gene	protein-coding
	Description	RAC-alpha serine/threonine-protein kinaseAKT1mPKB alphaRAC-PK-alphaprotein kinase B alphaproto-oncogene c-Aktrac protein kinase alphaserine-threonine protein kinasev-akt murine thymoma viral oncogene homolog 1v-akt murine thymoma viral oncogene-l
	Modification date	20200329
	UniProtAcc	A0A087WY56, A0A0S2Z3D6, A0A142IKA9, B0LPE5, G3V2I6, G3V3X1, G3V4I6, P31749, X2CV47, X2CVF3,
	Context	- 26178916(Association Between Polymorphisms of the AKT1 Gene Promoter and Risk of the Alzheimer's Disease in a Chinese Han Population With Type 2 Diabetes)

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

Gene	GO ID	GO term	PubMed ID
AKT1	GO:0001934	positive regulation of protein phosphorylation	19057511
AKT1	GO:0006468	protein phosphorylation	11994271\|14749367\|23431171
AKT1	GO:0007173	epidermal growth factor receptor signaling pathway	20878056
AKT1	GO:0016310	phosphorylation	20333297
AKT1	GO:0018105	peptidyl-serine phosphorylation	16139227
AKT1	GO:0018107	peptidyl-threonine phosphorylation	20605787
AKT1	GO:0030307	positive regulation of cell growth	19203586
AKT1	GO:0032079	positive regulation of endodeoxyribonuclease activity	20605787
AKT1	GO:0033138	positive regulation of peptidyl-serine phosphorylation	19667065
AKT1	GO:0035556	intracellular signal transduction	14749367
AKT1	GO:0035655	interleukin-18-mediated signaling pathway	21321938
AKT1	GO:0043066	negative regulation of apoptotic process	19203586
AKT1	GO:0043536	positive regulation of blood vessel endothelial cell migration	20011604
AKT1	GO:0048661	positive regulation of smooth muscle cell proliferation	21321938
AKT1	GO:0051091	positive regulation of DNA-binding transcription factor activity	19057511
AKT1	GO:0070141	response to UV-A	18483258

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Gene structures and expression levels for AKT1

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.

ENSG00000142208

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
CB	DOWN	ENST00000555458.5	AKT1-213:protein_coding:AKT1	1.263710e+01	-8.554239e-01	4.213134e-05	3.558329e-04
CB	UP	ENST00000554848.5	AKT1-211:protein_coding:AKT1	1.379154e+02	1.302036e+00	2.356973e-03	1.055671e-02

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 AKT1

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_178971	chr14	104780088:104780216:104792598:104792722:104795484:104795504	104792598:104792722
exon_skip_206593	chr14	104776671:104776770:104780088:104780216:104792598:104792722	104780088:104780216
exon_skip_215129	chr14	104792598:104792722:104793127:104793210:104795484:104795504	104793127:104793210
exon_skip_222716	chr14	104792598:104792722:104793127:104793210:104795484:104795499	104793127:104793210
exon_skip_242018	chr14	104792598:104792722:104793127:104793304:104795484:104795504	104793127:104793304
exon_skip_245253	chr14	104773251:104773379:104773455:104773580:104773912:104773980	104773455:104773580
exon_skip_263604	chr14	104780088:104780216:104792598:104792722:104794119:104794191	104792598:104792722
exon_skip_267188	chr14	104792598:104792722:104793127:104793304:104795484:104795499	104793127:104793304
exon_skip_291539	chr14	104792598:104792722:104793127:104793210:104795484:104795751	104793127:104793210
exon_skip_42898	chr14	104770745:104770847:104771722:104771816:104772365:104772452	104771722:104771816
exon_skip_74185	chr14	104770801:104770847:104771722:104771816:104772365:104772452	104771722:104771816

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 AKT1

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
ENST00000349310	104793127	104793210	3UTR-3UTR
ENST00000349310	104780088	104780216	In-frame
ENST00000402615	104780088	104780216	In-frame
ENST00000407796	104780088	104780216	In-frame
ENST00000554848	104780088	104780216	In-frame
ENST00000555528	104780088	104780216	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
ENST00000349310	104793127	104793210	3UTR-3UTR

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
ENST00000407796	104792598	104792722	3UTR-3CDS
ENST00000554848	104792598	104792722	3UTR-3CDS
ENST00000349310	104793127	104793210	3UTR-3UTR
ENST00000349310	104773455	104773580	In-frame
ENST00000402615	104773455	104773580	In-frame
ENST00000407796	104773455	104773580	In-frame
ENST00000554581	104773455	104773580	In-frame
ENST00000554848	104773455	104773580	In-frame
ENST00000555528	104773455	104773580	In-frame
ENST00000349310	104780088	104780216	In-frame
ENST00000402615	104780088	104780216	In-frame
ENST00000407796	104780088	104780216	In-frame
ENST00000554848	104780088	104780216	In-frame
ENST00000555528	104780088	104780216	In-frame

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Infer the effects of exon skipping event on protein functional features for AKT1

p-ENSG00000142208_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
ENST00000349310	2883	480	104780088	104780216	478	605	15	58
ENST00000402615	3930	480	104780088	104780216	1528	1655	15	58
ENST00000407796	2727	480	104780088	104780216	322	449	15	58
ENST00000554848	1612	480	104780088	104780216	199	326	15	58
ENST00000555528	3083	480	104780088	104780216	700	827	15	58

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
ENST00000349310	2883	480	104780088	104780216	478	605	15	58
ENST00000402615	3930	480	104780088	104780216	1528	1655	15	58
ENST00000407796	2727	480	104780088	104780216	322	449	15	58
ENST00000554848	1612	480	104780088	104780216	199	326	15	58
ENST00000555528	3083	480	104780088	104780216	700	827	15	58
ENST00000349310	2883	480	104773455	104773580	1134	1258	234	275
ENST00000402615	3930	480	104773455	104773580	2184	2308	234	275
ENST00000407796	2727	480	104773455	104773580	978	1102	234	275
ENST00000554581	3933	480	104773455	104773580	2184	2308	234	275
ENST00000554848	1612	480	104773455	104773580	855	979	234	275
ENST00000555528	3083	480	104773455	104773580	1356	1480	234	275

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
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding

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
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	1	62	Alternative sequence	ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:14702039;Dbxref=PMID:14702039
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	6	15	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	17	19	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	22	30	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	33	40	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	52	56	Beta strand	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	53	53	Binding site	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	5	108	Domain	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00145
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	45	48	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:1UNQ
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Modified residue	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	17	17	Mutagenesis	Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	20	20	Mutagenesis	Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:21775285;Dbxref=PMID:21775285
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	25	25	Mutagenesis	Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:12176338;Dbxref=PMID:12176338
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	17	17	Natural variant	ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	25	25	Natural variant	ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	14	19	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	15	58	23	25	Region	Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	274	274	Active site	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159,ECO:0000255\|PROSITE-ProRule:PRU10027
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	234	234	Binding site	Note=Inhibitor
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	1	480	Chain	ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	150	408	Domain	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	235	242	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	247	268	Helix	Ontology_term=ECO:0000244;evidence=ECO:0000244\|PDB:4GV1
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305
P31749	234	275	246	246	Sequence conflict	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305

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3'-UTR located exon skipping events that lost miRNA binding sites in AKT1

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
Mayo	ENST00000349310	104793127	104793210	hsa-miR-765	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
Mayo	ENST00000349310	104793127	104793210	hsa-miR-11181-3p	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
Mayo	ENST00000349310	104793127	104793210	hsa-miR-9500	chr14:104793198-104793205	8mer-1a	chr14:104793190-104793210	145.00	-20.60
MSBB	ENST00000349310	104793127	104793210	hsa-miR-765	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
MSBB	ENST00000349310	104793127	104793210	hsa-miR-11181-3p	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
MSBB	ENST00000349310	104793127	104793210	hsa-miR-9500	chr14:104793198-104793205	8mer-1a	chr14:104793190-104793210	145.00	-20.60
ROSMAP	ENST00000349310	104793127	104793210	hsa-miR-765	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
ROSMAP	ENST00000349310	104793127	104793210	hsa-miR-11181-3p	chr14:104793151-104793158	8mer-1a	chr14:104793145-104793167	165.00	-36.56
ROSMAP	ENST00000349310	104793127	104793210	hsa-miR-9500	chr14:104793198-104793205	8mer-1a	chr14:104793190-104793210	145.00	-20.60

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SNVs in the skipped exons for AKT1

- 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 AKT1

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 AKT1

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 AKT1

Correlated RBP and related information.

Tissue type

RBP name

Exon skip ID

Correlation coeifficient

P-value

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RelatedDrugs for AKT1

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

UniProtAcc	DrugBank ID	Drug name	Drug activity	Drug type	Drug status
P31749	approved\|investigational	DB01169	Arsenic trioxide	small molecule	P31749

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RelatedDiseases for AKT1

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 AKT1

Gene structures and expression levels for AKT1

Exon skipping events with PSIs in ROSMAP, MSBB, and Mayo for AKT1

Open reading frame (ORF) annotation in the exon skipping event for AKT1

Infer the effects of exon skipping event on protein functional features for AKT1

3'-UTR located exon skipping events that lost miRNA binding sites in AKT1

SNVs in the skipped exons for AKT1

AD stage-associated exon skippint events for AKT1

Splicing Quantitative Trait Loci (sQTL) in the exon skipping event for AKT1

Correlation with RNA binding proteins (RBPs) for AKT1

RelatedDrugs for AKT1

RelatedDiseases for AKT1