ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:DMPK

Protein Summary

Gene summary

Gene name: DMPK
ASpdb.0 ID: 1760
	Gene
Gene symbol	DMPK
Gene ID	1760
Gene name	DM1 protein kinase
Synonyms	DM\|DM1\|DM1PK\|DMK\|MDPK\|MT-PK
Cytomap	19q13.32
Type of gene	protein-coding
Description	myotonin-protein kinaseDM protein kinasedystrophia myotonica protein kinasemyotonic dystrophy associated protein kinasemyotonin protein kinase Athymopoietin homolog
Modification date	20240403
UniProtAcc	Q09013

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	DMPK	GO:0004674	protein serine/threonine kinase activity	10913253\|11287000
Gene	DMPK	GO:0005524	ATP binding	10913253
Gene	DMPK	GO:0005741	mitochondrial outer membrane	15684391
Gene	DMPK	GO:0006468	protein phosphorylation	10913253\|11287000
Gene	DMPK	GO:0008016	regulation of heart contraction	15598648
Gene	DMPK	GO:0010657	muscle cell apoptotic process	18729234
Gene	DMPK	GO:0017020	myosin phosphatase regulator activity	11287000

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
Q09013-9	Q09013-9_2vd5_A.pdb	2VD5	X-ray	2.8	A	11	416

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
Q09013	DMPK	Q09013-9	Q09013-10	629	535	534	535	Substitution	AV	GP	534	535
Q09013	DMPK	Q09013-9	Q09013-10	629	535	536	629	Deletion	none	none	535	535
Q09013	DMPK	Q09013-9	Q09013-11	629	624	378	382	Deletion	none	none	377	377
Q09013	DMPK	Q09013-9	Q09013-12	629	530	378	382	Deletion	none	none	377	377
Q09013	DMPK	Q09013-9	Q09013-12	629	530	534	535	Substitution	AV	GP	529	530
Q09013	DMPK	Q09013-9	Q09013-12	629	530	536	629	Deletion	none	none	530	530
Q09013	DMPK	Q09013-9	Q09013-15	629	625	378	382	Deletion	none	none	377	377
Q09013	DMPK	Q09013-9	Q09013-15	629	625	550	629	Substitution	LDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP	MAPRPWLWASARWWGQAPCTAATCCSLPGSLGLAYRRRFPCSCSPLFCLVPPPWAALGWWPTPANSPQSGAAQEPPALPEP	545	625
Q09013	DMPK	Q09013-9	Q09013-16	629	630	550	629	Substitution	LDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP	MAPRPWLWASARWWGQAPCTAATCCSLPGSLGLAYRRRFPCSCSPLFCLVPPPWAALGWWPTPANSPQSGAAQEPPALPEP	550	630
Q09013	DMPK	Q09013-9	Q09013-2	629	540	1	89	Deletion	none	none	0	0
Q09013	DMPK	Q09013-9	Q09013-6	629	634	1	53	Substitution	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQW	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPP	1	63
Q09013	DMPK	Q09013-9	Q09013-6	629	634	378	382	Deletion	none	none	387	387
Q09013	DMPK	Q09013-9	Q09013-7	629	609	1	53	Substitution	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQW	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPP	1	63
Q09013	DMPK	Q09013-9	Q09013-7	629	609	550	579	Deletion	none	none	559	559
Q09013	DMPK	Q09013-9	Q09013-8	629	545	1	53	Substitution	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQW	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPP	1	63
Q09013	DMPK	Q09013-9	Q09013-8	629	545	534	535	Substitution	AV	GP	544	545
Q09013	DMPK	Q09013-9	Q09013-8	629	545	536	629	Deletion	none	none	545	545

Multiple sequence alignment of our canonical and alternatively spliced DMPK

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of DMPK

UniProt-id	ENSG	ENST	ENSP
Q09013-9	ENSG00000104936.20	ENST00000291270.9	ENSP00000291270.4
Q09013-10	ENSG00000104936.20	ENST00000683086.1	ENSP00000508381.1
Q09013-11	ENSG00000104936.20	ENST00000447742.6	ENSP00000413417.1
Q09013-12	ENSG00000104936.20	ENST00000354227.9	ENSP00000346168.5
Q09013-15	ENSG00000104936.20	ENST00000458663.6	ENSP00000401753.1
Q09013-16	ENSG00000104936.20	ENST00000343373.10	ENSP00000345997.4

UniProt-id	NM ID	NP ID
Q09013-9	NM_004409.4	NP_004400.4
Q09013-11	NM_001081560.2	NP_001075029.1
Q09013-15	NM_001081562.2	NP_001075031.1

Amino acid sequences of our canonical and alternatively spliced DMPK

accession_id	Protein sequence
Q09013-9	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAE VAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPS
Q09013-10	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAE
Q09013-11	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPA AVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATD
Q09013-12	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPA
Q09013-15	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPA AVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATD
Q09013-16	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKM KQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIV MAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYE MFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEG ATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAE VAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPS PRATDPPSHMAPRPWLWASARWWGQAPCTAATCCSLPGSLGLAYRRRFPCSCSPLFCLVPPPWAALGWWPTPANSPQSGAAQEPPALPEP
Q09013-2	MKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEI VMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAY EMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFE GATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETA EVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVP SPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP
Q09013-6	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPPAEPIVVRLKEVRLQRDDFEILKVIGRG AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAE MARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECD WWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDS VPPFTPDFEGATDTCNFDLVEDGLTAMETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQ DETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAV TGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGA
Q09013-7	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPPAEPIVVRLKEVRLQRDDFEILKVIGRG AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAE MARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECD WWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDS VPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEP SVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAE
Q09013-8	MGGHFWPPEPYTVFMWGSPWEADSPRVKLRGREKGRQTEGGAFPLVSSALSGDPRFFSPTTPPAEPIVVRLKEVRLQRDDFEILKVIGRG AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAE MARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECD WWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDS VPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEP SVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAE

Protein Functional Features

Main function of this protein. (from UniProt)

DMPK (go to UniProt):Q09013

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=534;End=535
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=378;End=382
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=378;End=382
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=534;End=535
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=378;End=382
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=1;End=89
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=1;End=53
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=378;End=382
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=1;End=53
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=550;End=579
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=1;End=53
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=534;End=535
Q09013	Topological domain	1	590	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Transmembrane	591	611	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Transmembrane	591	611	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Transmembrane	591	611	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Transmembrane	591	611	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Transmembrane	591	611	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Topological domain	612	629	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Topological domain	612	629	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Topological domain	612	629	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Topological domain	612	629	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=550;End=629
Q09013	Topological domain	612	629	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=536;End=629
Q09013	Domain	71	339	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00159	Type=Deletion;Start=1;End=89
Q09013	Domain	340	415	Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00618	Type=Deletion;Start=378;End=382
Q09013	Domain	340	415	Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00618	Type=Deletion;Start=378;End=382
Q09013	Domain	340	415	Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00618	Type=Deletion;Start=378;End=382
Q09013	Domain	340	415	Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00618	Type=Deletion;Start=378;End=382
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383
Q09013	Coiled coil	457	536	"Ontology_term=ECO:0000269	ECO:0000269;evidence=ECO:0000269\|PubMed:15583383

Gene Isoform Structures and Expression Levels for DMPK

Gene structures of our canonical and alternative spliced genes of DMPK
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of Q09013-9

3D view using mol* of Q09013-10

3D view using mol* of Q09013-11

3D view using mol* of Q09013-12

3D view using mol* of Q09013-15

3D view using mol* of Q09013-16

3D view using mol* of Q09013-2

3D view using mol* of Q09013-6

3D view using mol* of Q09013-7

3D view using mol* of Q09013-8

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of Q09013-9

pLDDT distribution across the protein length of Q09013-10

pLDDT distribution across the protein length of Q09013-11

pLDDT distribution across the protein length of Q09013-12

pLDDT distribution across the protein length of Q09013-15

pLDDT distribution across the protein length of Q09013-16

pLDDT distribution across the protein length of Q09013-2

pLDDT distribution across the protein length of Q09013-6

pLDDT distribution across the protein length of Q09013-7

pLDDT distribution across the protein length of Q09013-8

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of Q09013-9

Ramachandran plot of Q09013-10

Ramachandran plot of Q09013-11

Ramachandran plot of Q09013-12

Ramachandran plot of Q09013-15

Ramachandran plot of Q09013-16

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
Q09013-9	1.088	168	1.134	304.927	0.455	0.764	1.007	1.395	0.812	1.718	0.832	23,27,30,31,34,62,65,66,67,68,104,136,137,138,139, 140,141,145,397,404,405,406
Q09013-10	1.086	170	1.026	452.074	0.437	0.827	1.064	0.74	1.26	0.588	1.033	77,78,79,80,81,82,83,85,98,100,102,107,113,114,115 ,116,119,123,132,148,149,150,151,155,157,158,195,1 97,199,200,202,212,213,214,215,216,232,233,367,368 ,370
Q09013-11	1.182	204	1.305	652.043	0.44	0.741	1.044	2.897	0.245	11.816	1.487	7,10,11,14,15,20,22,25,26,28,29,32,36,50,53,57,61, 393,396,570,571,572,573,574,576,582,585,586,587,58 9,590,591,593,594,596,597,598,599,600,601,604
Q09013-12	1.081	168	1.031	478.485	0.468	0.82	1.035	0.742	1.231	0.602	0.881	77,78,79,80,81,82,83,85,98,100,110,113,114,116,119 ,123,132,148,149,150,151,155,157,158,195,197,199,2 00,202,212,213,214,215,216,232,233,367,368,370
Q09013-15	1.128	104	1.185	163.611	0.438	0.795	1.082	1.678	0.711	2.359	0.667	27,30,31,34,62,65,66,67,68,104,138,139,140,141,142 ,392,395,396,399
Q09013-16	1.091	119	1.12	194.138	0.457	0.798	1.051	1.167	0.916	1.274	0.963	27,30,31,33,34,58,62,65,66,67,68,69,104,138,139,14 0,141,145,397,400,401,404
Q09013-2	0.969	156	1.002	380.73	0.622	0.63	0.79	0.365	0.97	0.376	0.719	68,71,72,75,76,77,148,180,181,184,185,186,187,188, 189,190,200,207,208,209,279,479,480,481,482,483,48 4
Q09013-6	1.033	268	1.012	981.666	0.572	0.748	0.94	0.573	1.157	0.495	0.764	87,88,89,90,91,92,93,94,95,108,110,116,117,119,120 ,122,123,124,125,126,129,133,142,158,159,160,161,1 65,167,168,204,205,207,209,210,212,222,223,224,225 ,226,242,243,377,378,379,380,381,387,388,571,572,5 73,575,576,577,578,579
Q09013-7	1.095	209	1.007	543.998	0.387	0.839	1.081	0.787	1.34	0.587	0.672	87,88,90,91,92,93,95,108,110,112,117,120,123,124,1 25,126,129,133,142,156,158,159,160,161,165,167,168 ,205,207,209,210,212,222,223,224,225,226,242,377,3 78,380
Q09013-8	1.041	199	0.93	469.567	0.441	0.759	1.034	0.246	1.428	0.172	0.585	105,106,107,133,134,135,136,138,139,141,143,144,14 5,159,160,161,162,214,215,216,218,220,358,371,415, 417,420,421,424,425,426,427,428,429,430,431

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of Q09013-9_Q09013-9_2vd5_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q09013-9_2vd5_A_Q09013-10.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-11.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-12.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-15.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-16.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-2.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-6.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-7.pdb

3D view using mol* of Q09013-9_2vd5_A_Q09013-8.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q09013-9_Q09013-10.pdb

3D view using mol* of Q09013-9_Q09013-11.pdb

3D view using mol* of Q09013-9_Q09013-12.pdb

3D view using mol* of Q09013-9_Q09013-15.pdb

3D view using mol* of Q09013-9_Q09013-16.pdb

3D view using mol* of Q09013-9_Q09013-2.pdb

3D view using mol* of Q09013-9_Q09013-6.pdb

3D view using mol* of Q09013-9_Q09013-7.pdb

3D view using mol* of Q09013-9_Q09013-8.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-10.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-11.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-12.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-15.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-16.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-2.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-6.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-7.png

./stats/secondary_structure/figure/Q09013-9_vs_Q09013-8.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/Q09013-9_vs_Q09013-10.png

./stats/relative_asa/Q09013-9_vs_Q09013-11.png

./stats/relative_asa/Q09013-9_vs_Q09013-12.png

./stats/relative_asa/Q09013-9_vs_Q09013-15.png

./stats/relative_asa/Q09013-9_vs_Q09013-16.png

./stats/relative_asa/Q09013-9_vs_Q09013-2.png

./stats/relative_asa/Q09013-9_vs_Q09013-6.png

./stats/relative_asa/Q09013-9_vs_Q09013-7.png

./stats/relative_asa/Q09013-9_vs_Q09013-8.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to DMPK

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession	Gene name	DrugBank ID	Drug name	Drug group	Actions
Q09013	DMPK	DB01946	Bisindolylmaleimide VIII	experimental

Related Diseases to DMPK

Previous studies relating to the alternative splicing of DMPK and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
DMPK	17846170	Defining early steps in mRNA transport: mutant mRNA in myotonic dystrophy type I is blocked at entry into SC-35 domains.	In myotonic dystrophy type 1 (DM1), triplet repeat expansion in the 3' untranslated region of dystrophia myotonica protein kinase (DMPK) causes the nuclear retention of mutant messenger RNA (mRNA). Although the DMPK gene locus positions precisely at the outer edge of a factor-rich SC-35 domain, the normal mRNA consistently accumulates within the domain, and this RNA is depleted upon transcriptional inhibition. In DM1, mutant transcripts detach from the gene but accumulate in granules that abut but do not enter SC-35 domains, suggesting that RNA entry into the domain is blocked. Despite their exclusion from these compartments, mutant transcripts are spliced. MBNL1 (muscleblind-like protein 1) is an alternative splicing factor that becomes highly concentrated with mutant RNA foci. Small interfering RNA-mediated knockdown of MBNL1 promotes the accumulation or entry of newly synthesized mutant transcripts in the SC-35 domain. Collectively, these data suggest that an initial step in the intranuclear path of some mRNAs is passage from the gene into an SC-35 domain and implicate these structures in postsplicing steps before export.	D009223	Myotonic Dystrophy
DMPK	20685272	Analysis of MTMR1 expression and correlation with muscle pathological features in juvenile/adult onset myotonic dystrophy type 1 (DM1) and in myotonic dystrophy type 2 (DM2).	Among genes abnormally expressed in myotonic dystrophy type1 (DM1), the myotubularin-related 1 gene (MTMR1) was related to impaired muscle differentiation. Therefore, we analyzed MTMR1 expression in correlation with CUG-binding protein1 (CUG-BP1) and muscleblind-like1 protein (MBNL1) steady-state levels and with morphological features in muscle tissues from DM1 and myotonic dystrophy type 2 (DM2) patients. Semi-quantitative RT-PCR for MTMR1 was done on muscle biopsies and primary muscle cultures. The presence of impaired muscle fiber maturation was evaluated using immunochemistry for neural cell adhesion molecule (NCAM), Vimentin and neonatal myosin heavy chain. CUG-BP1 and MBNL1 steady-state levels were estimated by Western blot. RNA-fluorescence in situ hybridization combined with immunochemistry for CUG-BP1, MBNL1 and NCAM were performed on serial muscle sections. An aberrant splicing of MTMR1 and a significant amount of NCAM-positive myofibers were detected in DM1 and DM2 muscle biopsies; these alterations correlated with DNA repeat expansion size only in DM1. CUG-BP1 levels were increased only in DM1 muscles, while MBNL1 levels were similar among DM1, DM2 and controls. Normal and NCAM-positive myofibers displayed no differences either in the amount of ribonuclear foci and the intracellular distribution of MBNL1 and CUG-BP1. In conclusion, an aberrant MTMR1 expression and signs of altered myofiber maturation were documented in both DM1 and in DM2 muscle tissues. The more severe dysregulation of MTMR1 expression in DM1 versus DM2, along with increased CUG-BP1 levels only in DM1 tissues, suggests that the mutual antagonism between MBNL1 and CUG-BP1 on alternative splicing is more unbalanced in DM1.	D009223	Myotonic Dystrophy
DMPK	23196502	[Misregulation of alternative splicing and microRNA processing in DM1 pathogenesis].	Myotonic dystrophy of type I (DM1) is an autosomal dominant inherited disease caused by an unstable CTG expansion in the 3' non-coding region of the DMPK gene that confers to the mutant transcript a toxic RNA gain-of-function. Nuclear accumulation of DMPK transcripts containing expanded CUG repeats alters the activities of the splicing regulators MBNL1 and CUGBP1 resulting in alternative splicing misregulation of a numerous of transcripts in DM1 tissues. In collaboration with N. Charlet we identified a new mis-splicing event in the muscles of DM1 patients: BIN1 exon11 splicing mis-regulation due to MBNL1 loss-of-function results in the expression of an inactive form of BIN1. Reproducing similar BIN1 mis-splicing defect in the muscles of wild type mice is sufficient to promote T-tubule alterations and muscle strength decrease, suggesting that alteration of BIN1 splicing contributes to DM1 muscle weakness. Interestingly, the RNA binding protein MBNL1 regulates also the processing of the microRNA miR-1 that was found mis-regulated in the heart of DM1 patients. The consequences of miR-1 mis-regulation on DM1 heart conduction defects are not fully understood yet, however this work may shed light on the alteration of this class of non-coding RNA as an additional molecular mechanisms involved in DM1 pathophysiology.	D009223	Myotonic Dystrophy
DMPK	24792155	DDX6 regulates sequestered nuclear CUG-expanded DMPK-mRNA in dystrophia myotonica type 1.	Myotonic dystrophy type 1 (DM1) is caused by CUG triplet expansions in the 3' UTR of dystrophia myotonica protein kinase (DMPK) messenger ribonucleic acid (mRNA). The etiology of this multi-systemic disease involves pre-mRNA splicing defects elicited by the ability of the CUG-expanded mRNA to 'sponge' splicing factors of the muscleblind family. Although nuclear aggregation of CUG-containing mRNPs in distinct foci is a hallmark of DM1, the mechanisms of their homeostasis have not been completely elucidated. Here we show that a DEAD-box helicase, DDX6, interacts with CUG triplet-repeat mRNA in primary fibroblasts from DM1 patients and with CUG-RNA in vitro. DDX6 overexpression relieves DM1 mis-splicing, and causes a significant reduction in nuclear DMPK-mRNA foci. Conversely, knockdown of endogenous DDX6 leads to a significant increase in DMPK-mRNA foci count and to increased sequestration of MBNL1 in the nucleus. While the level of CUG-expanded mRNA is unaffected by increased DDX6 expression, the mRNA re-localizes to the cytoplasm and its interaction partner MBNL1 becomes dispersed and also partially re-localized to the cytoplasm. Finally, we show that DDX6 unwinds CUG-repeat duplexes in vitro in an adenosinetriphosphate-dependent manner, suggesting that DDX6 can remodel and release nuclear DMPK messenger ribonucleoprotein foci, leading to normalization of pathogenic alternative splicing events.	D009223	Myotonic Dystrophy

Clinically important variants in DMPK

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance