DMPK_HUMAN - dbPTM
DMPK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DMPK_HUMAN
UniProt AC Q09013
Protein Name Myotonin-protein kinase
Gene Name DMPK
Organism Homo sapiens (Human).
Sequence Length 629
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type IV membrane protein
Cytoplasmic side. Nucleus outer membrane
Single-pass type IV membrane protein
Cytoplasmic side . Mitochondrion outer membrane
Single-pass type IV membrane protein . Sarcoplasmic r
Protein Description Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity..
Protein Sequence MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSAEVRLRR
------CCHHHHHHH		32.89-
47 (in isoform 6)Phosphorylation-5.1922210691
47 (in isoform 5)Phosphorylation-5.1922210691
47 (in isoform 1)Phosphorylation-5.1922210691
47 (in isoform 7)Phosphorylation-5.1922210691
47 (in isoform 8)Phosphorylation-5.1922210691
48 (in isoform 7)Phosphorylation-9.9622210691
48 (in isoform 6)Phosphorylation-9.9622210691
48 (in isoform 5)Phosphorylation-9.9622210691
48 (in isoform 1)Phosphorylation-9.9622210691
48 (in isoform 8)Phosphorylation-9.9622210691
51 (in isoform 7)Phosphorylation-4.2322210691
51 (in isoform 8)Phosphorylation-4.2322210691
51 (in isoform 1)Phosphorylation-4.2322210691
51 (in isoform 5)Phosphorylation-4.2322210691
51 (in isoform 6)Phosphorylation-4.2322210691
75UbiquitinationRDDFEILKVIGRGAF
CCCCHHHHHHCCCCC		37.15-
75 (in isoform 10)Ubiquitination-37.1521906983
75 (in isoform 11)Ubiquitination-37.1521906983
75 (in isoform 12)Ubiquitination-37.1521906983
75 (in isoform 15)Ubiquitination-37.1521906983
75 (in isoform 9)Ubiquitination-37.1521906983
85 (in isoform 8)Ubiquitination-4.7921906983
85 (in isoform 7)Ubiquitination-4.7921906983
85 (in isoform 1)Ubiquitination-4.7921906983
85 (in isoform 6)Ubiquitination-4.7921906983
85 (in isoform 5)Ubiquitination-4.7921906983
108 (in isoform 2)Ubiquitination-2.9521906983
161PhosphorylationGDLLTLLSKFGERIP
HHHHHHHHHHHCCCC		29.1124719451
197 (in isoform 12)Ubiquitination-51.0821906983
197 (in isoform 9)Ubiquitination-51.0821906983
197UbiquitinationGYVHRDIKPDNILLD
CCCCCCCCCCCEEEC		51.082190698
197 (in isoform 15)Ubiquitination-51.0821906983
197 (in isoform 11)Ubiquitination-51.0821906983
197 (in isoform 10)Ubiquitination-51.0821906983
207 (in isoform 5)Ubiquitination-21.8321906983
207 (in isoform 1)Ubiquitination-21.8321906983
207 (in isoform 6)Ubiquitination-21.8321906983
207 (in isoform 7)Ubiquitination-21.8321906983
207 (in isoform 8)Ubiquitination-21.8321906983
216PhosphorylationIRLADFGSCLKLRAD
EEECCCCCCEEECCC		19.10-
228PhosphorylationRADGTVRSLVAVGTP
CCCCCEEEEEECCCC		23.90-
234PhosphorylationRSLVAVGTPDYLSPE
EEEEECCCCCCCCHH		13.34-
386PhosphorylationSGGGETLSDIREGAP
CCCCCCHHHHHCCCC		38.1126091039
533PhosphorylationLLQAEGATAVTGVPS
HHHHCCCCCCCCCCC		32.30-
536PhosphorylationAEGATAVTGVPSPRA
HCCCCCCCCCCCCCC		29.96-
540PhosphorylationTAVTGVPSPRATDPP
CCCCCCCCCCCCCCC		25.3124719451
550PhosphorylationATDPPSHLDGPPAVA
CCCCCHHCCCCCEEE		10.7824719451
579MethylationRHLLLPARVPRPGLS
CEEECCCCCCCCCHH		36.71-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DMPK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DMPK_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DMPK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSPB2_HUMANHSPB2physical
9490724
HSPB2_HUMANHSPB2physical
10625651
RAC1_HUMANRAC1physical
10869570
GEMI4_HUMANGEMIN4physical
21988832
HXA2_HUMANHOXA2physical
24722188
PPLA_HUMANPLNphysical
15598648
Drug and Disease Associations
Kegg Disease
H00568 Myotonic dystrophy (DM)
OMIM Disease
160900Dystrophia myotonica 1 (DM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DMPK_HUMAN

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Related Literatures of Post-Translational Modification

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