Gene Symbol | DMD |
Entrez ID | 1756 |
Uniprot ID | P11532 |
Description | dystrophin |
Chromosomal Location | chrX: 31,097,677-33,339,441 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0002027 |
regulation of heart rate |
Any process that modulates the frequency or rate of heart contraction. |
IMP |
BP |
GO:0007010 |
cytoskeleton organization |
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. |
IEA |
BP |
GO:0007517 |
muscle organ development |
The process whose specific outcome is the progression of the muscle over time, from its formation to the mature structure. The muscle is an organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work. |
NAS |
BP |
GO:0010880 |
regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
Any process that modulates the rate, frequency or extent of release of sequestered calcium ion into cytosol by the sarcoplasmic reticulum, the process in which the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol occurs via calcium release channels. |
ISS |
BP |
GO:0010881 |
regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
Any process that modulates the frequency, rate or extent of cardiac muscle contraction via the regulation of the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol. The sarcoplasmic reticulum is the endoplasmic reticulum of striated muscle, specialised for the sequestration of calcium ions that are released upon receipt of a signal relayed by the T tubules from the neuromuscular junction. |
ISS |
BP |
GO:0014809 |
regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
Any process that modulates the frequency, rate or extent of skeletal muscle contraction via the regulation of the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol. The sarcoplasmic reticulum is the endoplasmic reticulum of striated muscle, specialised for the sequestration of calcium ions that are released upon receipt of a signal relayed by the T tubules from the neuromuscular junction. |
ISS |
BP |
GO:0014819 |
regulation of skeletal muscle contraction |
Any process that modulates the frequency, rate or extent of skeletal muscle contraction. |
ISS |
BP |
GO:0016203 |
muscle attachment |
The developmental process in which a skeletal muscle attaches to its target (such as bone or body wall). |
IEA |
BP |
GO:0030049 |
muscle filament sliding |
The sliding of actin thin filaments and myosin thick filaments past each other in muscle contraction. This involves a process of interaction of myosin located on a thick filament with actin located on a thin filament. During this process ATP is split and forces are generated. |
TAS |
BP |
GO:0033137 |
negative regulation of peptidyl-serine phosphorylation |
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of peptidyl-serine. |
ISS |
BP |
GO:0034613 |
cellular protein localization |
Any process in which a protein is transported to, and/or maintained in, a specific location at the level of a cell. Localization at the cellular level encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. |
IMP |
BP |
GO:0035994 |
response to muscle stretch |
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a myofibril being extended beyond its slack length. |
ISS |
BP |
GO:0043043 |
peptide biosynthetic process |
The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide. |
IDA |
BP |
GO:0043623 |
cellular protein complex assembly |
The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell. |
ISS |
BP |
GO:0046716 |
muscle cell cellular homeostasis |
The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state. |
ISS |
BP |
GO:0048747 |
muscle fiber development |
The process whose specific outcome is the progression of the muscle fiber over time, from its formation to the mature structure. In skeletal muscle, fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast. |
ISS |
BP |
GO:0060048 |
cardiac muscle contraction |
Muscle contraction of cardiac muscle tissue. |
IMP |
BP |
GO:0060314 |
regulation of ryanodine-sensitive calcium-release channel activity |
Any process that modulates the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts. |
ISS |
BP |
GO:0086001 |
cardiac muscle cell action potential |
An action potential that occurs in a cardiac muscle cell. |
ISS |
BP |
GO:1901385 |
regulation of voltage-gated calcium channel activity |
Any process that modulates the frequency, rate or extent of voltage-gated calcium channel activity. |
ISS |
BP |
GO:1902083 |
negative regulation of peptidyl-cysteine S-nitrosylation |
Any process that stops, prevents or reduces the frequency, rate or extent of peptidyl-cysteine S-nitrosylation. |
ISS |
BP |
GO:2000651 |
positive regulation of sodium ion transmembrane transporter activity |
Any process that activates or increases the frequency, rate or extent of sodium ion transmembrane transporter activity. |
ISS |
CC |
GO:0005829 |
cytosol |
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
TAS |
CC |
GO:0005856 |
cytoskeleton |
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
IEA |
CC |
GO:0009986 |
cell surface |
The external part of the cell wall and/or plasma membrane. |
IDA |
CC |
GO:0016010 |
dystrophin-associated glycoprotein complex |
A multiprotein complex that forms a strong mechanical link between the cytoskeleton and extracellular matrix; typical of, but not confined to, muscle cells. The complex is composed of transmembrane, cytoplasmic, and extracellular proteins, including dystrophin, sarcoglycans, dystroglycan, dystrobrevins, syntrophins, sarcospan, caveolin-3, and NO synthase. |
IDA|NAS|TAS |
CC |
GO:0016013 |
syntrophin complex |
A protein complex that includes alpha-, beta1-, beta2-syntrophins and syntrophin-like proteins; the syntrophin complex binds to the second half of the carboxy-terminal domain of dystrophin; also associates with neuronal nitric oxide synthase. |
TAS |
CC |
GO:0016328 |
lateral plasma membrane |
The portion of the plasma membrane at the lateral side of the cell. In epithelial cells, lateral plasma membranes are on the sides of cells which lie at the interface of adjacent cells. |
TAS |
CC |
GO:0030018 |
Z disc |
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
ISS |
CC |
GO:0030055 |
cell-substrate junction |
A cell junction that forms a connection between a cell and the extracellular matrix. |
ISS |
CC |
GO:0030175 |
filopodium |
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft. |
IDA |
CC |
GO:0031527 |
filopodium membrane |
The portion of the plasma membrane surrounding a filopodium. |
IDA |
CC |
GO:0042383 |
sarcolemma |
The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers. |
IDA |
CC |
GO:0043034 |
costamere |
Regular periodic sub membranous arrays of vinculin in skeletal and cardiac muscle cells, these arrays link Z-discs to the sarcolemma and are associated with links to extracellular matrix. |
IDA |
CC |
GO:0043234 |
protein complex |
A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical. |
IDA |
CC |
GO:0044306 |
neuron projection terminus |
The specialized, terminal region of a neuron projection such as an axon or a dendrite. |
ISS |
CC |
GO:0045121 |
membrane raft |
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
ISS |
CC |
GO:0045202 |
synapse |
The junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell; the site of interneuronal communication. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
ISS |
CC |
GO:0045211 |
postsynaptic membrane |
A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane. |
IEA |
MF |
GO:0002162 |
dystroglycan binding |
Interacting selectively and non-covalently with dystroglycan. Dystroglycan is glycoprotein found in non-muscle tissues as well as in muscle tissues, often in association with dystrophin. The native dystroglycan cleaved into two non-covalently associated subunits, alpha (N-terminal) and beta (C-terminal). |
IPI |
MF |
GO:0003779 |
actin binding |
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments. |
IDA|TAS |
MF |
GO:0005200 |
structural constituent of cytoskeleton |
The action of a molecule that contributes to the structural integrity of a cytoskeletal structure. |
IEA |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0008270 |
zinc ion binding |
Interacting selectively and non-covalently with zinc (Zn) ions. |
IEA |
MF |
GO:0008307 |
structural constituent of muscle |
The action of a molecule that contributes to the structural integrity of a muscle fiber. |
IDA|TAS |
MF |
GO:0017022 |
myosin binding |
Interacting selectively and non-covalently with any part of a myosin complex; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments. |
IDA |
MF |
GO:0017166 |
vinculin binding |
Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane. |
IPI |
MF |
GO:0050998 |
nitric-oxide synthase binding |
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase. |
ISS |
Domain ID | Description |
---|---|
IPR000433 |
Zinc finger, ZZ-type |
IPR001202 |
WW domain |
IPR001589 |
Actinin-type actin-binding domain, conserved site |
IPR001715 |
Calponin homology domain |
IPR002017 |
Spectrin repeat |
IPR011992 |
EF-hand domain pair |
IPR015153 |
EF-hand domain, type 1 |
IPR015154 |
EF-hand domain, type 2 |
IPR016344 |
Dystrophin |
IPR018159 |
Spectrin/alpha-actinin |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa05410 |
Hypertrophic cardiomyopathy (HCM) |
KEGG |
hsa05412 |
Arrhythmogenic right ventricular cardiomyopathy (ARVC) |
KEGG |
hsa05414 |
Dilated cardiomyopathy |
KEGG |
hsa05416 |
Viral myocarditis |
KEGG |
WP2118 |
Arrhythmogenic Right Ventricular Cardiomyopathy |
WikiPathways |
WP383 |
Striated Muscle Contraction |
WikiPathways |
WP2858 |
Ectoderm Differentiation |
WikiPathways |
h_agrPathway |
Agrin in Postsynaptic Differentiation |
BioCarta |
UMLS CUI | UMLS Term |
---|---|
C0006663 |
Calcinosis |
C0007193 |
Cardiomyopathy, Dilated |
C0013264 |
Muscular Dystrophy, Duchenne |
C0018800 |
Cardiomegaly |
C0023269 |
Leiomyosarcoma |
C0026850 |
Muscular Dystrophy |
C0026851 |
Muscular Dystrophy, Animal |
C0027540 |
Necrosis |
C0027626 |
Neoplasm Invasiveness |
C0027627 |
Neoplasm Metastasis |
C0038220 |
Status Epilepticus |
C0206656 |
Rhabdomyosarcoma, Embryonal |
C0238198 |
Gastrointestinal Stromal Tumors |
C0242973 |
Ventricular Dysfunction |
C0878544 |
Cardiomyopathies |
C0917713 |
Becker Muscular Dystrophy |
Database Name |
---|
DisGeNET |
Pubmed ID | Author | Year | Title |
---|---|---|---|
21411543 |
Savaris et al. |
2011 |
Progesterone Resistance in PCOS Endometrium: A Microarray Analysis in Clomiphene Citrate-Treated and Artificial Menstrual Cycles |
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
NEDD4 |
4734 |
P46934 |
0.49 |
FASLG |
356 |
P48023 |
0.52 |
NOS1 |
4842 |
P29475 |
0.52 |
UTRN |
7402 |
P46939 |
0.52 |
ANK2 |
287 |
Q01484 |
0.56 |
APP |
351 |
P05067 |
0.56 |
ACTC1 |
70 |
P68032 |
0.62 |
CDC25A |
993 |
P30304 |
0.63 |
SGK1 |
6446 |
O00141 |
0.63 |
CTNNAL1 |
8727 |
Q9UBT7 |
0.63 |
RANBP9 |
10048 |
Q96S59 |
0.63 |
AHNAK |
79026 |
Q09666 |
0.63 |
HAUS1 |
115106 |
Q96CS2 |
0.63 |
PTRF |
284119 |
Q6NZI2 |
0.63 |
KRT8 |
3856 |
P05787 |
0.67 |
DMD |
1756 |
P11532 |
0.68 |
DISC1 |
27185 |
Q9NRI5 |
0.73 |
KRT19 |
3880 |
P08727 |
0.77 |
ACTA1 |
58 |
P68133 |
0.87 |
DAG1 |
1605 |
Q14118 |
0.90 |
SNTA1 |
6640 |
Q13424 |
0.97 |
CTNNA1 |
1495 |
P35221 |
0.49 |
DGKZ |
8525 |
Q13574 |
0.52 |
SGCZ |
137868 |
Q96LD1 |
0.52 |
EEF1G |
1937 |
P26641 |
0.63 |
MARK2 |
2011 |
Q7KZI7 |
0.63 |
HDAC1 |
3065 |
Q13547 |
0.63 |
MCM2 |
4171 |
P49736 |
0.63 |
MAP3K5 |
4217 |
Q99683 |
0.63 |
NFX1 |
4799 |
Q12986 |
0.63 |
RPL6 |
6128 |
Q02878 |
0.63 |
TERF1 |
7013 |
P54274 |
0.63 |
TERF2 |
7014 |
Q15554 |
0.63 |
XPO1 |
7514 |
O14980 |
0.63 |
GAN |
8139 |
Q9H2C0 |
0.63 |
NUP58 |
9818 |
Q9BVL2 |
0.63 |
LPAR6 |
10161 |
P43657 |
0.63 |
TRAF3IP1 |
26146 |
Q8TDR0 |
0.63 |
LARP1B |
55132 |
Q659C4 |
0.63 |
KIF15 |
56992 |
Q9NS87 |
0.63 |
PGM5 |
5239 |
Q15124 |
0.65 |
SNTG2 |
54221 |
Q9NY99 |
0.67 |
CADPS |
8618 |
Q9ULU8 |
0.70 |
CADPS2 |
93664 |
Q86UW7 |
0.70 |
ALB |
213 |
P02768 |
0.72 |
ARRB1 |
408 |
P49407 |
0.72 |
KCNJ4 |
3761 |
P48050 |
0.72 |
KCNJ12 |
3768 |
Q14500 |
0.74 |
SNTG1 |
54212 |
Q9NSN8 |
0.77 |
SNTB2 |
6645 |
Q13425 |
0.93 |
SNTB1 |
6641 |
Q13884 |
0.95 |
DTNB |
1838 |
O60941 |
0.96 |
DTNA |
1837 |
Q9Y4J8 |
0.99 |