Gene Symbol | ACTN2 |
Entrez ID | 88 |
Uniprot ID | P35609 |
Description | actinin, alpha 2 |
Chromosomal Location | chr1: 236,686,454-236,764,631 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0000165 |
MAPK cascade |
An intracellular protein kinase cascade containing at least a MAPK, a MAPKK and a MAP3K. The cascade can also contain two additional tiers: the upstream MAP4K and the downstream MAP Kinase-activated kinase (MAPKAPK). The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell. |
TAS |
BP |
GO:0002576 |
platelet degranulation |
The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet. |
TAS |
BP |
GO:0007155 |
cell adhesion |
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
TAS |
BP |
GO:0030035 |
microspike assembly |
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell. |
IDA |
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:0042391 |
regulation of membrane potential |
Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane. |
IMP |
BP |
GO:0042981 |
regulation of apoptotic process |
Any process that modulates the occurrence or rate of cell death by apoptotic process. |
NAS |
BP |
GO:0043267 |
negative regulation of potassium ion transport |
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
IMP |
BP |
GO:0043268 |
positive regulation of potassium ion transport |
Any process that activates or increases the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
IDA |
BP |
GO:0043547 |
positive regulation of GTPase activity |
Any process that activates or increases the activity of a GTPase. |
IEA |
BP |
GO:0045214 |
sarcomere organization |
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
IMP |
BP |
GO:0048041 |
focal adhesion assembly |
The aggregation and bonding together of a set of components to form a focal adhesion, a complex of intracellular signaling and structural proteins that provides a structural link between the internal actin cytoskeleton and the ECM, and also function as a locus of signal transduction activity. |
IMP |
BP |
GO:0051289 |
protein homotetramerization |
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits. |
IDA |
BP |
GO:0051695 |
actin filament uncapping |
The removal of capping protein from the end of actin filaments to free the ends for addition, exchange or removal of further actin subunits. |
IMP |
BP |
GO:0055013 |
cardiac muscle cell development |
The process whose specific outcome is the progression of a cardiac muscle cell over time, from its formation to the mature state. |
IEA |
BP |
GO:0086097 |
phospholipase C-activating angiotensin-activated signaling pathway |
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores. |
IMP |
BP |
GO:0090002 |
establishment of protein localization to plasma membrane |
The directed movement of a protein to a specific location in the plasma membrane. |
IMP |
BP |
GO:1901017 |
negative regulation of potassium ion transmembrane transporter activity |
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transporter activity. |
IMP |
BP |
GO:1901018 |
positive regulation of potassium ion transmembrane transporter activity |
Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transporter activity. |
IDA |
BP |
GO:1903506 |
regulation of nucleic acid-templated transcription |
Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription. |
IEA |
BP |
GO:2000009 |
negative regulation of protein localization to cell surface |
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface. |
IMP |
BP |
GO:2000273 |
positive regulation of receptor activity |
Any process that activates or increases the frequency, rate or extent of receptor activity. |
IEA |
BP |
GO:2001137 |
positive regulation of endocytic recycling |
Any process that activates or increases the frequency, rate or extent of endocytic recycling. |
IMP |
BP |
GO:2001259 |
positive regulation of cation channel activity |
Any process that activates or increases the frequency, rate or extent of cation channel activity. |
IMP |
CC |
GO:0005576 |
extracellular region |
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
TAS |
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. |
NAS |
CC |
GO:0005884 |
actin filament |
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane. |
TAS |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
IDA |
CC |
GO:0005925 |
focal adhesion |
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. |
IMP |
CC |
GO:0030018 |
Z disc |
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
IDA |
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:0030864 |
cortical actin cytoskeleton |
The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane. |
IEA |
CC |
GO:0031093 |
platelet alpha granule lumen |
The volume enclosed by the membrane of the platelet alpha granule. |
TAS |
CC |
GO:0031143 |
pseudopodium |
A temporary protrusion or retractile process of a cell, associated with flowing movements of the protoplasm, and serving for locomotion and feeding. |
TAS |
CC |
GO:0043197 |
dendritic spine |
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including thin, stubby, mushroom, and branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
TAS |
CC |
GO:0070062 |
extracellular exosome |
A membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
IDA |
MF |
GO:0005088 |
Ras guanyl-nucleotide exchange factor activity |
Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ras superfamily. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. |
TAS |
MF |
GO:0005178 |
integrin binding |
Interacting selectively and non-covalently with an integrin. |
TAS |
MF |
GO:0005509 |
calcium ion binding |
Interacting selectively and non-covalently with calcium ions (Ca2+). |
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:0005546 |
phosphatidylinositol-4,5-bisphosphate binding |
Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions. |
IDA |
MF |
GO:0008092 |
cytoskeletal protein binding |
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). |
IDA |
MF |
GO:0008307 |
structural constituent of muscle |
The action of a molecule that contributes to the structural integrity of a muscle fiber. |
TAS |
MF |
GO:0019904 |
protein domain specific binding |
Interacting selectively and non-covalently with a specific domain of a protein. |
IPI |
MF |
GO:0030274 |
LIM domain binding |
Interacting selectively and non-covalently with a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions. |
IEA |
MF |
GO:0030375 |
thyroid hormone receptor coactivator activity |
The function of a transcription cofactor that activates transcription in conjunction with a thyroid hormone-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself. |
IEA |
MF |
GO:0031432 |
titin binding |
Interacting selectively and non-covalently with titin, any of a family of giant proteins found in striated and smooth muscle. In striated muscle, single titin molecules span half the sarcomere, with their N- and C-termini in the Z-disc and M-line, respectively. |
IPI |
MF |
GO:0042802 |
identical protein binding |
Interacting selectively and non-covalently with an identical protein or proteins. |
IPI |
MF |
GO:0042803 |
protein homodimerization activity |
Interacting selectively and non-covalently with an identical protein to form a homodimer. |
IMP |
MF |
GO:0044325 |
ion channel binding |
Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient. |
IPI |
MF |
GO:0046983 |
protein dimerization activity |
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. |
IDA |
MF |
GO:0051015 |
actin filament binding |
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
IEA |
MF |
GO:0051373 |
FATZ binding |
Interacting selectively and non-covalently with a member of the FATZ family of proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components. |
IDA |
MF |
GO:0070080 |
titin Z domain binding |
Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. |
IMP|IPI |
Domain ID | Description |
---|---|
IPR001589 |
Actinin-type actin-binding domain, conserved site |
IPR001715 |
Calponin homology domain |
IPR002017 |
Spectrin repeat |
IPR002048 |
EF-hand domain |
IPR011992 |
EF-hand domain pair |
IPR014837 |
EF-hand, Ca insensitive |
IPR018159 |
Spectrin/alpha-actinin |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa05412 |
Arrhythmogenic right ventricular cardiomyopathy (ARVC) |
KEGG |
WP2118 |
Arrhythmogenic Right Ventricular Cardiomyopathy |
WikiPathways |
WP383 |
Striated Muscle Contraction |
WikiPathways |
h_cell2cellPathway |
Cell to Cell Adhesion Signaling |
BioCarta |
h_integrinPathway |
Integrin Signaling Pathway |
BioCarta |
h_ucalpainPathway |
uCalpain and friends in Cell spread |
BioCarta |
UMLS CUI | UMLS Term |
---|---|
C0878544 |
Cardiomyopathies |
C0949658 |
Cardiomyopathy, Hypertrophic, Familial |
Tissue | Cell Type |
---|---|
heart muscle |
myocytes |
skeletal muscle |
myocytes |
Pubmed ID | Author | Year | Title |
---|---|---|---|
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 |
---|---|---|---|
PKN1 |
5585 |
Q16512 |
0.49 |
TNNI1 |
7135 |
P19237 |
0.49 |
TPM1 |
7168 |
P09493 |
0.49 |
TPM2 |
7169 |
P07951 |
0.49 |
EPS8L1 |
54869 |
Q8TE68 |
0.52 |
ACTN4 |
81 |
O43707 |
0.56 |
CALM2 |
805 |
P62158 |
0.63 |
CALM3 |
808 |
P62158 |
0.63 |
CAPN1 |
823 |
P07384 |
0.63 |
MOS |
4342 |
P00540 |
0.63 |
MYBPC2 |
4606 |
Q14324 |
0.63 |
NOS3 |
4846 |
P29474 |
0.63 |
ATXN2 |
6311 |
Q99700 |
0.63 |
SNAI1 |
6615 |
O95863 |
0.63 |
SP100 |
6672 |
P23497 |
0.63 |
TUBA4A |
7277 |
P68366 |
0.63 |
ZYX |
7791 |
Q15942 |
0.63 |
TUBA1A |
7846 |
Q71U36 |
0.63 |
DYSF |
8291 |
O75923 |
0.63 |
NCOA1 |
8648 |
Q15788 |
0.63 |
ASH2L |
9070 |
Q9UBL3 |
0.63 |
RPL35 |
11224 |
P42766 |
0.63 |
ITGB3BP |
23421 |
Q13352 |
0.63 |
APPL1 |
26060 |
Q9UKG1 |
0.63 |
ZNF446 |
55663 |
Q9NWS9 |
0.63 |
AKTIP |
64400 |
Q9H8T0 |
0.63 |
MICALL2 |
79778 |
Q8IY33 |
0.63 |
BRMS1L |
84312 |
Q5PSV4 |
0.63 |
SAXO1 |
158297 |
Q8IYX7 |
0.63 |
RTP5 |
285093 |
Q14D33 |
0.63 |
TNN |
63923 |
Q9UQP3 |
0.75 |
ACTN2 |
88 |
P35609 |
0.96 |
MYH1 |
4619 |
P12882 |
0.49 |
MYH2 |
4620 |
Q9UKX2 |
0.49 |
MYH3 |
4621 |
P11055 |
0.49 |
MYH4 |
4622 |
Q9Y623 |
0.49 |
MYH6 |
4624 |
P13533 |
0.49 |
MYH7 |
4625 |
P12883 |
0.49 |
MYH8 |
4626 |
P13535 |
0.49 |
TPM3 |
7170 |
P06753 |
0.49 |
TPM4 |
7171 |
P67936 |
0.49 |
ERBB2IP |
55914 |
Q96RT1 |
0.49 |
CAMK2D |
817 |
Q13557 |
0.52 |
CAMK2G |
818 |
Q13555 |
0.52 |
UTRN |
7402 |
P46939 |
0.52 |
NCOA2 |
10499 |
Q15596 |
0.52 |
ACTA2 |
59 |
P62736 |
0.55 |
MYOZ3 |
91977 |
Q8TDC0 |
0.55 |
ACTN1 |
87 |
P12814 |
0.56 |
KCNN2 |
3781 |
Q9H2S1 |
0.56 |
PSMB5 |
5693 |
P28074 |
0.56 |
CSRP3 |
8048 |
P50461 |
0.56 |
SYNPO2 |
171024 |
Q9UMS6 |
0.56 |
CAMK2A |
815 |
Q9UQM7 |
0.59 |
LRRC7 |
57554 |
Q96NW7 |
0.59 |
SELE |
6401 |
P16581 |
0.62 |
PALLD |
23022 |
Q8WX93 |
0.62 |
AKT2 |
208 |
P31751 |
0.63 |
HSPB1 |
3315 |
P04792 |
0.63 |
PSMA3 |
5684 |
P25788 |
0.63 |
ATXN7 |
6314 |
O15265 |
0.63 |
TULP3 |
7289 |
O75386 |
0.63 |
YWHAZ |
7534 |
P63104 |
0.63 |
ST7 |
7982 |
Q9NRC1 |
0.63 |
COIL |
8161 |
P38432 |
0.63 |
NRIP1 |
8204 |
P48552 |
0.63 |
CADPS |
8618 |
Q9ULU8 |
0.63 |
KAT2B |
8850 |
Q92831 |
0.63 |
NR1I2 |
8856 |
O75469 |
0.63 |
MYOM2 |
9172 |
P54296 |
0.63 |
MED14 |
9282 |
O60244 |
0.63 |
NCOR1 |
9611 |
O75376 |
0.63 |
FEZ1 |
9638 |
Q99689 |
0.63 |
YWHAQ |
10971 |
P27348 |
0.63 |
SNW1 |
22938 |
Q13573 |
0.63 |
MAST2 |
23139 |
Q6P0Q8 |
0.63 |
SNAPIN |
23557 |
O95295 |
0.63 |
IGSF8 |
93185 |
Q969P0 |
0.63 |
PKD2 |
5311 |
Q13563 |
0.67 |
SUMO3 |
6612 |
P55854 |
0.70 |
LRP12 |
29967 |
Q9Y561 |
0.73 |
MYPN |
84665 |
Q86TC9 |
0.73 |
SSX2IP |
117178 |
Q9Y2D8 |
0.73 |
FBXL22 |
283807 |
Q6P050 |
0.73 |
RAVER1 |
125950 |
Q8IY67 |
0.75 |
ANG |
283 |
P03950 |
0.78 |
MYOZ2 |
51778 |
Q9NPC6 |
0.78 |
SUMO1 |
7341 |
P63165 |
0.79 |
KCNA4 |
3739 |
P22459 |
0.80 |
PDLIM3 |
27295 |
Q53GG5 |
0.82 |
DLG1 |
1739 |
Q12959 |
0.83 |
GRIN2B |
2904 |
Q13224 |
0.84 |
PDLIM1 |
9124 |
O00151 |
0.84 |
ADORA2A |
135 |
P29274 |
0.85 |
DLG4 |
1742 |
P78352 |
0.85 |
GRIN1 |
2902 |
Q05586 |
0.85 |
ADAM12 |
8038 |
O43184 |
0.88 |
DISC1 |
27185 |
Q9NRI5 |
0.88 |
MYOZ1 |
58529 |
Q9NP98 |
0.88 |
ACTN3 |
89 |
Q08043 |
0.90 |
KCNA5 |
3741 |
P22460 |
0.90 |
TTN |
7273 |
Q8WZ42 |
0.90 |
LDB3 |
11155 |
O75112 |
0.94 |