Protein Description

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

No databases found.

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