Q29502

SS
Gene name
PAK2
Protein name
Serine/threonine-protein kinase PAK 2
Names
Gamma-PAK, p21-activated kinase 2, PAK-2, p21-activated protein kinase I, PAKI
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100009535
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

The p21-activated kinases (PAKs) controls cytoskeletal actin assembly and activate MAP-kinase pathways. In a study with PAK1, the kinase domain in the C terminus of PAK1 is inhibited by the IS domain via the C lobe, in which the kinase inhibitory segment hinders a part of the kinase domain and stabilizes a disabled catalytic site.

Autoinhibitory domains (AIDs)

69-146 (IS domain) SS

Target domain

249-500 (Protein kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

385-408 (Activation loop from InterPro)

Target domain

229-524 (Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q29502

Entry ID Method Resolution Chain Position Source
AF-Q29502-F1 Predicted AlphaFoldDB

No variants for Q29502

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q29502

No associated diseases with Q29502

5 regional properties for Q29502

Type Name Position InterPro Accession
domain Pancreatic trypsin inhibitor Kunitz domain 33 - 87 IPR002223-1
domain Pancreatic trypsin inhibitor Kunitz domain 94 - 147 IPR002223-2
domain Pancreatic trypsin inhibitor Kunitz domain 154 - 207 IPR002223-3
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 64 - 82 IPR020901-1
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 184 - 202 IPR020901-2

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • [Serine/threonine-protein kinase PAK 2]: Cytoplasm
  • Nucleus
  • MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cell-cell junction A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.

8 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
identical protein binding Binding to an identical protein or proteins.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine/threonine/tyrosine kinase activity Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
protein tyrosine kinase activator activity Increases the activity of a protein tyrosine kinase, an enzyme which phosphorylates a tyrosyl phenolic group on a protein.
small GTPase binding Binding to a small monomeric GTPase.

12 GO annotations of biological process

Name Definition
adherens junction assembly The aggregation, arrangement and bonding together of a set of components to form an adherens junction. An adherens junction is a cell-cell junction composed of the epithelial cadherin-catenin complex at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
bicellular tight junction assembly The aggregation, arrangement and bonding together of a set of components to form a tight junction, an occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet.
cellular response to organic cyclic compound Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organic cyclic compound stimulus.
dendritic spine development The process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure. A dendritic spine is a protrusion from a dendrite and a specialized subcellular compartment involved in synaptic transmission.
execution phase of apoptosis A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Any process that stops, prevents or reduces the frequency, rate or extent of cysteine-type endopeptidase activity involved in execution phase of apoptosis.
negative regulation of stress fiber assembly Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of extrinsic apoptotic signaling pathway Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
protein localization to cell-cell junction A process in which a protein is transported to, or maintained, in a location within a cell-cell junction.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR NKIISIFSGT
70 80 90 100 110 120
EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP
130 140 150 160 170 180
QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGAPALNTK VSETSAVVTE EDDDDEEAAP
190 200 210 220 230 240
PVIAPRPDHT KSIYTRSVID PIPAPVGDSH VDSGAKSSDK QKKKTKMTDE EIMEKLRTIV
250 260 270 280 290 300
SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE
310 320 330 340 350 360
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH
370 380 390 400 410 420
ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY
430 440 450 460 470 480
GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC
490 500 510 520
LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLIMAAKEAM KSNR