G5EGQ3

SS
Gene name
max-2 (Y38F1A.10)
Protein name
Serine/threonine-protein kinase max-2
Names
EC 2.7.11.1 , Motor axon guidance protein 2 , p21-activated kinase
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_Y38F1A.10
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

The p21-activated protein kinases5 (PAK5) belongs to group II PAK family and is involved in actin cytoskeleton regulation, cell growth, migration and survival, and so on. Group II PAKs (PAK4, 5, and 6) harbor well-conserved pseudosubstrate sequences. For PAK4, the N-terminal inhibitory segment contains two pseudopeptide sequences (FTGLPR at 32th and RPKPLV at 49th) that bind to the active site of the kinase domain as a pseudosubstrate. Like PAK4, PAK6 catalytic activity is inhibited by a peptide corresponding to its N-terminal pseudosubstrate (RRPKPVVDP at 49th). <br> PAKs are activated by the binding of GTP-loaded Cdc42 (or Rac) to the CRIB domain, which disrupts the dimer and unfolds autoinhibitory region. After releasing autoinhibitory region, kinase domain is then autophosphorylated for full activation.

Autoinhibitory domains (AIDs)

50-56 (Inhibitory segment) SS

Target domain

376-627 (Protein kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

513-535 (Activation loop from InterPro)

Target domain

376-627 (Protein kinase domain)

Relief mechanism

Assay

513-535 (Activation loop from InterPro)

Target domain

376-627 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for G5EGQ3

Entry ID Method Resolution Chain Position Source
AF-G5EGQ3-F1 Predicted AlphaFoldDB

No variants for G5EGQ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for G5EGQ3

No associated diseases with G5EGQ3

4 regional properties for G5EGQ3

Type Name Position InterPro Accession
domain CRIB domain 40 - 94 IPR000095
domain Protein kinase domain 376 - 627 IPR000719
active_site Serine/threonine-protein kinase, active site 492 - 504 IPR008271
binding_site Protein kinase, ATP binding site 382 - 410 IPR017441

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Perikaryon
  • Cell projection, dendrite
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
perikaryon The portion of the cell soma (neuronal cell body) that excludes the nucleus.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
mitogen-activated protein kinase kinase kinase binding Binding to a mitogen-activated protein kinase kinase kinase, a protein that can phosphorylate a MAP kinase kinase.
protein serine kinase activity Catalysis of the reactions
protein serine/threonine kinase activity Catalysis of the reactions
small GTPase binding Binding to a small monomeric GTPase.

12 GO annotations of biological process

Name Definition
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues.
gonad morphogenesis The process in which the anatomical structures of the gonads are generated and organized. A gonad is an animal organ producing gametes, e.g. the testes or the ovary in mammals.
gonadal mesoderm development The process whose specific outcome is the progression of the gonadal mesoderm over time, from its formation to the mature structure. The gonadal mesoderm is the middle layer of the three primary germ layers of the embryo which will go on to form the gonads of the organism.
inductive cell migration Migration of a cell in a multicellular organism that, having changed its location, is required to induce normal properties in one or more cells at its new location. An example of this would be the distal tip cells of Caenorhabditis elegans.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
JNK cascade An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier
motor neuron axon guidance The process in which the migration of an axon growth cone of a motor neuron is directed to a specific target site in response to a combination of attractive and repulsive cues.
netrin-activated signaling pathway The series of molecular signals initiated by the binding of a netrin protein to its receptor on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
regulation of axonogenesis Any process that modulates the frequency, rate or extent of axonogenesis, the generation of an axon, the long process of a neuron.
regulation of MAPK cascade Any process that modulates the frequency, rate or extent of signal transduction mediated by the MAP kinase (MAPK) cascade.
response to copper ion 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 copper ion stimulus.

22 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12469 SKM1 Serine/threonine-protein kinase SKM1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q08E52 PAK1 Serine/threonine-protein kinase PAK 1 Bos taurus (Bovine) SS
Q7YQL4 PAK3 Serine/threonine-protein kinase PAK 3 Pan troglodytes (Chimpanzee) SS
Q9VXE5 mbt Serine/threonine-protein kinase PAK mbt Drosophila melanogaster (Fruit fly) PR
Q9P286 PAK5 Serine/threonine-protein kinase PAK 5 Homo sapiens (Human) EV
Q9NQU5 PAK6 Serine/threonine-protein kinase PAK 6 Homo sapiens (Human) EV
O96013 PAK4 Serine/threonine-protein kinase PAK 4 Homo sapiens (Human) EV
Q13153 PAK1 Serine/threonine-protein kinase PAK 1 Homo sapiens (Human) EV
O75914 PAK3 Serine/threonine-protein kinase PAK 3 Homo sapiens (Human) SS
Q13177 PAK2 Serine/threonine-protein kinase PAK 2 Homo sapiens (Human) EV
Q8C015 Pak5 Serine/threonine-protein kinase PAK 5 Mus musculus (Mouse) SS
Q3ULB5 Pak6 Serine/threonine-protein kinase PAK 6 Mus musculus (Mouse) PR
Q61036 Pak3 Serine/threonine-protein kinase PAK 3 Mus musculus (Mouse) SS
Q8CIN4 Pak2 Serine/threonine-protein kinase PAK 2 Mus musculus (Mouse) SS
O88643 Pak1 Serine/threonine-protein kinase PAK 1 Mus musculus (Mouse) SS
D4A280 Pak5 Serine/threonine-protein kinase PAK 5 Rattus norvegicus (Rat) SS
Q64303 Pak2 Serine/threonine-protein kinase PAK 2 Rattus norvegicus (Rat) SS
P35465 Pak1 Serine/threonine-protein kinase PAK 1 Rattus norvegicus (Rat) SS
Q62829 Pak3 Serine/threonine-protein kinase PAK 3 Rattus norvegicus (Rat) SS
Q17850 pak-1 Serine/threonine-protein kinase pak-1 Caenorhabditis elegans PR
G5EFU0 pak-2 Serine/threonine-protein kinase pak-2 Caenorhabditis elegans PR
Q9NB31 cst-1 Serine/threonine-protein kinase cst-1 Caenorhabditis elegans PR
10 20 30 40 50 60
MSTSKSSKVR IRNFIGRIFS PSDKDKDRDD EMKPSSSAMD ISQPYNTVHR VHVGYDGQKF
70 80 90 100 110 120
SGLPQPWMDI LLRDISLADQ KKDPNAVVTA LKFYAQSMKE NEKTKFMTTN SVFTNSDDDD
130 140 150 160 170 180
VDVQLTGQVT EHLRNLQCSN GSATSPSTSV SASSSSARPL TNGNNHLSTA SSTDTSLSLS
190 200 210 220 230 240
ERNNVPSPAP VPYSESAPQL KTFTGETPKL HPRSPFPPQP PVLPQRSKTA SAVATTTTNP
250 260 270 280 290 300
TTSNGAPPPV PGSKGPPVPP KPSHLKIASS TVSSGCSSPQ QYSSARSVGN SLSNGSVVST
310 320 330 340 350 360
TSSDGDVQLS NKENSNDKSV GDKNGNTTTN KTTVEPPPPE EPPVRVRASH REKLSDSEVL
370 380 390 400 410 420
NQLREIVNPS NPLGKYEMKK QIGVGASGTV FVANVAGSTD VVAVKRMAFK TQPKKEMLLT
430 440 450 460 470 480
EIKVMKQYRH PNLVNYIESY LVDADDLWVV MDYLEGGNLT DVVVKTELDE GQIAAVLQEC
490 500 510 520 530 540
LKALHFLHRH SIVHRDIKSD NVLLGMNGEV KLTDMGFCAQ IQPGSKRDTV VGTPYWMSPE
550 560 570 580 590 600
ILNKKQYNYK VDIWSLGIMA LEMIDGEPPY LRETPLKAIY LIAQNGKPEI KQRDRLSSEF
610 620 630 640
NNFLDKCLVV DPDQRADTTE LLAHPFLKKA KPLSSLIPYI RAVREK