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IID00244
UniprotQ13177
ProteinSerine/threonine-protein kinase PAK 2
GenePAK2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
524
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 121-136 Hetero dimer : Q7DB50
 Evidence X-RAY 3pcs H Reference
       Region 3pcs H 121-121 disorder
       Region 3pcs H 122-134 order
       Region 3pcs H 135-136 disorder
 Evidence X-RAY 3pcs G Reference
       Region 3pcs G 121-122 disorder
       Region 3pcs G 123-132 order
       Region 3pcs G 133-136 disorder
 Evidence X-RAY 3pcs F Reference
       Region 3pcs F 121-121 disorder
       Region 3pcs F 122-133 order
       Region 3pcs F 134-136 disorder
 Evidence X-RAY 3pcs E Reference
       Region 3pcs E 121-121 disorder
       Region 3pcs E 122-135 order
       Region 3pcs E 136-136 disorder
Seqphosphorylation
    169-169 Phosphothreonine
    64-64 Phosphoserine
    197-197 Phosphoserine
    402-402 Phosphothreonine; by autocatalysis
    60-60 Phosphothreonine
    2-2 Phosphoserine
    20-20 Phosphoserine
    55-55 Phosphoserine
    58-58 Phosphoserine
    154-154 Phosphothreonine
    134-134 Phosphothreonine
    139-139 Phosphotyrosine
    141-141 Phosphoserine
    143-143 Phosphothreonine
    152-152 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    62-62 N6-acetyllysine
    128-128 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-79,110-132,137-224,518-524
Order 80-109,133-136,225-517
ProS 7-18,72-79,110-132,137-153,177-184,214-224,518-524
AlphaFold
Disorder 1-72,80-84,132-225,523-524
Order 73-79,85-131,226-522
Pfam Hmmer
PF00786 73-131 4.9e-31
PF00069 249-500 7.9e-99
SEG 58-70 ,162-182
Function
Function in SwissProt
Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation.