ID  Q8CIN4;
PN  PAK-2p34;
GN  Pak2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm {ECO:0000250|UniProtKB:Q13177}. Nucleus {ECO:0000250|UniProtKB:Q13177}. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000250|UniProtKB:Q13177}. [PAK-2p34]: Nucleus {ECO:0000250|UniProtKB:Q13177}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13177}. Membrane {ECO:0000250|UniProtKB:Q13177}; Lipid-anchor {ECO:0000250|UniProtKB:Q13177}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane. {ECO:0000250|UniProtKB:Q13177}.
DR  UNIPROT: Q8CIN4;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: 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 (PubMed:11278362). Acts as downstream effector of the small GTPases CDC42 and RAC1 (By similarity). 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 (By similarity). Full-length PAK2 stimulates cell survival and cell growth (By similarity). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (By similarity). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (By similarity). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:11278362). Phosphorylates CASP7, thereby preventing its activity (By similarity). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (By similarity). 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 (By similarity). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity). {ECO:0000250|UniProtKB:Q13177, ECO:0000269|PubMed:11278362}.
DE  Reference Proteome: Yes;
DE  Interaction: P28867; IntAct: EBI-16006728; Score: 0.35
DE  Interaction: Q96B97; IntAct: EBI-6953756; Score: 0.40
DE  Interaction: Q01112; IntAct: EBI-1559309; Score: 0.40
DE  Interaction: P42858; IntAct: EBI-5327215; Score: 0.40
DE  Interaction: P42859; IntAct: EBI-5327412; Score: 0.40
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-16881295; Score: 0.37
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0030141;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0031267;
GO  GO:0034333;
GO  GO:0006915;
GO  GO:0070830;
GO  GO:0003300;
GO  GO:0071407;
GO  GO:0071560;
GO  GO:0060996;
GO  GO:0035556;
GO  GO:0043066;
GO  GO:2001271;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:2001238;
GO  GO:0050731;
GO  GO:0046777;
GO  GO:0150105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0051493;
GO  GO:0043408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13177};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSGTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNTK
SQ  GSETSAVVTEEDDDDEDAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSNVDSGAKSSDKQKKKAKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSNR
//