Q13153

FUNCTION: The activated kinase acts on a variety of targets. Likely to be the GTPase effector that links the Rho-related GTPases to the JNK MAP kinase pathway. Activated by CDC42 and RAC1. Involved in dissolution of stress fibers and reorganization of focal complexes. Involved in regulation of microtubule biogenesis through phosphorylation of TBCB. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium. ENZYME REGULATION: Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-423 and allows the kinase domain to adopt an active structure. Also activated by binding to GTP-bound CDC42, independent of the phosphorylation state of Thr-423. Phosphorylation of Thr-84 by OXSR1 inhibits this activation (By similarity). Phosphorylation at Thr-423 by PDPK1 results in its activation. SUBUNIT: Homodimer in its autoinhibited state. Active as monomer. Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1. Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and GIT1. Interacts with ARHGEF7. Also interacts with CRIPAK. Interacts with NISCH (By similarity). Interacts with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1. Interacts with SCRIB. Interacts with PDPK1. Interacts (via kinase domain) with RAF1. Interaction with NCK1 and NCK2. SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Note=Recruited to focal adhesions upon activation. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q13153-1; Sequence=Displayed; Name=2; Synonyms=PAK1B; IsoId=Q13153-2; Sequence=VSP_017507; PTM: Autophosphorylated when activated by CDC42/p21 and RAC1. Phosphorylation at Thr-423 by PDPK1 results in its activation. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. SIMILARITY: Contains 1 CRIB domain. SIMILARITY: Contains 1 protein kinase domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/PAK1ID41633ch11q13.html"; GENE SYNONYMS:PAK1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 545 AA; 60647 MW; 1A95CD5F2195CD7B CRC64;

PAK1_HUMAN

urn:biopax:ModificationFeature:PAK1_HUMAN_1, urn:biopax:ModificationFeature:PAK1_HUMAN_10, urn:biopax:ModificationFeature:PAK1_HUMAN_11, urn:biopax:ModificationFeature:PAK1_HUMAN_12, urn:biopax:ModificationFeature:PAK1_HUMAN_13, urn:biopax:ModificationFeature:PAK1_HUMAN_14, urn:biopax:ModificationFeature:PAK1_HUMAN_15, urn:biopax:ModificationFeature:PAK1_HUMAN_16, urn:biopax:ModificationFeature:PAK1_HUMAN_17, urn:biopax:ModificationFeature:PAK1_HUMAN_2, urn:biopax:ModificationFeature:PAK1_HUMAN_3, urn:biopax:ModificationFeature:PAK1_HUMAN_4, urn:biopax:ModificationFeature:PAK1_HUMAN_5, urn:biopax:ModificationFeature:PAK1_HUMAN_6, urn:biopax:ModificationFeature:PAK1_HUMAN_7, urn:biopax:ModificationFeature:PAK1_HUMAN_8, urn:biopax:ModificationFeature:PAK1_HUMAN_9

MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH