{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q13177","secondaryAccessions":["Q13154","Q6ISC3"],"uniProtkbId":"PAK2_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":244,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Serine/threonine-protein kinase PAK 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21555521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"}],"value":"2.7.11.1"}]},"alternativeNames":[{"fullName":{"value":"Gamma-PAK"}},{"fullName":{"value":"PAK65"}},{"fullName":{"value":"S6/H4 kinase"}},{"fullName":{"value":"p21-activated kinase 2"},"shortNames":[{"value":"PAK-2"}]},{"fullName":{"value":"p58"}}],"contains":[{"recommendedName":{"fullName":{"value":"PAK-2p27"},"shortNames":[{"value":"p27"}]}},{"recommendedName":{"fullName":{"value":"PAK-2p34"},"shortNames":[{"value":"p34"}]},"alternativeNames":[{"fullName":{"value":"C-t-PAK2"}}]}]},"genes":[{"geneName":{"value":"PAK2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12853446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16617111"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19273597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19923322"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21555521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33693784"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7744004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9171063"}],"value":"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:12853446, PubMed:16617111, PubMed:19273597, PubMed:19923322, PubMed:33693784, PubMed:7744004, PubMed:9171063). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). 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 (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). 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 (PubMed:12853446, PubMed:16617111, PubMed:9171063). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21555521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33693784"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17990"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33693784"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21555521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889207"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15234964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21177766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21317288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21724829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889207"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q13153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9786869"}],"value":"Activated by binding small G proteins (By similarity). Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-402 and allows the kinase domain to adopt an active structure (By similarity). Following caspase cleavage, autophosphorylated PAK-2p34 is constitutively active (PubMed:9786869)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15471851"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16374509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18716323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19273597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20696164"}],"value":"Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1 (PubMed:20696164). Interacts with SH3MD4 (PubMed:16374509). Interacts with SCRIB (PubMed:18716323). Interacts with ARHGEF7 and GIT1 (PubMed:19273597). PAK-2p34 interacts with ARHGAP10 (PubMed:15471851)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11070003"}],"value":"(Microbial infection) Interacts with and activated by HIV-1 Nef"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q9NYB9-2","geneName":"ABI2","intActId":"EBI-11096309"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q15052","geneName":"ARHGEF6","intActId":"EBI-1642523"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q14155","geneName":"ARHGEF7","intActId":"EBI-717515"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P55210","geneName":"CASP7","intActId":"EBI-523958"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P60953","geneName":"CDC42","intActId":"EBI-81752"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P62993","geneName":"GRB2","intActId":"EBI-401755"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P08631","geneName":"HCK","intActId":"EBI-346340"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P53667","geneName":"LIMK1","intActId":"EBI-444403"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P16333","geneName":"NCK1","intActId":"EBI-389883"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"O43639","geneName":"NCK2","intActId":"EBI-713635"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q13177","geneName":"PAK2","intActId":"EBI-1045887"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P63000","geneName":"RAC1","intActId":"EBI-413628"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P04049","geneName":"RAF1","intActId":"EBI-365996"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q9H4E5","geneName":"RHOJ","intActId":"EBI-6285694"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q8TEJ3","geneName":"SH3RF3","intActId":"EBI-7975674"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q9BX66","geneName":"SORBS1","intActId":"EBI-433642"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"O94875","geneName":"SORBS2","intActId":"EBI-311323"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"O60504","geneName":"SORBS3","intActId":"EBI-741237"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"P12931","geneName":"SRC","intActId":"EBI-621482"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"O55043","geneName":"Arhgef7","intActId":"EBI-3649585"},"numberOfExperiments":8,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q13177","intActId":"EBI-1045887"},"interactantTwo":{"uniProtKBAccession":"Q5PP90","geneName":"US3(L)","intActId":"EBI-15780451"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR 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cytoplasmic perinuclear region (PubMed:15471851). Myristoylation changes PAK-2p34 location to the membrane (PubMed:16617111)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12853446"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15471851"}],"value":"Cytoplasm, perinuclear region","id":"SL-0198"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16617111"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16617111"}],"value":"Lipid-anchor","id":"SL-9901"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7744004"}],"value":"Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21098037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7673144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9786869"}],"value":"Full-length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated, with PAK-2p27 being phosphorylated on serine and PAK-2p34 on threonine residues, respectively. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12853446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9171063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9786869"}],"value":"During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12853446"}],"value":"Ubiquitinated, leading to its proteasomal degradation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16617111"}],"value":"PAK-2p34 is myristoylated"}],"commentType":"PTM","molecule":"PAK-2p34"},{"commentType":"DISEASE","disease":{"diseaseId":"Knobloch syndrome 2","diseaseAccession":"DI-06463","acronym":"KNO2","description":"An autosomal dominant form of Knobloch syndrome characterized by high myopia, vitreoretinal degeneration, retinal detachment, occipital encephalocele or scalp lesions, and mild to severe psychomotor delay.","diseaseCrossReference":{"database":"MIM","id":"618458"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33693784"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/41634/PAK2","ftp":false}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"20068231"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"22223895"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"22814378"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Serine/threonine-protein kinase PAK 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