ID PAK2_HUMAN Reviewed; 524 AA. AC Q13177; Q13154; Q6ISC3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 3. DT 27-MAR-2024, entry version 234. DE RecName: Full=Serine/threonine-protein kinase PAK 2; DE EC=2.7.11.1 {ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:21724829}; DE AltName: Full=Gamma-PAK; DE AltName: Full=PAK65; DE AltName: Full=S6/H4 kinase; DE AltName: Full=p21-activated kinase 2; DE Short=PAK-2; DE AltName: Full=p58; DE Contains: DE RecName: Full=PAK-2p27; DE Short=p27; DE Contains: DE RecName: Full=PAK-2p34; DE Short=p34; DE AltName: Full=C-t-PAK2; GN Name=PAK2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Sells M., Knause U.J., Bagrodia S., Ambrose D., Bokoch G.M., Chernoff J.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-524, PROTEIN SEQUENCE OF 401-417, RP FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=7744004; DOI=10.1002/j.1460-2075.1995.tb07189.x; RA Martin G.A., Bollag G., McCormick F., Abo A.; RT "A novel serine kinase activated by rac1/CDC42Hs-dependent RT autophosphorylation is related to PAK65 and STE20."; RL EMBO J. 14:1970-1978(1995). RN [4] RP ERRATUM OF PUBMED:7744004. RX PubMed=7556080; DOI=10.1002/j.1460-2075.1995.tb00113.x; RA Martin G.A., Bollag G., McCormick F., Abo A.; RL EMBO J. 14:4385-4385(1995). RN [5] RP AUTOPHOSPHORYLATION. RX PubMed=7673144; DOI=10.1074/jbc.270.36.21121; RA Benner G.E., Dennis P.B., Masaracchia R.A.; RT "Activation of an S6/H4 kinase (PAK 65) from human placenta by RT intramolecular and intermolecular autophosphorylation."; RL J. Biol. Chem. 270:21121-21128(1995). RN [6] RP PROTEOLYTIC CLEAVAGE AT ASP-212 BY CASPASE-3, FUNCTION, AND MUTAGENESIS OF RP ASP-212. RX PubMed=9171063; DOI=10.1126/science.276.5318.1571; RA Rudel T., Bokoch G.M.; RT "Membrane and morphological changes in apoptotic cells regulated by RT caspase-mediated activation of PAK2."; RL Science 276:1571-1574(1997). RN [7] RP PROTEOLYTIC CLEAVAGE AT ASP-212 BY CASPASE-3, AUTOPHOSPHORYLATION, RP PHOSPHORYLATION AT THR-402, AND MUTAGENESIS OF LYS-278 AND THR-402. RX PubMed=9786869; DOI=10.1074/jbc.273.44.28733; RA Walter B.N., Huang Z., Jakobi R., Tuazon P.T., Alnemri E.S., Litwack G., RA Traugh J.A.; RT "Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 RT (caspase 3). Effects of autophosphorylation on activity."; RL J. Biol. Chem. 273:28733-28739(1998). RN [8] RP INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION). RX PubMed=11070003; DOI=10.1128/jvi.74.23.11081-11087.2000; RA Arora V.K., Molina R.P., Foster J.L., Blakemore J.L., Chernoff J., RA Fredericksen B.L., Garcia J.V.; RT "Lentivirus Nef specifically activates Pak2."; RL J. Virol. 74:11081-11087(2000). RN [9] RP FUNCTION (PAK-2P34), UBIQUITINATION, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF 239-ILE--GLY-243 AND 246-LYS--LYS-248. RX PubMed=12853446; DOI=10.1074/jbc.m306494200; RA Jakobi R., McCarthy C.C., Koeppel M.A., Stringer D.K.; RT "Caspase-activated PAK-2 is regulated by subcellular targeting and RT proteasomal degradation."; RL J. Biol. Chem. 278:38675-38685(2003). RN [10] RP FUNCTION IN PHOSPHORYLATION OF MKNK1, AND CATALYTIC ACTIVITY. RX PubMed=15234964; DOI=10.1074/jbc.m407337200; RA Orton K.C., Ling J., Waskiewicz A.J., Cooper J.A., Merrick W.C., RA Korneeva N.L., Rhoads R.E., Sonenberg N., Traugh J.A.; RT "Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits RT phosphorylation and interaction of eIF4G with Mnk."; RL J. Biol. Chem. 279:38649-38657(2004). RN [11] RP INTERACTION WITH ARHGAP10, AND SUBCELLULAR LOCATION. RX PubMed=15471851; DOI=10.1074/jbc.m410530200; RA Koeppel M.A., McCarthy C.C., Moertl E., Jakobi R.; RT "Identification and characterization of PS-GAP as a novel regulator of RT caspase-activated PAK-2."; RL J. Biol. Chem. 279:53653-53664(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP INTERACTION WITH SH3MD4. RX PubMed=16374509; DOI=10.1038/sj.embor.7400596; RA Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M., RA Renkema G.H., Liss M., Wagner R., Saksela K.; RT "Identification of preferred protein interactions by phage-display of the RT human Src homology-3 proteome."; RL EMBO Rep. 7:186-191(2006). RN [14] RP FUNCTION (PAK-2P34), MYRISTOYLATION AT GLY-213 (PAK-2P34), SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF GLY-213. RX PubMed=16617111; DOI=10.1073/pnas.0600824103; RA Vilas G.L., Corvi M.M., Plummer G.J., Seime A.M., Lambkin G.R., RA Berthiaume L.G.; RT "Posttranslational myristoylation of caspase-activated p21-activated RT protein kinase 2 (PAK2) potentiates late apoptotic events."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6542-6547(2006). RN [15] RP INTERACTION WITH SCRIB. RX PubMed=18716323; DOI=10.1093/hmg/ddn248; RA Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S., RA Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S., RA Borg J.-P., Santoni M.-J.; RT "Scrib regulates PAK activity during the cell migration process."; RL Hum. Mol. Genet. 17:3552-3565(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-141 AND THR-169, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP FUNCTION, AND INTERACTION WITH ARHGEF7 AND GIT1. RX PubMed=19273597; DOI=10.1128/mcb.01713-08; RA Mitsushima M., Toyoshima F., Nishida E.; RT "Dual role of Cdc42 in spindle orientation control of adherent cells."; RL Mol. Cell. Biol. 29:2816-2827(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-197, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP INTERACTION WITH RAC1. RX PubMed=20696164; DOI=10.1016/j.febslet.2010.07.060; RA Kaerkkaeinen S., van der Linden M., Renkema G.H.; RT "POSH2 is a RING finger E3 ligase with Rac1 binding activity through a RT partial CRIB domain."; RL FEBS Lett. 584:3867-3872(2010). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19923322; DOI=10.1091/mbc.e09-03-0232; RA Hsu R.M., Tsai M.H., Hsieh Y.J., Lyu P.C., Yu J.S.; RT "Identification of MYO18A as a novel interacting partner of the RT PAK2/betaPIX/GIT1 complex and its potential function in modulating RT epithelial cell migration."; RL Mol. Biol. Cell 21:287-301(2010). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2 AND SER-141, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP AUTOPHOSPHORYLATION. RX PubMed=21098037; DOI=10.1074/jbc.m110.156505; RA Wang J., Wu J.W., Wang Z.X.; RT "Mechanistic studies of the autoactivation of PAK2: a two-step model of cis RT initiation followed by trans amplification."; RL J. Biol. Chem. 286:2689-2695(2011). RN [26] RP FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6, AND CATALYTIC ACTIVITY. RX PubMed=21317288; DOI=10.1074/jbc.m110.181743; RA De la Mota-Peynado A., Chernoff J., Beeser A.; RT "Identification of the atypical MAPK Erk3 as a novel substrate for p21- RT activated kinase (Pak) activity."; RL J. Biol. Chem. 286:13603-13611(2011). RN [27] RP FUNCTION IN PHOSPHORYLATION OF CASP7, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=21555521; DOI=10.1074/jbc.m111.236596; RA Li X., Wen W., Liu K., Zhu F., Malakhova M., Peng C., Li T., Kim H.G., RA Ma W., Cho Y.Y., Bode A.M., Dong Z., Dong Z.; RT "Phosphorylation of caspase-7 by p21-activated protein kinase (PAK) 2 RT inhibits chemotherapeutic drug-induced apoptosis of breast cancer cell RT lines."; RL J. Biol. Chem. 286:22291-22299(2011). RN [28] RP FUNCTION IN PHOSPHORYLATION OF JUN, AND CATALYTIC ACTIVITY. RX PubMed=21177766; DOI=10.1093/carcin/bgq271; RA Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C., Ma W., RA Shi G., Dong Z., Bode A.M., Dong Z.; RT "P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 RT threonine sites promotes cell transformation."; RL Carcinogenesis 32:659-666(2011). RN [29] RP FUNCTION IN PHOSPHORYLATION OF HISTONE H4, AND CATALYTIC ACTIVITY. RX PubMed=21724829; DOI=10.1101/gad.2055511; RA Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z.; RT "Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly."; RL Genes Dev. 25:1359-1364(2011). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2; SER-141 AND THR-169, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-20; SER-55; SER-58; RP THR-60; SER-64; THR-134; SER-141; THR-143; THR-154; THR-169 AND SER-197, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139 AND SER-141, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [35] RP FUNCTION IN PHOSPHORYLATION OF CASP7, AND CATALYTIC ACTIVITY. RX PubMed=27889207; DOI=10.1016/j.str.2016.11.001; RA Eron S.J., Raghupathi K., Hardy J.A.; RT "Dual site phosphorylation of caspase-7 by PAK2 blocks apoptotic activity RT by two distinct mechanisms."; RL Structure 25:27-39(2017). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 121-136. RX PubMed=21170023; DOI=10.1038/nature09593; RA Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C., RA Bresson S.M., Tomchick D.R., Alto N.M.; RT "The assembly of a GTPase-kinase signalling complex by a bacterial RT catalytic scaffold."; RL Nature 469:107-111(2011). RN [37] RP INVOLVEMENT IN KNO2, VARIANT KNO2 LYS-435, CHARACTERIZATION OF VARIANT KNO2 RP LYS-435, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=33693784; DOI=10.1093/hmg/ddab026; RA Antonarakis S.E., Holoubek A., Rapti M., Rademaker J., Meylan J., RA Iwaszkiewicz J., Zoete V., Wilson C., Taylor J., Ansar M., Borel C., RA Menzel O., Kuzelova K., Santoni F.A.; RT "Dominant monoallelic variant in the PAK2 gene causes Knobloch syndrome RT type 2."; RL Hum. Mol. Genet. 31:1-9(2021). CC -!- FUNCTION: Serine/threonine protein kinase that plays a role in a CC variety of different signaling pathways including cytoskeleton CC regulation, cell motility, cell cycle progression, apoptosis or CC proliferation (PubMed:7744004, PubMed:19273597, PubMed:19923322, CC PubMed:9171063, PubMed:12853446, PubMed:16617111, PubMed:33693784). CC Acts as a downstream effector of the small GTPases CDC42 and RAC1 CC (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 CC results in a conformational change and a subsequent autophosphorylation CC on several serine and/or threonine residues (PubMed:7744004). Full- CC length PAK2 stimulates cell survival and cell growth (PubMed:7744004). CC Phosphorylates MAPK4 and MAPK6 and activates the downstream target CC MAPKAPK5, a regulator of F-actin polymerization and cell migration CC (PubMed:21317288). Phosphorylates JUN and plays an important role in CC EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many CC other substrates including histone H4 to promote assembly of H3.3 and CC H4 into nucleosomes, BAD, ribosomal protein S6, or MBP CC (PubMed:21724829). Phosphorylates CASP7, thereby preventing its CC activity (PubMed:21555521, PubMed:27889207). Additionally, associates CC with ARHGEF7 and GIT1 to perform kinase-independent functions such as CC spindle orientation control during mitosis (PubMed:19273597, CC PubMed:19923322). On the other hand, apoptotic stimuli such as DNA CC damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, CC an active p34 fragment that translocates to the nucleus and promotes CC cellular apoptosis involving the JNK signaling pathway (PubMed:9171063, CC PubMed:12853446, PubMed:16617111). Caspase-activated PAK2 CC phosphorylates MKNK1 and reduces cellular translation CC (PubMed:15234964). {ECO:0000269|PubMed:12853446, CC ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, CC ECO:0000269|PubMed:19273597, ECO:0000269|PubMed:19923322, CC ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, CC ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:21724829, CC ECO:0000269|PubMed:27889207, ECO:0000269|PubMed:33693784, CC ECO:0000269|PubMed:7744004, ECO:0000269|PubMed:9171063}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:21177766, CC ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21555521, CC ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:27889207, CC ECO:0000269|PubMed:33693784}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:21177766, CC ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829, CC ECO:0000269|PubMed:27889207, ECO:0000269|PubMed:33693784}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15234964, CC ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, CC ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:21724829, CC ECO:0000269|PubMed:27889207}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:21177766, CC ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829, CC ECO:0000269|PubMed:27889207}; CC -!- ACTIVITY REGULATION: Activated by binding small G proteins (By CC similarity). Binding of GTP-bound CDC42 or RAC1 to the autoregulatory CC region releases monomers from the autoinhibited dimer, enables CC phosphorylation of Thr-402 and allows the kinase domain to adopt an CC active structure (By similarity). Following caspase cleavage, CC autophosphorylated PAK-2p34 is constitutively active (PubMed:9786869). CC {ECO:0000250|UniProtKB:Q13153, ECO:0000269|PubMed:9786869}. CC -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 CC and RAC1 (PubMed:20696164). Interacts with SH3MD4 (PubMed:16374509). CC Interacts with SCRIB (PubMed:18716323). Interacts with ARHGEF7 and GIT1 CC (PubMed:19273597). PAK-2p34 interacts with ARHGAP10 (PubMed:15471851). CC {ECO:0000269|PubMed:15471851, ECO:0000269|PubMed:16374509, CC ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19273597, CC ECO:0000269|PubMed:20696164}. CC -!- SUBUNIT: (Microbial infection) Interacts with and activated by HIV-1 CC Nef. {ECO:0000269|PubMed:11070003}. CC -!- INTERACTION: CC Q13177; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-1045887, EBI-11096309; CC Q13177; Q15052: ARHGEF6; NbExp=5; IntAct=EBI-1045887, EBI-1642523; CC Q13177; Q14155: ARHGEF7; NbExp=4; IntAct=EBI-1045887, EBI-717515; CC Q13177; P55210: CASP7; NbExp=6; IntAct=EBI-1045887, EBI-523958; CC Q13177; P60953: CDC42; NbExp=8; IntAct=EBI-1045887, EBI-81752; CC Q13177; P62993: GRB2; NbExp=2; IntAct=EBI-1045887, EBI-401755; CC Q13177; P08631: HCK; NbExp=2; IntAct=EBI-1045887, EBI-346340; CC Q13177; P42858: HTT; NbExp=2; IntAct=EBI-1045887, EBI-466029; CC Q13177; P53667: LIMK1; NbExp=2; IntAct=EBI-1045887, EBI-444403; CC Q13177; P16333: NCK1; NbExp=5; IntAct=EBI-1045887, EBI-389883; CC Q13177; O43639: NCK2; NbExp=8; IntAct=EBI-1045887, EBI-713635; CC Q13177; Q13177: PAK2; NbExp=3; IntAct=EBI-1045887, EBI-1045887; CC Q13177; P63000: RAC1; NbExp=5; IntAct=EBI-1045887, EBI-413628; CC Q13177; P04049: RAF1; NbExp=2; IntAct=EBI-1045887, EBI-365996; CC Q13177; Q9H4E5: RHOJ; NbExp=6; IntAct=EBI-1045887, EBI-6285694; CC Q13177; Q8TEJ3: SH3RF3; NbExp=2; IntAct=EBI-1045887, EBI-7975674; CC Q13177; Q9BX66: SORBS1; NbExp=2; IntAct=EBI-1045887, EBI-433642; CC Q13177; O94875: SORBS2; NbExp=2; IntAct=EBI-1045887, EBI-311323; CC Q13177; O60504: SORBS3; NbExp=6; IntAct=EBI-1045887, EBI-741237; CC Q13177; P12931: SRC; NbExp=2; IntAct=EBI-1045887, EBI-621482; CC Q13177; O55043: Arhgef7; Xeno; NbExp=8; IntAct=EBI-1045887, EBI-3649585; CC Q13177; Q5PP90: US3(L); Xeno; NbExp=2; IntAct=EBI-1045887, EBI-15780451; CC -!- SUBCELLULAR LOCATION: [Serine/threonine-protein kinase PAK 2]: CC Cytoplasm {ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21555521}. CC Nucleus {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:21555521}. CC Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 CC complex to the inner surface of the cell membrane. CC {ECO:0000269|PubMed:19923322}. CC -!- SUBCELLULAR LOCATION: [PAK-2p34]: Nucleus CC {ECO:0000269|PubMed:12853446}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:15471851}. Membrane {ECO:0000269|PubMed:16617111}; CC Lipid-anchor {ECO:0000269|PubMed:16617111}. Note=Interaction with CC ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear CC region (PubMed:15471851). Myristoylation changes PAK-2p34 location to CC the membrane (PubMed:16617111). {ECO:0000269|PubMed:15471851, CC ECO:0000269|PubMed:16617111}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels seen in CC skeletal muscle, ovary, thymus and spleen. CC {ECO:0000269|PubMed:7744004}. CC -!- PTM: Full-length PAK2 is autophosphorylated when activated by CC CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, CC become highly autophosphorylated, with PAK-2p27 being phosphorylated on CC serine and PAK-2p34 on threonine residues, respectively. CC Autophosphorylation of PAK-2p27 can occur in the absence of any CC effectors and is dependent on phosphorylation of Thr-402, because PAK- CC 2p27 is acting as an exogenous substrate. {ECO:0000269|PubMed:21098037, CC ECO:0000269|PubMed:7673144, ECO:0000269|PubMed:9786869}. CC -!- PTM: During apoptosis proteolytically cleaved by caspase-3 or caspase- CC 3-like proteases to yield active PAK-2p34. CC {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:9171063, CC ECO:0000269|PubMed:9786869}. CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation. CC {ECO:0000269|PubMed:12853446}. CC -!- PTM: [PAK-2p34]: PAK-2p34 is myristoylated. CC {ECO:0000269|PubMed:16617111}. CC -!- DISEASE: Knobloch syndrome 2 (KNO2) [MIM:618458]: An autosomal dominant CC form of Knobloch syndrome characterized by high myopia, vitreoretinal CC degeneration, retinal detachment, occipital encephalocele or scalp CC lesions, and mild to severe psychomotor delay. CC {ECO:0000269|PubMed:33693784}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41634/PAK2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U24153; AAA65442.1; -; mRNA. DR EMBL; BC069613; AAH69613.1; -; mRNA. DR EMBL; U25975; AAA75468.1; -; mRNA. DR CCDS; CCDS3321.1; -. DR PIR; S58682; S58682. DR RefSeq; NP_002568.2; NM_002577.4. DR RefSeq; XP_011511172.1; XM_011512870.2. DR RefSeq; XP_016861990.1; XM_017006501.1. DR PDB; 3PCS; X-ray; 2.86 A; E/F/G/H=121-136. DR PDBsum; 3PCS; -. DR AlphaFoldDB; Q13177; -. DR SMR; Q13177; -. DR BioGRID; 111098; 204. DR DIP; DIP-38249N; -. DR ELM; Q13177; -. DR IntAct; Q13177; 75. DR MINT; Q13177; -. DR STRING; 9606.ENSP00000314067; -. DR BindingDB; Q13177; -. DR ChEMBL; CHEMBL4487; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q13177; -. DR GuidetoPHARMACOLOGY; 2134; -. DR GlyCosmos; Q13177; 2 sites, 1 glycan. DR GlyGen; Q13177; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q13177; -. DR MetOSite; Q13177; -. DR PhosphoSitePlus; Q13177; -. DR SwissPalm; Q13177; -. DR BioMuta; PAK2; -. DR DMDM; 143811432; -. DR OGP; Q13177; -. DR CPTAC; CPTAC-1628; -. DR CPTAC; CPTAC-1726; -. DR EPD; Q13177; -. DR jPOST; Q13177; -. DR MassIVE; Q13177; -. DR MaxQB; Q13177; -. DR PaxDb; 9606-ENSP00000314067; -. DR PeptideAtlas; Q13177; -. DR ProteomicsDB; 59208; -. DR Pumba; Q13177; -. DR Antibodypedia; 3583; 964 antibodies from 43 providers. DR DNASU; 5062; -. DR Ensembl; ENST00000327134.7; ENSP00000314067.3; ENSG00000180370.10. DR GeneID; 5062; -. DR KEGG; hsa:5062; -. DR MANE-Select; ENST00000327134.7; ENSP00000314067.3; NM_002577.4; NP_002568.2. DR UCSC; uc003fwy.4; human. DR AGR; HGNC:8591; -. DR CTD; 5062; -. DR DisGeNET; 5062; -. DR GeneCards; PAK2; -. DR HGNC; HGNC:8591; PAK2. DR HPA; ENSG00000180370; Low tissue specificity. DR MalaCards; PAK2; -. DR MIM; 605022; gene. DR MIM; 618458; phenotype. DR neXtProt; NX_Q13177; -. DR OpenTargets; ENSG00000180370; -. DR Orphanet; 1571; Knobloch syndrome. DR PharmGKB; PA32918; -. DR VEuPathDB; HostDB:ENSG00000180370; -. DR eggNOG; KOG0578; Eukaryota. DR GeneTree; ENSGT00950000182988; -. DR HOGENOM; CLU_000288_26_6_1; -. DR InParanoid; Q13177; -. DR OMA; MDFPPLR; -. DR OrthoDB; 460351at2759; -. DR PhylomeDB; Q13177; -. DR TreeFam; TF105351; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; Q13177; -. DR Reactome; R-HSA-164944; Nef and signal transduction. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-211728; Regulation of PAK-2p34 activity by PS-GAP/RHG10. DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; R-HSA-211736; Stimulation of the cell death response by PAK-2p34. DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway. DR Reactome; R-HSA-3928664; Ephrin signaling. DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion. DR Reactome; R-HSA-428540; Activation of RAC1. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013407; RHOH GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9013420; RHOU GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9013424; RHOV GTPase cycle. DR SignaLink; Q13177; -. DR SIGNOR; Q13177; -. DR BioGRID-ORCS; 5062; 107 hits in 1197 CRISPR screens. DR ChiTaRS; PAK2; human. DR EvolutionaryTrace; Q13177; -. DR GeneWiki; PAK2; -. DR GenomeRNAi; 5062; -. DR Pharos; Q13177; Tchem. DR PRO; PR:Q13177; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q13177; Protein. DR Bgee; ENSG00000180370; Expressed in ganglionic eminence and 210 other cell types or tissues. DR ExpressionAtlas; Q13177; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:CAFA. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0030141; C:secretory granule; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL. DR GO; GO:0031267; F:small GTPase binding; IPI:CAFA. DR GO; GO:0034333; P:adherens junction assembly; IMP:ARUK-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:ARUK-UCL. DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0060996; P:dendritic spine development; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0051179; P:localization; IMP:DisProt. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProt. DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc. DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:ARUK-UCL. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL. DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL. DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI. DR GO; GO:0150105; P:protein localization to cell-cell junction; IMP:ARUK-UCL. DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI. DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:ARUK-UCL. DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR CDD; cd01093; CRIB_PAK_like; 1. DR CDD; cd06655; STKc_PAK2; 1. DR Gene3D; 3.90.810.10; CRIB domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00244; -. DR InterPro; IPR000095; CRIB_dom. DR InterPro; IPR036936; CRIB_dom_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR033923; PAK_BD. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR035064; STK_PAK2. DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1. DR PANTHER; PTHR48015:SF22; SERINE_THREONINE-PROTEIN KINASE PAK 2; 1. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00285; PBD; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50108; CRIB; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q13177; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Apoptosis; ATP-binding; KW Cytoplasm; Direct protein sequencing; Disease variant; Growth regulation; KW Host-virus interaction; Kinase; Lipoprotein; Membrane; Myristate; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..524 FT /note="Serine/threonine-protein kinase PAK 2" FT /id="PRO_0000086465" FT CHAIN 2..212 FT /note="PAK-2p27" FT /id="PRO_0000304922" FT CHAIN 213..524 FT /note="PAK-2p34" FT /id="PRO_0000304923" FT DOMAIN 74..87 FT /note="CRIB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057" FT DOMAIN 249..499 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 69..137 FT /note="Autoregulatory region" FT /evidence="ECO:0000250|UniProtKB:Q13153" FT REGION 69..112 FT /note="GTPase-binding" FT /evidence="ECO:0000250|UniProtKB:Q13153" FT REGION 143..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 169..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 245..251 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:12853446" FT COMPBIAS 41..78 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 367 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 255..263 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 278 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 212..213 FT /note="Cleavage; by caspase-3 or caspase-3-like proteases" FT /evidence="ECO:0000269|PubMed:9171063, FT ECO:0000269|PubMed:9786869" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 60 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 62 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CIN4" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 128 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 134 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 139 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33693784, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 143 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CIN4" FT MOD_RES 154 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 169 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 402 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000305|PubMed:9786869" FT LIPID 213 FT /note="N-myristoyl glycine; in form PAK-2p34" FT /evidence="ECO:0000269|PubMed:16617111" FT VARIANT 435 FT /note="E -> K (in KNO2; loss of protein serine/threonine FT kinase activity)" FT /evidence="ECO:0000269|PubMed:33693784" FT /id="VAR_087512" FT MUTAGEN 212 FT /note="D->N: Inhibits caspase-mediated cleavage." FT /evidence="ECO:0000269|PubMed:9171063" FT MUTAGEN 213 FT /note="G->A: Abolishes myristoylation of PAK-2p34 and FT membrane location." FT /evidence="ECO:0000269|PubMed:16617111" FT MUTAGEN 239..243 FT /note="IVSIG->REGRS: Abolishes nuclear export." FT /evidence="ECO:0000269|PubMed:12853446" FT MUTAGEN 246..248 FT /note="KKK->MHE: Greatly inhibits nuclear localization." FT /evidence="ECO:0000269|PubMed:12853446" FT MUTAGEN 278 FT /note="K->R: Abolishes kinase activity and FT autophosphorylation." FT /evidence="ECO:0000269|PubMed:9786869" FT MUTAGEN 402 FT /note="T->A: Abolishes kinase activity and greatly inhibits FT autophosphorylation of PAK-2p27 and PAK-2p34." FT /evidence="ECO:0000269|PubMed:9786869" FT CONFLICT 90 FT /note="A -> T (in Ref. 3; AAA75468)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="F -> L (in Ref. 1; AAA65442)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="T -> P (in Ref. 1; AAA65442)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="G -> R (in Ref. 2; AAH69613)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="G -> R (in Ref. 3; AAA75468)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="T -> TA (in Ref. 1; AAA65442)" FT /evidence="ECO:0000305" FT HELIX 123..126 FT /evidence="ECO:0007829|PDB:3PCS" SQ SEQUENCE 524 AA; 58043 MW; 00A7CD15F93D4180 CRC64; MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR HKIISIFSGT EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNAK GTEAPAVVTE EEDDDEETAP PVIAPRPDHT KSIYTRSVID PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLIMAAKEAM KSNR //