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Serine/threonine-protein kinase PAK 2 (EC 2.7.11.1) (Gamma-PAK) (PAK65) (S6/H4 kinase) (p21-activated kinase 2) (PAK-2) (p58) [Cleaved into: PAK-2p27 (p27); PAK-2p34 (p34) (C-t-PAK2)]

 PAK2_HUMAN              Reviewed;         524 AA.
Q13177; Q13154; Q6ISC3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 3.
25-OCT-2017, entry version 191.
RecName: Full=Serine/threonine-protein kinase PAK 2;
EC=2.7.11.1;
AltName: Full=Gamma-PAK;
AltName: Full=PAK65;
AltName: Full=S6/H4 kinase;
AltName: Full=p21-activated kinase 2;
Short=PAK-2;
AltName: Full=p58;
Contains:
RecName: Full=PAK-2p27;
Short=p27;
Contains:
RecName: Full=PAK-2p34;
Short=p34;
AltName: Full=C-t-PAK2;
Name=PAK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Sells M., Knause U.J., Bagrodia S., Ambrose D., Bokoch G.M.,
Chernoff J.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-524, AND PROTEIN SEQUENCE OF 401-417.
TISSUE=Placenta;
PubMed=7744004;
Martin G.A., Bollag G., McCormick F., Abo A.;
"A novel serine kinase activated by rac1/CDC42Hs-dependent
autophosphorylation is related to PAK65 and STE20.";
EMBO J. 14:1970-1978(1995).
[4]
ERRATUM.
PubMed=7556080;
Martin G.A., Bollag G., McCormick F., Abo A.;
EMBO J. 14:4385-4385(1995).
[5]
AUTOPHOSPHORYLATION.
PubMed=7673144; DOI=10.1074/jbc.270.36.21121;
Benner G.E., Dennis P.B., Masaracchia R.A.;
"Activation of an S6/H4 kinase (PAK 65) from human placenta by
intramolecular and intermolecular autophosphorylation.";
J. Biol. Chem. 270:21121-21128(1995).
[6]
CASPASE-3 CLEAVAGE AT ASP-512, FUNCTION, AND MUTAGENESIS OF ASP-212.
PubMed=9171063; DOI=10.1126/science.276.5318.1571;
Rudel T., Bokoch G.M.;
"Membrane and morphological changes in apoptotic cells regulated by
caspase-mediated activation of PAK2.";
Science 276:1571-1574(1997).
[7]
CASPASE-3 CLEAVAGE AT ASP-512, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
LYS-278 AND THR-402.
PubMed=9786869; DOI=10.1074/jbc.273.44.28733;
Walter B.N., Huang Z., Jakobi R., Tuazon P.T., Alnemri E.S.,
Litwack G., Traugh J.A.;
"Cleavage and activation of p21-activated protein kinase gamma-PAK by
CPP32 (caspase 3). Effects of autophosphorylation on activity.";
J. Biol. Chem. 273:28733-28739(1998).
[8]
INTERACTION WITH HIV-1 NEF.
PubMed=11070003; DOI=10.1128/JVI.74.23.11081-11087.2000;
Arora V.K., Molina R.P., Foster J.L., Blakemore J.L., Chernoff J.,
Fredericksen B.L., Garcia J.V.;
"Lentivirus Nef specifically activates Pak2.";
J. Virol. 74:11081-11087(2000).
[9]
FUNCTION (PAK-2P34), UBIQUITINATION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 239-ILE--GLY-243 AND 246-LYS--LYS-248.
PubMed=12853446; DOI=10.1074/jbc.M306494200;
Jakobi R., McCarthy C.C., Koeppel M.A., Stringer D.K.;
"Caspase-activated PAK-2 is regulated by subcellular targeting and
proteasomal degradation.";
J. Biol. Chem. 278:38675-38685(2003).
[10]
FUNCTION IN PHOSPHORYLATION OF MKNK1.
PubMed=15234964; DOI=10.1074/jbc.M407337200;
Orton K.C., Ling J., Waskiewicz A.J., Cooper J.A., Merrick W.C.,
Korneeva N.L., Rhoads R.E., Sonenberg N., Traugh J.A.;
"Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits
phosphorylation and interaction of eIF4G with Mnk.";
J. Biol. Chem. 279:38649-38657(2004).
[11]
INTERACTION WITH ARHGAP10, AND SUBCELLULAR LOCATION.
PubMed=15471851; DOI=10.1074/jbc.M410530200;
Koeppel M.A., McCarthy C.C., Moertl E., Jakobi R.;
"Identification and characterization of PS-GAP as a novel regulator of
caspase-activated PAK-2.";
J. Biol. Chem. 279:53653-53664(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
INTERACTION WITH SH3MD4.
PubMed=16374509; DOI=10.1038/sj.embor.7400596;
Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I.,
Vaehae-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K.;
"Identification of preferred protein interactions by phage-display of
the human Src homology-3 proteome.";
EMBO Rep. 7:186-191(2006).
[14]
FUNCTION (PAK-2P34), MYRISTOYLATION AT GLY-213 (PAK-2P34), AND
SUBCELLULAR LOCATION.
PubMed=16617111; DOI=10.1073/pnas.0600824103;
Vilas G.L., Corvi M.M., Plummer G.J., Seime A.M., Lambkin G.R.,
Berthiaume L.G.;
"Posttranslational myristoylation of caspase-activated p21-activated
protein kinase 2 (PAK2) potentiates late apoptotic events.";
Proc. Natl. Acad. Sci. U.S.A. 103:6542-6547(2006).
[15]
INTERACTION WITH SCRIB.
PubMed=18716323; DOI=10.1093/hmg/ddn248;
Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
Navarro C., Rachel R., Montcouquiol M., Sans N.,
Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
"Scrib regulates PAK activity during the cell migration process.";
Hum. Mol. Genet. 17:3552-3565(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-141 AND THR-169,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
INTERACTION WITH ARHGEF7 AND GIT1.
PubMed=19273597; DOI=10.1128/MCB.01713-08;
Mitsushima M., Toyoshima F., Nishida E.;
"Dual role of Cdc42 in spindle orientation control of adherent
cells.";
Mol. Cell. Biol. 29:2816-2827(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-197, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19923322; DOI=10.1091/mbc.E09-03-0232;
Hsu R.M., Tsai M.H., Hsieh Y.J., Lyu P.C., Yu J.S.;
"Identification of MYO18A as a novel interacting partner of the
PAK2/betaPIX/GIT1 complex and its potential function in modulating
epithelial cell migration.";
Mol. Biol. Cell 21:287-301(2010).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2 AND SER-141, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
AUTOPHOSPHORYLATION.
PubMed=21098037; DOI=10.1074/jbc.M110.156505;
Wang J., Wu J.W., Wang Z.X.;
"Mechanistic studies of the autoactivation of PAK2: a two-step model
of cis initiation followed by trans amplification.";
J. Biol. Chem. 286:2689-2695(2011).
[25]
FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6.
PubMed=21317288; DOI=10.1074/jbc.M110.181743;
De la Mota-Peynado A., Chernoff J., Beeser A.;
"Identification of the atypical MAPK Erk3 as a novel substrate for
p21-activated kinase (Pak) activity.";
J. Biol. Chem. 286:13603-13611(2011).
[26]
FUNCTION IN PHOSPHORYLATION OF JUN.
PubMed=21177766; DOI=10.1093/carcin/bgq271;
Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C.,
Ma W., Shi G., Dong Z., Bode A.M., Dong Z.;
"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at
5 threonine sites promotes cell transformation.";
Carcinogenesis 32:659-666(2011).
[27]
FUNCTION IN PHOSPHORYLATION OF HISTONE H4.
PubMed=21724829; DOI=10.1101/gad.2055511;
Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B.,
Zhang Z.;
"Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome
assembly.";
Genes Dev. 25:1359-1364(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-141 AND THR-169, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-20; SER-55;
SER-58; THR-60; SER-64; THR-134; SER-141; THR-143; THR-154; THR-169
AND SER-197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139 AND SER-141, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 121-136.
PubMed=21170023; DOI=10.1038/nature09593;
Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C.,
Bresson S.M., Tomchick D.R., Alto N.M.;
"The assembly of a GTPase-kinase signalling complex by a bacterial
catalytic scaffold.";
Nature 469:107-111(2011).
-!- 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. 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. {ECO:0000269|PubMed:12853446,
ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111,
ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766,
ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829,
ECO:0000269|PubMed:9171063}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- 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-402 and allows the kinase domain to adopt an active structure
(By similarity). Following caspase cleavage, autophosphorylated
PAK-2p34 is constitutively active. {ECO:0000250}.
-!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound
CDC42/p21 and RAC1. Interacts with SH3MD4. Interacts with and
activated by HIV-1 Nef. Interacts with SCRIB. Interacts with
ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10.
{ECO:0000269|PubMed:11070003, ECO:0000269|PubMed:15471851,
ECO:0000269|PubMed:16374509, ECO:0000269|PubMed:18716323,
ECO:0000269|PubMed:19273597}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1045887, EBI-1045887;
Q15052:ARHGEF6; NbExp=4; IntAct=EBI-1045887, EBI-1642523;
Q14155:ARHGEF7; NbExp=4; IntAct=EBI-1045887, EBI-717515;
O55043:Arhgef7 (xeno); NbExp=8; IntAct=EBI-1045887, EBI-3649585;
P55210:CASP7; NbExp=6; IntAct=EBI-1045887, EBI-523958;
P60953:CDC42; NbExp=4; IntAct=EBI-1045887, EBI-81752;
P62993:GRB2; NbExp=2; IntAct=EBI-1045887, EBI-401755;
P08631:HCK; NbExp=2; IntAct=EBI-1045887, EBI-346340;
P42858:HTT; NbExp=2; IntAct=EBI-1045887, EBI-466029;
P53667:LIMK1; NbExp=2; IntAct=EBI-1045887, EBI-444403;
P16333:NCK1; NbExp=2; IntAct=EBI-1045887, EBI-389883;
P63000:RAC1; NbExp=4; IntAct=EBI-1045887, EBI-413628;
P04049:RAF1; NbExp=2; IntAct=EBI-1045887, EBI-365996;
Q9H4E5:RHOJ; NbExp=5; IntAct=EBI-1045887, EBI-6285694;
Q8TEJ3:SH3RF3; NbExp=2; IntAct=EBI-1045887, EBI-7975674;
Q9BX66:SORBS1; NbExp=2; IntAct=EBI-1045887, EBI-433642;
O94875:SORBS2; NbExp=2; IntAct=EBI-1045887, EBI-311323;
O60504:SORBS3; NbExp=6; IntAct=EBI-1045887, EBI-741237;
P12931:SRC; NbExp=2; IntAct=EBI-1045887, EBI-621482;
Q5PP90:US3(L) (xeno); NbExp=2; IntAct=EBI-1045887, EBI-15780451;
-!- SUBCELLULAR LOCATION: Serine/threonine-protein kinase PAK 2:
Cytoplasm. Note=MYO18A mediates the cellular distribution of the
PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell
membrane.
-!- SUBCELLULAR LOCATION: PAK-2p34: Nucleus. Cytoplasm, perinuclear
region. Membrane; Lipid-anchor. Note=Interaction with ARHGAP10
probably changes PAK-2p34 location to cytoplasmic perinuclear
region. Myristoylation changes PAK-2p34 location to the membrane.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Higher levels seen in
skeletal muscle, ovary, thymus and spleen.
-!- PTM: 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.
-!- PTM: During apoptosis proteolytically cleaved by caspase-3 or
caspase-3-like proteases to yield active PAK-2p34.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000269|PubMed:12853446}.
-!- PTM: PAK-2p34 is myristoylated. {ECO:0000269|PubMed:16617111}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PAK2ID41634ch3q29.html";
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EMBL; U24153; AAA65442.1; -; mRNA.
EMBL; BC069613; AAH69613.1; -; mRNA.
EMBL; U25975; AAA75468.1; -; mRNA.
CCDS; CCDS3321.1; -.
PIR; S58682; S58682.
RefSeq; NP_002568.2; NM_002577.4.
RefSeq; XP_011511172.1; XM_011512870.2.
RefSeq; XP_016861990.1; XM_017006501.1.
UniGene; Hs.518530; -.
PDB; 3PCS; X-ray; 2.86 A; E/F/G/H=121-136.
PDBsum; 3PCS; -.
ProteinModelPortal; Q13177; -.
SMR; Q13177; -.
BioGrid; 111098; 92.
DIP; DIP-38249N; -.
ELM; Q13177; -.
IntAct; Q13177; 49.
MINT; MINT-235655; -.
STRING; 9606.ENSP00000314067; -.
BindingDB; Q13177; -.
ChEMBL; CHEMBL4487; -.
GuidetoPHARMACOLOGY; 2134; -.
iPTMnet; Q13177; -.
PhosphoSitePlus; Q13177; -.
SwissPalm; Q13177; -.
BioMuta; PAK2; -.
DMDM; 143811432; -.
OGP; Q13177; -.
EPD; Q13177; -.
MaxQB; Q13177; -.
PaxDb; Q13177; -.
PeptideAtlas; Q13177; -.
PRIDE; Q13177; -.
DNASU; 5062; -.
Ensembl; ENST00000327134; ENSP00000314067; ENSG00000180370.
GeneID; 5062; -.
KEGG; hsa:5062; -.
UCSC; uc003fwy.4; human.
CTD; 5062; -.
DisGeNET; 5062; -.
EuPathDB; HostDB:ENSG00000180370.10; -.
GeneCards; PAK2; -.
H-InvDB; HIX0030815; -.
HGNC; HGNC:8591; PAK2.
HPA; CAB007794; -.
MIM; 605022; gene.
neXtProt; NX_Q13177; -.
OpenTargets; ENSG00000180370; -.
PharmGKB; PA32918; -.
eggNOG; KOG0578; Eukaryota.
eggNOG; ENOG410XP4K; LUCA.
GeneTree; ENSGT00900000140851; -.
HOGENOM; HOG000234202; -.
HOVERGEN; HBG108518; -.
InParanoid; Q13177; -.
KO; K04410; -.
OMA; DSGVCED; -.
OrthoDB; EOG091G04H8; -.
PhylomeDB; Q13177; -.
TreeFam; TF105351; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-211728; Regulation of PAK-2p34 activity by PS-GAP/RHG10.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-211736; Stimulation of the cell death response by PAK-2p34.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-428540; Activation of Rac.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SignaLink; Q13177; -.
SIGNOR; Q13177; -.
ChiTaRS; PAK2; human.
EvolutionaryTrace; Q13177; -.
GeneWiki; PAK2; -.
GenomeRNAi; 5062; -.
PMAP-CutDB; Q13177; -.
PRO; PR:Q13177; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000180370; -.
CleanEx; HS_PAK2; -.
ExpressionAtlas; Q13177; baseline and differential.
Genevisible; Q13177; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL.
GO; GO:0048365; F:Rac GTPase binding; IPI:CAFA.
GO; GO:0031267; F:small GTPase binding; IPI:CAFA.
GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd01093; CRIB_PAK_like; 1.
CDD; cd06655; STKc_PAK2; 1.
Gene3D; 3.90.810.10; -; 1.
InterPro; IPR000095; CRIB_dom.
InterPro; IPR036936; CRIB_dom_sf.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR035065; PAK2/3.
InterPro; IPR033923; PAK_BD.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR035064; STK_PAK2.
PANTHER; PTHR24361:SF250; PTHR24361:SF250; 1.
Pfam; PF00786; PBD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00285; PBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50108; CRIB; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Apoptosis; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing;
Growth regulation; Host-virus interaction; Kinase; Lipoprotein;
Membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 524 Serine/threonine-protein kinase PAK 2.
/FTId=PRO_0000086465.
CHAIN 2 212 PAK-2p27.
/FTId=PRO_0000304922.
CHAIN 213 524 PAK-2p34.
/FTId=PRO_0000304923.
DOMAIN 74 87 CRIB. {ECO:0000255|PROSITE-
ProRule:PRU00057}.
DOMAIN 249 499 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 255 263 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 69 137 Autoregulatory region. {ECO:0000250}.
REGION 69 112 GTPase-binding. {ECO:0000250}.
MOTIF 245 251 Nuclear localization signal.
ACT_SITE 367 367 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 278 278 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 212 213 Cleavage; by caspase-3 or caspase-3-like
proteases.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 60 60 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CIN4}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 134 134 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 139 139 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CIN4}.
MOD_RES 154 154 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 402 402 Phosphothreonine; by autocatalysis.
{ECO:0000305}.
LIPID 213 213 N-myristoyl glycine; in form PAK-2p34.
{ECO:0000269|PubMed:16617111}.
MUTAGEN 212 212 D->N: Inhibits caspase-mediated cleavage.
{ECO:0000269|PubMed:9171063}.
MUTAGEN 213 213 G->A: Abolishes myristoylation of PAK-
2p34 and membrane location.
MUTAGEN 239 243 IVSIG->REGRS: Abolishes nuclear export.
{ECO:0000269|PubMed:12853446}.
MUTAGEN 246 248 KKK->MHE: Greatly inhibits nuclear
localization.
{ECO:0000269|PubMed:12853446}.
MUTAGEN 278 278 K->R: Abolishes kinase activity and
autophosphorylation.
{ECO:0000269|PubMed:9786869}.
MUTAGEN 402 402 T->A: Abolishes kinase activity and
greatly inhibits autophosphorylation of
PAK-2p27 and PAK-2p34.
{ECO:0000269|PubMed:9786869}.
CONFLICT 90 90 A -> T (in Ref. 3; AAA75468).
{ECO:0000305}.
CONFLICT 150 150 F -> L (in Ref. 1; AAA65442).
{ECO:0000305}.
CONFLICT 225 225 T -> P (in Ref. 1; AAA65442).
{ECO:0000305}.
CONFLICT 258 258 G -> R (in Ref. 2; AAH69613).
{ECO:0000305}.
CONFLICT 329 329 G -> R (in Ref. 3; AAA75468).
{ECO:0000305}.
CONFLICT 338 338 T -> TA (in Ref. 1; AAA65442).
{ECO:0000305}.
HELIX 123 126 {ECO:0000244|PDB:3PCS}.
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


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