CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016909
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase PAK 2 
Protein Synonyms/Alias
 Gamma-PAK; p21-activated kinase 2; PAK-2; PAK-2p27; PAK-2p34 
Gene Name
 Pak2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
38LSANHSLKPLPSVPEacetylation[1]
52EEKKPRNKIISIFSGacetylation[1]
62SIFSGTEKGSKKKEKacetylation[1, 2]
136FYDSNTVKQKYLSFTubiquitination[3]
235TDEEIMEKLRTIVSIubiquitination[3]
370QVIHRDIKSDNVLLGubiquitination[3]
504HPFLKLAKPLSSLTPacetylation[1]
504HPFLKLAKPLSSLTPsuccinylation[1]
517TPLILAAKEAMKSNRacetylation[4]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 74 87 CRIB.
 DOMAIN 249 499 Protein kinase.
 NP_BIND 255 263 ATP (By similarity).
 REGION 69 137 Autoregulatory region (By similarity).
 REGION 69 112 GTPase-binding (By similarity).
 MOTIF 245 251 Nuclear localization signal (By
 ACT_SITE 367 367 Proton acceptor (By similarity).
 BINDING 278 278 ATP (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 2 2 Phosphoserine (By similarity).
 MOD_RES 58 58 Phosphoserine (By similarity).
 MOD_RES 128 128 N6-acetyllysine (By similarity).
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 143 143 Phosphothreonine.
 MOD_RES 169 169 Phosphothreonine (By similarity).
 MOD_RES 197 197 Phosphoserine (By similarity).
 MOD_RES 402 402 Phosphothreonine; by autocatalysis (By  
Keyword
 Acetylation; Allosteric enzyme; Apoptosis; ATP-binding; Complete proteome; Cytoplasm; Growth regulation; Kinase; Lipoprotein; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR NKIISIFSGT 60
EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP 120
QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNTK GSETSAVVTE EDDDDEDAAP 180
PVIAPRPDHT KSIYTRSVID PIPAPVGDSN VDSGAKSSDK QKKKAKMTDE EIMEKLRTIV 240
SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE 300
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH 360
ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY 420
GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC 480
LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLILAAKEAM KSNR 524 
Gene Ontology
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
 GO:0030296; F:protein tyrosine kinase activator activity; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:Compara.
 GO:0018105; P:peptidyl-serine phosphorylation; IEA:Compara.
 GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Compara.
 GO:0046777; P:protein autophosphorylation; ISO:MGI.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000095; PAK_box_Rho-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00786; PBD
 PF00069; Pkinase 
SMART
 SM00285; PBD
 SM00220; S_TKc 
PROSITE
 PS50108; CRIB
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS