Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00484
Entry Name
UniProt Accession
Theoretical PI
5.69
Molecular Weight
58042.61
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
PAK-2p34
Protein Synonyms/Alias
2.7.11.1; Gamma-PAK; PAK65; S6/H4 kinase; p21-activated kinase 2; PAK-2; p58; p27; p34; C-t-PAK2;
Gene Name
PAK2
Gene Synonyms/Alias
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
213
Canonical
VGDSHVDGAAKSLDK
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Vilas GL, Corvi MM, Plummer GJ, Seime AM, Lambkin GR, Berthiaume LG.Posttranslational myristoylation of caspase-activated p21-activated proteinkinase 2 (PAK2) potentiates late apoptotic events. Proc Natl Acad Sci U S A. 2006Apr 25;103(17):6542-7. Epub 2006 Apr 14.[PMID:16617111]
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.
Sequence Annotation
Domain: 74 87 CRIB.
Domain: 249 499 Protein kinase.
Nucleotide-binding: 255 263 ATP.
Region: 69 137 Autoregulatory region.
Region: 69 112 GTPase-binding.
Motif: 245 251 Nuclear localization signal.
Active site: 367 367 Proton acceptor.
Binding site: 278 278 ATP.
Functional site: 212 213 Cleavage; by caspase-3 or caspase-3-likeproteases.
Modified residue: 2 2 N-acetylserine.
Modified residue: 2 2 Phosphoserine.
Modified residue: 58 58 Phosphoserine.
Modified residue: 62 62 N6-acetyllysine.
Modified residue: 128 128 N6-acetyllysine.
Modified residue: 141 141 Phosphoserine.
Modified residue: 169 169 Phosphothreonine.
Modified residue: 197 197 Phosphoserine.
Modified residue: 402 402 Phosphothreonine; by autocatalysis.
Protein Length
524 AA.
Protein Sequence
(Canonical)
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR HKIISIFSGT  60
EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP  120
QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNAK GTEAPAVVTE EEDDDEETAP  180
PVIAPRPDHT KSIYTRSVID PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE 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 PLIMAAKEAM KSNR                   524
FASTA
(Canonical)
>LipidDB-9606-00484|Q13177
MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGT
EKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNP
QAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAP
PVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIV
SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKE
LKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLH
ANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAY
GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR
Gene Ontology
GO:0005737; C:cytoplasm; IDA:HPA
GO:0005829; C:cytosol; TAS:Reactome
GO:0005634; C:nucleus; IDA:HPA
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0042802; F:identical protein binding; IPI:IntAct
GO:0004672; F:protein kinase activity; TAS:ProtInc
GO:0019901; F:protein kinase binding; IPI:BHF-UCL
GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL
GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL
GO:0006915; P:apoptotic process; TAS:Reactome
GO:0007411; P:axon guidance; TAS:Reactome
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome
GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome
GO:0045087; P:innate immune response; TAS:Reactome
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB
GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:UniProtKB
GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc
GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL
GO:0016310; P:phosphorylation; IDA:UniProtKB
GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL
GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:GOC
GO:0046777; P:protein autophosphorylation; IDA:MGI
GO:0006468; P:protein phosphorylation; IDA:MGI
GO:0042981; P:regulation of apoptotic process; TAS:Reactome
GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome
GO:0040008; P:regulation of growth; IEA:UniProtKB-KW
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0031295; P:T cell costimulation; TAS:Reactome
GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome
GO:0016032; P:viral process; TAS:Reactome
Interpro
InterPro; IPR000095; CRIB_dom
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00786; PBD;
Pfam; PF00069; Pkinase;
SMART
SMART; SM00285; PBD;
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS50108; CRIB;
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS