EKS-HOS-00324
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00324
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
STE/STE20348.61.1E-103249500252
StatusReviewed
Ensembl ProteinENSP00000314067
UniProt AccessionQ13177; Q13154; Q6ISC3;
Protein NamePAK-2p34
Protein Synonyms/Alias Gamma-PAK; PAK65; S6/H4 kinase; p21-activated kinase 2; PAK-2; p58; p27; p34; C-t-PAK2;
Gene NamePAK2
Gene Synonyms/Alias PAK2;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000180370ENSP00000402927ENST00000426668
ENSG00000180370ENSP00000314067ENST00000327134
OrganismHomo sapiens
Functional DescriptionSerine/threonine protein kinase that plays a role in avariety 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.
Protein Length524
Protein Sequence
(FASTA)
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
Nucleotide Sequence
(FASTA)
ATGTCTGATA ACGGAGAACT GGAAGATAAG CCTCCAGCAC CTCCTGTGCG AATGAGCAGC 60
ACCATCTTTA GCACTGGAGG CAAAGACCCT TTGTCAGCCA ATCACAGTTT GAAACCTTTG 120
CCCTCTGTTC CAGAAGAGAA AAAGCCCAGG CATAAAATCA TCTCCATATT CTCAGGCACA 180
GAGAAAGGAA GTAAAAAGAA AGAAAAGGAA CGGCCAGAAA TTTCTCCTCC ATCTGATTTT 240
GAGCACACCA TCCATGTTGG CTTTGATGCT GTTACTGGAG AATTCACTGG CATGCCAGAA 300
CAGTGGGCTC GATTACTACA GACCTCCAAT ATCACCAAAC TAGAGCAAAA GAAGAATCCT 360
CAGGCTGTGC TGGATGTCCT AAAGTTCTAC GACTCCAACA CAGTGAAGCA GAAATATCTG 420
AGCTTTACTC CTCCTGAGAA AGATGGCTTT CCTTCTGGAA CACCAGCACT GAATGCCAAG 480
GGAACAGAAG CACCCGCAGT AGTGACAGAG GAGGAGGATG ATGATGAAGA GACTGCTCCT 540
CCCGTTATTG CCCCGCGACC GGATCATACG AAATCAATTT ACACACGGTC TGTAATTGAC 600
CCTGTTCCTG CACCAGTTGG TGATTCACAT GTTGATGGTG CTGCCAAGTC TTTAGACAAA 660
CAGAAAAAGA AGACTAAGAT GACAGATGAA GAGATTATGG AGAAATTAAG AACTATCGTG 720
AGCATAGGTG ACCCTAAGAA AAAATATACA AGATATGAAA AAATTGGACA AGGGGCTTCT 780
GGTACAGTTT TCACTGCTAC TGACGTTGCA CTGGGACAGG AGGTTGCTAT CAAACAAATT 840
AATTTACAGA AACAGCCAAA GAAGGAACTG ATCATTAACG AGATTCTGGT GATGAAAGAA 900
TTGAAAAATC CCAACATCGT TAACTTTTTG GACAGTTACC TGGTAGGAGA TGAATTGTTT 960
GTGGTCATGG AATACCTTGC TGGGGGGTCA CTCACTGATG TGGTAACAGA AACGTGCATG 1020
GATGAAGCAC AGATTGCTGC TGTATGCAGA GAGTGTTTAC AGGCATTGGA GTTTTTACAT 1080
GCTAATCAAG TGATCCACAG AGACATCAAA AGTGACAATG TACTTTTGGG AATGGAAGGA 1140
TCTGTTAAGC TCACTGACTT TGGTTTCTGT GCCCAGATCA CCCCTGAGCA GAGCAAACGC 1200
AGTACCATGG TCGGAACGCC ATACTGGATG GCACCAGAGG TGGTTACACG GAAAGCTTAT 1260
GGCCCTAAAG TCGACATATG GTCTCTGGGT ATCATGGCTA TTGAGATGGT AGAAGGAGAG 1320
CCTCCATACC TCAATGAAAA TCCCTTGAGG GCCTTGTACC TAATAGCAAC TAATGGAACC 1380
CCAGAACTTC AGAATCCAGA GAAACTTTCC CCAATATTTC GGGATTTCTT AAATCGATGT 1440
TTGGAAATGG ATGTGGAAAA AAGGGGTTCA GCCAAAGAAT TATTACAGCA TCCTTTCCTG 1500
AAACTGGCCA AACCGTTATC TAGCTTGACA CCACTGATCA TGGCAGCTAA AGAAGCAATG 1560
AAGAGTAACC GTTAA 1575
Domain Profile
S: 1     yelleeigkGalgkvylarekktgelvaikkinlekqekleelqkeisvlkklkhpnive  60
         y+ +e+ig+Ga+g+v++a+++  g+ vaik+inl+kq+k+e++++ei v+k+lk+pniv+
Q: 249   YTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVN  308
         7889********************************************************
S: 61    ylesflkeeelwlvmeylagGslsdlvkeelkselkEeqiayilrevlkaLeylHskkvi  120
         +l+s+l+ +el++vmeylagGsl+d+v+   ++ ++E qia+++re+l+aLe+lH+++vi
Q: 309   FLDSYLVGDELFVVMEYLAGGSLTDVVT---ETCMDEAQIAAVCRECLQALEFLHANQVI  365
         ****************************...9****************************
S: 121   HrdikakniLlteegeVkLsdfgvaaqlektrkkrktvvgtpywmAPEviaqeekgYdek  180
         Hrdik++n+Ll +eg+VkL+dfg++aq++ +++kr+t+vgtpywmAPEv++  +k Y  k
Q: 366   HRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT--RKAYGPK  423
         ***************************************************..9******
S: 181   aDiwslGItaielaegepPfkdleplkallkilkneppklkskkkfskefkefvekclqk  240
         +DiwslGI+aie++egepP+ +++pl+al++i++n +p+l++++k+s+ f++f+++cl+ 
Q: 424   VDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEM  483
         ************************************************************
S: 241   npekRpsasellkhkFl  257
         ++ekR sa+ell+h+Fl
Q: 484   DVEKRGSAKELLQHPFL  500
         ****************7
Domain Sequence
(FASTA)
YTRYEKIGQG ASGTVFTATD VALGQEVAIK QINLQKQPKK ELIINEILVM KELKNPNIVN 60
FLDSYLVGDE LFVVMEYLAG GSLTDVVTET CMDEAQIAAV CRECLQALEF LHANQVIHRD 120
IKSDNVLLGM EGSVKLTDFG FCAQITPEQS KRSTMVGTPY WMAPEVVTRK AYGPKVDIWS 180
LGIMAIEMVE GEPPYLNENP LRALYLIATN GTPELQNPEK LSPIFRDFLN RCLEMDVEKR 240
GSAKELLQHP FL 252
Keyword3D-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.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Danio rerio"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Oreochromis niloticus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sorex araneus"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00293
EKS-ANC-00305
EKS-BOT-00317
EKS-CAJ-00323
EKS-CAF-00319
EKS-CAP-00349
EKS-DAR-00670
EKS-EQC-00307
EKS-FEC-00302
EKS-GAM-00198
EKS-GAG-00264
EKS-GAA-00392
EKS-GOG-00315
EKS-ICT-00295
EKS-LOA-00324
EKS-MAM-00318
EKS-MEG-00269
EKS-MOD-00309
EKS-MUM-00348
EKS-MUP-00310
EKS-MYL-00311
EKS-NOL-00290
EKS-OCP-00054
EKS-ORN-00414
EKS-ORC-00298
EKS-ORL-00375
EKS-OTG-00321
EKS-PAT-00302
EKS-PES-00277
EKS-POA-00309
EKS-PRC-00046
EKS-PTV-00071
EKS-RAN-00331
EKS-SAH-00292
EKS-SOA-00035
EKS-SUS-00293
EKS-TAG-00328
EKS-TAR-00415
EKS-TAS-00030
EKS-TEN-00409
EKS-XET-00386
EKS-XIM-00406
Gene Ontology
GO:0005829; C:cytosol
GO:0005634; C:nucleus
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0005524; F:ATP binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0030296; F:protein tyrosine kinase activator activity
GO:0007411; P:axon guidance
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis
GO:0043066; P:negative regulation of apoptotic process
GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis
GO:0006469; P:negative regulation of protein kinase activity
GO:0018105; P:peptidyl-serine phosphorylation
GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway
GO:0046777; P:protein autophosphorylation
GO:0050690; P:regulation of defense response to virus by virus
GO:0040008; P:regulation of growth
GO:0031295; P:T cell costimulation
GO:0050852; P:T cell receptor signaling pathway
GO:0016032; P:viral reproduction
GO:0019048; P:virus-host interaction
KEGG
hsa:5062;
InterPros
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; 1.
PF00069; Pkinase; 1.
SMARTs
SM00285; PBD; 1.
SM00220; S_TKc; 1.
Prosites
PS50108; CRIB; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013