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Q13177

- PAK2_HUMAN

UniProt

Q13177 - PAK2_HUMAN

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Protein
Serine/threonine-protein kinase PAK 2
Gene
PAK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei212 – 2132Cleavage; by caspase-3 or caspase-3-like proteases
Binding sitei278 – 2781ATP By similarity
Active sitei367 – 3671Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi255 – 2639ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. protein binding Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein kinase binding Source: BHF-UCL
  6. protein serine/threonine kinase activity Source: BHF-UCL
  7. protein tyrosine kinase activator activity Source: BHF-UCL
  8. receptor signaling protein serine/threonine kinase activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. T cell costimulation Source: Reactome
  3. T cell receptor signaling pathway Source: Reactome
  4. actin cytoskeleton organization Source: RefGenome
  5. apoptotic process Source: Reactome
  6. axon guidance Source: Reactome
  7. axonogenesis Source: RefGenome
  8. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  9. innate immune response Source: Reactome
  10. negative regulation of apoptotic process Source: UniProtKB
  11. negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
  12. negative regulation of protein kinase activity Source: ProtInc
  13. peptidyl-serine phosphorylation Source: BHF-UCL
  14. phosphorylation Source: UniProtKB
  15. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  16. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  17. positive regulation of protein tyrosine kinase activity Source: GOC
  18. protein autophosphorylation Source: MGI
  19. protein phosphorylation Source: MGI
  20. regulation of apoptotic process Source: Reactome
  21. regulation of defense response to virus by virus Source: Reactome
  22. regulation of growth Source: UniProtKB-KW
  23. signal transduction Source: ProtInc
  24. signal transduction by phosphorylation Source: GOC
  25. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Growth regulation, Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_11068. Nef and signal transduction.
REACT_12623. Generation of second messenger molecules.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13528. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
REACT_13532. Stimulation of the cell death response by PAK-2p34.
REACT_163701. FCERI mediated MAPK activation.
REACT_19226. Activation of Rac.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19238. CD28 dependent Vav1 pathway.
SignaLinkiQ13177.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 2 (EC:2.7.11.1)
Alternative name(s):
Gamma-PAK
PAK65
S6/H4 kinase
p21-activated kinase 2
Short name:
PAK-2
p58
Cleaved into the following 2 chains:
PAK-2p27
Short name:
p27
PAK-2p34
Short name:
p34
Alternative name(s):
C-t-PAK2
Gene namesi
Name:PAK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:8591. PAK2.

Subcellular locationi

Chain 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.4 Publications
Chain PAK-2p34 : Nucleus. Cytoplasmperinuclear 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.4 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi212 – 2121D → N: Inhibits caspase-mediated cleavage. 1 Publication
Mutagenesisi213 – 2131G → A: Abolishes myristoylation of PAK-2p34 and membrane location.
Mutagenesisi239 – 2435IVSIG → REGRS: Abolishes nuclear export. 1 Publication
Mutagenesisi246 – 2483KKK → MHE: Greatly inhibits nuclear localization. 1 Publication
Mutagenesisi278 – 2781K → R: Abolishes kinase activity and autophosphorylation. 1 Publication
Mutagenesisi402 – 4021T → A: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34. 1 Publication

Organism-specific databases

PharmGKBiPA32918.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 524523Serine/threonine-protein kinase PAK 2
PRO_0000086465Add
BLAST
Chaini2 – 212211PAK-2p27
PRO_0000304922Add
BLAST
Chaini213 – 524312PAK-2p34
PRO_0000304923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei62 – 621N6-acetyllysine By similarity
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei141 – 1411Phosphoserine4 Publications
Modified residuei169 – 1691Phosphothreonine2 Publications
Modified residuei197 – 1971Phosphoserine1 Publication
Lipidationi213 – 2131N-myristoyl glycine; in form PAK-2p341 Publication
Modified residuei402 – 4021Phosphothreonine; by autocatalysis Inferred

Post-translational modificationi

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.3 Publications
During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34.2 Publications
Ubiquitinated, leading to its proteasomal degradation.1 Publication
PAK-2p34 is myristoylated.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13177.
PaxDbiQ13177.
PRIDEiQ13177.

2D gel databases

OGPiQ13177.

PTM databases

PhosphoSiteiQ13177.

Miscellaneous databases

PMAP-CutDBQ13177.

Expressioni

Tissue specificityi

Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.

Gene expression databases

ArrayExpressiQ13177.
BgeeiQ13177.
CleanExiHS_PAK2.
GenevestigatoriQ13177.

Organism-specific databases

HPAiCAB007794.
HPA036205.

Interactioni

Subunit structurei

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 ARHGAP10.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1045887,EBI-1045887
ARHGEF6Q150522EBI-1045887,EBI-1642523
ARHGEF7Q141554EBI-1045887,EBI-717515
Arhgef7O550438EBI-1045887,EBI-3649585From a different organism.
CASP7P552106EBI-1045887,EBI-523958
GRB2P629932EBI-1045887,EBI-401755
HCKP086312EBI-1045887,EBI-346340
HTTP428582EBI-1045887,EBI-466029
LIMK1P536672EBI-1045887,EBI-444403
NCK1P163332EBI-1045887,EBI-389883
RAC1P630004EBI-1045887,EBI-413628
RAF1P040492EBI-1045887,EBI-365996
SH3RF3Q8TEJ32EBI-1045887,EBI-7975674
SORBS1Q9BX662EBI-1045887,EBI-433642
SORBS2O948752EBI-1045887,EBI-311323
SORBS3O605043EBI-1045887,EBI-741237
SRCP129312EBI-1045887,EBI-621482

Protein-protein interaction databases

BioGridi111098. 53 interactions.
DIPiDIP-38249N.
IntActiQ13177. 31 interactions.
MINTiMINT-235655.
STRINGi9606.ENSP00000314067.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 1264

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PCSX-ray2.86E/F/G/H121-136[»]
ProteinModelPortaliQ13177.
SMRiQ13177. Positions 69-143, 228-519.

Miscellaneous databases

EvolutionaryTraceiQ13177.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 8714CRIB
Add
BLAST
Domaini249 – 499251Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 13769Autoregulatory region By similarity
Add
BLAST
Regioni69 – 11244GTPase-binding By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 2517Nuclear localization signal

Sequence similaritiesi

Contains 1 CRIB domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
InParanoidiQ13177.
KOiK04410.
OMAiFSGAEKG.
PhylomeDBiQ13177.
TreeFamiTF105351.

Family and domain databases

Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13177-1 [UniParc]FASTAAdd to Basket

« Hide

MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR    50
HKIISIFSGT EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE 100
QWARLLQTSN ITKLEQKKNP QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF 150
PSGTPALNAK GTEAPAVVTE EEDDDEETAP PVIAPRPDHT KSIYTRSVID 200
PVPAPVGDSH VDGAAKSLDK QKKKTKMTDE EIMEKLRTIV SIGDPKKKYT 250
RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE 300
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR 350
ECLQALEFLH ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR 400
STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE PPYLNENPLR 450
ALYLIATNGT PELQNPEKLS PIFRDFLNRC LEMDVEKRGS AKELLQHPFL 500
KLAKPLSSLT PLIMAAKEAM KSNR 524
Length:524
Mass (Da):58,043
Last modified:April 3, 2007 - v3
Checksum:i00A7CD15F93D4180
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901A → T in AAA75468. 1 Publication
Sequence conflicti150 – 1501F → L in AAA65442. 1 Publication
Sequence conflicti225 – 2251T → P in AAA65442. 1 Publication
Sequence conflicti258 – 2581G → R in AAH69613. 1 Publication
Sequence conflicti329 – 3291G → R in AAA75468. 1 Publication
Sequence conflicti338 – 3381T → TA in AAA65442. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24153 mRNA. Translation: AAA65442.1.
BC069613 mRNA. Translation: AAH69613.1.
U25975 mRNA. Translation: AAA75468.1.
CCDSiCCDS3321.1.
PIRiS58682.
RefSeqiNP_002568.2. NM_002577.4.
UniGeneiHs.518530.

Genome annotation databases

EnsembliENST00000327134; ENSP00000314067; ENSG00000180370.
GeneIDi5062.
KEGGihsa:5062.
UCSCiuc003fwy.4. human.

Polymorphism databases

DMDMi143811432.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24153 mRNA. Translation: AAA65442.1 .
BC069613 mRNA. Translation: AAH69613.1 .
U25975 mRNA. Translation: AAA75468.1 .
CCDSi CCDS3321.1.
PIRi S58682.
RefSeqi NP_002568.2. NM_002577.4.
UniGenei Hs.518530.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PCS X-ray 2.86 E/F/G/H 121-136 [» ]
ProteinModelPortali Q13177.
SMRi Q13177. Positions 69-143, 228-519.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111098. 53 interactions.
DIPi DIP-38249N.
IntActi Q13177. 31 interactions.
MINTi MINT-235655.
STRINGi 9606.ENSP00000314067.

Chemistry

BindingDBi Q13177.
ChEMBLi CHEMBL4487.
GuidetoPHARMACOLOGYi 2134.

PTM databases

PhosphoSitei Q13177.

Polymorphism databases

DMDMi 143811432.

2D gel databases

OGPi Q13177.

Proteomic databases

MaxQBi Q13177.
PaxDbi Q13177.
PRIDEi Q13177.

Protocols and materials databases

DNASUi 5062.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327134 ; ENSP00000314067 ; ENSG00000180370 .
GeneIDi 5062.
KEGGi hsa:5062.
UCSCi uc003fwy.4. human.

Organism-specific databases

CTDi 5062.
GeneCardsi GC03P196466.
H-InvDB HIX0030815.
HGNCi HGNC:8591. PAK2.
HPAi CAB007794.
HPA036205.
MIMi 605022. gene.
neXtProti NX_Q13177.
PharmGKBi PA32918.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000234202.
HOVERGENi HBG108518.
InParanoidi Q13177.
KOi K04410.
OMAi FSGAEKG.
PhylomeDBi Q13177.
TreeFami TF105351.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_11068. Nef and signal transduction.
REACT_12623. Generation of second messenger molecules.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13528. Regulation of PAK-2p34 activity by PS-GAP/RHG10.
REACT_13532. Stimulation of the cell death response by PAK-2p34.
REACT_163701. FCERI mediated MAPK activation.
REACT_19226. Activation of Rac.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19238. CD28 dependent Vav1 pathway.
SignaLinki Q13177.

Miscellaneous databases

ChiTaRSi PAK2. human.
EvolutionaryTracei Q13177.
GeneWikii PAK2.
GenomeRNAii 5062.
NextBioi 19496.
PMAP-CutDB Q13177.
PROi Q13177.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13177.
Bgeei Q13177.
CleanExi HS_PAK2.
Genevestigatori Q13177.

Family and domain databases

Gene3Di 3.90.810.10. 1 hit.
InterProi IPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Sells M., Knause U.J., Bagrodia S., Ambrose D., Bokoch G.M., Chernoff J.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20."
    Martin G.A., Bollag G., McCormick F., Abo A.
    EMBO J. 14:1970-1978(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-524, PROTEIN SEQUENCE OF 401-417.
    Tissue: Placenta.
  4. Erratum
    Martin G.A., Bollag G., McCormick F., Abo A.
    EMBO J. 14:4385-4385(1995) [PubMed] [Europe PMC] [Abstract]
  5. "Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation."
    Benner G.E., Dennis P.B., Masaracchia R.A.
    J. Biol. Chem. 270:21121-21128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  6. "Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2."
    Rudel T., Bokoch G.M.
    Science 276:1571-1574(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CASPASE-3 CLEAVAGE AT ASP-512, FUNCTION, MUTAGENESIS OF ASP-212.
  7. "Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity."
    Walter B.N., Huang Z., Jakobi R., Tuazon P.T., Alnemri E.S., Litwack G., Traugh J.A.
    J. Biol. Chem. 273:28733-28739(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CASPASE-3 CLEAVAGE AT ASP-512, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-278 AND THR-402.
  8. Cited for: INTERACTION WITH HIV-1 NEF.
  9. "Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation."
    Jakobi R., McCarthy C.C., Koeppel M.A., Stringer D.K.
    J. Biol. Chem. 278:38675-38685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PAK-2P34), UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 239-ILE--GLY-243 AND 246-LYS--LYS-248.
  10. "Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk."
    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.
    J. Biol. Chem. 279:38649-38657(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MKNK1.
  11. "Identification and characterization of PS-GAP as a novel regulator of caspase-activated PAK-2."
    Koeppel M.A., McCarthy C.C., Moertl E., Jakobi R.
    J. Biol. Chem. 279:53653-53664(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP10, SUBCELLULAR LOCATION.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome."
    Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K.
    EMBO Rep. 7:186-191(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3MD4.
  14. "Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events."
    Vilas G.L., Corvi M.M., Plummer G.J., Seime A.M., Lambkin G.R., Berthiaume L.G.
    Proc. Natl. Acad. Sci. U.S.A. 103:6542-6547(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PAK-2P34), MYRISTOYLATION AT GLY-213 (PAK-2P34), SUBCELLULAR LOCATION.
  15. Cited for: INTERACTION WITH SCRIB.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-141 AND THR-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Dual role of Cdc42 in spindle orientation control of adherent cells."
    Mitsushima M., Toyoshima F., Nishida E.
    Mol. Cell. Biol. 29:2816-2827(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF7 AND GIT1.
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration."
    Hsu R.M., Tsai M.H., Hsieh Y.J., Lyu P.C., Yu J.S.
    Mol. Biol. Cell 21:287-301(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Mechanistic studies of the autoactivation of PAK2: a two-step model of cis initiation followed by trans amplification."
    Wang J., Wu J.W., Wang Z.X.
    J. Biol. Chem. 286:2689-2695(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  25. "Identification of the atypical MAPK Erk3 as a novel substrate for p21-activated kinase (Pak) activity."
    De la Mota-Peynado A., Chernoff J., Beeser A.
    J. Biol. Chem. 286:13603-13611(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6.
  26. "P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 threonine sites promotes cell transformation."
    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.
    Carcinogenesis 32:659-666(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF JUN.
  27. "Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly."
    Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z.
    Genes Dev. 25:1359-1364(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H4.
  28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-141 AND THR-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold."
    Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C., Bresson S.M., Tomchick D.R., Alto N.M.
    Nature 469:107-111(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 121-136.

Entry informationi

Entry nameiPAK2_HUMAN
AccessioniPrimary (citable) accession number: Q13177
Secondary accession number(s): Q13154, Q6ISC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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