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Protein

Serine/threonine-protein kinase PAK 1

Gene

Pak1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Enzyme regulationi

Phosphorylation of Thr-84 by OXSR1 inhibits activation (By similarity). Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, and enables activation by phosphorylation of Thr-422.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei298 – 2981ATPPROSITE-ProRule annotation
Active sitei388 – 3881Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi275 – 2839ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • collagen binding Source: UniProtKB
  • MAP kinase kinase kinase activity Source: RGD
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: RGD
  • protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of MAPKK activity Source: GOC
  • apoptotic process Source: UniProtKB-KW
  • branching morphogenesis of an epithelial tube Source: UniProtKB
  • cellular response to insulin stimulus Source: RGD
  • exocytosis Source: UniProtKB-KW
  • intracellular signal transduction Source: RGD
  • MAPK cascade Source: GOC
  • negative regulation of cell proliferation involved in contact inhibition Source: UniProtKB
  • neuron projection morphogenesis Source: RGD
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  • positive regulation of JUN kinase activity Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: RGD
  • response to hypoxia Source: RGD
  • response to organic substance Source: RGD
  • small GTPase mediated signal transduction Source: RGD
  • wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Exocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 5301.
ReactomeiR-RNO-202433. Generation of second messenger molecules.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-376172. DSCAM interactions.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-3928664. Ephrin signaling.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445144. Signal transduction by L1.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5621575. CD209 (DC-SIGN) signaling.
R-RNO-5627123. RHO GTPases activate PAKs.
R-RNO-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 1 (EC:2.7.11.1)
Alternative name(s):
Alpha-PAK
Protein kinase MUK2
p21-activated kinase 1
Short name:
PAK-1
p68-PAK
Gene namesi
Name:Pak1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3250. Pak1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell junctionfocal adhesion By similarity
  • Cell membrane By similarity
  • Cell projectionruffle membrane By similarity
  • Cell projectioninvadopodium By similarity

  • Note: Recruited to the cell membrane by interaction with CDC42 and RAC1. Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Colocalizes with RUFY3, F-actin and other core migration components in invadopodia at the cell periphery (By similarity).By similarity

GO - Cellular componenti

  • axon Source: RGD
  • cell-cell junction Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • dendrite Source: RGD
  • focal adhesion Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB
  • intercalated disc Source: RGD
  • invadopodium Source: UniProtKB
  • membrane Source: RGD
  • nuclear membrane Source: RGD
  • plasma membrane Source: UniProtKB
  • protein complex Source: Ensembl
  • ruffle Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
  • Z disc Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-86. Reduces NMDA receptor-mediated synaptic currents; when associated with L-86 and R-299. 2 Publications
Mutagenesisi84 – 841T → A: Constitutively active. 1 Publication
Mutagenesisi84 – 841T → E: Inhibits activation by binding to CDC42. 1 Publication
Mutagenesisi86 – 861H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83. Reduces NMDA receptor-mediated synaptic currents; when associated with L-83 and R-299. 2 Publications
Mutagenesisi107 – 1071L → F: Abolishes autoinhibition, leading to constitutive kinase activation. 1 Publication
Mutagenesisi144 – 1441S → A: Decreases activity; when associated with A-149. 1 Publication
Mutagenesisi149 – 1491S → A: Decreases activity; when associated with A-144. 1 Publication
Mutagenesisi298 – 2981K → R: Reduces NMDA receptor-mediated synaptic currents; when associated with L-83 and L-86. 1 Publication
Mutagenesisi404 – 4041L → S: Decreases kinase activity. 1 Publication
Mutagenesisi422 – 4221T → A: Decreases activity. 3 Publications
Mutagenesisi422 – 4221T → E: Increases constitutive activity. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 544543Serine/threonine-protein kinase PAK 1PRO_0000086462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei21 – 211Phosphoserine; by PKB and autocatalysis1 Publication
Modified residuei57 – 571Phosphoserine; by autocatalysis1 Publication
Modified residuei84 – 841Phosphothreonine; by OXSR11 Publication
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei131 – 1311PhosphotyrosineBy similarity
Modified residuei142 – 1421PhosphotyrosineBy similarity
Modified residuei144 – 1441Phosphoserine; by autocatalysis1 Publication
Modified residuei149 – 1491Phosphoserine; by autocatalysis1 Publication
Modified residuei153 – 1531Phosphotyrosine; by JAK2By similarity
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei184 – 1841PhosphothreonineBy similarity
Modified residuei198 – 1981Phosphoserine; by autocatalysis1 Publication
Modified residuei200 – 2001Phosphotyrosine; by JAK2By similarity
Modified residuei203 – 2031Phosphoserine; by autocatalysis1 Publication
Modified residuei211 – 2111PhosphothreonineBy similarity
Modified residuei218 – 2181PhosphothreonineBy similarity
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei222 – 2221PhosphoserineCombined sources
Modified residuei224 – 2241PhosphothreonineBy similarity
Modified residuei228 – 2281PhosphothreonineBy similarity
Modified residuei229 – 2291PhosphothreonineBy similarity
Modified residuei284 – 2841Phosphotyrosine; by JAK2By similarity
Modified residuei422 – 4221Phosphothreonine; by autocatalysis, BRSK2 and PDPK13 Publications

Post-translational modificationi

Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-422 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-422 by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites (By similarity). Activated by phosphorylation at Thr-422 by BRSK2.By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP35465.
PRIDEiP35465.

PTM databases

iPTMnetiP35465.
PhosphoSiteiP35465.

Expressioni

Tissue specificityi

Expressed predominantly in the brain, with higher expression in neuronal groups associated with motor function, and at lower levels in the spleen.1 Publication

Developmental stagei

Found in the embryonic CNS with little expression elsewhere.

Gene expression databases

GenevisibleiP35465. RN.

Interactioni

Subunit structurei

Homodimer in its autoinhibited state. Active as monomer. Component of cytoplasmic complexes, which also contains PXN, ARHGEF6 and GIT1. Interacts with NISCH. Interacts with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins. Interacts with ARHGEF7. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1. Interacts with SCRIB. Interacts with PDPK1. Interacts (via kinase domain) with RAF1. Interacts with NCK1 and NCK2. Interacts with TBCB. Interacts with CRIPAK. Interacts with BRSK2 (By similarity). Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1. Interacts with SNAI1. Interacts with CIB1 (via N-terminal region); the interaction is direct, promotes PAK1 activity and occurs in a calcium-dependent manner (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
VimP201522EBI-444379,EBI-299269From a different organism.

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi248078. 1 interaction.
DIPiDIP-32990N.
IntActiP35465. 5 interactions.
MINTiMINT-124033.
STRINGi10116.ENSRNOP00000045832.

Structurei

Secondary structure

1
544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi88 – 903Combined sources
Helixi91 – 933Combined sources
Beta strandi95 – 984Combined sources
Helixi101 – 1066Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi113 – 1153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0ANMR-B75-118[»]
ProteinModelPortaliP35465.
SMRiP35465. Positions 78-147, 248-540.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35465.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 8814CRIBPROSITE-ProRule annotationAdd
BLAST
Domaini269 – 520252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 14071Autoregulatory regionAdd
BLAST
Regioni70 – 10536GTPase-bindingAdd
BLAST
Regioni132 – 269138Interaction with CRIPAKBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
InParanoidiP35465.
KOiK04409.
OMAiNSSNTLX.
OrthoDBiEOG7CK36J.
PhylomeDBiP35465.
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.
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.

P35465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNNGLDVQD KPPAPPMRNT STMIGAGSKD PGTLNHGSKP LPPNPEEKKK
60 70 80 90 100
KDRFYRSILA GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP
110 120 130 140 150
EQWARLLQTS NITKSEQKKN PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA
160 170 180 190 200
EDYNSSNTLN VKTVSETPAV PPVSEDEDDD DDATPPPVIA PRPEHTKSVY
210 220 230 240 250
TRSVIEPLPV TPTRDVATSP ISPTENNTTP PDALTRNTEK QKKKPKMSDE
260 270 280 290 300
EILEKLRSIV SVGDPKKKYT RFEKIGQGAS GTVYTAMDVA TGQEVAIKQM
310 320 330 340 350
NLQQQPKKEL IINEILVMRE NKNPNIVNYL DSYLVGDELW VVMEYLAGGS
360 370 380 390 400
LTDVVTETCM DEGQIAAVCR ECLQALEFLH SNQVIHRDIK SDNILLGMDG
410 420 430 440 450
SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY GPKVDIWSLG
460 470 480 490 500
IMAIEMIEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS AIFRDFLNRC
510 520 530 540
LEMDVEKRGS AKELLQHQFL KIAKPLSSLT PLIAAAKEAT KNNH
Length:544
Mass (Da):60,578
Last modified:December 15, 1998 - v3
Checksum:i93BE32D8222F5B7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23443 mRNA. Translation: AAB95646.1.
U49953 mRNA. Translation: AAB61533.1.
PIRiS40482.
RefSeqiNP_058894.1. NM_017198.1.
XP_006229814.1. XM_006229752.1.
XP_006229815.1. XM_006229753.1.
XP_006229816.1. XM_006229754.2.
UniGeneiRn.9149.

Genome annotation databases

EnsembliENSRNOT00000049321; ENSRNOP00000045832; ENSRNOG00000029784.
ENSRNOT00000091952; ENSRNOP00000073036; ENSRNOG00000029784.
GeneIDi29431.
KEGGirno:29431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23443 mRNA. Translation: AAB95646.1.
U49953 mRNA. Translation: AAB61533.1.
PIRiS40482.
RefSeqiNP_058894.1. NM_017198.1.
XP_006229814.1. XM_006229752.1.
XP_006229815.1. XM_006229753.1.
XP_006229816.1. XM_006229754.2.
UniGeneiRn.9149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0ANMR-B75-118[»]
ProteinModelPortaliP35465.
SMRiP35465. Positions 78-147, 248-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248078. 1 interaction.
DIPiDIP-32990N.
IntActiP35465. 5 interactions.
MINTiMINT-124033.
STRINGi10116.ENSRNOP00000045832.

PTM databases

iPTMnetiP35465.
PhosphoSiteiP35465.

Proteomic databases

PaxDbiP35465.
PRIDEiP35465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049321; ENSRNOP00000045832; ENSRNOG00000029784.
ENSRNOT00000091952; ENSRNOP00000073036; ENSRNOG00000029784.
GeneIDi29431.
KEGGirno:29431.

Organism-specific databases

CTDi5058.
RGDi3250. Pak1.

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00840000129718.
HOGENOMiHOG000234202.
HOVERGENiHBG108518.
InParanoidiP35465.
KOiK04409.
OMAiNSSNTLX.
OrthoDBiEOG7CK36J.
PhylomeDBiP35465.
TreeFamiTF105351.

Enzyme and pathway databases

BRENDAi2.7.11.1. 5301.
ReactomeiR-RNO-202433. Generation of second messenger molecules.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-376172. DSCAM interactions.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-3928664. Ephrin signaling.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445144. Signal transduction by L1.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5621575. CD209 (DC-SIGN) signaling.
R-RNO-5627123. RHO GTPases activate PAKs.
R-RNO-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

EvolutionaryTraceiP35465.
NextBioi609154.
PROiP35465.

Gene expression databases

GenevisibleiP35465. RN.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A brain serine/threonine protein kinase activated by Cdc42 and Rac1."
    Manser E., Leung T., Salihuddin H., Zhao Z.-S., Lim L.
    Nature 367:40-46(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Zhao Z.-S.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Osada S., Izawa M., Saito R., Mizuno K., Suzuki A., Hirai S., Ohno S.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family."
    Manser E., Chong C., Zhao Z.-S., Leung T., Michael G., Hall C., Lim L.
    J. Biol. Chem. 270:25070-25078(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes."
    Manser E., Huang H.Y., Loo T.H., Chen X.Q., Dong J.M., Leung T., Lim L.
    Mol. Cell. Biol. 17:1129-1143(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH CDC42 AND RAC1, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-404 AND THR-422, PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-21; SER-57; SER-144; SER-149; SER-198; SER-203 AND THR-422.
  6. "Delineation of the Cdc42/Rac-binding domain of p21-activated kinase."
    Thompson G., Owen D., Chalk P.A., Lowe P.N.
    Biochemistry 37:7885-7891(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN GTPASE BINDING.
  7. "Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation."
    Frost J.A., Khokhlatchev A., Stippec S., White M.A., Cobb M.H.
    J. Biol. Chem. 273:28191-28198(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AUTOREGULATORY REGION, MUTAGENESIS OF HIS-83; HIS-86 AND LEU-107.
  8. "A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1."
    Zhao Z.S., Manser E., Chen X.Q., Chong C., Leung T., Lim L.
    Mol. Cell. Biol. 18:2153-2163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOREGULATORY DOMAIN.
  9. "The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity."
    Chong C., Tan L., Lim L., Manser E.
    J. Biol. Chem. 276:17347-17353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-144; SER-149 AND THR-422.
  10. Cited for: FUNCTION.
  11. "Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily."
    Chen W., Yazicioglu M., Cobb M.H.
    J. Biol. Chem. 279:11129-11136(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH OXSR1, PHOSPHORYLATION AT THR-84, MUTAGENESIS OF THR-84.
  12. "Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
    Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
    Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Synapses of amphids defective (SAD-A) kinase promotes glucose-stimulated insulin secretion through activation of p21-activated kinase (PAK1) in pancreatic beta-Cells."
    Nie J., Sun C., Faruque O., Ye G., Li J., Liang Q., Chang Z., Yang W., Han X., Shi Y.
    J. Biol. Chem. 287:26435-26444(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-422.
  14. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Shank3 deficiency induces NMDA receptor hypofunction via an actin-dependent mechanism."
    Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T., Yan Z.
    J. Neurosci. 33:15767-15778(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIN POLYMERIZATION, PHOSPHORYLATION AT THR-422, MUTAGENESIS OF HIS-83; HIS-86; LYS-298 AND THR-422.
  16. Cited for: STRUCTURE BY NMR OF 75-118 IN COMPLEX WITH CDC42, INTERACTION WITH CDC42.

Entry informationi

Entry nameiPAK1_RAT
AccessioniPrimary (citable) accession number: P35465
Secondary accession number(s): Q62934
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: May 11, 2016
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.