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Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (p21-activated kinase 1) (PAK-1) (p65-PAK)

 PAK1_HUMAN              Reviewed;         545 AA.
Q13153; O75561; Q13567; Q32M53; Q32M54; Q86W79;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
25-OCT-2017, entry version 199.
RecName: Full=Serine/threonine-protein kinase PAK 1 {ECO:0000303|PubMed:8805275};
EC=2.7.11.1 {ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:9032240};
AltName: Full=Alpha-PAK {ECO:0000303|PubMed:9528787};
AltName: Full=p21-activated kinase 1 {ECO:0000303|PubMed:9395435};
Short=PAK-1;
AltName: Full=p65-PAK {ECO:0000250|UniProtKB:P35465};
Name=PAK1 {ECO:0000312|HGNC:HGNC:8590};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Placenta;
PubMed=8805275; DOI=10.1016/S0960-9822(02)00546-8;
Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J.;
"Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
pathway.";
Curr. Biol. 6:598-605(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=9395435; DOI=10.1016/S0960-9822(97)70091-5;
Sells M.A., Knaus U.G., Bagrodia S., Ambrose D.M., Bokoch G.M.,
Chernoff J.;
"Human p21-activated kinase (Pak1) regulates actin organization in
mammalian cells.";
Curr. Biol. 7:202-210(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Reid T., Aspenstroem P., Bertoglio J.;
"Human PAK1B.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION,
AND SUBCELLULAR LOCATION.
PubMed=9032240; DOI=10.1128/MCB.17.3.1129;
Manser E., Huang H.Y., Loo T.H., Chen X.Q., Dong J.M., Leung T.,
Lim L.;
"Expression of constitutively active alpha-PAK reveals effects of the
kinase on actin and focal complexes.";
Mol. Cell. Biol. 17:1129-1143(1997).
[7]
MUTAGENESIS OF HIS-83 AND HIS-86.
PubMed=9774440; DOI=10.1074/jbc.273.43.28191;
Frost J.A., Khokhlatchev A., Stippec S., White M.A., Cobb M.H.;
"Differential effects of PAK1-activating mutations reveal activity-
dependent and -independent effects on cytoskeletal regulation.";
J. Biol. Chem. 273:28191-28198(1998).
[8]
FUNCTION, AND AUTOREGULATORY DOMAIN.
PubMed=9528787; DOI=10.1128/MCB.18.4.2153;
Zhao Z.S., Manser E., Chen X.Q., Chong C., Leung T., Lim L.;
"A conserved negative regulatory region in alphaPAK: inhibition of PAK
kinases reveals their morphological roles downstream of Cdc42 and
Rac1.";
Mol. Cell. Biol. 18:2153-2163(1998).
[9]
INTERACTION WITH NCK1 AND NCK2.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[10]
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AUTOREGULATORY REGION,
FUNCTION, INTERACTION WITH CDC42, PHOSPHORYLATION AT THR-423, AND
MUTAGENESIS OF HIS-83; HIS-86; LEU-107 AND THR-423.
PubMed=10551809; DOI=10.1074/jbc.274.46.32565;
Zenke F.T., King C.C., Bohl B.P., Bokoch G.M.;
"Identification of a central phosphorylation site in p21-activated
kinase regulating autoinhibition and kinase activity.";
J. Biol. Chem. 274:32565-32573(1999).
[11]
PHOSPHORYLATION AT THR-423 BY PDPK1, INTERACTION WITH PDPK1, AND
ENZYME REGULATION.
PubMed=10995762; DOI=10.1074/jbc.M006553200;
King C.C., Gardiner E.M., Zenke F.T., Bohl B.P., Newton A.C.,
Hemmings B.A., Bokoch G.M.;
"p21-activated kinase (PAK1) is phosphorylated and activated by 3-
phosphoinositide-dependent kinase-1 (PDK1).";
J. Biol. Chem. 275:41201-41209(2000).
[12]
FUNCTION IN PHOSPHORYLATION OF RAF1, AND INTERACTION WITH RAF1.
PubMed=11733498; DOI=10.1074/jbc.M110000200;
Zang M., Hayne C., Luo Z.;
"Interaction between active Pak1 and Raf-1 is necessary for
phosphorylation and activation of Raf-1.";
J. Biol. Chem. 277:4395-4405(2002).
[13]
SUBUNIT, AND ENZYME REGULATION.
PubMed=11804587; DOI=10.1016/S1097-2765(01)00428-2;
Parrini M.C., Lei M., Harrison S.C., Mayer B.J.;
"Pak1 kinase homodimers are autoinhibited in trans and dissociated
upon activation by Cdc42 and Rac1.";
Mol. Cell 9:73-83(2002).
[14]
FUNCTION, AND INTERACTION WITH CDC2L1 AND CDC2L2.
PubMed=12624090; DOI=10.1074/jbc.M300818200;
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S.,
Zong H., Hu Y., Yuan Z., Shen Z., Gu J.;
"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein
kinase (p110C) associates with p21-activated kinase 1 and inhibits its
activity during anoikis.";
J. Biol. Chem. 278:20029-20036(2003).
[15]
FUNCTION.
PubMed=12876277; DOI=10.1083/jcb.200212141;
Slack-Davis J.K., Eblen S.T., Zecevic M., Boerner S.A.,
Tarcsafalvi A., Diaz H.B., Marshall M.S., Weber M.J., Parsons J.T.,
Catling A.D.;
"PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK
activation.";
J. Cell Biol. 162:281-291(2003).
[16]
PHOSPHORYLATION AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, INTERACTION WITH NCK1, AND SUBCELLULAR LOCATION.
PubMed=14585966; DOI=10.1128/MCB.23.22.8058-8069.2003;
Zhou G.L., Zhuo Y., King C.C., Fryer B.H., Bokoch G.M., Field J.;
"Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and
cell migration.";
Mol. Cell. Biol. 23:8058-8069(2003).
[17]
INTERACTION WITH DSCAM.
PubMed=15169762; DOI=10.1074/jbc.M401878200;
Li W., Guan K.L.;
"The Down syndrome cell adhesion molecule (DSCAM) interacts with and
activates Pak.";
J. Biol. Chem. 279:32824-32831(2004).
[18]
FUNCTION, AND INTERACTION WITH SNAI1.
PubMed=15833848; DOI=10.1158/0008-5472.CAN-05-0236;
Yang Z., Rayala S., Nguyen D., Vadlamudi R.K., Chen S., Kumar R.;
"Pak1 phosphorylation of snail, a master regulator of epithelial-to-
mesenchyme transition, modulates snail's subcellular localization and
functions.";
Cancer Res. 65:3179-3184(2005).
[19]
FUNCTION.
PubMed=15611088; DOI=10.1074/jbc.M411900200;
Zhou H., Kramer R.H.;
"Integrin engagement differentially modulates epithelial cell motility
by RhoA/ROCK and PAK1.";
J. Biol. Chem. 280:10624-10635(2005).
[20]
INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
PubMed=16061695; DOI=10.1083/jcb.200502090;
Leisner T.M., Liu M., Jaffer Z.M., Chernoff J., Parise L.V.;
"Essential role of CIB1 in regulating PAK1 activation and cell
migration.";
J. Cell Biol. 170:465-476(2005).
[21]
FUNCTION, AND INTERACTION WITH TBCB.
PubMed=15831477; DOI=10.1128/MCB.25.9.3726-3736.2005;
Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S.,
Marcus S., Goodson H.V., Sahin A.A., Kumar R.;
"p21-activated kinase 1 regulates microtubule dynamics by
phosphorylating tubulin cofactor B.";
Mol. Cell. Biol. 25:3726-3736(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[23]
FUNCTION, AND INTERACTION WITH CRIPAK.
PubMed=16278681; DOI=10.1038/sj.onc.1209172;
Talukder A.H., Meng Q., Kumar R.;
"CRIPak, a novel endogenous Pak1 inhibitor.";
Oncogene 25:1311-1319(2006).
[24]
FUNCTION, PHOSPHORYLATION AT TYR-153; TYR-201 AND TYR-285, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17726028; DOI=10.1074/jbc.M701794200;
Rider L., Shatrova A., Feener E.P., Webb L., Diakonova M.;
"JAK2 tyrosine kinase phosphorylates PAK1 and regulates PAK1 activity
and functions.";
J. Biol. Chem. 282:30985-30996(2007).
[25]
FUNCTION, PHOSPHORYLATION AT SER-21; SER-57; TYR-131; TYR-142;
TYR-153; SER-174; THR-185; THR-212 AND TYR-285, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=17989089; DOI=10.1242/jcs.008177;
Mayhew M.W., Jeffery E.D., Sherman N.E., Nelson K., Polefrone J.M.,
Pratt S.J., Shabanowitz J., Parsons J.T., Fox J.W., Hunt D.F.,
Horwitz A.F.;
"Identification of phosphorylation sites in betaPIX and PAK1.";
J. Cell Sci. 120:3911-3918(2007).
[26]
INTERACTION WITH RAC1 AND CDC42.
PubMed=18325335; DOI=10.1016/j.febslet.2008.01.064;
Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H.,
Nishino I., Hayashi Y.K.;
"Affixin activates Rac1 via betaPIX in C2C12 myoblast.";
FEBS Lett. 582:1189-1196(2008).
[27]
INTERACTION WITH SCRIB.
PubMed=18716323; DOI=10.1093/hmg/ddn248;
Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
Navarro C., Rachel R., Montcouquiol M., Sans N.,
Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
"Scrib regulates PAK activity during the cell migration process.";
Hum. Mol. Genet. 17:3552-3565(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; THR-212; THR-219;
SER-220 AND THR-230, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-149; SER-174;
SER-223 AND THR-230, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
FUNCTION, INTERACTION WITH BRSK2, AND PHOSPHORYLATION AT THR-423.
PubMed=22669945; DOI=10.1074/jbc.M112.378372;
Nie J., Sun C., Faruque O., Ye G., Li J., Liang Q., Chang Z., Yang W.,
Han X., Shi Y.;
"Synapses of amphids defective (SAD-A) kinase promotes glucose-
stimulated insulin secretion through activation of p21-activated
kinase (PAK1) in pancreatic beta-Cells.";
J. Biol. Chem. 287:26435-26444(2012).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
INTERACTION WITH CIB1 ISOFORM 2.
TISSUE=Brain;
PubMed=23503467; DOI=10.1038/onc.2013.43;
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V.,
Vandoninck S., Van Lint J., Illing A., Seufferlein T.;
"A novel splice variant of calcium and integrin-binding protein 1
mediates protein kinase D2-stimulated tumour growth by regulating
angiogenesis.";
Oncogene 33:1167-1180(2014).
[38]
FUNCTION, AND PHOSPHORYLATION.
PubMed=23633677; DOI=10.1126/scisignal.2003627;
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A.,
Bonecchi R., Locati M.;
"Beta-arrestin-dependent activation of the cofilin pathway is required
for the scavenging activity of the atypical chemokine receptor D6.";
Sci. Signal. 6:RA30-RA30(2013).
[39]
FUNCTION, COLOCALIZATION WITH RUFY3, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=25766321; DOI=10.1038/cddis.2015.50;
Wang G., Zhang Q., Song Y., Wang X., Guo Q., Zhang J., Li J., Han Y.,
Miao Z., Li F.;
"PAK1 regulates RUFY3-mediated gastric cancer cell migration and
invasion.";
Cell Death Dis. 6:E1682-E1682(2015).
[40]
INTERACTION WITH INPP5K.
PubMed=26940976; DOI=10.1111/gtc.12353;
Ijuin T., Hatano N., Takenawa T.;
"Glucose-regulated protein 78 (GRP78) binds directly to PIP3
phosphatase SKIP and determines its localization.";
Genes Cells 21:457-465(2016).
[41]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 70-545.
PubMed=10975528; DOI=10.1016/S0092-8674(00)00043-X;
Lei M., Lu W., Meng W., Parrini M.C., Eck M.J., Mayer B.J.,
Harrison S.C.;
"Structure of PAK1 in an autoinhibited conformation reveals a
multistage activation switch.";
Cell 102:387-397(2000).
[42]
STRUCTURE BY NMR OF 183-204 IN COMPLEX WITH ARHGEF7, AND INTERACTION
WITH ARHGEF7.
PubMed=16101281; DOI=10.1021/bi050374a;
Mott H.R., Nietlispach D., Evetts K.A., Owen D.;
"Structural analysis of the SH3 domain of beta-PIX and its interaction
with alpha-p21 activated kinase (PAK).";
Biochemistry 44:10977-10983(2005).
[43]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-545, AND ENZYME
REGULATION.
PubMed=15893667; DOI=10.1016/j.str.2005.03.007;
Lei M., Robinson M.A., Harrison S.C.;
"The active conformation of the PAK1 kinase domain.";
Structure 13:769-778(2005).
[44]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 248-545 OF MUTANT ARG-299 IN
COMPLEX WITH ATP ANALOG AMP-PNP, MUTAGENESIS OF LYS-299 AND ASP-389,
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, AND PHOSPHORYLATION
AT THR-423.
PubMed=22153498; DOI=10.1016/j.str.2011.10.013;
Wang J., Wu J.W., Wang Z.X.;
"Structural insights into the autoactivation mechanism of p21-
activated protein kinase.";
Structure 19:1752-1761(2011).
-!- FUNCTION: 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
(PubMed:25766321). {ECO:0000269|PubMed:10551809,
ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:12624090,
ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14585966,
ECO:0000269|PubMed:15611088, ECO:0000269|PubMed:15831477,
ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:16278681,
ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089,
ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677,
ECO:0000269|PubMed:25766321, ECO:0000269|PubMed:8805275,
ECO:0000269|PubMed:9032240, ECO:0000269|PubMed:9395435,
ECO:0000269|PubMed:9528787}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:22153498,
ECO:0000269|PubMed:9032240}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: 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-423.
{ECO:0000250|UniProtKB:P35465, ECO:0000269|PubMed:10995762,
ECO:0000269|PubMed:11804587, ECO:0000269|PubMed:15893667,
ECO:0000269|PubMed:9032240}.
-!- SUBUNIT: Homodimer in its autoinhibited state. Active as monomer.
Component of cytoplasmic complexes, which also contains PXN,
ARHGEF6 and GIT1. Interacts with NISCH (By similarity). Interacts
with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary
complex involved in AChR clustering (By similarity). Binds to the
caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not
the full-length proteins (PubMed:12624090). Interacts with ARHGEF7
(PubMed:16101281). Interacts tightly with GTP-bound but not GDP-
bound CDC42/P21 and RAC1 (By similarity). 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 (PubMed:15169762). Interacts with
SCRIB (PubMed:18716323). Interacts with PDPK1 (PubMed:10995762).
Interacts (via kinase domain) with RAF1 (PubMed:11733498).
Interacts with NCK1 and NCK2 (PubMed:10026169). Interacts with
TBCB (PubMed:15831477). Interacts with CRIPAK (PubMed:16278681).
Interacts with BRSK2 (By similarity). Interacts with SNAI1
(PubMed:15833848). Interacts with CIB1 isoform 2
(PubMed:23503467). Interacts with CIB1 (via N-terminal region);
the interaction is direct, promotes PAK1 activity and occurs in a
calcium-dependent manner. Interacts with INPP5K (PubMed:26940976).
{ECO:0000250|UniProtKB:O88643, ECO:0000250|UniProtKB:P35465,
ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:10551809,
ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:11733498,
ECO:0000269|PubMed:11804587, ECO:0000269|PubMed:12624090,
ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:15169762,
ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:15833848,
ECO:0000269|PubMed:16061695, ECO:0000269|PubMed:16101281,
ECO:0000269|PubMed:16278681, ECO:0000269|PubMed:18325335,
ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:22153498,
ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23503467,
ECO:0000269|PubMed:26940976}.
-!- INTERACTION:
Q14155:ARHGEF7; NbExp=7; IntAct=EBI-1307, EBI-717515;
P60953:CDC42; NbExp=12; IntAct=EBI-1307, EBI-81752;
P60766:Cdc42 (xeno); NbExp=3; IntAct=EBI-1307, EBI-81763;
P21127:CDK11B; NbExp=4; IntAct=EBI-1307, EBI-1298;
Q8N1N5:CRIPAK; NbExp=6; IntAct=EBI-1307, EBI-1205846;
Q9Y2X7:GIT1; NbExp=3; IntAct=EBI-1307, EBI-466061;
P53667:LIMK1; NbExp=5; IntAct=EBI-1307, EBI-444403;
O43639:NCK2; NbExp=6; IntAct=EBI-1307, EBI-713635;
Q15365:PCBP1; NbExp=5; IntAct=EBI-15628682, EBI-946095;
P63000:RAC1; NbExp=25; IntAct=EBI-1307, EBI-413628;
P63000-1:RAC1; NbExp=3; IntAct=EBI-1307, EBI-7212896;
P63001:Rac1 (xeno); NbExp=3; IntAct=EBI-1307, EBI-413646;
Q7L0Q8:RHOU; NbExp=2; IntAct=EBI-1019502, EBI-1638043;
Q5PP90:US3(L) (xeno); NbExp=2; IntAct=EBI-1307, EBI-15780451;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25766321}.
Cell junction, focal adhesion {ECO:0000269|PubMed:25766321}. Cell
membrane {ECO:0000269|PubMed:25766321}. Cell projection, ruffle
membrane {ECO:0000269|PubMed:25766321}. Cell projection,
invadopodium {ECO:0000269|PubMed:25766321}. Note=Colocalizes with
RUFY3, F-actin and other core migration components in invadopodia
at the cell periphery (PubMed:25766321). 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.
{ECO:0000250|UniProtKB:P35465, ECO:0000269|PubMed:25766321}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13153-1; Sequence=Displayed;
Name=2; Synonyms=PAK1B;
IsoId=Q13153-2; Sequence=VSP_017507;
-!- TISSUE SPECIFICITY: Overexpressed in gastric cancer cells and
tissues (at protein level) (PubMed:25766321).
{ECO:0000269|PubMed:25766321}.
-!- PTM: Autophosphorylated in trans, meaning that in a dimer, one
kinase molecule phosphorylates the other one. Activated by
autophosphorylation at Thr-423 in response to a conformation
change, triggered by interaction with GTP-bound CDC42 or RAC1.
Activated by phosphorylation at Thr-423 by BRSK2 and 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.
{ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762,
ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:17726028,
ECO:0000269|PubMed:17989089, ECO:0000269|PubMed:22153498,
ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PAK1ID41633ch11q13.html";
-----------------------------------------------------------------------
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EMBL; U51120; AAC50590.1; -; mRNA.
EMBL; U24152; AAA65441.1; -; mRNA.
EMBL; AF071884; AAC24716.1; -; mRNA.
EMBL; AP000486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC109299; AAI09300.1; -; mRNA.
CCDS; CCDS44687.1; -. [Q13153-2]
CCDS; CCDS8250.1; -. [Q13153-1]
PIR; G01773; G01773.
RefSeq; NP_001122092.1; NM_001128620.1. [Q13153-2]
RefSeq; NP_002567.3; NM_002576.4. [Q13153-1]
RefSeq; XP_011543382.1; XM_011545080.2. [Q13153-2]
RefSeq; XP_011543383.1; XM_011545081.2. [Q13153-2]
RefSeq; XP_011543384.1; XM_011545082.2. [Q13153-2]
RefSeq; XP_011543385.1; XM_011545083.2. [Q13153-2]
RefSeq; XP_011543386.1; XM_011545084.2. [Q13153-2]
RefSeq; XP_016873335.1; XM_017017846.1. [Q13153-1]
RefSeq; XP_016873336.1; XM_017017847.1. [Q13153-1]
RefSeq; XP_016873337.1; XM_017017848.1. [Q13153-1]
RefSeq; XP_016873338.1; XM_017017849.1. [Q13153-1]
RefSeq; XP_016873339.1; XM_017017850.1. [Q13153-1]
UniGene; Hs.435714; -.
PDB; 1F3M; X-ray; 2.30 A; A/B=70-149, C/D=249-545.
PDB; 1YHV; X-ray; 1.80 A; A=249-545.
PDB; 1YHW; X-ray; 1.80 A; A=249-545.
PDB; 1ZSG; NMR; -; B=183-204.
PDB; 2HY8; X-ray; 2.00 A; 1=249-545.
PDB; 2QME; X-ray; 1.75 A; I=74-109.
PDB; 3DVP; X-ray; 2.50 A; C/D=212-221.
PDB; 3FXZ; X-ray; 1.64 A; A=249-545.
PDB; 3FY0; X-ray; 2.35 A; A=249-545.
PDB; 3Q4Z; X-ray; 1.89 A; A/B=248-545.
PDB; 3Q52; X-ray; 1.80 A; A=248-545.
PDB; 3Q53; X-ray; 2.09 A; A=248-545.
PDB; 4DAW; X-ray; 2.00 A; A=249-545.
PDB; 4EQC; X-ray; 2.01 A; A=249-545.
PDB; 4O0R; X-ray; 2.40 A; A/B=249-545.
PDB; 4O0T; X-ray; 2.60 A; A/B=249-545.
PDB; 4P90; X-ray; 2.49 A; A/B=249-545.
PDB; 4ZJI; X-ray; 1.99 A; A/B/C/D=249-545.
PDB; 4ZJJ; X-ray; 2.20 A; A/B/C/D=249-545.
PDB; 4ZLO; X-ray; 2.50 A; A/B=249-545.
PDB; 4ZY4; X-ray; 2.60 A; A/B=249-545.
PDB; 4ZY5; X-ray; 2.35 A; A/B=249-545.
PDB; 4ZY6; X-ray; 2.15 A; A/B=249-545.
PDB; 5DEW; X-ray; 1.90 A; A/B=249-545.
PDB; 5DEY; X-ray; 2.10 A; A/B=249-545.
PDB; 5DFP; X-ray; 2.20 A; A=249-545.
PDB; 5IME; X-ray; 2.22 A; A/B=249-545.
PDB; 5KBQ; X-ray; 2.58 A; A/B=254-542.
PDB; 5KBR; X-ray; 2.36 A; A/B=254-542.
PDBsum; 1F3M; -.
PDBsum; 1YHV; -.
PDBsum; 1YHW; -.
PDBsum; 1ZSG; -.
PDBsum; 2HY8; -.
PDBsum; 2QME; -.
PDBsum; 3DVP; -.
PDBsum; 3FXZ; -.
PDBsum; 3FY0; -.
PDBsum; 3Q4Z; -.
PDBsum; 3Q52; -.
PDBsum; 3Q53; -.
PDBsum; 4DAW; -.
PDBsum; 4EQC; -.
PDBsum; 4O0R; -.
PDBsum; 4O0T; -.
PDBsum; 4P90; -.
PDBsum; 4ZJI; -.
PDBsum; 4ZJJ; -.
PDBsum; 4ZLO; -.
PDBsum; 4ZY4; -.
PDBsum; 4ZY5; -.
PDBsum; 4ZY6; -.
PDBsum; 5DEW; -.
PDBsum; 5DEY; -.
PDBsum; 5DFP; -.
PDBsum; 5IME; -.
PDBsum; 5KBQ; -.
PDBsum; 5KBR; -.
ProteinModelPortal; Q13153; -.
SMR; Q13153; -.
BioGrid; 111095; 87.
CORUM; Q13153; -.
DIP; DIP-31016N; -.
ELM; Q13153; -.
IntAct; Q13153; 66.
MINT; MINT-92897; -.
STRING; 9606.ENSP00000278568; -.
BindingDB; Q13153; -.
ChEMBL; CHEMBL4600; -.
GuidetoPHARMACOLOGY; 2133; -.
iPTMnet; Q13153; -.
PhosphoSitePlus; Q13153; -.
BioMuta; PAK1; -.
DMDM; 90111767; -.
EPD; Q13153; -.
MaxQB; Q13153; -.
PaxDb; Q13153; -.
PeptideAtlas; Q13153; -.
PRIDE; Q13153; -.
DNASU; 5058; -.
Ensembl; ENST00000278568; ENSP00000278568; ENSG00000149269. [Q13153-2]
Ensembl; ENST00000356341; ENSP00000348696; ENSG00000149269. [Q13153-1]
GeneID; 5058; -.
KEGG; hsa:5058; -.
UCSC; uc001oyg.5; human. [Q13153-1]
CTD; 5058; -.
DisGeNET; 5058; -.
EuPathDB; HostDB:ENSG00000149269.9; -.
GeneCards; PAK1; -.
HGNC; HGNC:8590; PAK1.
HPA; CAB005312; -.
HPA; HPA003565; -.
MIM; 602590; gene.
neXtProt; NX_Q13153; -.
OpenTargets; ENSG00000149269; -.
PharmGKB; PA32917; -.
eggNOG; KOG0578; Eukaryota.
eggNOG; ENOG410XP4K; LUCA.
GeneTree; ENSGT00900000140851; -.
HOGENOM; HOG000234202; -.
HOVERGEN; HBG108518; -.
InParanoid; Q13153; -.
KO; K04409; -.
OMA; AGTLNHG; -.
OrthoDB; EOG091G04H8; -.
PhylomeDB; Q13153; -.
TreeFam; TF105351; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-428540; Activation of Rac.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
SignaLink; Q13153; -.
SIGNOR; Q13153; -.
ChiTaRS; PAK1; human.
EvolutionaryTrace; Q13153; -.
GeneWiki; PAK1; -.
GenomeRNAi; 5058; -.
PRO; PR:Q13153; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149269; -.
CleanEx; HS_PAK1; -.
ExpressionAtlas; Q13153; baseline and differential.
Genevisible; Q13153; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
GO; GO:0071437; C:invadopodium; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IBA:GO_Central.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:CAFA.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IMP:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:CAFA.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0042060; P:wound healing; IMP:UniProtKB.
CDD; cd01093; CRIB_PAK_like; 1.
Gene3D; 3.90.810.10; -; 1.
InterPro; IPR000095; CRIB_dom.
InterPro; IPR036936; CRIB_dom_sf.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR033923; PAK_BD.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00786; PBD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00285; PBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50108; CRIB; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
Apoptosis; ATP-binding; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Exocytosis; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 545 Serine/threonine-protein kinase PAK 1.
/FTId=PRO_0000086460.
DOMAIN 75 88 CRIB. {ECO:0000255|PROSITE-
ProRule:PRU00057}.
DOMAIN 270 521 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 276 284 ATP.
NP_BIND 345 347 ATP.
REGION 70 140 Autoregulatory region.
REGION 75 105 GTPase-binding.
REGION 132 270 Interaction with CRIPAK.
{ECO:0000269|PubMed:16278681}.
ACT_SITE 389 389 Proton acceptor.
BINDING 299 299 ATP.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 21 21 Phosphoserine; by PKB and autocatalysis.
{ECO:0000269|PubMed:14585966,
ECO:0000269|PubMed:17989089}.
MOD_RES 57 57 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:17989089}.
MOD_RES 84 84 Phosphothreonine; by OXSR1.
{ECO:0000250|UniProtKB:P35465}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 131 131 Phosphotyrosine.
{ECO:0000269|PubMed:17989089}.
MOD_RES 142 142 Phosphotyrosine.
{ECO:0000269|PubMed:17989089}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 153 153 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:17726028,
ECO:0000269|PubMed:17989089}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:17989089}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000269|PubMed:17989089}.
MOD_RES 199 199 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 201 201 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:17726028}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 212 212 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:17989089}.
MOD_RES 219 219 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 225 225 Phosphothreonine.
{ECO:0000250|UniProtKB:O88643}.
MOD_RES 229 229 Phosphothreonine.
{ECO:0000250|UniProtKB:O88643}.
MOD_RES 230 230 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 285 285 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:17726028,
ECO:0000269|PubMed:17989089}.
MOD_RES 423 423 Phosphothreonine; by autocatalysis, BRSK2
and PDPK1. {ECO:0000269|PubMed:10551809,
ECO:0000269|PubMed:10995762,
ECO:0000269|PubMed:22153498,
ECO:0000269|PubMed:22669945}.
VAR_SEQ 518 545 HQFLKIAKPLSSLTPLIAAAKEATKNNH -> VRKLRFQVF
SNFSMIAASIPEDCQAPLQPHSTDCCS (in isoform
2). {ECO:0000303|Ref.3}.
/FTId=VSP_017507.
VARIANT 515 515 L -> V (in dbSNP:rs35345144).
/FTId=VAR_051654.
MUTAGEN 83 83 H->L: Abolishes interaction with CDC42,
leading to strongly decreased activity;
when associated with L-86.
{ECO:0000269|PubMed:10551809,
ECO:0000269|PubMed:9774440}.
MUTAGEN 86 86 H->L: Abolishes interaction with CDC42,
leading to strongly decreased activity;
when associated with L-83.
{ECO:0000269|PubMed:10551809,
ECO:0000269|PubMed:9774440}.
MUTAGEN 107 107 L->F: Abolishes autoinhibition, leading
to constitutive kinase activity.
{ECO:0000269|PubMed:10551809}.
MUTAGEN 299 299 K->R: Strongly decreases activity.
Abolishes kinase activity; when
associated with N-389.
{ECO:0000269|PubMed:22153498}.
MUTAGEN 389 389 D->N: Abolishes kinase activity; when
associated with R-299.
{ECO:0000269|PubMed:22153498}.
MUTAGEN 393 393 D->A: Abolishes autophosphorylation at
Thr-423.
MUTAGEN 423 423 T->A: Decreases CDC42-stimulated activity
and autophosphorylation.
{ECO:0000269|PubMed:10551809}.
MUTAGEN 423 423 T->E: Constitutive kinase activity.
{ECO:0000269|PubMed:10551809}.
CONFLICT 26 26 A -> V (in Ref. 2; AAA65441 and 3;
AAC24716). {ECO:0000305}.
CONFLICT 237 237 R -> L (in Ref. 1; AAC50590).
{ECO:0000305}.
CONFLICT 379 379 F -> S (in Ref. 1; AAC50590).
{ECO:0000305}.
CONFLICT 503 503 E -> D (in Ref. 2; AAA65441).
{ECO:0000305}.
STRAND 79 87 {ECO:0000244|PDB:2QME}.
TURN 91 94 {ECO:0000244|PDB:2QME}.
STRAND 95 98 {ECO:0000244|PDB:1F3M}.
HELIX 101 108 {ECO:0000244|PDB:1F3M}.
HELIX 114 119 {ECO:0000244|PDB:1F3M}.
HELIX 121 135 {ECO:0000244|PDB:1F3M}.
STRAND 195 198 {ECO:0000244|PDB:1ZSG}.
STRAND 214 219 {ECO:0000244|PDB:3DVP}.
HELIX 250 260 {ECO:0000244|PDB:3FXZ}.
STRAND 261 264 {ECO:0000244|PDB:3FXZ}.
HELIX 266 268 {ECO:0000244|PDB:3FXZ}.
STRAND 270 272 {ECO:0000244|PDB:3Q4Z}.
STRAND 274 279 {ECO:0000244|PDB:3FXZ}.
STRAND 282 289 {ECO:0000244|PDB:3FXZ}.
TURN 290 292 {ECO:0000244|PDB:3FXZ}.
STRAND 295 302 {ECO:0000244|PDB:3FXZ}.
HELIX 303 305 {ECO:0000244|PDB:3FXZ}.
HELIX 309 321 {ECO:0000244|PDB:3FXZ}.
STRAND 330 336 {ECO:0000244|PDB:3FXZ}.
STRAND 339 345 {ECO:0000244|PDB:3FXZ}.
STRAND 349 351 {ECO:0000244|PDB:4ZJI}.
HELIX 352 358 {ECO:0000244|PDB:3FXZ}.
HELIX 363 382 {ECO:0000244|PDB:3FXZ}.
HELIX 392 394 {ECO:0000244|PDB:3FXZ}.
STRAND 395 397 {ECO:0000244|PDB:3FXZ}.
STRAND 403 405 {ECO:0000244|PDB:3FXZ}.
STRAND 408 410 {ECO:0000244|PDB:1F3M}.
STRAND 416 418 {ECO:0000244|PDB:3Q52}.
HELIX 428 430 {ECO:0000244|PDB:3FXZ}.
HELIX 433 437 {ECO:0000244|PDB:3FXZ}.
HELIX 444 459 {ECO:0000244|PDB:3FXZ}.
TURN 463 466 {ECO:0000244|PDB:3FXZ}.
HELIX 469 479 {ECO:0000244|PDB:3FXZ}.
HELIX 487 489 {ECO:0000244|PDB:3FXZ}.
HELIX 492 501 {ECO:0000244|PDB:3FXZ}.
TURN 506 508 {ECO:0000244|PDB:3FXZ}.
HELIX 512 515 {ECO:0000244|PDB:3FXZ}.
HELIX 519 523 {ECO:0000244|PDB:3FXZ}.
HELIX 527 530 {ECO:0000244|PDB:3FXZ}.
HELIX 531 540 {ECO:0000244|PDB:3FXZ}.
SEQUENCE 545 AA; 60647 MW; 1A95CD5F2195CD7B CRC64;
MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK KDRFYRSILP
GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP EQWARLLQTS NITKSEQKKN
PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA EDYNSSNALN VKAVSETPAV PPVSEDEDDD
DDDATPPPVI APRPEHTKSV YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE
KQKKKPKMSD EEILEKLRSI VSVGDPKKKY TRFEKIGQGA SGTVYTAMDV ATGQEVAIKQ
MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG SLTDVVTETC
MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD GSVKLTDFGF CAQITPEQSK
RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL GIMAIEMIEG EPPYLNENPL RALYLIATNG
TPELQNPEKL SAIFRDFLNR CLEMDVEKRG SAKELLQHQF LKIAKPLSSL TPLIAAAKEA
TKNNH


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