CDC42BPA

Identifiers

CDC42BPA, MRCK, MRCKA, PK428, CDC42 binding protein kinase alpha

External IDs

MGI: 2441841 HomoloGene: 55765 GeneCards: CDC42BPA

Gene ontology
Molecular function	• transferase activity • nucleotide binding • protein serine/threonine kinase activity • protein kinase activity • protein binding • ATP binding • magnesium ion binding • metal ion binding • identical protein binding • kinase activity
Cellular component	• cytoplasm • actomyosin • extracellular exosome • cell leading edge • cell-cell junction
Biological process	• actin cytoskeleton reorganization • protein phosphorylation • actomyosin structure organization • intracellular signal transduction • cell migration • phosphorylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


8476


226751

Ensembl


ENSG00000143776


ENSMUSG00000026490

UniProt


Q5VT25


Q3UU96

RefSeq (mRNA)


NM_003607 NM_014826


NM_001033285

RefSeq (protein)


NP_003598.2 NP_055641.3


XP_006496873.1

Location (UCSC)

Chr 1: 226.99 – 227.32 Mb

Chr 1: 179.96 – 180.17 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.^[3]

The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.^[3]

References

Zhao Y, Loyer P, Li H, et al. (1997). "Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases.". J. Biol. Chem. 272 (15): 10013–20. doi:10.1074/jbc.272.15.10013. PMID 9092543.
Leung T, Chen XQ, Tan I, et al. (1998). "Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization.". Mol. Cell. Biol. 18 (1): 130–40. doi:10.1128/mcb.18.1.130. PMC 121465. PMID 9418861.
Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain.". DNA Res. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
Moncrieff CL, Bailey ME, Morrison N, Johnson KJ (1999). "Cloning and chromosomal localization of human Cdc42-binding protein kinase beta.". Genomics. 57 (2): 297–300. doi:10.1006/geno.1999.5769. PMID 10198171.
Edwards DC, Sanders LC, Bokoch GM, Gill GN (1999). "Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.". Nat. Cell Biol. 1 (5): 253–9. doi:10.1038/12963. PMID 10559936.
Ohashi K, Nagata K, Maekawa M, et al. (2000). "Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop.". J. Biol. Chem. 275 (5): 3577–82. doi:10.1074/jbc.275.5.3577. PMID 10652353.
Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
Nakamura N, Oshiro N, Fukata Y, et al. (2000). "Phosphorylation of ERM proteins at filopodia induced by Cdc42.". Genes Cells. 5 (7): 571–81. doi:10.1046/j.1365-2443.2000.00348.x. PMID 10947843.
Lam LT, Pham YC, Nguyen TM, Morris GE (2000). "Characterization of a monoclonal antibody panel shows that the myotonic dystrophy protein kinase, DMPK, is expressed almost exclusively in muscle and heart.". Hum. Mol. Genet. 9 (14): 2167–73. doi:10.1093/hmg/9.14.2167. PMID 10958655.
Tan I, Seow KT, Lim L, Leung T (2001). "Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha.". Mol. Cell. Biol. 21 (8): 2767–78. doi:10.1128/MCB.21.8.2767-2778.2001. PMC 86907. PMID 11283256.
Sumi T, Matsumoto K, Shibuya A, Nakamura T (2001). "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha.". J. Biol. Chem. 276 (25): 23092–6. doi:10.1074/jbc.C100196200. PMID 11340065.
Lemercier C, Brocard MP, Puvion-Dutilleul F, et al. (2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor.". J. Biol. Chem. 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
Dong JM, Leung T, Manser E, Lim L (2003). "Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation.". Eur. J. Cell Biol. 81 (4): 231–42. doi:10.1078/0171-9335-00238. PMID 12018391.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Tan I, Cheong A, Lim L, Leung T (2003). "Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity.". Gene. 304: 107–15. doi:10.1016/S0378-1119(02)01185-X. PMID 12568720.
Wilkinson S, Paterson HF, Marshall CJ (2005). "Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion.". Nat. Cell Biol. 7 (3): 255–61. doi:10.1038/ncb1230. PMID 15723050.
Cmejla R, Petrak J, Cmejlova J (2006). "A novel iron responsive element in the 3'UTR of human MRCKalpha.". Biochem. Biophys. Res. Commun. 341 (1): 158–66. doi:10.1016/j.bbrc.2005.12.155. PMID 16412980.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
Lefort K, Mandinova A, Ostano P, et al. (2007). "Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKalpha kinases.". Genes Dev. 21 (5): 562–77. doi:10.1101/gad.1484707. PMC 1820898. PMID 17344417.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

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CDC42BPA

References

Further reading