CDC42BPA

Protein-coding gene in the species Homo sapiens
CDC42BPA
Identifiers
AliasesCDC42BPA, MRCK, MRCKA, PK428, CDC42 binding protein kinase alpha
External IDsOMIM: 603412; MGI: 2441841; HomoloGene: 55765; GeneCards: CDC42BPA; OMA:CDC42BPA - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CDC42BPA
Genomic location for CDC42BPA
Band1q42.13Start226,989,865 bp[1]
End227,318,492 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for CDC42BPA
Genomic location for CDC42BPA
Band1|1 H4Start179,788,037 bp[2]
End179,993,168 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • internal globus pallidus

  • pylorus

  • tibia

  • lateral nuclear group of thalamus

  • secondary oocyte

  • external globus pallidus

  • pars reticulata

  • renal medulla

  • Brodmann area 23

  • corpus callosum
Top expressed in
  • zygote

  • superior frontal gyrus

  • primary visual cortex

  • cerebellar cortex

  • dentate gyrus of hippocampal formation granule cell

  • genital tubercle

  • central gray substance of midbrain

  • neural layer of retina

  • medial geniculate nucleus

  • nucleus of stria terminalis
More reference expression data
BioGPS




More reference expression data
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
  • lamellipodium
  • cell projection
  • cytoskeleton
Biological process
  • protein phosphorylation
  • actomyosin structure organization
  • intracellular signal transduction
  • cell migration
  • phosphorylation
  • actin cytoskeleton reorganization
  • actin cytoskeleton organization
  • peptidyl-threonine phosphorylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8476

226751

Ensembl

ENSG00000143776

ENSMUSG00000026490

UniProt

Q5VT25

Q3UU96

RefSeq (mRNA)
NM_003607
NM_014826
NM_001366010
NM_001366011
NM_001366019

NM_001387550
NM_001394014

NM_001033285
NM_001346804
NM_001346805
NM_001359541
NM_001359542

NM_001359543
NM_001359544
NM_001359545
NM_001359546
NM_001359547
NM_001359548
NM_001359549

RefSeq (protein)

NP_003598
NP_055641
NP_001352939
NP_001352940
NP_001352948

NP_001028457
NP_001333733
NP_001333734
NP_001346470
NP_001346471

NP_001346472
NP_001346473
NP_001346474
NP_001346475
NP_001346476
NP_001346477
NP_001346478

Location (UCSC)Chr 1: 226.99 – 227.32 MbChr 1: 179.79 – 179.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.[5]

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.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143776 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026490 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: CDC42BPA CDC42 binding protein kinase alpha (DMPK-like)".

Further reading

  • 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. S2CID 25250183.
  • 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. Bibcode:2000PNAS...97.3491D. 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. S2CID 10022990.
  • 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. Bibcode:2002PNAS...9916899M. 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. S2CID 34732713.
  • 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. Bibcode:2006Natur.441..315G. 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.
  • v
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
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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)
MAP2K


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