CDK13

Protein-coding gene in the species Homo sapiens
CDK13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5EFQ

Identifiers
AliasesCDK13, CDC2L, CDC2L5, CHED, hcyclin-dependent kinase 13, cyclin dependent kinase 13, CHDFIDD
External IDsOMIM: 603309 MGI: 1916812 HomoloGene: 135707 GeneCards: CDK13
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for CDK13
Genomic location for CDK13
Band7p14.1Start39,950,121 bp[1]
End40,099,580 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for CDK13
Genomic location for CDK13
Band13|13 A2Start17,884,900 bp[2]
End17,979,682 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • renal medulla

  • visceral pleura

  • pylorus

  • nipple

  • cardia

  • endothelial cell

  • ventral tegmental area

  • inferior ganglion of vagus nerve

  • parietal pleura

  • external globus pallidus
Top expressed in
  • spermatocyte

  • hand

  • spermatid

  • thymus

  • spleen

  • lymph node

  • secondary oocyte

  • otolith organ

  • foot

  • ganglionic eminence
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein kinase activity
  • nucleotide binding
  • kinase activity
  • protein serine/threonine kinase activity
  • protein binding
  • RNA polymerase II CTD heptapeptide repeat kinase activity
  • ATP binding
  • cyclin binding
  • cyclin-dependent protein serine/threonine kinase activity
  • transcription factor binding
  • protein kinase binding
  • RNA binding
Cellular component
  • Golgi apparatus
  • nuclear speck
  • nuclear cyclin-dependent protein kinase holoenzyme complex
  • cyclin K-CDK13 complex
  • nucleus
  • extracellular region
  • extracellular space
  • nucleoplasm
  • chromosome
  • cytosol
  • cyclin/CDK positive transcription elongation factor complex
  • ficolin-1-rich granule lumen
  • cyclin-dependent protein kinase holoenzyme complex
Biological process
  • hemopoiesis
  • phosphorylation of RNA polymerase II C-terminal domain
  • phosphorylation
  • mRNA processing
  • multicellular organism development
  • protein phosphorylation
  • RNA splicing
  • positive regulation of cell population proliferation
  • viral process
  • alternative mRNA splicing, via spliceosome
  • regulation of mitotic nuclear division
  • transcription elongation from RNA polymerase II promoter
  • neutrophil degranulation
  • positive regulation of transcription by RNA polymerase II
  • negative regulation of stem cell differentiation
  • positive regulation of transcription elongation from RNA polymerase II promoter
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8621

69562

Ensembl

ENSG00000065883

ENSMUSG00000041297

UniProt

Q14004

Q69ZA1

RefSeq (mRNA)

NM_003718
NM_031267

NM_001081058
NM_027118

RefSeq (protein)

NP_003709
NP_112557

NP_001074527
NP_081394

Location (UCSC)Chr 7: 39.95 – 40.1 MbChr 13: 17.88 – 17.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cyclin dependent kinase 13 is an enzyme that in humans is encoded by the CDK13 gene.[5][6]

The protein encoded by this gene is a member of the cyclin-dependent serine/threonine protein kinase family. Members of this family are well known for their essential roles as master switches in cell cycle control. Some of the cell cycle control kinases are able to phosphorylate proteins that are important for cell differentiation and apoptosis, thus provide connections between cell proliferation, differentiation, and apoptosis. Proteins of this family may also be involved in non-cell cycle-related functions, such as neurocytoskeleton dynamics. The exact function of this protein has not yet been determined. It has unusually large N- and C-termini and is ubiquitously expressed in many tissues. Two alternatively spliced variants are described.[6]

Clinical significance

Mutations in CDK13 cause CDK13-related disorder. A 2017 study of children with rare developmental disorders found 11 children in the United Kingdom who had a fault in their CDK13 gene.[7] This fault affected the children's communication and language skills as well as causing learning difficulties.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000065883 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041297 – 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. ^ Lapidot-Lifson Y, Patinkin D, Prody CA, Ehrlich G, Seidman S, Ben-Aziz R, et al. (Feb 1992). "Cloning and antisense oligodeoxynucleotide inhibition of a human homolog of cdc2 required in hematopoiesis". Proc Natl Acad Sci U S A. 89 (2): 579–83. Bibcode:1992PNAS...89..579L. doi:10.1073/pnas.89.2.579. PMC 48282. PMID 1731328.
  6. ^ a b "Entrez Gene: CDC2L5 cell division cycle 2-like 5 (cholinesterase-related cell division controller)".
  7. ^ McRae JF, Clayton S, Fitzgerald TW, Kaplanis J, Prigmore E, Rajan D, et al. (2017). "Prevalence and architecture of de novo mutations in developmental disorders" (PDF). Nature. 542 (7642): 433–438. Bibcode:2017Natur.542..433M. doi:10.1038/nature21062. hdl:20.500.11820/a89badba-7288-4be1-b3c5-a9b9e61d920d. PMC 6016744. PMID 28135719.
  8. ^ Walsh F (2017-01-25). "Child gene study identifies new developmental disorders". BBC News. Retrieved 2017-01-27.

External links

  • Human CDK13 genome location and CDK13 gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: Q14004 (Cyclin-dependent kinase 13) at the PDBe-KB.

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Mackenzie LF, Brooke GS, Cutfield JF, Sullivan PA, Withers SG (1997). "Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase". J. Biol. Chem. 272 (6): 3161–7. doi:10.1074/jbc.272.6.3161. PMID 9013549.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • <Please add first missing authors to populate metadata.> (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
  • Marqués F, Moreau JL, Peaucellier G, Lozano JC, Schatt P, Picard A, et al. (2001). "A new subfamily of high molecular mass CDC2-related kinases with PITAI/VRE motifs". Biochem. Biophys. Res. Commun. 279 (3): 832–7. doi:10.1006/bbrc.2000.4042. PMID 11162436.
  • Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O (2001). "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 8 (2): 85–95. doi:10.1093/dnares/8.2.85. PMID 11347906.
  • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, 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.
  • Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-Mcpherson C, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
  • Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Even Y, Durieux S, Escande ML, Lozano JC, Peaucellier G, Weil D, et al. (2007). "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo". J. Cell. Biochem. 99 (3): 890–904. doi:10.1002/jcb.20986. PMID 16721827. S2CID 21022091.
  • Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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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)
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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)
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