CDC2L1

Protein-coding gene in the species Homo sapiens
CDK11B
Identifiers
AliasesCDK11B, CDC2L1, CDK11, CDK11-p110, CDK11-p46, CDK11-p58, CLK-1, PITSLREA, PK58, p58, p58CDC2L1, p58CLK-1, cyclin-dependent kinase 11B, cyclin dependent kinase 11B
External IDsOMIM: 176873 MGI: 88353 HomoloGene: 137644 GeneCards: CDK11B
EC number2.7.11.22
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CDK11B
Genomic location for CDK11B
Band1p36.33Start1,635,225 bp[1]
End1,659,012 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for CDK11B
Genomic location for CDK11B
Band4 E2|4 86.73 cMStart155,624,854 bp[2]
End155,649,938 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sural nerve

  • gastrocnemius muscle

  • gastric mucosa

  • right lung

  • spleen

  • skeletal muscle tissue

  • fundus

  • left ventricle

  • substantia nigra

  • blood
Top expressed in
  • saccule

  • otic placode

  • body of femur

  • duodenum

  • crypt of lieberkuhn of small intestine

  • ankle

  • primitive streak

  • yolk sac

  • jejunum

  • abdominal wall
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • kinase activity
  • nucleotide binding
  • transferase activity
  • protein serine/threonine kinase activity
  • ATP binding
  • protein kinase activity
  • cyclin-dependent protein serine/threonine kinase activity
  • RNA binding
Cellular component
  • nucleus
  • cytoplasm
Biological process
  • regulation of transcription, DNA-templated
  • phosphorylation
  • cell cycle
  • regulation of cell growth
  • cell population proliferation
  • regulation of mRNA processing
  • apoptotic process
  • protein phosphorylation
  • regulation of mitotic cell cycle
  • mitotic cell cycle
  • regulation of cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

984

12537

Ensembl

ENSG00000248333

ENSMUSG00000029062

UniProt

P21127

P24788

RefSeq (mRNA)
NM_001291345
NM_001787
NM_033486
NM_033487
NM_033488

NM_033489
NM_033490
NM_033492
NM_033493

NM_007661
NM_001347308
NM_001355567
NM_001355568
NM_001355569

RefSeq (protein)
NP_001278274
NP_001778
NP_277021
NP_277022
NP_277024

NP_277025

NP_001334237
NP_031687
NP_001342496
NP_001342497
NP_001342498

Location (UCSC)Chr 1: 1.64 – 1.66 MbChr 4: 155.62 – 155.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

PITSLRE serine/threonine-protein kinase CDC2L1 is an enzyme that in humans is encoded by the CDK11B gene.[5][6][7]

This gene encodes a member of the p34Cdc2 protein kinase family. p34Cdc2 kinase family members are known to be essential for eukaryotic cell cycle control. This gene is in close proximity to CDC2L2, a nearly identical gene in the same chromosomal region. The gene loci including this gene, CDC2L2, as well as metalloprotease MMP21/22, consist of two identical, tandemly linked genomic regions which are thought to be a part of the larger region that has been duplicated. This gene and CDC2L2 were shown to be deleted or altered frequently in neuroblastoma with amplified MYCN genes. The protein kinase encoded by this gene could be cleaved by caspases and was demonstrated to play roles in cell apoptosis. Several alternatively spliced variants of this gene have been reported.[7]

Interactions

CDC2L1 has been shown to interact with Cyclin D3.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000248333 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029062 – 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. ^ Eipers PG, Barnoski BL, Han J, Carroll AJ, Kidd VJ (Mar 1992). "Localization of the expressed human p58 protein kinase chromosomal gene to chromosome 1p36 and a highly related sequence to chromosome 15". Genomics. 11 (3): 621–9. doi:10.1016/0888-7543(91)90069-Q. PMID 1774066.
  6. ^ Mikolajczyk M, Shi J, Vaillancourt RR, Sachs NA, Nelson M (Sep 2003). "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM". Biochem. Biophys. Res. Commun. 310 (1): 14–8. doi:10.1016/j.bbrc.2003.08.116. PMID 14511641.
  7. ^ a b "Entrez Gene: CDC2L1 cell division cycle 2-like 1 (PITSLRE proteins)".
  8. ^ Zhang, Songwen; Cai Mingmei; Zhang Si; Xu Songli; Chen She; Chen Xiaoning; Chen Chun; Gu Jianxin (Sep 2002). "Interaction of p58(PITSLRE), a G2/M-specific protein kinase, with cyclin D3". J. Biol. Chem. 277 (38): 35314–22. doi:10.1074/jbc.M202179200. ISSN 0021-9258. PMID 12082095.

External links

Further reading

  • Eipers PG, Lahti JM, Kidd VJ (1992). "Structure and expression of the human p58clk-1 protein kinase chromosomal gene". Genomics. 13 (3): 613–21. doi:10.1016/0888-7543(92)90132-C. PMID 1639388.
  • Bunnell BA, Heath LS, Adams DE, et al. (1990). "Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle". Proc. Natl. Acad. Sci. U.S.A. 87 (19): 7467–71. Bibcode:1990PNAS...87.7467B. doi:10.1073/pnas.87.19.7467. PMC 54768. PMID 2217177.
  • White PS, Maris JM, Beltinger C, et al. (1995). "A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5520–4. Bibcode:1995PNAS...92.5520W. doi:10.1073/pnas.92.12.5520. PMC 41727. PMID 7777541.
  • Lahti JM, Valentine M, Xiang J, et al. (1994). "Alterations in the PITSLRE protein kinase gene complex on chromosome 1p36 in childhood neuroblastoma". Nat. Genet. 7 (3): 370–5. doi:10.1038/ng0794-370. PMID 7920654. S2CID 2065302.
  • Xiang J, Lahti JM, Grenet J, et al. (1994). "Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms". J. Biol. Chem. 269 (22): 15786–94. doi:10.1016/S0021-9258(17)40749-6. PMID 8195233.
  • Beyaert R, Kidd VJ, Cornelis S, et al. (1997). "Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor". J. Biol. Chem. 272 (18): 11694–7. doi:10.1074/jbc.272.18.11694. PMID 9115219.
  • Loyer P, Trembley JH, Lahti JM, Kidd VJ (1998). "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo". J. Cell Sci. 111 (11): 1495–506. doi:10.1242/jcs.111.11.1495. PMID 9580558.
  • Tang D, Gururajan R, Kidd VJ (1998). "Phosphorylation of PITSLRE p110 isoforms accompanies their processing by caspases during Fas-mediated cell death". J. Biol. Chem. 273 (26): 16601–7. doi:10.1074/jbc.273.26.16601. PMID 9632733.
  • Gururajan R, Lahti JM, Grenet J, et al. (1998). "Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2". Genome Res. 8 (9): 929–39. doi:10.1101/gr.8.9.929. PMC 310781. PMID 9750192.
  • Cornelis S, Bruynooghe Y, Denecker G, et al. (2000). "Identification and characterization of a novel cell cycle-regulated internal ribosome entry site". Mol. Cell. 5 (4): 597–605. doi:10.1016/S1097-2765(00)80239-7. PMID 10882096.
  • Trembley JH, Hu D, Hsu LC, et al. (2002). "PITSLRE p110 protein kinases associate with transcription complexes and affect their activity". J. Biol. Chem. 277 (4): 2589–96. doi:10.1074/jbc.M109755200. PMID 11709559.
  • Zhang S, Cai M, Zhang S, et al. (2002). "Interaction of p58(PITSLRE), a G2/M-specific protein kinase, with cyclin D3". J. Biol. Chem. 277 (38): 35314–22. doi:10.1074/jbc.M202179200. PMID 12082095.
  • 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.
  • Hu D, Mayeda A, Trembley JH, et al. (2003). "CDK11 complexes promote pre-mRNA splicing". J. Biol. Chem. 278 (10): 8623–9. doi:10.1074/jbc.M210057200. PMID 12501247.
  • Chen S, Yin X, Zhu X, et al. (2003). "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 (22): 20029–36. doi:10.1074/jbc.M300818200. PMID 12624090.
  • de Graaf K, Hekerman P, Spelten O, et al. (2004). "Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors". J. Biol. Chem. 279 (6): 4612–24. doi:10.1074/jbc.M310794200. PMID 14623875.
  • Sachs NA, Vaillancourt RR (2004). "Cyclin-dependent kinase 11p110 and casein kinase 2 (CK2) inhibit the interaction between tyrosine hydroxylase and 14-3-3". J. Neurochem. 88 (1): 51–62. doi:10.1046/j.1471-4159.2003.02119.x. PMID 14675149.
  • Yang L, Li N, Wang C, et al. (2004). "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells". J. Biol. Chem. 279 (12): 11639–48. doi:10.1074/jbc.M312895200. PMID 14684736.
  • v
  • t
  • e
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)
  • -
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
Portal:
  • icon Biology


Stub icon

This protein-related article is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e