CDC2L1

CDK11B

Identifiers

CDK11B, 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 IDs

HomoloGene: 137644 GeneCards: CDK11B

EC number

2.7.11.22

Gene ontology
Molecular function	• protein binding • cyclin-dependent protein serine/threonine kinase activity • kinase activity • poly(A) RNA binding • nucleotide binding • transferase activity • protein serine/threonine kinase activity • ATP binding • protein kinase activity
Cellular component	• nucleus • cytoplasm
Biological process	• regulation of cell cycle • regulation of transcription, DNA-templated • phosphorylation • cell cycle • regulation of cell growth • cell proliferation • regulation of mRNA processing • mitotic nuclear division • apoptotic process • protein phosphorylation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


984


n/a

Ensembl


ENSG00000248333


n/a

UniProt


P21127


n/a

RefSeq (mRNA)

NM_001291345 NM_001787 NM_033486 NM_033487 NM_033488
NM_033489 NM_033490 NM_033492 NM_033493


n/a

RefSeq (protein)


NP_277022.1 NP_277025.1


n/a

Location (UCSC)

Chr 1: 1.64 – 1.66 Mb

n/a

PubMed search

^[1]

n/a

Wikidata

View/Edit Human

PITSLRE serine/threonine-protein kinase CDC2L1 is an enzyme that in humans is encoded by the CDC2L1 gene.^[2]^[3]^[4]

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.^[4]

Interactions

CDC2L1 has been shown to interact with Cyclin D3.^[5]

References

↑ "Human PubMed Reference:".
↑ 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.
↑ 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.
1 2 "Entrez Gene: CDC2L1 cell division cycle 2-like 1 (PITSLRE proteins)".
↑ 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. United States. 277 (38): 35314–22. doi:10.1074/jbc.M202179200. ISSN 0021-9258. PMID 12082095.

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. 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. 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.
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. 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. 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. 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.

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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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CDC2L1

Interactions

References

Further reading