Phosphorylation of RUNX2-P1 serine site S465 (corresponds to mouse Runx2-P1 serine residue S472) by the CDK4:CCND1 complex has been reported to target RUNX2 for ubiquitination and proteasome-mediated degradation, but the responsible ubiquitin ligase has not been identified (Shen et al. 2006). BMP2 signaling was reported to interfere with CDK4-induced RUNX2 protein degradation (Shu et al. 2011). Parathyroid hormone-related protein (PTHLH, also known as PTHrP) is implicated in positive regulation of CCND1-mediated degradation of RUNX2 (Zhang et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-9008412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9008412"
}
]
},
{
"id": "R-HSA-9018017",
"name": "RB1 binds and inhibits E2F1/2/3:DP1/2 complexes",
"equation": "",
"summary": "RB1 tumor suppressor, the product of the retinoblastoma susceptibility gene, binds to E2F transcription factors E2F1, E2F2 and E2F3, presumably heterodimerized with TFDP1 or TFDP2. The interaction involves the pocket domain of RB1. RB1 binding inhibits transcriptional activity of E2F1/2/3:TFDP1/2 complexes, resulting in prevention of G1/S transition (Chellappan et al. 1991, Bagchi et al. 1991, Chittenden et al. 1991, Lees et al. 1993, Hiebert 1993, Wu et al. 2001). Once RB1 is phosphorylated on serine residue S795 by Cyclin D:CDK4/6 complexes, it can no longer associate with and inhibit E2F1/2/3:TFDP1/2 complexes. Thus, CDK4/6-mediated phosphorylation of RB1 leads to transcriptional activation of E2F1/2/3 target genes needed for the S phase of the cell cycle (Connell-Crowley et al. 1997).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1",
"P24941-1",
"Q00534-1"
],
"evidence": [
{
"id": "R-HSA-9018017",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9018017"
}
]
},
{
"id": "R-HSA-912429",
"name": "Resolution of meiotic holliday junction",
"equation": "",
"summary": "Meiotic Holliday junctions are cleaved to yield either crossovers or non?crossovers (gene conversions). The resolvase or resolvases responsible for cleavage are unknown but a resolvase complex may include SLX4 and/or GEN1.
Two classes of crossovers have been defined: class I crossovers are dependent on the MutL homologs, MLH1 and MLH3, while class II crossovers are dependent on the MUS81-EME1 endonuclease. Class I crossovers constitute 90-95% of all crossovers, and correspond to meiotic nodules that contain MLH1and MLH3. These arise as a subset of the many hundreds of MSH4/MSH5-positive meiotic nodules that arise at the time of double Holliday junction formation. What happens to all the other meiotic nodules is not clear, but they most likely follow a second pathway that results in non-crossovers (or gene conversions). MLH1 and MLH3 form heterodimers that repair mismatches in duplex DNA. In mouse, MLH1 is required for crossovers but not for non?crossover resolution of Holliday junctions. About 10% of early meiotic nodules are somehow selected to become Class I crossover events, possibly by first losing BLM (and probably associated TOP3A), and acquiring MLH1 and MLH3.
The selection of sites for class II crossovers follows an, as yet, unknown pathway, but almost certainly stems from the same initiating D-loop intermediate.
In the process known as crossover interference, the presence of a crossover nodule inhibits formation of nearby crossover nodules so that crossovers are not clustered and each chromosome bivalent has at least one crossover. In mouse, crossover interference is seen among nodules at two stages: RPA?containing nodules during late zygonema and MLH1?containing nodules during pachynema. Class II crossovers are not subject to interference constraints.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-68365",
"R-HSA-912478",
"R-HSA-912495"
],
"output_participant_list": [
"R-HSA-113843",
"R-HSA-174881",
"R-HSA-50951"
],
"enzyme_list": [
"Q13315-1",
"P54132-1",
"Q13472-1",
"P11802-1",
"P24941-1"
],
"evidence": [
{
"id": "R-HSA-912429",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912429"
}
]
},
{
"id": "R-HSA-912458",
"name": "Formation of meiotic heteroduplex",
"equation": "",
"summary": "Following double strand break (DSB) formation and strand resection, RAD51 and DMC1 coat single-stranded 3' ends of DNA and catalyze the search for homology and strand invasion into the DNA duplex of the chromosomal homolog (Baumann et al. 1996, Barlow et al. 1997, Benson et al. 1998, Baumann and West 1999, Masson et al. 1999, Sehorn et al. 2004, Murayama et al. 2008). The invading strand displaces the original strand of the chromosomal homolog creating a D-loop structure. Other proteins present in the complex are inferred from cytology (Barlow et al. 1997, Oliver-Bonet et al. 2005, Oliver-Bonet et al. 2007).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-912458",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912458"
}
]
},
{
"id": "R-HSA-912496",
"name": "Formation of meiotic holliday junction",
"equation": "",
"summary": "The 3' end of the invading strand is extended by an unknown DNA polymerase and the extended strand is then ligated back to the original homolog, generating a double Holliday junction. MSH4 and MSH5 form heterodimers which bind Holliday junctions and, in the presence of ATP, slide along the parental duplexes (Bocker et al. 1999, Snowden et al. 2004, Snowden et al. 2008). MSH4 is present at hundreds of meiotic nodules during late zygotene but only about 10% of these nodules become crossovers (Oliver-Bonet et al. 2005). Bloom Syndrome protein (BLM) and Topoisomerase IIIa (TOP3A) are also present and may promote homologous recombination repair without crossing over (Johnson et al. 2000, Wu et al. 2000).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-912435",
"R-HSA-912452",
"R-HSA-912455"
],
"output_participant_list": [
"R-HSA-912490"
],
"enzyme_list": [
"Q13315-1",
"P54132-1",
"Q13472-1",
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-912496",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912496"
}
]
},
{
"id": "R-HSA-912503",
"name": "Formation of meiotic single-stranded DNA invasion complex",
"equation": "",
"summary": "Two RecA homologs, RAD51 and the meiosis-specific DMC1, coat single-stranded 3' ends of DNA produced by resection of double-strand breaks (Barlow et al. 1997, Masson et al. 1999, Sehorn et al. 2004, Sheridan et al. 2008, Okorokov et al. 2010). RAD51 and DMC1 interact and colocalize to the same early recombination nodules (Masson et al. 1999). Knockouts of DMC1 abolish recombination and synapsis therefore RAD51 is not sufficient for recombination.
Immunocytology shows the RPA heterotrimer arrives at recombination nodules with or after RAD51 and DMC1 (Golub et al. 1999, Oliver-Bonet et al. 2005, Oliver-Bonet et al. 2007)). (In mitotic recombination RPA precedes RAD51.)
BRCA1 and BRCA2 are found extensively distributed on synaptonemal complexes. Results from human cells and knockout mice indicate that BRCA2, RAD51C, and TEX15 participate in loading RAD51 and DMC1 onto single-stranded DNA (Thorslund et al. 2007). BRCA1 participates in loading RAD51 but not DMC1 (Scully et al. 1997).
The kinase ATM is also localized to double-strand breaks where it phosphorylates histone H2AX.
In human spermatocytes about 350 early recombination nodules form but only about 10% will continue on to make crossovers. The remaining 90% are believed to be resolved by synthesis-dependent strand annealing, which transfers short segments of DNA (about 0.2-2.0 kilobases) between homologs.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-912503",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912503"
}
]
},
{
"id": "R-HSA-9624112",
"name": "CEBPA binds CDK4",
"equation": "",
"summary": "CEBPA binds CDK4, inhibits the kinase activity of CDK4, and enhances the proteasomal degradation of CDK4 (Wang et al. 2001, Wang et al. 2002). These mechanisms may contribute to the inhibition of cell proliferation observed in response to CEBPA. CEBPA interacts with the T loop region of CDK4. In mouse liver cells, 5%-10% of Cdk4 is associated with Cebpa (Wang et al. 2001).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-9624112",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9624112"
}
]
},
{
"id": "R-HSA-9630792",
"name": "p16INK4A mutants do not bind CDK4",
"equation": "",
"summary": "Wild type p16INK4A is able to form a complex with either CDK4 or CDK6 and prevent formation of catalytically active CDK complexes consisting of CDK4 or CDK6 and D-type cyclins (CCND). Several CDKN2A missense mutations found in cancer lead to amino acid substitutions in p16INK4A that impair binding of p16INK4A mutants to CDK4 while binding of these mutants to CDK6 is preserved. Functionally tested p16INK4A mutants that bind to CDK6 but not to CDK4 are:
p16INK4A R24P (Harland et al. 1997, Becker et al. 2001, Jones et al. 2007, McKenzie et al. 2010)
p16INK4A E88K (Ruas et al. 1999)
p16INK4A R112_L113insR (Ruas et al. 1999)
p16INK4A R24P is partially functional in inhibiting cellular proliferation (Jones et al. 2007), but its activity is severely reduced (Becker et al. 2001). Partial functionality in inhibition of cellular proliferation is also attributed to p16INK4A E88K (Ruas et al. 1999), but experimental evidence is lacking. The ability of p16INK4A R112_L113insR to inhibit cellular proliferation has not been tested.
A number of p16INK4A missense mutants have only been tested for their ability to bind to CDK4, but not CDK6. Mutants impaired in CDK4 binding whose binding to CDK6 has not been established include:
p16INK4A T18_A19dup (Kannengiesser et al. 2009)
p16INK4A G23D (Scaini et al. 2009, Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A G35A (Kannengiesser et al. 2009, McKenzie et al. 2010, Scaini et al. 2014)
p16INK4A G35V (Kannengiesser et al. 2009, McKenzie et al. 2010, Scaini et al. 2014)
p16INK4A A60R (Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A A60V (Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A G67_N71del (Kannengiesser et al. 2009)
p16INK4A D74Y (Kannengiesser et al. 2009)
p16INK4A T77P (Kannengiesser et al. 2009)
p16INK4A R80P (Kannengiesser et al. 2009)
p16INK4A L97R (Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A R99P (Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A G23D shows a reduced ability to prevent CDK4-mediated phosphorylation of RB1 (Scaini et al. 2009) and to inhibit cellular proliferation (Scaini et al. 2014). Impairment of ability to inhibit cellular proliferation was also demonstrated for p16INK4A G35A and p16INK4A G35V (Scaini et al. 2014), p16INK4A D74Y (Scaini et al. 2014), p16INK4A R80P (Jenkins et al. 2013) and p16INK4A R99P (Jenkins et al. 2013).
Based on sequence change similarity, the following p16INK4A mutants that have not been tested for their ability to bind to CDK4 or CDK6, but have been reported in cancer and predicted to be pathogenic ( COSMIC database: Forbes et al. 2017) are annotated as candidates:
p16INK4A G23S
p16INK4A G23V
p16INK4A G35E
p16INK4A G35R
p16INK4A G35W
p16INK4A A60E
p16INK4A A60S
p16INK4A T77S
p16INK4A L97P
p16INK4A G23S and p16INK4A G23V show reduced ability to inhibit cellular proliferation (Scaini et al. 2014). p16INK4A G35E and p16INK4A G35R were shown to be markedly impaired in their ability to inhibit cellular proliferation, while p16INK4A G35W is somewhat impaired (Scaini et al. 2014). p16INK4A D74N (p16INK4A Asp74Ans) was not annotated because, while it is predicted to be pathogenic, it retains the ability to bind CDK4 and CDK6 (Yarbrough et al. 1999).
Mechanistic consequences of some p16INK4A mutations have not yet been elucidated. For example, substitution of alanine to proline at position 36, which is a consequence of a missense mutation in the exon 1alpha of CDKN2A, thus affecting only p16INK4A, results in expression of a mutant p16INK4A A36P protein. p16INK4A A36P retains the ability to bind to CDK4 (Becker et al. 2001, although not reproduced by McKenzie et al. 2010), but is not able to consistently inhibit CDK4-mediated phosphorylation of RB1 (Haferkamp et al. 2008), and is impaired in its ability to induce cell cycle arrest (Becker et al. 2001, Haferkamp et al. 2008). Another study shows that p16INK4A A36P retains cell cycle arrest-inducing ability, but is impaired in its ability to regulate intracellular oxidative stress (Jenkins et al. 2013).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1"
],
"evidence": [
{
"id": "R-HSA-9630792",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9630792"
}
]
},
{
"id": "R-HSA-9630795",
"name": "p16INK4A mutants do not bind CDK4,CDK6",
"equation": "",
"summary": "Wild type p16INK4A is able to form a complex with either CDK4 or CDK6 and prevent formation of catalytically active CDK complexes consisting of CDK4 or CDK6 and D-type cyclins (CCND). Several CDKN2A missense mutations found in cancer lead to amino acid substitutions in p16INK4A that impair binding of p16INK4A mutants to both CDK4 and CDK6. Missense mutations in p16INK4A are recessive and are usually found in combination with genomic deletion or epigenetic silencing of the other CDKN2A allele (Kamb et al. 1994, Castellano et al. 1997, Liew et al. 1999). Inactivating mutations in the coding sequence of p16INK4A can also be accompanied with loss of heterozygosity (LOH) (Castellano et al. 1997, Kumar et al. 1999 , Liew et al. 1999). Functionally tested p16INK4A mutants that are unable to bind to either CDK4 or CDK6 or show little residual binding, and are unable to inhibit cellular proliferation are:
p16INK4A A20P (Ruas et al. 1999, Jones et al. 2007)
p16INK4A M53I (Harland et al. 1997, Walker et al. 1999, Becker et al. 2001)
p16INK4A P81L (Walker et al. 1999)
p16INK4A P81T (Kannengiesser et al. 2009, McKenzie et al. 2010)
p16INK4A D84G (Yarbrough et al. 1999)
p16INK4A D84H (Ruas et al. 1999)
p16INK4A D84N (Ruas et al. 1999)
p16INK4A D84V (Yarbrough et al. 1999)
p16INK4A D84Y (Ruas et al. 1999)
p16INK4A R87P (Walker et al. 1999, Yarbrough et al. 1999)
p16INK4A G101W (Walker et al. 1999, Kannengiesser et al. 2009, McKenzie et al. 2010, Scaini et al. 2014)
p16INK4A P114L (Harland et al. 1997)
p16INK4A V126D (Walker et al. 1999, Becker et al. 2001)
Based on the affected amino acid residue, the following p16INK4A missense mutants that have not been tested for their ability to bind to CDK4 or CDK6, but have been reported in cancer and predicted to be pathogenic ( COSMIC database: Forbes et al. 2017) are annotated as candidates:
p16INK4A A20E
p16INK4A A20T
p16INK4A P81H
p16INK4A P81R
p16INK4A P81S
p16INK4A D84A
p16INK4A G101V
p16INK4A P114H
p16INK4A P114R
p16INK4A P114S
p16INK4A P114T
p16INK4A V126A
p16INK4A V126F
p16INK4A V126I
.p16INK4A P114S was shown to have a reduced binding to CDK4 (Kannengiesser et al. 2009) and a reduced ability to inhibit cellular proliferation (Scaini et al. 2014). p16INK4A A20S retains the ability to bind to CDK4 and CDK6 and to inhibit cellular proliferation (Yarbrough et al. 1999). p16INK4A R87W (Walker et al. 1999) and p16INK4A R87L (Yarbrough et al. 1999) retain the ability to bind to CDK4 and CDK6, but are unable to induce cell cycle arrest. Mutants p16INK4A A20S, p16INK4A R87W and p16INK4A R87L have not been annotated.
Some p16INK4A missense mutants are temperature sensitive, and their ability to bind to CDK4 and CDK6 can only be properly assessed at the physiological temperature of 37 degrees Celsius (Becker et al. 2001). Not controlling experimental temperature can be one source of inconsistencies when evaluating functionality of p16INK4A mutants, but many other variabilities in experimental systems and techniques can also influence the results of binding assays. A p16INK4A mutant with a preserved ability to bind to CDK4 and CDK6 may still not be able to inhibit their cyclin-dependent activation. However, the loss of CDK inhibitory function in p16INK4A mutants that do bind to CDK4 and CDK6 has not been tested directly.
Nonsense mutations in the second exon of the CDKN2A gene that lead to premature termination of p16INK4A mRNA translation are frequent in cancer. While the mRNAs of predicted p16INK4A truncation mutants can be detected, the truncated proteins cannot:
p16INK4A R58* (Castellano et al. 1997)
p16INK4A R80* (Fahham et al. 2010)
p16INK4A E88* (Castellano et al. 1997)
p16INK4A W110* (Castellano et al. 1997)
In addition, it was shown that the C-terminal half of p16INK4A is critical for binding to CDK4 and CDK6, and inhibition of cellular proliferation (Fahham et al. 2010).
The following nonsense and frameshift truncation mutants have not been functionally tested and are annotated as candidates:
p16INK4A E10*
p16INK4A S12*
p16INK4A W15*
p16INK4A E26*
p16INK4A E27*
p16INK4A E33*
p16INK4A Y44*
p16INK4A Q50*
p16INK4A E61*
p16INK4A E69*
p16INK4A C72*
p16INK4A P75*
p16INK4A E119*
p16INK4A E120*
The following recurrent frameshift truncations mutants that lack the C-terminal half of wild type p16INK4A and are therefore assumed to be unable to bind to CDK4 or CDK6 are also annotated as candidates:
p16INK4A S7fs*8
p16INK4A W15fs*1
p16INK4A L16fs*9
p16INK4A T18fs*15
p16INK4A T18fs*8
p16INK4A G23fs*3
p16INK4A A36fs*17
p16INK4A L37fs*16
p16INK4A N39fs*14
p16INK4A Y44fs*1
",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1",
"Q00534-1"
],
"evidence": [
{
"id": "R-HSA-9630795",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9630795"
}
]
},
{
"id": "R-HSA-9659782",
"name": "Defective RB1 does not bind E2F1,(E2F2,E2F3)",
"equation": "",
"summary": "Low penetrance germline RB1 mutants RB1 N480del and RB1 R661W, reported in retinoblastoma, localize to the nucleus but have >95% reduced binding to E2F1. These two mutations lie in the pocket region of RB1, N480del in the pocket domain A (amino acid residues 373 579) and R661W in the pocket domain B (amino acid residues 640 771). Binding of RB1 N480del and RB1 R661W to E2F2 and E2F3 has not been tested but is assumed to be affected like E2F1 binding (Otterson et al. 1997). RB1 T738_R775del mutant (also known as RB1 delEx22) is a cancer mutant that is generated by an in-frame deletion or by a splice site mutation, which both result in a mutant protein that lacks the amino acid sequence encoded by exon 22 of the RB1 gene. This mutant lacks a part of the pocket domain B and is unable to bind to the adenoviral oncoprotein E1A (Templeton et al. 1991). RB1 T738_R775del is not able to inhibit E2F1-mediate transcriptional transactivation (Helin et al. 1993) and is unable to bind to E2Fs (Ji et al. 2004).
RB1 R661Q mutant has been reported in cancer and is predicted to be pathogenic, but has not been functionally tested; it is annotated as a candidate based on its similarity with RB1 R661W.
RB1 C706F mutant, reported in lung and breast cancer, maps to the pocket domain B and shows a complete loss of binding to E2F1 (Otterson et al. 1997). Based on its similarity with RB1 C706F, RB1 C706Y mutant, reported in lung cancer, has been annotated as a candidate.
Another in-frame deletion mutant of RB1, RB1 I703_E737del (also known as RB1 delEx21) has been reported in several different cancer types. This mutant is generated by an in-frame deletion of exon 21 and is assumed to have impaired binding to E2Fs, due to its partially deleted pocket domain B. RB1 I703_E737del is annotated as a candidate for impaired binding to E2F1, E2F2 and E2F3.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11802-1",
"P24941-1",
"Q00534-1"
],
"evidence": [
{
"id": "R-HSA-9659782",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9659782"
}
]
},
{
"id": "R-HSA-9754130",
"name": "CDK4 inhibitors bind CDK4",
"equation": "",
"summary": "The following small kinase inhibitors have been shown to compete with ATP binding and inhibit the catalytic activity of CDK4 in the context of the CDK4 complex with cyclin D1 (CCND1):
Abemaciclib (LY2835219): inhibits phosphorylation of RB1 at residue S780 by the complex of CDK4 and CCND1 (Gelbert et al. 2014);
Alvocidib (flavopiridol): inhibits CDK4-mediated phosphorylation of RB1 (Carlson et al. 1996);
Fascaplysin: inhibits phosphorylation of RB1 at residues S780 and S795 (Soni et al. 2000); shows negligible activity against the complex of CDK4 and cyclin D2 (CCND2), and the complex of CDK4 and cyclin D3 (CCND3);
Lerociclib (G1T38): inhibits phosphorylation of RB1 at residues S807 amd S811 (Bisi et al. 2017);
Palbociclib (PD-0332991): binds to the dimers of CDK4 and CCND1 and inhibits CDK4:CCND1-mediated phosphorylation of RB1 (Fry et al. 2004; Guiley et al. 2019) on residues S780 and S795 (Fry et al. 2004); ineffective against trimers of CDK4, CCND1 and p27 (Guiley et al. 2019);
R547: inhibits phosphorylation of RB1 at residues S780 and S795 (DePinto et al. 2006);
RGB-286638: inhibits phosphorylation of RB1 at residues S807 and S811, to a lesser extent at S780 (Cirstea et al. 2013);
Ribociclib: inhibits CDK4:CCND1-mediated phosphorylation of RB1; ineffective against trimers of CDK4, CCND1 and p27 (Guiley et al. 2019);
Riviciclib (P276-00): inhibits CDK4-mediated phosphorylation of RB1 on residue S780 (Joshi et al. 2007);
RO-0505124: inhibits CDK4-mediated phosphorylation of RB1 at residue S795 (Burgess et al. 2006);
RO-0506220: inhibits CDK4-mediated phosphorylation at residue S795 (Burgess et al. 2006);
Trilaciclib (G1T28): inhibits phosphorylation of RB1 at residues S807 amd S811 (Bisi et al. 2016);
Voruciclib (P1446A): ~5 times less potent against the complex of CDK4 and CCND1 (~4 nM) than against CDK9 (~0.7 nM) (Dey et al. 2017); inhibits phosphorylation of RB1 on residues S780 and T821 (Paiva et al. 2015);
Dalpiciclib (SHR6390): annotated as a candidate CDK4 inhibitor; binding to and inhibition of CDK4 have not been tested outside the patent registration (patent number WO2014183520A1); inhibits RB1 phosphorylation at residue S780 (Wang et al. 2017, Long et al. 2019);
K00024 (indolocarbazole derivative 4d): annotated as a candidate CDK4 inhibitor; competes with ATP for binding to activated CDK4 (tested using CDK4 complex with CCND1 - species from which the CDK4:CCND1 complex was derived was not specified in the study); the effect on RB1 phosphorylation has not been tested (Zhu et al. 2003);
Milciclib (PHA848125): annotated as a candidate CDK4 inhibitor; moderately inhibits the complex of CDK4 and CCND1; the effect on RB1 phosphorylation has not been tested (Jorda et al. 2018);
PF-06873600 (ebvaciclib): annotated as a candidate CDK4 inhibitor; competes with ATP for binding to activated CDK4 (tested using CDK4 complex with CCND1), primarily targeting CDK2 and showing higher efficacy against CDK6 than CDK4; inhibition of RB1 phosphorylation observed but publication pending (Freeman-Cook et al. 2021).
The following small kinase inhibitors are annotated as candidate inhibitors of the CDK4 in complex with cyclin D2 (CCND2):
Abemaciclib: annotated as a candidate; inhibits proliferation of acute myeloid leukemia (AML) cells expressing high levels of CCND2 (Nakatani et al. 2021);
Dalpiciclib (SHR6390): annotated as a candidate CDK4 inhibitor; binding to and inhibition of CDK4 have not been tested outside the patent registration (patent numberWO2014183520A1); inhibits RB1 phosphorylation at residue S780 (Wang et al. 2017, Long et al. 2019);
Palbociclib (PD-0332991): annotated as a candidate; leads to G1 arrest in CCND2 expressing cells (Smith et al. 2016, Nakatani et al. 2021).
The following small kinase inhibitors have been shown to compete with ATP binding and inhibit the catalytic activity of CDK4 in the context of the CDK4 complex with cyclin D3 (CCND3):
Abemaciclib (LY2835219): also shown to inhibit RB1 phosphorylation at S807 and S811 (Chen et al. 2016);
Dinaciclib (SHC727965): inhibits CDK4-mediated phosphorylation of RB1 on residues S807 and S811 (Chen et al. 2016);
Palbociclib (PD-0332991): inhibits the complex of CDK4 and CCND3 (Fry et al. 2004; Chen et al. 2016); inhibits CDK4-mediated phosphorylation of RB1 on residues S780 and S795 (Fry et al. 2004), as well as S807 and S811 (Chen et al. 2016); the effect may depend on the association of the CDK4:CCND3 dimer with p21 and p27, so that palbociclib is effective against the trimers of CDK4, CCND3 and p21/p27, and ineffective against CDK4:CCND3 dimers (Paternot et al. 2014);
Ribociclib (LE-0011): inhibits CDK4-mediated phosphorylation of RB1 on residues S807 and S811, but is less potent than palbociclib (Chen et al. 2016);
Dalpiciclib (SHR6390): annotated as a candidate CDK4 inhibitor; binding to and inhibition of CDK4 have not been tested outside the patent registration (patent number WO2014183520A1); inhibits RB1 phosphorylation at residue S780 (Wang et al. 2017, Long et al. 2019).",
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}
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}
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},
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{
"ec_number": "2.7.11.25",
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}
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},
{
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}
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},
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}
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}
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},
{
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},
{
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}
]
},
{
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}
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{
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}
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},
{
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}
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]
},
{
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]
}
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},
{
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]
}
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},
{
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]
}
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{
"ec_number": "2.3.2.27",
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]
},
{
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}
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]
},
{
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]
}
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]
},
{
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]
}
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},
{
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}
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},
{
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]
}
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},
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{
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},
{
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]
}
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]
},
{
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}
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]
},
{
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]
}
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},
{
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}
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{
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{
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}
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},
{
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}
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},
{
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}
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]
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},
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}
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},
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{
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"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
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]
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{
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]
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]
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]
},
{
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}
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]
},
{
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]
},
{
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]
},
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]
}
]
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]
},
{
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]
}
]
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]
},
{
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"id": "Q14296",
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]
},
{
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]
},
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"id": "Q14296",
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]
}
]
},
{
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"ec_number": "2.7.11.1",
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]
},
{
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]
},
{
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"id": "Q14680",
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]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
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]
},
{
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]
},
{
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{
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}
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}
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}
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{
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}
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}
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{
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{
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}
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{
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{
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{
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{
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{
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}
]
},
{
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]
},
{
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]
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]
},
{
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]
},
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{
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{
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{
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{
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{
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{
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]
},
{
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]
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{
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