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Search results 201 to 300 out of 323 for Cdt1

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Type Details Score
Publication
31670387 | J:282102
     
First Author: CaƱizares MA
Year: 2019
Journal: J Anat
Title: Multiple steps characterise ventricular layer attrition to form the ependymal cell lining of the adult mouse spinal cord central canal.
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Publication
21543332 | J:344854
First Author: Pefani DE
Year: 2011
Journal: J Biol Chem
Title: Idas, a novel phylogenetically conserved geminin-related protein, binds to geminin and is required for cell cycle progression.
Volume: 286
Issue: 26
Pages: 23234-46
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Publication
21098278 | J:167149
First Author: Ohno Y
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: Hoxb4 transduction down-regulates Geminin protein, providing hematopoietic stem and progenitor cells with proliferation potential.
Volume: 107
Issue: 50
Pages: 21529-34
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Publication
18339895 | J:138468
First Author: Waning DL
Year: 2008
Journal: Blood
Title: Cul4A is required for hematopoietic cell viability and its deficiency leads to apoptosis.
Volume: 112
Issue: 2
Pages: 320-9
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Publication
17556357 | J:124806
First Author: Srinivasan SV
Year: 2007
Journal: J Biol Chem
Title: RB loss promotes aberrant ploidy by deregulating levels and activity of DNA replication factors.
Volume: 282
Issue: 33
Pages: 23867-77
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Publication
20454618 | J:160923
First Author: Chen P
Year: 2010
Journal: PLoS One
Title: Jnk2 effects on tumor development, genetic instability and replicative stress in an oncogene-driven mouse mammary tumor model.
Volume: 5
Issue: 5
Pages: e10443
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Publication
24154524 | J:204962
First Author: Sakaue-Sawano A
Year: 2013
Journal: Development
Title: Visualizing developmentally programmed endoreplication in mammals using ubiquitin oscillators.
Volume: 140
Issue: 22
Pages: 4624-32
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Publication
14973488 | J:89075
First Author: Del Bene F
Year: 2004
Journal: Nature
Title: Direct interaction of geminin and Six3 in eye development.
Volume: 427
Issue: 6976
Pages: 745-9
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Publication
23026135 | J:192049
First Author: Shen L
Year: 2012
Journal: Cancer Res
Title: Geminin functions downstream of p53 in K-ras-induced gene amplification of dihydrofolate reductase.
Volume: 72
Issue: 23
Pages: 6153-62
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Publication
24648314 | J:210976
First Author: Yang YL
Year: 2014
Journal: J Pathol
Title: Lung tumourigenesis in a conditional Cul4A transgenic mouse model.
Volume: 233
Issue: 2
Pages: 113-23
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Protein Coding Gene
MGI:1354944 | Orc3
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
29599208 | J:261429
First Author: Carroll TD
Year: 2018
Journal: J Cell Biol
Title: Lgr5+ intestinal stem cells reside in an unlicensed G1 phase.
Volume: 217
Issue: 5
Pages: 1667-1685
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Publication
29872037 | J:353594
First Author: Muta Y
Year: 2018
Journal: Nat Commun
Title: Composite regulation of ERK activity dynamics underlying tumour-specific traits in the intestine.
Volume: 9
Issue: 1
Pages: 2174
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Publication
32494068 | J:294099
First Author: Muench DE
Year: 2020
Journal: Nature
Title: Mouse models of neutropenia reveal progenitor-stage-specific defects.
Volume: 582
Issue: 7810
Pages: 109-114
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Publication
37642236 | J:342025
First Author: De Chiara L
Year: 2023
Journal: Am J Physiol Cell Physiol
Title: Polyploid tubular cells initiate a TGF-Ī²1 controlled loop that sustains polyploidization and fibrosis after acute kidney injury.
Volume: 325
Issue: 4
Pages: C849-C861
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Publication
33257474 | J:302342
 
First Author: Bornes L
Year: 2021
Journal: Life Sci Alliance
Title: Scratch-induced partial skin wounds re-epithelialize by sheets of independently migrating keratinocytes.
Volume: 4
Issue: 1
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Publication
35730565 | J:327325
 
First Author: Osaki Y
Year: 2022
Journal: JCI Insight
Title: Blocking cell cycle progression through CDK4/6 protects against chronic kidney disease.
Volume: 7
Issue: 12
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Publication
30654924 | J:279523
First Author: Spitzer SO
Year: 2019
Journal: Neuron
Title: Oligodendrocyte Progenitor Cells Become Regionally Diverse and Heterogeneous with Age.
Volume: 101
Issue: 3
Pages: 459-471.e5
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Protein Domain
IPR038437 | GINS_Psf3_sf
Type: Homologous_superfamily
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the pre-replication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp. This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].The GINS complex is essential for initiation of DNA replication in Xenopus egg extracts []. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes. This superfamily represents the Psf3 component.
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Protein Domain
IPR010492 | GINS_Psf3
Type: Family
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the pre-replication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp. This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].The GINS complex is essential for initiation of DNA replication in Xenopusegg extracts []. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes. This family of proteins represents the Psf3 component.
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Protein Domain
IPR007257 | GINS_Psf2
Type: Family
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the prereplication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp.This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].The GINS complex is essential for initiation of DNA replication in Xenopus egg extracts []. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes. This family of proteins represents the Psf2 component.
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Protein Domain
IPR005339 | GINS_Psf1
Type: Family
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the prereplication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp.This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].This family of proteins represents the PSF1 component (for partner of SLD five) of the GINS complex.
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Publication
35443279 | J:326289
First Author: Leung W
Year: 2022
Journal: Cancer Discov
Title: SETD2 Haploinsufficiency Enhances Germinal Center-Associated AICDA Somatic Hypermutation to Drive B-cell Lymphomagenesis.
Volume: 12
Issue: 7
Pages: 1782-1803
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Publication
35578835 | J:325655
   
First Author: Miyao T
Year: 2022
Journal: Elife
Title: Integrative analysis of scRNA-seq and scATAC-seq revealed transit-amplifying thymic epithelial cells expressing autoimmune regulator.
Volume: 11
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Publication
36414418 | J:339566
First Author: Medina Rangel PX
Year: 2023
Journal: J Am Soc Nephrol
Title: Cell Cycle and Senescence Regulation by Podocyte Histone Deacetylase 1 and 2.
Volume: 34
Issue: 3
Pages: 433-450
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Publication
37847555 | J:343540
 
First Author: Tian X
Year: 2023
Journal: J Clin Invest
Title: Profilin1 is required for prevention of mitotic catastrophe in murine and human glomerular diseases.
Volume: 133
Issue: 24
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Publication
36195583 | J:332739
First Author: De Chiara L
Year: 2022
Journal: Nat Commun
Title: Tubular cell polyploidy protects from lethal acute kidney injury but promotes consequent chronic kidney disease.
Volume: 13
Issue: 1
Pages: 5805
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Publication
38706869 | J:351970
First Author: Krotenberg Garcia A
Year: 2024
Journal: iScience
Title: Cell competition promotes metastatic intestinal cancer through a multistage process.
Volume: 27
Issue: 5
Pages: 109718
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Publication
29700333 | J:346821
First Author: Murata T
Year: 2018
Journal: Sci Rep
Title: Transient elevation of cytoplasmic calcium ion concentration at a single cell level precedes morphological changes of epidermal keratinocytes during cornification.
Volume: 8
Issue: 1
Pages: 6610
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Publication
25486356 | J:222845
First Author: Mort RL
Year: 2014
Journal: Cell Cycle
Title: Fucci2a: a bicistronic cell cycle reporter that allows Cre mediated tissue specific expression in mice.
Volume: 13
Issue: 17
Pages: 2681-96
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Publication
12730133 | -
First Author: Kubota Y
Year: 2003
Journal: Genes Dev
Title: A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication.
Volume: 17
Issue: 9
Pages: 1141-52
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Publication
12730134 | -
First Author: Takayama Y
Year: 2003
Journal: Genes Dev
Title: GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast.
Volume: 17
Issue: 9
Pages: 1153-65
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Protein
Q9CZ15
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
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Protein
Q8K1A2
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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Protein
Q6ZQH1
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Publication
16485022 | -
First Author: Marinsek N
Year: 2006
Journal: EMBO Rep
Title: GINS, a central nexus in the archaeal DNA replication fork.
Volume: 7
Issue: 5
Pages: 539-45
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Protein
Q9CY94
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
A0A1D5RLV2
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein Domain
IPR021151 | GINS_A
Type: Domain
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the pre-replication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp. This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].The GINS complex is essential for initiation of DNA replication in Xenopus egg extracts []. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes []. The archaeal GINS complex contains two subunits (SSO0772/gins23 and SO1049/gins15 in Sulfolobus) that are poorly conserved homologues of the eukaryotic GINS subunits []. Only Gins23 is included in this entry.The eukaryotic GINS subunits are homologous. The four subunits of the complex consist of two domains each, termed the Ī±-helical (A) and Ī²-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3 [].
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Protein Domain
IPR036224 | GINS_bundle-like_dom_sf
Type: Homologous_superfamily
Description: DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the pre-replication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [, ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases []. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [, ]. Electron microscopy of GINS shows that it forms a ring-like structure [], reminiscent of the structure of PCNA [], the DNA polymerase delta replication clamp. This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [].The GINS complex is essential for initiation of DNA replication in Xenopus egg extracts []. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes []. The archaeal GINS complex contains two subunits (SSO0772/gins23 and SO1049/gins15 in Sulfolobus) that are poorly conserved homologues of the eukaryotic GINS subunits []. Only Gins23 is included in this entry.The eukaryotic GINS subunits are homologous. The four subunits of the complex consist of two domains each, termed the Ī±-helical (A) and Ī²-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3 [].
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Protein
Q9D600
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
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Publication
25847135 | J:278555
First Author: Glover JD
Year: 2015
Journal: Pigment Cell Melanoma Res
Title: Maintenance of distinct melanocyte populations in the interfollicular epidermis.
Volume: 28
Issue: 4
Pages: 476-80
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Publication
28894084 | J:247623
First Author: Ichijo R
Year: 2017
Journal: Nat Commun
Title: Tbx3-dependent amplifying stem cell progeny drives interfollicular epidermal expansion during pregnancy and regeneration.
Volume: 8
Issue: 1
Pages: 508
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Publication
38428422 | J:346164
First Author: Collins A
Year: 2024
Journal: Cell
Title: Maternal inflammation regulates fetal emergency myelopoiesis.
Volume: 187
Issue: 6
Pages: 1402-1421.e21
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Publication
38849354 | J:349721
First Author: Borisova E
Year: 2024
Journal: Nat Commun
Title: Protein translation rate determines neocortical neuron fate.
Volume: 15
Issue: 1
Pages: 4879
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Publication
33972733 | J:311421
First Author: McGinn J
Year: 2021
Journal: Nat Cell Biol
Title: A biomechanical switch regulates the transition towards homeostasis in oesophageal epithelium.
Volume: 23
Issue: 5
Pages: 511-525
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Publication
27867006 | J:252213
First Author: Matsu-Ura T
Year: 2016
Journal: Mol Cell
Title: Intercellular Coupling of the Cell Cycle and Circadian Clock in Adult Stem Cell Culture.
Volume: 64
Issue: 5
Pages: 900-912
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Publication
39423130 | J:358092
First Author: PivoňkovĆ” H
Year: 2024
Journal: Cell Rep
Title: Heterogeneity in oligodendrocyte precursor cell proliferation is dynamic and driven by passive bioelectrical properties.
Volume: 43
Issue: 11
Pages: 114873
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Publication
30458140 | J:267034
First Author: Ford MJ
Year: 2018
Journal: Dev Cell
Title: A Cell/Cilia Cycle Biosensor for Single-Cell Kinetics Reveals Persistence of Cilia after G1/S Transition Is a General Property in Cells and Mice.
Volume: 47
Issue: 4
Pages: 509-523.e5
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Publication
8001157 | -
First Author: Krishna TS
Year: 1994
Journal: Cell
Title: Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA.
Volume: 79
Issue: 7
Pages: 1233-43
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Publication
20130679 | -
First Author: Kawakami H
Year: 2010
Journal: Biochem Cell Biol
Title: DnaA, ORC, and Cdc6: similarity beyond the domains of life and diversity.
Volume: 88
Issue: 1
Pages: 49-62
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Publication
19344485 | -
First Author: Duncker BP
Year: 2009
Journal: Genome Biol
Title: The origin recognition complex protein family.
Volume: 10
Issue: 3
Pages: 214
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Publication
18048387 | -
First Author: Borlado LR
Year: 2008
Journal: Carcinogenesis
Title: CDC6: from DNA replication to cell cycle checkpoints and oncogenesis.
Volume: 29
Issue: 2
Pages: 237-43
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Publication
12628342 | -
First Author: Pelizon C
Year: 2003
Journal: Trends Cell Biol
Title: Down to the origin: Cdc6 protein and the competence to replicate.
Volume: 13
Issue: 3
Pages: 110-3
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Publication
15004237 | -
First Author: Ofir Y
Year: 2004
Journal: Mol Biol Cell
Title: The role and regulation of the preRC component Cdc6 in the initiation of premeiotic DNA replication.
Volume: 15
Issue: 5
Pages: 2230-42
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Protein Domain
IPR016811 | ORC6_fun
Type: Family
Description: The Origin Recognition Complex (ORC) is a six-subunit ATP-dependent DNA-binding complex encoded in yeast by ORC1-6 []. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle []. ORC directs DNA replication throughout the genome and is required for its initiation [, , ]. ORC bound at replication origins serves as the foundation for assembly of the pre-replicative complex (pre-RC), which includes Cdc6, Tah11 (aka Cdt1), and the Mcm2-7 complex [, , ]. Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase [, , ]. Cell cycle-regulated phosphorylation of ORC2, ORC6, Cdc6, and MCM by the cyclin-dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocking reinitiation in G2/M phase [, , , ]. In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR) [, , ]. ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers [, , ]. Both ORC1 and ORC5 bind ATP, although only ORC1 has ATPase activity []. The binding of ATP by ORC1 is required for ORC binding to DNA and is essential for cell viability []. The ATPase activity of ORC1 is involved in formation of the pre-RC [, , ]. ATP binding by ORC5 is crucial for the stability of ORC as a whole. Only the ORC1-5 subunits are required for origin binding; ORC6 is essential for maintenance of pre-RCs once formed []. Interactions within ORC suggest that ORC2-3-6 may form a core complex []. ORC homologues have been found in various eukaryotes, including fission yeast, insects, amphibians, and humans []. This entry represents subunit 6, which directs DNA replication by binding to replication origins and is also involved in transcriptional silencing; interacts with Spp1 and with trimethylated histone H3; phosphorylated by Cdc28 [, ]. In Saccharomyces cerevisiae (Baker's yeast), both ends of the Orc6 interact with Cdt1 []and the N terminus mediates an interaction with the S-phase cyclin Clb5 [].
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Protein Domain
IPR008721 | ORC6
Type: Family
Description: The Origin Recognition Complex (ORC) is a six-subunit ATP-dependent DNA-binding complex encoded in yeast by ORC1-6 []. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle []. ORC directs DNA replication throughout the genome and is required for its initiation [, , ]. ORC bound at replication origins serves as the foundation for assembly of the pre-replicative complex (pre-RC), which includes Cdc6, Tah11 (aka Cdt1), and the Mcm2-7 complex [, , ]. Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase [, , ]. Cell cycle-regulated phosphorylation of ORC2, ORC6, Cdc6, and MCM by the cyclin-dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocking reinitiation in G2/M phase [, , , ]. In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR) [, , ]. ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers [, , ]. Both ORC1 and ORC5 bind ATP, although only ORC1 has ATPase activity []. The binding of ATP by ORC1 is required for ORC binding to DNA and is essential for cell viability []. The ATPase activity of ORC1 is involved in formation of the pre-RC [, , ]. ATP binding by ORC5 is crucial for the stability of ORC as a whole. Only the ORC1-5 subunits are required for origin binding; ORC6 is essential for maintenance of pre-RCs once formed []. Interactions within ORC suggest that ORC2-3-6 may form a core complex []. ORC homologues have been found in various eukaryotes, including fission yeast, insects, amphibians, and humans []. This entry represents subunit 6, which directs DNA replication by binding to replication origins and is also involved in transcriptional silencing; interacts with Spp1 and with trimethylated histone H3; phosphorylated by Cdc28 [, ]. In Saccharomyces cerevisiae (Baker's yeast), both ends of the Orc6 interact with Cdt1 []and the N terminus mediates an interaction with the S-phase cyclin Clb5 [].
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Protein Domain
IPR015163 | Cdc6_C
Type: Domain
Description: Cdc6 (also known as Cell division cycle 6 or Cdc18) functions as a regulator at the early stages of DNA replication, by helping to recruit and load the Minichromosome Maintenance Complex (MCM) onto DNA and may have additional roles in the control of mitotic entry. Precise duplication of chromosomal DNA is required for genomic stability during replication. Cdc6 has an essential role in DNA replication and irregular expression of Cdc6 may lead to genomic instability. Cdc6 over-expression is observed in many cancerous lesions. DNA replication begins when an origin recognition complex (ORC) binds to a replication origin site on the chromatin. Studies indicate that Cdc6 interacts with ORC through the Orc1 subunit, and that this association increases the specificity of the ORC-origins interaction. Further studies suggest that hydrolysis of Cdc6-bound ATP promotes the association of the replication licensing factor Cdt1 with origins through an interaction with Orc6 and this in turn promotes the loading of MCM2-7 helicase onto chromatin. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication. S-Cdk (S-phase cyclin and cyclin-dependent kinase complex) prevents rereplication by causing the Cdc6 protein to dissociate from ORC and prevents the Cdc6 and MCM proteins from reassembling at any origin. By phosphorylating Cdc6, S-Cdk also triggers Cdc6's ubiquitination. The Cdc6 protein is composed of three domains, an N-terminal AAA+ domain with Walker A and B, and Sensor-1 and -2 motifs. The central region contains a conserved nucleotide binding/ATPase domain and is a member of the ATPase superfamily. [, , , , ].The C-terminal domain of cell division control protein 6 (CDC6) assumes a winged helix fold, with a five Ī±-helical bundle (Ī±15-Ī±19) structure, backed on one side by three beta strands (Ī²6-Ī²8). It has been shown that this domain acts as a DNA-localisation factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate CDC6 activity [].
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Protein
Q99LZ3
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Publication
14574415 | -
First Author: Ubersax JA
Year: 2003
Journal: Nature
Title: Targets of the cyclin-dependent kinase Cdk1.
Volume: 425
Issue: 6960
Pages: 859-64
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Publication
15105375 | -
First Author: Wilmes GM
Year: 2004
Journal: Genes Dev
Title: Interaction of the S-phase cyclin Clb5 with an "RXL" docking sequence in the initiator protein Orc6 provides an origin-localized replication control switch.
Volume: 18
Issue: 9
Pages: 981-91
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Publication
17417653 | -
First Author: Kamada K
Year: 2007
Journal: Nat Struct Mol Biol
Title: Structure of the human GINS complex and its assembly and functional interface in replication initiation.
Volume: 14
Issue: 5
Pages: 388-96
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Publication
34260928 | J:323596
First Author: Kohnke S
Year: 2021
Journal: Cell Rep
Title: Nutritional regulation of oligodendrocyte differentiation regulates perineuronal net remodeling in the median eminence.
Volume: 36
Issue: 2
Pages: 109362
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Publication
30595533 | J:272582
First Author: Gupta K
Year: 2019
Journal: Dev Cell
Title: Single-Cell Analysis Reveals a Hair Follicle Dermal Niche Molecular Differentiation Trajectory that Begins Prior to Morphogenesis.
Volume: 48
Issue: 1
Pages: 17-31.e6
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Publication
35421372 | J:324528
First Author: Qu R
Year: 2022
Journal: Dev Cell
Title: Decomposing a deterministic path to mesenchymal niche formation by two intersecting morphogen gradients.
Volume: 57
Issue: 8
Pages: 1053-1067.e5
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Publication
33504783 | J:301277
First Author: Renders S
Year: 2021
Journal: Nat Commun
Title: Niche derived netrin-1 regulates hematopoietic stem cell dormancy via its receptor neogenin-1.
Volume: 12
Issue: 1
Pages: 608
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Publication
23175634 | J:196795
First Author: Abe T
Year: 2013
Journal: Development
Title: Visualization of cell cycle in mouse embryos with Fucci2 reporter directed by Rosa26 promoter.
Volume: 140
Issue: 1
Pages: 237-46
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Publication
29849154 | J:262422
First Author: Wong FK
Year: 2018
Journal: Nature
Title: Pyramidal cell regulation of interneuron survival sculpts cortical networks.
Volume: 557
Issue: 7707
Pages: 668-673
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Publication
35793629 | J:337662
First Author: Wong FK
Year: 2022
Journal: Cell Rep
Title: Serotonergic regulation of bipolar cell survival in the developing cerebral cortex.
Volume: 40
Issue: 1
Pages: 111037
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Publication
36460641 | J:332132
First Author: Cattaneo P
Year: 2022
Journal: Nat Commun
Title: DOT1L regulates chamber-specific transcriptional networks during cardiogenesis and mediates postnatal cell cycle withdrawal.
Volume: 13
Issue: 1
Pages: 7444
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Publication
37330549 | J:347041
First Author: Zhu F
Year: 2023
Journal: Nat Commun
Title: Spatiotemporal resolution of germinal center Tfh cell differentiation and divergence from central memory CD4(+) T cell fate.
Volume: 14
Issue: 1
Pages: 3611
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Publication
35947676 | J:343830
First Author: Melica ME
Year: 2022
Journal: Sci Transl Med
Title: Differentiation of crescent-forming kidney progenitor cells into podocytes attenuates severe glomerulonephritis in mice.
Volume: 14
Issue: 657
Pages: eabg3277
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Publication
30063206 | J:267642
   
First Author: Biggs LC
Year: 2018
Journal: Elife
Title: Hair follicle dermal condensation forms via Fgf20 primed cell cycle exit, cell motility, and aggregation.
Volume: 7
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Publication
11030343 | -
First Author: Liu J
Year: 2000
Journal: Mol Cell
Title: Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.
Volume: 6
Issue: 3
Pages: 637-48
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Publication
11914271 | -
First Author: Bell SP
Year: 2002
Journal: Genes Dev
Title: The origin recognition complex: from simple origins to complex functions.
Volume: 16
Issue: 6
Pages: 659-72
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Publication
38441552 | J:346767
   
First Author: Lan Q
Year: 2024
Journal: Elife
Title: Mesenchyme instructs growth while epithelium directs branching in the mouse mammary gland.
Volume: 13
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Publication
32619424 | J:292118
First Author: Venturutti L
Year: 2020
Journal: Cell
Title: TBL1XR1 Mutations Drive Extranodal Lymphoma by Inducing a Pro-tumorigenic Memory Fate.
Volume: 182
Issue: 2
Pages: 297-316.e27
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Publication
32396861 | J:289028
First Author: BĆ©guelin W
Year: 2020
Journal: Cancer Cell
Title: Mutant EZH2 Induces a Pre-malignant Lymphoma Niche by Reprogramming the Immune Response.
Volume: 37
Issue: 5
Pages: 655-673.e11
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Publication
37367826 | J:337680
 
First Author: MyllymƤki SM
Year: 2023
Journal: J Cell Biol
Title: Spatially coordinated cell cycle activity and motility govern bifurcation of mammary branches.
Volume: 222
Issue: 9
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Publication
31422913 | J:287443
First Author: Han S
Year: 2019
Journal: Cell Stem Cell
Title: Defining the Identity and Dynamics of Adult Gastric Isthmus Stem Cells.
Volume: 25
Issue: 3
Pages: 342-356.e7
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Publication
31736464 | J:292767
   
First Author: Llorca A
Year: 2019
Journal: Elife
Title: A stochastic framework of neurogenesis underlies the assembly of neocortical cytoarchitecture.
Volume: 8
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Protein
Q9WUJ8
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
A0A1B0GR56
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
Q66JV6
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
A0A1B0GRE5
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
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Protein
A0A1B0GSE2
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
O89033
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
A0A0R4J145
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q8C5L1
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: true
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Protein
P97311
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q9Z1N2
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: false
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Protein
Q542I2
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q3UC10
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q3UR71
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: false
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Protein
Q3TPY7
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: false
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Protein
Q59IX2
Organism: Mus musculus/domesticus
Length: 805  
Fragment?: false
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Protein
Q8C9G3
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: false
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Protein
Q8CFY7
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: true
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Protein
Q3ULG5
Organism: Mus musculus/domesticus
Length: 794  
Fragment?: false
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Publication
17241905 | -
 
First Author: Chesnokov IN
Year: 2007
Journal: Int Rev Cytol
Title: Multiple functions of the origin recognition complex.
Volume: 256
Pages: 69-109
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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