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Search results 201 to 300 out of 1163 for Cdc6

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Type Details Score
Publication
12614612 | J:82383
First Author: Kneissl M
Year: 2003
Journal: J Mol Biol
Title: Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells.
Volume: 327
Issue: 1
Pages: 111-28
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Publication
23624920 | J:212365
First Author: Ito K
Year: 2014
Journal: Oncogene
Title: Overexpression of Cdk6 and Ccnd1 in chondrocytes inhibited chondrocyte maturation and caused p53-dependent apoptosis without enhancing proliferation.
Volume: 33
Issue: 14
Pages: 1862-71
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Protein
A0A0R4J145
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein Coding Gene
MGI:1289325 | Anapc16
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:102685 | Cdc27
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913406 | Anapc11
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:107411 | Ube2e1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098815 | Cdc23
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2139135 | Anapc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:103097 | Anapc1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915862 | Ube2c
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913690 | Cdc26
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098673 | Anapc4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1929711 | Anapc7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1929722 | Anapc5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1925141 | Ube2s
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:88316 | Ccne1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1922680 | Anapc15
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1917207 | Cdc16
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1916249 | Anapc10
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q8BGZ4
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
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Protein
Q8K2H6
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
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Protein
P60007
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: false
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Protein
Q61457
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Protein
Q91W96
Organism: Mus musculus/domesticus
Length: 807  
Fragment?: false
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Protein
P53995
Organism: Mus musculus/domesticus
Length: 1944  
Fragment?: false
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Protein
Q8BTZ4
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
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Protein
Q9CPX9
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: false
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Protein
Q9CPV2
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: false
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Protein
Q9WVM3
Organism: Mus musculus/domesticus
Length: 565  
Fragment?: false
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Protein
Q8R349
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false
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Protein
Q99JP4
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: false
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Protein
A2A6Q5
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
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Protein
P52482
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
Q9D1C1
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q921J4
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
Q9D8W5
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
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Publication
1600944 | -
First Author: Bueno A
Year: 1992
Journal: EMBO J
Title: Dual functions of CDC6: a yeast protein required for DNA replication also inhibits nuclear division.
Volume: 11
Issue: 6
Pages: 2167-76
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Publication
9312054 | -
First Author: Drury LS
Year: 1997
Journal: EMBO J
Title: The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast.
Volume: 16
Issue: 19
Pages: 5966-76
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Publication
7916658 | -
First Author: Kelly TJ
Year: 1993
Journal: Cell
Title: The fission yeast cdc18+ gene product couples S phase to START and mitosis.
Volume: 74
Issue: 2
Pages: 371-82
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Publication
8521469 | -
First Author: Nishitani H
Year: 1995
Journal: Cell
Title: p65cdc18 plays a major role controlling the initiation of DNA replication in fission yeast.
Volume: 83
Issue: 3
Pages: 397-405
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Publication
9203581 | -
First Author: Kominami K
Year: 1997
Journal: Genes Dev
Title: Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18.
Volume: 11
Issue: 12
Pages: 1548-60
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Publication
10766248 | -
First Author: Nishitani H
Year: 2000
Journal: Nature
Title: The Cdt1 protein is required to license DNA for replication in fission yeast.
Volume: 404
Issue: 6778
Pages: 625-8
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Publication
11988741 | -
First Author: Murakami H
Year: 2002
Journal: Nat Cell Biol
Title: Maintenance of replication forks and the S-phase checkpoint by Cdc18p and Orp1p.
Volume: 4
Issue: 5
Pages: 384-8
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Publication
11532929 | -
First Author: Yanow SK
Year: 2001
Journal: EMBO J
Title: Expression of Cdc18/Cdc6 and Cdt1 during G2 phase induces initiation of DNA replication.
Volume: 20
Issue: 17
Pages: 4648-56
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Protein Domain
IPR016314 | Cdc6/18
Type: Family
Description: This group represents the cell division control protein Cdc6 and Cdc18, which are essential initiation factors for DNA replication [].Cdc6 appears to have an important and perhaps unique dual role in S phase, it is first required for the initiation of DNA replication and then actively participates in the suppression of nuclear division. It interacts with the origin recognition complex (ORC). It targeted for degradation by the E3 ubiquitin ligase complex SCF (Cdc4) [, ].Cdc18 is part of the checkpoint control that prevents mitosis from occurring until S phase is completed. It plays a key role in coupling S phase to start and mitosis. It acts at the initiation of DNA replication and plays a major role in controlling the onset of S-phase. Together with orp1, it is involved in the maintenance of replication forks and activation of cds1-dependent S-phase checkpoint [, , , , ].
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Protein Coding Gene
MGI:104772 | Cdk2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108069 | Ccna2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108042 | Ccna1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P51943
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q61456
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
P97377
Organism: Mus musculus/domesticus
Length: 346  
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 Coding Gene
MGI:2384911 | Ube2d1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P61080
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Publication
15286659 | J:116246
First Author: Lee C
Year: 2004
Journal: Nature
Title: Structural basis for inhibition of the replication licensing factor Cdt1 by geminin.
Volume: 430
Issue: 7002
Pages: 913-7
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Publication
15989956 | -
First Author: Chen D
Year: 2005
Journal: Cell
Title: ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor.
Volume: 121
Issue: 7
Pages: 1071-83
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Publication
18488021 | J:145660
First Author: Zhao X
Year: 2008
Journal: Nat Cell Biol
Title: The HECT-domain ubiquitin ligase Huwe1 controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.
Volume: 10
Issue: 6
Pages: 643-53
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Protein
P63325
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
Q3UW83
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Publication
15989957 | -
First Author: Zhong Q
Year: 2005
Journal: Cell
Title: Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis.
Volume: 121
Issue: 7
Pages: 1085-95
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Protein
A0A338P731
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
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Protein
A0A338P7K4
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: false
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Protein
Q3U9P0
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
Q9D6F5
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
Q5M9K7
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Publication
8248124 | J:20862
First Author: Lai E
Year: 1993
Journal: Proc Natl Acad Sci U S A
Title: Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: a family of transcription factors of diverse biologic function.
Volume: 90
Issue: 22
Pages: 10421-3
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Publication
11292844 | -
First Author: Cicero MP
Year: 2001
Journal: Nucleic Acids Res
Title: The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity.
Volume: 29
Issue: 8
Pages: 1715-23
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Publication
8577730 | -
First Author: Clubb RT
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition.
Volume: 93
Issue: 3
Pages: 1146-50
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Publication
15567145 | -
First Author: Yoon SY
Year: 2005
Journal: Biochem Biophys Res Commun
Title: Over-expression of human UREB1 in colorectal cancer: HECT domain of human UREB1 inhibits the activity of tumor suppressor p53 protein.
Volume: 326
Issue: 1
Pages: 7-17
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Publication
19713937 | -
First Author: Parsons JL
Year: 2009
Journal: EMBO J
Title: Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.
Volume: 28
Issue: 20
Pages: 3207-15
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Publication
19906994 | -
First Author: De Marco V
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing.
Volume: 106
Issue: 47
Pages: 19807-12
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Publication
12059957 | -
First Author: Nishitani H
Year: 2002
Journal: Genes Cells
Title: Control of DNA replication licensing in a cell cycle.
Volume: 7
Issue: 6
Pages: 523-34
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Protein Domain
IPR041918 | UBA_HUWE1
Type: Domain
Description: HUWE1 (also known as HECT, UBA and WWE domain-containing protein 1, or Mcl-1 ubiquitin ligase E3, amongst other names) may function as a ubiquitin-protein ligase involved in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase, and modulates base excision repair (BER) []. HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation []. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involved in DNA damage-induced apoptosis []. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation [].HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N terminus and a HECT domain at the C terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain is involved in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway [].
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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
IPR036388 | WH-like_DNA-bd_sf
Type: Homologous_superfamily
Description: Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif, where the "wings", or loops, are small β-sheets. The winged helix motif consists of two wings (W1, W2), three α-helices (H1, H2, H3) and three β-sheets (S1, S2, S3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 []. The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA, while the wings make different DNA contacts, often with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain, including transcriptional repressors such as biotin repressor, LexA repressor and the arginine repressor []; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation, heat-shock transcription factor, and the general transcription factors TFIIE and TFIIF [, ]; helicases such as RuvB that promotes branch migration at the Holliday junction, and CDC6 in the pre-replication complex [, ]; endonucleases such as FokI and TnsA []; histones; and Mu transposase, where the flexible wing of the enhancer-binding domain is essential for efficient transposition [].
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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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Protein Domain
IPR045173 | Cdt1
Type: Family
Description: Precise duplication of chromosomal DNA is required for genomic stability during replication. A process called replication licensing ensures that chromosomes are replicated only once per cell cycle. To form a pre-replicative complex on replication origins in the G phase, ORC first binds origin DNA and triggers the binding of Cdc6 and Cdt1. These two factors recruit a putative replicative helicase and the MCM2-7. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication in S-phase. Cdt1 is present during G1 and early S phase of the cell cycle and degraded during the late S, G2, and M phases [, ].This entry represents Cdt1, which can be divided into three regions based on sequence comparison and biochemical analyses: the N-terminal region (Cdt1_n) binds DNA in a sequence-, strand-, and conformation-independent manner; the middle winged helix fold (Cdt1_m) binds geminin to inhibit both binding of the MCM complex to origins of replication and DNA; and the C-terminal region (Cdt1_c) is essential for Cdt1 activity and directly interacts with the MCM2-7 helicase. The winged helix fold structure of Cdt1_m is similar to the structures of Cdt1_c and other archaeal homologues of the eukaryotic replication initiator, without apparent sequence similarity [, ].
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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
Q9R0A0
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
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Protein
Q9CY94
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
F6VZ99
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
A0A1D5RLV2
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
D6RH82
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
Q3UG93
Organism: Mus musculus/domesticus
Length: 432  
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 α-helical (A) and β-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 α-helical (A) and β-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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Protein Coding Gene
MGI:1917497 | Psmd1
Type: protein_coding_gene
Organism: mouse, laboratory
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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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