Affinage

ORC3

Origin recognition complex subunit 3 · UniProt Q9UBD5

Length
711 aa
Mass
82.3 kDa
Annotated
2026-06-10
45 papers in source corpus 22 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ORC3 is a core structural subunit of the six-member origin recognition complex (ORC), the eukaryotic replication initiator that licenses origins for DNA replication (PMID:7585959, PMID:10402192). Within the complex it occupies a defined position in the Orc1:Orc4:Orc5:Orc2:Orc3 arrangement, where it forms part of the stable ORC2-5 core and contributes a hinge at the ORC5·ORC3 interface that supports the conformational opening needed for DNA binding (PMID:22405012, PMID:32808929). ORC3 directly binds ORC6 through a dedicated domain, an interaction required for assembly of functional ORC and for loading of the MCM2-7 helicase; disruption of this interface underlies a Meier-Gorlin syndrome mutation in ORC6 (PMID:24137536). During helicase loading ORC3, together with ORC6, recruits ORC to the MCM hexamer dimerization interface and provides an 'ORC3 tether' element that enables an ORC6-independent loading route, while the Mcm5 C-terminus contacts ORC3 to drive a pre-RC assembly step that triggers Mcm4 ATP hydrolysis and Cdt1 release (PMID:39604729, PMID:39747125). ORC3 activity is cell-cycle regulated: cyclin A/CDK2 phosphorylation of ORC2 dissociates ORC3 from chromatin, and PP1-mediated dephosphorylation restores binding (PMID:24792176, PMID:24732362), while multi-mono-ubiquitylation of chromatin-bound ORC3 by the OBI1 ligase during S phase is required to activate origin firing (PMID:31160578). Beyond replication, ORC3 directly binds HP1alpha through coiled-coil and mod-interacting region domains to anchor ORC at heterochromatin and maintain satellite-repeat compaction (PMID:20689044), and it is required for replication-dependent proliferation of neural and glial progenitors in vivo (PMID:23110156). The protein additionally interacts with the TREX-2 mRNA export machinery (PMID:27016737) and supports neuronal maturation by suppressing Rho GTPase signaling (PMID:20674557), indicating functions extending beyond origin licensing.

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 High

    Establishing ORC3 as a bona fide subunit of the replication initiator was the first step in defining its function, answering whether the 62 kDa species was a stable structural component of ORC.

    Evidence Recombinant expression in insect cells and reconstitution of the complete six-subunit complex

    PMID:7585959

    Open questions at the time
    • Does not define ORC3's specific contacts within the complex
    • No DNA-binding or origin-recognition role assigned to ORC3 itself
  2. 1999 High

    Cross-species genetics established ORC3 as a conserved, replication-essential subunit, showing the requirement extends to organismal proliferation rather than being an in vitro artifact.

    Evidence Co-IP with ORC2, transgene rescue, and analysis of lethal Drosophila lat mutants

    PMID:10402192

    Open questions at the time
    • Mechanism by which ORC3 loss blocks proliferation not resolved at molecular level
  3. 1999 Medium

    Localization of the ORC3 ortholog to synapses with electrophysiological defects raised the possibility of a non-replication, neuronal function for ORC3.

    Evidence Immunolocalization and electrophysiological recordings at the Drosophila NMJ in lat mutants

    PMID:10402193

    Open questions at the time
    • Molecular mechanism linking ORC3 to synaptic transmission unknown
    • Whether the synaptic role is separable from the replication role unresolved
  4. 2000 Medium

    Detection of ORC subunits in non-proliferating cells supported a function for ORC3 outside replication initiation and hinted at associations with non-ORC proteins.

    Evidence Co-IP under varying extraction stringency and immunohistochemistry across tissues

    PMID:10954718

    Open questions at the time
    • Identity of the non-ORC associated proteins not determined
    • Functional consequence of ORC3 in post-mitotic cells not established here
  5. 2007 Medium

    Defining a direct ORC6-ORC3 contact and cell-cycle-dependent ORC disassembly clarified how ORC3 anchors ORC6 and how the complex is dynamically regulated through S phase.

    Evidence Immunoprecipitation, immunofluorescence, and recombinant expression; complemented by BRET/BiFC showing nuclear and cytoplasmic ORC2-ORC3 interaction

    PMID:17680271 PMID:17716973

    Open questions at the time
    • Domain mediating the ORC6 contact not yet mapped
    • Functional meaning of cytoplasmic ORC2-ORC3 interaction unclear
  6. 2008 High

    Structural mapping placed ORC3 within the subunit arrangement, answering where it sits in the complex relative to ORC2 and ORC6.

    Evidence Single-particle EM with MBP-fusion subunit localization and in vitro IP in S. cerevisiae

    PMID:18647841

    Open questions at the time
    • No DNA-bound conformation resolved
    • Human ORC3 architecture not directly addressed
  7. 2010 High

    Identifying ORC3 as a direct HP1alpha-binding protein established a replication-independent role in heterochromatin organization, defining two distinct interaction domains.

    Evidence Direct binding assays, microscopy, siRNA depletion, and FRAP in human cells

    PMID:20689044

    Open questions at the time
    • Whether heterochromatin anchoring is coupled to origin licensing not resolved
    • Structural basis of dual-domain HP1alpha binding not determined
  8. 2010 Medium

    Placing ORC3 upstream of Rho signaling extended its function to neuronal maturation, linking a receptor input (mGlu4) to ORC3 levels and cytoskeletal signaling.

    Evidence siRNA knockdown with MAP-2/PSD-95/active-Rho readouts and mGlu4 pharmacology in cerebellar granule cells

    PMID:20674557

    Open questions at the time
    • Direct molecular link between ORC3 and Rho regulation not identified
    • Single-lab, in vitro neuronal system only
  9. 2012 High

    Cryo-EM of ORC-Cdc6-DNA defined how the complex engages origin DNA, situating ORC3 in the DNA-wrapping crescent.

    Evidence Single-particle cryo-EM and docking of S. cerevisiae ORC-Cdc6-DNA

    PMID:22405012

    Open questions at the time
    • Direct ORC3-DNA contacts not delineated
    • Human complex not resolved
  10. 2012 Medium

    Conditional knockout established that ORC3 is required in vivo for replication-dependent glial progenitor proliferation, with secondary effects on cortical vasculature.

    Evidence Glial-progenitor conditional knockout in mouse with histological and vascular analysis

    PMID:23110156

    Open questions at the time
    • Does not distinguish replication role from possible non-replication functions in vivo
    • Mechanism of secondary vascular phenotype indirect
  11. 2013 High

    Mapping the ORC6-binding domain of ORC3 and linking its disruption to Meier-Gorlin syndrome connected the ORC3-ORC6 interface directly to MCM2-7 loading and human disease.

    Evidence 3D EM of metazoan ORC, binding assays, mutagenesis, and in vivo MCM loading assays

    PMID:24137536

    Open questions at the time
    • Atomic-resolution structure of the ORC3-ORC6 interface not provided
    • Full spectrum of disease alleles affecting ORC3 not surveyed
  12. 2014 Medium

    Defining cyclin A/CDK2 phosphorylation of ORC2 and PP1 dephosphorylation as the switch controlling ORC3 chromatin binding explained how ORC3 association is dynamically gated across S phase.

    Evidence Co-IP, chromatin fractionation, PP1 inhibitor/overexpression/siRNA in human cells

    PMID:24732362 PMID:24792176

    Open questions at the time
    • ORC3 regulation is indirect via ORC2 phosphorylation; no direct ORC3 modification site identified here
    • Kinetics relative to origin firing not resolved
  13. 2016 Medium

    Identifying a physical ORC-TREX-2 interaction and an mRNA export defect upon Orc3 depletion revealed a role for ORC3 in mRNP nuclear export distinct from replication.

    Evidence Biochemical purification, Co-IP, and RNAi with nuclear mRNA accumulation assay in Drosophila

    PMID:27016737

    Open questions at the time
    • Direct ORC3-TREX-2 contact within ORC not pinpointed here
    • Whether export function requires intact ORC unknown
  14. 2019 High

    Identifying OBI1-catalyzed multi-mono-ubiquitylation of ORC3 as a signal required for origin firing established a post-licensing activation step acting on ORC3.

    Evidence Pre-RC interactome, ubiquitylation and CMG assays, and origin firing analysis with non-ubiquitylable mutants

    PMID:31160578

    Open questions at the time
    • Downstream reader of the ubiquitin mark not identified
    • How ubiquitylation mechanistically licenses firing not fully resolved
  15. 2020 High

    Human ORC cryo-EM structures defined ORC2-5 as a stable core and identified the ORC5·ORC3 hinge governing the conformational dynamics needed for DNA engagement.

    Evidence Five independent single-particle cryo-EM structures of human ORC

    PMID:32808929

    Open questions at the time
    • DNA-bound human ORC not captured in these states
    • Functional test of hinge mutants not reported
  16. 2024 High

    Reconstitution of human MCM loading defined the mechanistic role of ORC3 and its tether in recruiting ORC to the MCM hexamer and enabling ORC6-independent loading.

    Evidence Biochemical reconstitution of human MCM loading with EM of loading intermediates

    PMID:39604729

    Open questions at the time
    • Atomic details of the ORC3 tether-MCM contact not fully resolved here
    • Relative usage of ORC6-dependent vs -independent routes in cells unknown
  17. 2025 High

    A cryo-EM intermediate showing the Mcm5 C-terminus contacting ORC3 pinpointed how ORC3 reads the closed MCM2/Mcm5 ring to trigger Mcm4 ATP hydrolysis and Cdt1 release during pre-RC assembly.

    Evidence Cryo-EM of an ORC-Cdc6-Cdt1-MCM2-7 intermediate with interface mutagenesis and loading assays

    PMID:39747125

    Open questions at the time
    • Whether this step is conserved in ORC6-independent loading not addressed
    • Timing relative to ORC3 ubiquitylation not integrated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ORC3's distinct activities — origin licensing, heterochromatin anchoring, mRNA export, and neuronal Rho signaling — are coordinated and whether they share a common molecular basis remains unresolved.
  • No unified model connecting replication and non-replication ORC3 functions
  • Human ORC3-TREX-2 interface only inferred from low-confidence Co-IP
  • Direct molecular link between ORC3 and Rho regulation undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0060090 molecular adaptor activity 3 GO:0003677 DNA binding 1 GO:0140096 catalytic activity, acting on a protein 1
Localization
GO:0000228 nuclear chromosome 2 GO:0005634 nucleus 2 GO:0005829 cytosol 1
Pathway
R-HSA-69306 DNA Replication 3 R-HSA-1640170 Cell Cycle 2 R-HSA-1643685 Disease 1 R-HSA-4839726 Chromatin organization 1 R-HSA-8953854 Metabolism of RNA 1
Complex memberships
ORC (origin recognition complex)TREX-2/THSCpre-replicative complex (pre-RC)

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 ORC3 (62 kDa subunit) is one of the six subunits of the origin recognition complex (ORC); all six subunits were reconstituted as a complete complex after expression in insect cells, establishing ORC3 as a core structural component of the replication initiator. Recombinant protein expression in insect cells and complex reconstitution Cell High 7585959
1999 Drosophila Latheo (ORC3 ortholog) associates with ORC2 and is functionally related to yeast ORC3, establishing that LAT/ORC3 is a conserved subunit required for DNA replication and cell proliferation; homozygous lethal lat mutants show absence of imaginal discs and lack CNS cell proliferation, rescued by a lat+ transgene. Co-immunoprecipitation, transgene rescue, genetic analysis of lethal mutants Neuron High 10402192
1999 Drosophila LAT (ORC3 ortholog) protein localizes to synaptic connections at the larval NMJ and is enriched in presynaptic boutons; lat mutants show elevated basal synaptic transmission and loss of Ca2+-dependent synaptic facilitation and posttetanic potentiation. Immunological localization, electrophysiological recordings at NMJ in lat mutants Neuron Medium 10402193
2000 Human ORC2, ORC3, and ORC5 are detected in non-proliferating cells (cardiac myocytes, adrenal cortical cells, neurons), suggesting ORC3 functions outside of its role in DNA replication initiation; ORC2-5 co-immunoprecipitate under mild but not stringent extraction conditions, and ORC3 under stringent conditions associates with unidentified non-ORC proteins. Co-immunoprecipitation under varying extraction conditions, immunohistochemistry in tissue The Journal of biological chemistry Medium 10954718
2007 Human ORC6 binds directly to ORC3 and interacts as part of ORC in vivo; immunoprecipitation shows ORC disassembles as cells progress through S phase; anti-Orc3 immunofluorescence shows cell cycle-dependent association with a nuclear structure. Immunoprecipitation, immunofluorescence staining, recombinant protein expression The Journal of biological chemistry Medium 17716973
2008 In the S. cerevisiae ORC structure determined by single-particle EM, subunits are arranged as Orc1:Orc4:Orc5:Orc2:Orc3, with Orc6 localized near Orc2 and Orc3; subunit-subunit interactions confirmed by in vitro immunoprecipitation of subunits synthesized in vitro. Single-particle electron microscopy, MBP-fusion tag localization, in vitro immunoprecipitation Proceedings of the National Academy of Sciences of the United States of America High 18647841
2010 Human ORC3 directly binds HP1alpha; two independent domains of ORC3 (a coiled-coil domain and a mod-interacting region domain) can each independently bind HP1alpha, but both are required together for in vivo localization of ORC3 to heterochromatic foci; depletion of ORC3 by siRNA causes loss of HP1alpha association to heterochromatin and loss of compaction at satellite repeats. Direct binding assays, fluorescence microscopy, siRNA knockdown, FRAP Proceedings of the National Academy of Sciences of the United States of America High 20689044
2012 In the cryo-EM structure of S. cerevisiae ORC-Cdc6-DNA, the six ORC subunits are arranged as Orc1:Orc4:Orc5:Orc2:Orc3 with Orc6 binding to Orc2; the complex bends and wraps origin DNA along the interior crescent surface; Cdc6 binding reorients the Orc1 N-terminal BAH domain. Single-particle cryo-electron microscopy, 3D reconstruction, docking with archaeal crystal structure Structure High 22405012
2012 Conditional deletion of orc3 from glial progenitors in mouse dramatically reduces glial progenitor cell number in the subventricular zone and astrocytes in the postnatal cortex, demonstrating that ORC3 is required for DNA replication-dependent glial progenitor proliferation; loss of astroglia secondarily impairs cortical blood vessel density and branching. Conditional genetic knockout in mouse, histological and immunofluorescence analysis of cortex and vasculature PloS one Medium 23110156
2013 A Meier-Gorlin syndrome mutation in the Orc6 C-terminus impedes its recruitment into ORC by disrupting binding to a previously uncharacterized domain of ORC3; this Orc6-Orc3 interaction is required for ORC function and MCM2-7 loading in vivo. 3D electron microscopy of metazoan ORC, biochemical binding assays, in vivo functional assays eLife High 24137536
2007 ORC2 and ORC3 interact in live mammalian cells not only in the nucleus but also in the cytoplasm, as demonstrated by BRET and BiFC assays; NLS-depleted ORC3 still interacts with ORC2, indicating the interaction is not restricted to nuclear localization. Bioluminescence resonance energy transfer (BRET), bimolecular fluorescence complementation (BiFC) in live cells Molecular genetics and genomics Medium 17680271
2014 Phosphorylation of ORC2 by cyclin A/CDK2 during S phase leads to dissociation of ORC2, ORC3, ORC4, and ORC5 from human chromatin and replication origins; PP1 dephosphorylates ORC2 via the consensus motif 119-KSVSF-123, and this dephosphorylation is required for re-binding of these subunits (including ORC3) to chromatin. Co-immunoprecipitation, chromatin fractionation, PP1 inhibitor treatment, PP1 isoform overexpression and siRNA knockdown Biochemical and biophysical research communications Medium 24732362 24792176
2019 The ubiquitin ligase OBI1 (C13ORF7/RNF219) catalyzes multi-mono-ubiquitylation of chromatin-bound ORC3 (and ORC5) during S phase; expression of non-ubiquitylable ORC3/5 mutants impairs origin firing without affecting pre-RC establishment, identifying ORC3 ubiquitylation as a signal required for replication origin activation. Proteomic interactome of pre-RC, ubiquitylation assays, CMG formation assay, origin firing analysis with non-ubiquitylable mutants Nature communications High 31160578
2020 Five cryo-EM structures of human ORC reveal that ORC2-5 forms a compact stable core; introduction of ORC1 opens the complex into dynamic conformations; a hinge at the ORC5·ORC3 interface mediates twist and pinch motions in an open ORC conformation that may facilitate DNA binding. Single-particle cryo-electron microscopy, five independent structures eLife High 32808929
2010 In cultured cerebellar granule cells (CGCs), ORC3 knockdown by siRNA reduces expression of neuronal maturation markers MAP-2 and PSD-95 and increases active GTP-bound Rho, while mGlu4 receptor activation increases ORC3 and reduces Rho activation; these effects are abrogated by ORC3 siRNA, indicating ORC3 supports neuronal maturation by inhibiting the Rho signaling pathway. siRNA knockdown, western blot for MAP-2/PSD-95/active Rho, pharmacological manipulation of mGlu4 receptors Brain research Medium 20674557
2016 Drosophila ORC (including Orc3) physically interacts with the THSC/TREX-2 mRNA nuclear export complex; Orc3 knockdown increases the level of mRNP-bound Nxf1 and causes nuclear mRNA accumulation, indicating ORC3 participates in regulating mRNP export. Biochemical purification from Drosophila embryo extract, Co-IP, RNAi knockdown with nuclear mRNA accumulation assay Nucleic acids research Medium 27016737
2021 In Drosophila, the TREX-2 platform protein Xmas-2 interacts with Orc3 through its C-terminal region downstream of the CID domain, defining the molecular interface of the TREX-2-ORC interaction. Deletion mapping of Xmas-2 interaction domains with Orc3 by pulldown/co-IP Doklady. Biochemistry and biophysics Low 33689068
2023 The human TREX-2-ORC joint complex is formed in human cells, extending the Drosophila finding; ORC3 is implicated as part of this interaction. Co-immunoprecipitation in human cells Doklady. Biochemistry and biophysics Low 38066323
2024 Biochemical reconstitution of human MCM loading shows that ORC6 and ORC3 facilitate ORC recruitment to the dimerization interface of the first MCM hexamer to form MCM-ORC (MO) complexes; ORC3 contributes an element (the ORC3 tether) that supports an ORC6-independent MCM loading mechanism, and both ORC6 and ORC3 orient ORC for second MCM hexamer loading. Biochemical reconstitution of human MCM loading, electron microscopy of loading intermediates Nature High 39604729
2025 A cryo-EM structure of an ORC-Cdc6-Cdt1-MCM2-7 intermediate shows that the Mcm5 C-terminus contacts ORC3 and specifically recognizes the closed MCM2/Mcm5 ring interface, linking ORC3 to a step in pre-RC assembly that triggers Mcm4 ATP hydrolysis and Cdt1 release. Cryo-EM structure determination, mutagenesis of Mcm2/Mcm5 interface, helicase loading assays Nature communications High 39747125
2025 AlphaFold-guided phylogenetic analysis reveals that ORC3 contains an 'ORC3 tether' element that interacts with MCM to facilitate ORC6-independent MCM loading, and this element is broadly conserved across Metazoa even in lineages that have lost ORC6. AlphaFold2 Multimer structural predictions, phylogenetic analysis across metazoan lineages The EMBO journal Low 41310087

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1995 The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing. Cell 229 7585959
2010 Human origin recognition complex is essential for HP1 binding to chromatin and heterochromatin organization. Proceedings of the National Academy of Sciences of the United States of America 115 20689044
1992 latheo, a new gene involved in associative learning and memory in Drosophila melanogaster, identified from P element mutagenesis. Genetics 113 1321066
1999 latheo encodes a subunit of the origin recognition complex and disrupts neuronal proliferation and adult olfactory memory when mutant. Neuron 94 10402192
1999 latheo, a Drosophila gene involved in learning, regulates functional synaptic plasticity. Neuron 77 10402193
2008 The genetics of symptom-based phenotypes: toward a molecular classification of schizophrenia. Schizophrenia bulletin 76 18628273
2007 ATP-dependent assembly of the human origin recognition complex. The Journal of biological chemistry 75 17716973
2008 The architecture of the DNA replication origin recognition complex in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America 61 18647841
2012 Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy. Structure (London, England : 1993) 56 22405012
2012 A functional requirement for astroglia in promoting blood vessel development in the early postnatal brain. PloS one 56 23110156
2003 Uridine binding motifs of human concentrative nucleoside transporters 1 and 3 produced in Saccharomyces cerevisiae. Molecular pharmacology 52 14645682
2013 A Meier-Gorlin syndrome mutation in a conserved C-terminal helix of Orc6 impedes origin recognition complex formation. eLife 50 24137536
2000 Subsets of human origin recognition complex (ORC) subunits are expressed in non-proliferating cells and associate with non-ORC proteins. The Journal of biological chemistry 45 10954718
2008 Ku is involved in cell growth, DNA replication and G1-S transition. Journal of cell science 40 18252799
2000 Surprises from Drosophila: genetic mechanisms of synaptic development and plasticity. Brain research bulletin 39 11165785
2013 OsORC3 is required for lateral root development in rice. The Plant journal : for cell and molecular biology 37 23346890
2016 An apomixis-linked ORC3-like pseudogene is associated with silencing of its functional homolog in apomictic Paspalum simplex. Journal of experimental botany 35 26842983
2020 The dynamic nature of the human origin recognition complex revealed through five cryoEM structures. eLife 32 32808929
2020 A human cancer cell line initiates DNA replication normally in the absence of ORC5 and ORC2 proteins. The Journal of biological chemistry 29 32989049
2019 The ORC ubiquitin ligase OBI1 promotes DNA replication origin firing. Nature communications 29 31160578
2021 Human ORC/MCM density is low in active genes and correlates with replication time but does not delimit initiation zones. eLife 28 33683199
2016 ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila. Nucleic acids research 26 27016737
2017 Methionine Sulfoxide Reductase A (MsrA) and Its Function in Ubiquitin-Like Protein Modification in Archaea. mBio 24 28874471
2024 Multiple mechanisms for licensing human replication origins. Nature 23 39604729
2020 Novel candidate biomarkers of origin recognition complex 1, 5 and 6 for survival surveillance in patients with hepatocellular carcinoma. Journal of Cancer 20 32194798
2015 Place memory retention in Drosophila. Neurobiology of learning and memory 13 26143995
2015 ORC4 surrounds extruded chromatin in female meiosis. Journal of cellular biochemistry 12 25502171
2019 Comprehensive Analysis of Replication Origins in Saccharomyces cerevisiae Genomes. Frontiers in microbiology 10 31572328
2007 Interactions and subcellular distribution of DNA replication initiation proteins in eukaryotic cells. Molecular genetics and genomics : MGG 10 17680271
2018 TORC1 signaling regulates DNA replication via DNA replication protein levels. Biochemical and biophysical research communications 8 30316513
2005 Novel splicing variant of mouse Orc1 is deficient in nuclear translocation and resistant for proteasome-mediated degradation. The Journal of biological chemistry 8 15634681
2025 MCM2-7 ring closure involves the Mcm5 C-terminus and triggers Mcm4 ATP hydrolysis. Nature communications 7 39747125
2019 Lysine-specific demethylase 2A enhances binding of various nuclear factors to CpG-rich genomic DNAs by action of its CXXC-PHD domain. Scientific reports 7 30940825
1999 Identification and chromosomal localization of murine ORC3, a new member of the mouse origin recognition complex. Cytogenetics and cell genetics 6 10702681
2016 Epigenetic Studies Point to DNA Replication/Repair Genes as a Basis for the Heritable Nature of Long Term Complications in Diabetes. Journal of diabetes research 5 26981540
2014 Dephosphorylation of Orc2 by protein phosphatase 1 promotes the binding of the origin recognition complex to chromatin. Biochemical and biophysical research communications 5 24792176
2010 The origin recognition complex subunit, ORC3, is developmentally regulated and supports the expression of biochemical markers of neuronal maturation in cultured cerebellar granule cells. Brain research 5 20674557
2025 Utility of a Large Series of B-Cell Precursor Acute Lymphoblastic Leukemia Cell Lines as a Model System. Cancer medicine 3 40022573
2021 Study of the Interaction between Xmas-2, the Main Protein of TREX-2 mRNA Export Complex, and the Orc3 Protein, a Subunit of ORC Complex of D. melanogaster. Doklady. Biochemistry and biophysics 3 33689068
2014 Protein phosphatase 1 dephosphorylates Orc2. Biochemical and biophysical research communications 2 24732362
2025 AlphaFold-guided phylogenetic analyses suggest surprising heterogeneity in metazoan replication origin licensing mechanisms. The EMBO journal 1 41310087
2025 A Trade-Off between Body Mass and Cancer Resistance in Cetaceans Is Mediated by Cell Cycle-Related Gene Evolution. Molecular biology and evolution 0 40658797
2023 In Silico Characterization of RNASEH2A Pathogenic Variants and Identification of Novel Splice Site Donor Variant c.549+1G>T in Indian Population. Cureus 0 37456470
2023 The Human TREX-2 Complex Interacts with Subunits of the ORC Complex. Doklady. Biochemistry and biophysics 0 38066323
2021 Stability of proteins involved in initiation of DNA replication in UV damaged human cells. Zeitschrift fur Naturforschung. C, Journal of biosciences 0 34333892

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