Affinage

NUBP2

Cytosolic Fe-S cluster assembly factor NUBP2 · UniProt Q9Y5Y2

Round 2 corrected
Length
271 aa
Mass
28.8 kDa
Annotated
2026-04-29
51 papers in source corpus 16 papers cited in narrative 16 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUBP2 is a cytosolic P-loop NTPase that functions as an essential scaffold for the assembly and transfer of iron-sulfur ([Fe-S]) clusters to cytosolic and nuclear Fe-S proteins, and additionally serves as a negative regulator of centriole duplication and ciliogenesis. NUBP2 forms a heterotetrameric complex with NUBP1 (NBP35) in which the conserved C-terminal CPXC motifs of both subunits coordinate a bridging [4Fe-4S] cluster; NUBP2 controls nucleotide binding order within the heterodimer, lacks intrinsic ATPase activity as a homodimer but becomes hydrolysis-competent when partnered with NUBP1, and increases the kinetic lability of assembled clusters on NUBP1 to facilitate transfer to target apoproteins via downstream CIA factors (PMID:17401378, PMID:22362766, PMID:30201724, PMID:30785732). Independent of its Fe-S assembly role, NUBP2 localizes to centrioles and basal bodies and, together with NUBP1 and KIFC5A, restrains ciliogenesis and centriole reduplication; loss of NUBP2 causes supernumerary centrosomes, aberrant cilia formation, cranial neural crest apoptosis leading to craniofacial clefting, and primary microcephaly in mouse models and human patients (PMID:23807208, PMID:16638812, PMID:31733190).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1999 Medium

    Identification of NUBP2 as a member of the MRP/MinD P-loop NTPase family established its evolutionary conservation and predicted nucleotide-binding capacity, distinguishing it from NUBP1 by the absence of an N-terminal four-cysteine motif.

    Evidence Phylogenetic analysis, Northern blot, and chromosomal mapping in mouse

    PMID:10486206

    Open questions at the time
    • No functional data; role was inferred solely from sequence homology
    • Nucleotide specificity (ATP vs GTP) not determined
  2. 2003 High

    Genetic studies in yeast demonstrated that Cfd1 (NUBP2 ortholog) is the first identified cytoplasmic Fe-S cluster assembly factor, answering whether Fe-S biogenesis occurs outside mitochondria and establishing cytosolic specificity of NUBP2 function.

    Evidence Hypomorphic cfd1-1 mutant with >90% reduction in cytosolic Fe-S enzyme activities (c-aconitase, Leu1p) but intact mitochondrial Fe-S proteins; subcellular fractionation and EPR spectroscopy in S. cerevisiae

    PMID:12970194

    Open questions at the time
    • Whether NUBP2 directly binds Fe-S clusters or acts indirectly was unknown
    • Human relevance not yet tested
  3. 2006 Medium

    Discovery that NUBP2 physically interacts with KIFC5A and NUBP1 and that their co-depletion causes centrosome amplification revealed a second, unexpected role for NUBP2 in centrosome duplication control, independent of its Fe-S function.

    Evidence Co-immunoprecipitation and RNAi knockdown phenotyping (centrosome counting, cell cycle analysis) in mammalian cells

    PMID:16638812

    Open questions at the time
    • Whether centrosome phenotype is linked to Fe-S assembly or represents an independent function
    • Single laboratory; mechanism of centriole duplication control not defined
  4. 2007 High

    Biochemical reconstitution established that Cfd1 and Nbp35 form a heterotetrameric scaffold coordinating up to three [4Fe-4S] clusters via C-terminal CPXC motifs, with these clusters being transferable to target apoproteins in a Nar1/Cia1-dependent manner, resolving the molecular mechanism of cytosolic Fe-S assembly.

    Evidence In vivo/in vitro Fe-S reconstitution, 55Fe radiolabeling, Mössbauer and EPR spectroscopy, co-IP, cluster transfer assays in yeast

    PMID:17401378

    Open questions at the time
    • Structural basis of cluster coordination not yet resolved
    • How nucleotide binding regulates cluster assembly was unclear
  5. 2008 High

    Extension of the yeast findings to human cells confirmed that the NUBP1–NUBP2 complex is required for cytosolic Fe-S protein maturation (including IRP1) and cellular iron homeostasis in HeLa cells, validating conservation of the CIA pathway.

    Evidence RNAi knockdown of NUBP1/NUBP2 in HeLa cells, co-IP, Fe-S enzyme assays, 55Fe radiolabeling, transferrin uptake

    PMID:18573874

    Open questions at the time
    • Specific contribution of NUBP2 versus NUBP1 to the human complex not individually dissected
  6. 2012 High

    Mutagenesis demonstrated that the C-terminal CPXC cysteines of Cfd1 are essential for cell viability, Fe-S cluster coordination, and heterotetramer integrity, and that nucleotide binding is a prerequisite for Fe-S loading onto the scaffold, coupling ATPase function to cluster assembly.

    Evidence Cysteine and Walker motif mutagenesis combined with Mössbauer/EPR spectroscopy, 55Fe labeling, and size-exclusion chromatography in yeast

    PMID:22362766

    Open questions at the time
    • Order of nucleotide binding within the heterodimer unknown
    • Structural basis of nucleotide-cluster coupling not resolved
  7. 2013 High

    Two parallel advances clarified distinct aspects of NUBP2 function: (1) Cfd1 does not bind iron alone but increases the kinetic lability of Fe-S clusters on Nbp35 to facilitate transfer, defining NUBP2 as a cluster-release factor rather than a primary iron binder; (2) NUBP1/NUBP2 localize to centrioles and basal bodies throughout the cell cycle and act as negative regulators of ciliogenesis.

    Evidence (1) 55Fe radiolabeling, size-exclusion chromatography, and mutagenesis in yeast; (2) immunofluorescence, RNAi, cilium counting, and genetic epistasis in NIH 3T3 cells and C. elegans

    PMID:23798678 PMID:23807208

    Open questions at the time
    • Structural mechanism by which Cfd1 destabilizes clusters on Nbp35 not resolved
    • Whether centriolar and Fe-S roles are mechanistically linked remained unclear
  8. 2015 High

    Biochemical characterization established that the Nbp35-Cfd1 heterodimer is an ATPase with defined nucleotide specificity, with Cfd1 homodimer having no/negligible ATPase activity, and identified KATNAL2 as a physical interactor that phenocopies NUBP2 perturbation in centriole duplication and ciliogenesis.

    Evidence In vitro ATPase assays, mantATP fluorescence binding, mutagenesis; co-IP, yeast two-hybrid, shRNAi in mammalian cells

    PMID:26153462 PMID:26195633

    Open questions at the time
    • How ATP hydrolysis is mechanistically coupled to Fe-S cluster transfer remained undefined
    • KATNAL2–NUBP2 relationship characterized in single laboratory only
  9. 2018 High

    The crystal structure of Cfd1 at 2.6 Å resolution revealed a surface-exposed bridging [4Fe-4S] cluster between two monomers coordinated by conserved cysteines, and showed that Cfd1 specifically binds ATP (not GTP) at the dimer interface, providing the atomic-level basis for NUBP2's scaffold and nucleotide-binding functions.

    Evidence X-ray crystallography of Chaetomium thermophilum holo-Cfd1, nucleotide binding assays, HeLa cell depletion with Fe-S protein maturation readouts

    PMID:30201724

    Open questions at the time
    • Structure of the full NUBP1–NUBP2 heterotetramer not yet determined
    • How cluster transfer to downstream CIA factors is structurally mediated
  10. 2019 Medium

    Nucleotide binding order in the CIA scaffold was resolved: ATP must first bind Cfd1 before Nbp35 can bind nucleotide, and Cfd1 gains hydrolysis competence only in the heterocomplex context, establishing an allosteric communication mechanism within the scaffold.

    Evidence Fluorescence nucleotide titrations and site-directed mutagenesis with purified yeast proteins

    PMID:30785732

    Open questions at the time
    • How sequential ATP binding triggers conformational changes for cluster maturation is unknown
    • Findings from single laboratory; limited replication
  11. 2019 High

    In vivo conditional knockout of Nubp2 in the neural crest lineage demonstrated that NUBP2 is required for cranial neural crest cell survival; the craniofacial clefting phenotype results from increased apoptosis rather than altered ciliogenesis or SHH/FGF/BMP signaling, distinguishing the essential survival function from the ciliogenesis-regulatory role.

    Evidence ENU forward genetic screen (dorothy mutant), Wnt1-Cre conditional knockout, complementation with null allele, apoptosis and signaling pathway analysis in mouse

    PMID:31733190

    Open questions at the time
    • Whether the apoptosis is driven by loss of Fe-S cluster assembly, centrosome defects, or both was not resolved
    • Downstream apoptotic pathway not identified
  12. 2025 Medium

    Forebrain-specific deletion of Nubp2 causes severe primary microcephaly through supernumerary centrosomes, aberrant cilia, and p53-independent cell death, and human patients with biallelic NUBP2 variants display profound microcephaly, establishing NUBP2 as a primary microcephaly gene (preprint).

    Evidence Emx1-Cre conditional knockout mouse, patient variant identification and neurosphere complementation, centrosome/cilia counting, p53 genetic epistasis (preprint)

    PMID:39867373

    Open questions at the time
    • Not yet peer-reviewed
    • Relative contribution of Fe-S assembly defects versus centrosome/cilia defects to microcephaly pathogenesis unresolved
    • p53-independent cell death pathway not characterized

Open questions

Synthesis pass · forward-looking unresolved questions
  • A central unresolved question is whether NUBP2's roles in Fe-S cluster assembly and centrosome/cilia biology are mechanistically linked or represent truly independent functions, and the structural basis of the full NUBP1–NUBP2 heterotetramer with bound clusters remains undetermined.
  • No structure of the complete NUBP1–NUBP2 heterotetramer
  • Mechanistic link (or independence) of Fe-S and centrosome functions not experimentally dissected
  • Downstream apoptotic pathways in neural crest and forebrain progenitors not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140657 ATP-dependent activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005829 cytosol 4 GO:0005815 microtubule organizing center 3 GO:0005929 cilium 1
Pathway
R-HSA-1430728 Metabolism 6 R-HSA-1852241 Organelle biogenesis and maintenance 3 R-HSA-1640170 Cell Cycle 2
Partners
KATNAL2KIFC5ANUBP1
Complex memberships
NUBP1–NUBP2 (Nbp35–Cfd1) CIA scaffold complex

Evidence

Reading pass · 16 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 NUBP2 (mouse Nubp2/human NUBP2) was identified as a novel eukaryotic nucleotide-binding protein related to prokaryotic MRP/MinD proteins, defining the short-form branch of the NUBP/MRP gene family. It shares conserved ATP/GTP-binding P-loop motifs and two highly conserved NUBP/MRP sequence motifs (alpha and beta) with Nubp1, but lacks the unique N-terminal four-cysteine sequence present in Nubp1/Nbp35. Mouse Nubp2 was mapped to the t-complex region of chromosome 17. Phylogenetic analysis, Northern blot, chromosomal mapping Genomics Medium 10486206
2003 CFD1 (the yeast ortholog of NUBP2) was identified as the first cytoplasmic Fe-S cluster assembly factor in eukaryotes. A hypomorphic cfd1-1 mutation reduced cytosolic Fe-S enzyme activities (c-aconitase/IRP1 and Leu1p) by >90% without affecting mitochondrial Fe-S proteins, and Cfd1p was localized to the cytoplasm. Genetic screen, enzyme activity assays, EPR spectroscopy, subcellular fractionation/localization The EMBO journal High 12970194
2007 Cfd1 (NUBP2 ortholog) and Nbp35 (NUBP1 ortholog) form a heterotetrameric complex in the yeast cytosol and together bind up to three [4Fe-4S] clusters—one at the N-terminus of Nbp35 and one each at a C-terminal cysteine-rich (CPXC) motif in both proteins. These labile clusters can be transferred to target Fe-S apoproteins in a Nar1- and Cia1-dependent manner, establishing the Cfd1-Nbp35 complex as a scaffold for cytosolic Fe-S protein assembly. In vivo and in vitro Fe-S cluster reconstitution, 55Fe radiolabeling, Mössbauer and EPR spectroscopy, co-immunoprecipitation, cluster transfer assays Nature chemical biology High 17401378
2008 Human CFD1 (NUBP2) forms a complex with its close homologue huCfd1 (Nubp2)/huNbp35 (Nubp1) in vivo in HeLa cells. Depletion of huNbp35 (Nubp1) impairs maturation of cytosolic Fe-S proteins (including IRP1), while mitochondrial Fe-S proteins remain intact, demonstrating that the heteromeric Nubp1-Nubp2 P-loop NTPase complex is required for cytosolic Fe-S protein assembly and cellular iron homeostasis. RNAi knockdown, co-immunoprecipitation, Fe-S enzyme activity assays, 55Fe radiolabeling, transferrin uptake assays Molecular and cellular biology High 18573874
2009 GFP fusion experiments in HeLa cells showed that N-terminal GFP tagging of NUBP2 induces nuclear localization of the fusion protein, whereas untagged or C-terminally modified forms remain cytoplasmic, suggesting that the N-terminal region of NUBP2 influences nuclear targeting. GFP fusion protein imaging in HeLa cells Molecular biology reports Low 19263241
2012 The two central cysteine residues (CPXC motif) of the C-terminal domain of Cfd1 (NUBP2 ortholog) are essential for cell viability, Fe-S cluster coordination, and Cfd1-Nbp35 hetero-tetramer formation. The C-terminal CPXC motifs of Cfd1 and Nbp35 coordinate a bridging [4Fe-4S] cluster. Nucleotide binding is required for Fe-S cluster loading onto these scaffold proteins, as mutation of the nucleotide-binding motifs abolishes Fe-S assembly unless wild-type copies are present in trans. Cysteine mutagenesis, genetic complementation, Mössbauer and EPR spectroscopy, 55Fe radiolabeling, size-exclusion chromatography The Journal of biological chemistry High 22362766
2013 In yeast, Nbp35 (NUBP1 ortholog) readily binds 55Fe whereas free Cfd1 (NUBP2 ortholog) does not detectably bind iron alone. Interaction of Cfd1 with Nbp35 increases the kinetic lability of assembled Fe-S clusters on Nbp35, facilitating their transfer to target apo-Fe-S proteins. A Cfd1 mutation impairing heterocomplex stability supported iron binding to Nbp35 but blocked iron release. 55Fe radiolabeling in yeast, size-exclusion chromatography, co-immunoprecipitation, site-directed mutagenesis The Journal of biological chemistry High 23798678
2013 Nubp1 and Nubp2 are integral components of centrioles throughout the cell cycle, localizing at the basal body of the primary cilium in quiescent vertebrate cells and sensory cilia in invertebrates, independently of KIFC5A. RNAi-mediated knockdown of Nubp1 or Nubp2 in quiescent NIH 3T3 cells markedly increases the number of ciliated cells, identifying Nubp1 and Nubp2 as negative regulators of ciliogenesis. Simultaneous knockdown of Nubp1 + KIFC5A restored ciliation to control levels, placing these proteins in the same pathway. Immunofluorescence microscopy, RNAi knockdown, cilium counting assays, genetic epistasis (double knockdown), C. elegans RNAi Cellular and molecular life sciences : CMLS High 23807208
2015 The Nbp35-Cfd1 heterodimer (NUBP1-NUBP2 complex) is an ATPase. The Nbp35 homodimer and the Nbp35-Cfd1 heterodimer hydrolyze ATP, while the Cfd1 homodimer has no or very low ATPase activity. Mutation of key Walker motif residues abolishes activity. The fluorescent ATP analog mantATP binds stoichiometrically to Nbp35 with KD = 15.6 μM, and a hydrolysis-defective Nbp35 mutant shows increased KD for mantATP. In vitro ATPase assays, site-directed mutagenesis, fluorescence nucleotide binding (mantATP) The Journal of biological chemistry High 26195633
2015 KATNAL2 isoforms directly and independently interact with both Nubp1 and Nubp2 (MRP/MinD-type P-loop NTPases) in vivo. shRNAi knockdown of Katnal2 causes enlarged cells, supernumerary centrioles, multipolar spindles, and reduced ciliogenesis, phenocopying effects of Nubp1/Nubp2 perturbation, placing KATNAL2 in the same pathway as Nubp1/Nubp2 in centriole duplication and ciliogenesis regulation. Co-immunoprecipitation, yeast two-hybrid, shRNAi, immunofluorescence, cell cycle analysis Cellular and molecular life sciences : CMLS Medium 26153462
2018 Human CFD1 (NUBP2), in complex with NBP35 (NUBP1), performs a crucial scaffold role in the maturation of all tested cytosolic and nuclear Fe-S proteins in HeLa cells, including those involved in protein translation, DNA maintenance, and iron regulatory protein 1 (IRP1). Crystal structure of Chaetomium thermophilum holo-Cfd1 at 2.6-Å resolution revealed that two Cfd1 monomers coordinate a bridging [4Fe-4S] cluster via two conserved cysteine residues in a surface-exposed topology, and Cfd1 specifically binds ATP near the dimer interface via the Walker motif, while Nbp35 preferentially binds GTP. CFD1 depletion in HeLa cells, Fe-S enzyme activity assays, 55Fe radiolabeling, X-ray crystallography (2.6 Å), nucleotide binding assays Proceedings of the National Academy of Sciences of the United States of America High 30201724
2019 The Cfd1 subunit of the Nbp35-Cfd1 scaffold controls nucleotide binding order: ATP must bind to Cfd1 before it can bind to Nbp35 in the heterodimer. Although the Cfd1 homodimer has no ATPase activity, Cfd1 becomes hydrolysis competent when bound to Nbp35 in the heterodimer. All forms of the CIA scaffold are specific for adenosine nucleotides and not guanosine nucleotides. Fluorescence nucleotide titrations, site-directed mutagenesis, ATPase assays Biochemistry Medium 30785732
2019 Conditional ablation of Nubp2 in the neural crest lineage (Wnt1-Cre) in mice recapitulates the dorothy craniofacial phenotype (severe midfacial clefting) caused by a missense mutation in Nubp2. The phenotype results from markedly increased apoptosis in craniofacial mesenchyme rather than from altered ciliogenesis or SHH/FGF/BMP signaling pathway changes, demonstrating that Nubp2 is required for cranial neural crest cell survival. ENU forward genetic screen, exome sequencing, complementation assay with null allele, conditional Cre-lox knockout, immunofluorescence, apoptosis assays, signaling pathway marker analysis Developmental biology High 31733190
2006 KIFC5A (a minus-end-directed motor protein) physically interacts with both Nubp1 and Nubp2, and Nubp1 and Nubp2 interact with each other. Knockdown of Nubp1 alone or double knockdown of Nubp1 and Nubp2 phenocopies KIFC5A silencing, causing centrosome amplification via centriole reduplication and cytokinesis defects, implicating Nubp2 in a KIFC5A-dependent pathway controlling centrosome duplication. Co-immunoprecipitation, RNAi knockdown, centrosome counting, cell cycle analysis, immunofluorescence Journal of cell science Medium 16638812
2024 ISP I (isovalerylspiramycin I) directly targets NUBP2, and through this interaction increases the cell-membrane levels of VNN1 (vascular non-inflammatory molecule-1), which inhibits oxidative stress and fibrosis. NUBP2 knockdown or drug-mediated targeting reduced liver fibrosis markers in LX-2 cells and in BDL rat and CCl4 mouse models. Drug-target binding assay, VNN1 membrane fractionation, cell-based knockdown, in vivo fibrosis models Journal of pharmaceutical analysis Low 40177065
2025 Conditional deletion of Nubp2 from the mouse forebrain (Emx1-Cre) causes severe primary microcephaly beginning at E18.5, associated with increased canonical and non-canonical cell death, altered neuronal proliferation and migration, and supernumerary centrosomes and cilia. Loss of p53 failed to rescue microcephaly, indicating a p53-independent mechanism. Human patients with homozygous NUBP2 variants display profound primary microcephaly, implicating NUBP2's role in centrosome and cilia regulation as critical for proper neurogenesis. Conditional Cre-lox knockout mouse model, patient variant identification and neurosphere complementation, immunofluorescence, cell death assays, centrosome/cilia counting, genetic epistasis (p53 rescue experiment) medRxivpreprint Medium 39867373

Source papers

Stage 0 corpus · 51 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2014 An atlas of genetic influences on human blood metabolites. Nature genetics 1209 24816252
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2014 A proteome-scale map of the human interactome network. Cell 977 25416956
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2021 Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature 532 33845483
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2015 A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. Cell 433 26638075
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
1996 Normalization and subtraction: two approaches to facilitate gene discovery. Genome research 401 8889548
2018 DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity. Cell 379 29656893
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2012 A high-throughput approach for measuring temporal changes in the interactome. Nature methods 273 22863883
1996 A pancreatic cancer-specific expression profile. Oncogene 151 8895530
2020 A High-Density Human Mitochondrial Proximity Interaction Network. Cell metabolism 148 32877691
2007 The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nature chemical biology 143 17401378
2017 RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination. BMC biology 135 29117863
2003 A novel eukaryotic factor for cytosolic Fe-S cluster assembly. The EMBO journal 134 12970194
2017 Mammalian APE1 controls miRNA processing and its interactome is linked to cancer RNA metabolism. Nature communications 99 28986522
2014 Proteomic analysis of the epidermal growth factor receptor (EGFR) interactome and post-translational modifications associated with receptor endocytosis in response to EGF and stress. Molecular & cellular proteomics : MCP 99 24797263
2020 Histone methyltransferase DOT1L coordinates AR and MYC stability in prostate cancer. Nature communications 90 32814769
2020 Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases. Molecular cell 88 32707033
2008 Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis. Molecular and cellular biology 87 18573874
2021 SARS-CoV-2-host proteome interactions for antiviral drug discovery. Molecular systems biology 86 34709727
2012 A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation. The Journal of biological chemistry 86 22362766
2014 Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation. Cell reports 80 24981860
2017 A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III. Cell metabolism 78 28380382
2008 The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage. The Journal of biological chemistry 54 18957412
2015 A novel family of katanin-like 2 protein isoforms (KATNAL2), interacting with nucleotide-binding proteins Nubp1 and Nubp2, are key regulators of different MT-based processes in mammalian cells. Cellular and molecular life sciences : CMLS 30 26153462
2013 Interaction with Cfd1 increases the kinetic lability of FeS on the Nbp35 scaffold. The Journal of biological chemistry 29 23798678
2006 Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication. Journal of cell science 29 16638812
2018 Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins. Proceedings of the National Academy of Sciences of the United States of America 24 30201724
2013 The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis. Cellular and molecular life sciences : CMLS 24 23807208
2019 Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1. Ecotoxicology and environmental safety 23 31759739
2015 The Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPase. The Journal of biological chemistry 19 26195633
1999 Two novel mouse genes--Nubp2, mapped to the t-complex on chromosome 17, and Nubp1, mapped to chromosome 16--establish a new gene family of nucleotide-binding proteins in eukaryotes. Genomics 17 10486206
2014 Interaction between Nbp35 and Cfd1 proteins of cytosolic Fe-S cluster assembly reveals a stable complex formation in Entamoeba histolytica. PloS one 14 25271645
2009 Comparison of intracellular localization of Nubp1 and Nubp2 using GFP fusion proteins. Molecular biology reports 11 19263241
2022 Comparative Genomic Analysis of Carbofuran-Degrading Sphingomonads Reveals the Carbofuran Catabolism Mechanism in Sphingobium sp. Strain CFD-1. Applied and environmental microbiology 5 36314801
2023 Serum autoantibody profiling of oral squamous cell carcinoma patients reveals NUBP2 as a potential diagnostic marker. Frontiers in oncology 4 37810966
2019 The Cfd1 Subunit of the Nbp35-Cfd1 Iron Sulfur Cluster Scaffolding Complex Controls Nucleotide Binding. Biochemistry 3 30785732
2023 Interaction between Cfd1 and Nbp35 proteins involved in cytosolic FeS cluster assembly machinery deciphers a stable complexation in Leishmania donovani. International journal of biological macromolecules 2 37774824
2019 Nubp2 is required for cranial neural crest survival in the mouse. Developmental biology 2 31733190
2024 Isovalerylspiramycin I alleviates liver injury and liver fibrosis by targeting the nucleotide-binding protein 2 (NUBP2)-vascular non-inflammatory molecule-1 (VNN1) pathway. Journal of pharmaceutical analysis 1 40177065
2025 NUBP2 deficiency disrupts the centrosome-check point in the brain and causes primary microcephaly. medRxiv : the preprint server for health sciences 0 39867373
2024 Abnormal upregulation of NUBP2 contributes to cancer progression in colorectal cancer. Molecular and cellular biochemistry 0 38492158