Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation.
Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32.
Localization of P32 protein (gC1q-R) in mitochondria and at specific extramitochondrial locations in normal tissues.
-
Primary localization is mitochondrial
-
Cell surface localization in endothelial cells and acinar cells
-
Nuclear localization in splenic lymphocytes
Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation.
Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells.
Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading.
The N-terminal conserved domain of rubella virus capsid interacts with the C-terminal region of cellular p32 and overexpression of p32 enhances the viral infectivity.
The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein.
A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.
Physical and functional interaction between BH3-only protein Hrk and mitochondrial pore-forming protein p32.
-
C1QBP interacts with HRK in mitochondria
-
p32 knockdown protects against Hrk-induced apoptosis
-
C1QBP facilitates but is not directly apoptotic
Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro.
-
C1QBP interacts with NF-YB (CBF-B)
-
Acts as transcriptional corepressor
-
Present in cytosol and nucleus
Chemotaxis of human monocyte-derived dendritic cells to complement component C1q is mediated by the receptors gC1qR and cC1qR.
gC1q receptor ligation selectively down-regulates human IL-12 production through activation of the phosphoinositide 3-kinase pathway.
CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo.
The autophagic inducer smARF interacts with and is stabilized by the mitochondrial p32 protein.
HCV core protein interaction with gC1q receptor inhibits Th1 differentiation of CD4+ T cells via suppression of dendritic cell IL-12 production.
Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP functions as mitochondrial RNA granule.
Human p32 is a novel FOXC1-interacting protein that regulates FOXC1 transcriptional activity in ocular cells.
Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria.
An alternative role of C1q in cell migration and tissue remodeling: contribution to trophoblast invasion and placental development.
Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles.
Protein interactome reveals converging molecular pathways among autism disorders.
Toward an understanding of the protein interaction network of the human liver.
NONO and RALY proteins are required for YB-1 oxaliplatin induced resistance in colon adenocarcinoma cell lines.
Binding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifs.
A host YB-1 ribonucleoprotein complex is hijacked by hepatitis C virus for the control of NS3-dependent particle production.
Exploration of panviral proteome: high-throughput cloning and functional implications in virus-host interactions.
C1QBP negatively regulates the activation of oncoprotein YBX1 in the renal cell carcinoma as revealed by interactomics analysis.
Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection of Novel Stress Granule Proteins.
Homologous Transcription Factors DUX4 and DUX4c Associate with Cytoplasmic Proteins during Muscle Differentiation.
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
Architecture of the human interactome defines protein communities and disease networks.
C1QBP is upregulated in colon cancer and binds to apolipoprotein A-I.
Biallelic C1QBP mutations cause severe neonatal-, childhood-, or later-onset cardiomyopathy associated with combined respiratory-chain deficiencies.
C1QBP Promotes Homologous Recombination by Stabilizing MRE11 and Controlling the Assembly and Activation of MRE11/RAD50/NBS1 Complex.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
A reference map of the human binary protein interactome.
Unusually efficient CUG initiation of an overlapping reading frame in POLG mRNA yields novel protein POLGARF.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
The double homeodomain protein DUX4c is associated with regenerating muscle fibers and RNA-binding proteins.
RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for degradation and cytosolic release.
-
C1QBP recognizes m5C-modified mitochondrial RNAs
-
Promotes recruitment of mitochondrial degradosome
-
Key role in mitochondrial RNA quality control
Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q.
-
Original identification of C1QBP as gC1qR
-
Binds globular heads of C1q
-
Cell surface glycoprotein
Molecular cloning of human fibroblast hyaluronic acid-binding protein confirms its identity with P-32, a protein co-purified with splicing factor SF2. Hyaluronic acid-binding protein as P-32 protein, co-purified with splicing factor SF2.
Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor.
Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: identity with the receptor that binds to the globular "heads" of C1q (gC1q-R).
The binding protein for globular heads of complement C1q, gC1qR. Functional expression and characterization as a novel vitronectin binding factor.
p32 protein, a splicing factor 2-associated protein, is localized in mitochondrial matrix and is functionally important in maintaining oxidative phosphorylation.
C1q-mediated chemotaxis by human neutrophils: involvement of gClqR and G-protein signalling mechanisms.
prekallikrein + kininogen:C1q binding protein tetramer -> prekallikrein:kininogen:C1q binding protein tetramer
prekallikrein:kininogen:C1q binding protein tetramer -> kallikrein:kininogen:C1q binding protein tetramer
kallikrein:kininogen:C1q binding protein tetramer -> kallikrein + activated kininogen:C1q binding protein tetramer + bradykinin
factor XII -> factor XIIa
kininogen + C1q binding protein tetramer -> kininogen:C1q binding protein tetramer
C1QBP promotes translocation of p14ARF to the mitochondrial matrix
p14ARF mutants do not bind C1QBP
C1QBP deep research summary (Falcon 2024)
-
Core functions are mitochondrial translation support and C1q receptor
-
Over-expressed in cancers
-
Proposed as checkpoint-like immune modulator
-
Biallelic mutations cause COXPD33 with cardiomyopathy
Deep research report on C1QBP