C1QBP a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. Originally identified via its binding interactions with Splicing Factor (SF-2). Multiple, diverse binding partners of C1QBP were subsequently identified, including the globular heads of complement component C1q, hyaluronic acid, selected protein kinases, the tumor suppressor ARF, and multiple antigens of bacterial and viral origin. Overexpressed in a number of cancer cell types, and has been implicated in the Warburg effect, whereby cancer cells shift their metabolism from oxidative phosphorylation to glycolysis. Inhibits the Mitochondrial Permeability Transition (MPT) pore, possibly serving a protective function against damage from oxidative stress. Binding to C1q inhibits C1. In complex with cytokeratin-1/KRT1 is a high affinty receptor for kininogen-1/HMWK. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. The cell surface form may require docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. Belongs to the MAM33 family. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Motility/polarity/chemotaxis; Nucleolus; Receptor, misc.
Chromosomal Location of Human Ortholog: 17p13.2
Cellular Component:  cell surface; cytoplasm; cytosol; extracellular space; GABA-ergic synapse; glutamatergic synapse; membrane; mitochondrial matrix; mitochondrion; nucleolus; nucleus; plasma membrane; presynaptic active zone
Molecular Function:  adrenergic receptor binding; complement component C1q binding; hyaluronic acid binding; kininogen binding; mitochondrial ribosome binding; mRNA binding; protein binding; protein kinase C binding; transcription corepressor activity; transcription factor binding
Biological Process:  apoptotic process; blood coagulation, intrinsic pathway; complement activation, classical pathway; immune response; innate immune response; mature ribosome assembly; mRNA processing; negative regulation of defense response to virus; negative regulation of interferon-gamma production; negative regulation of interleukin-12 production; negative regulation of MDA-5 signaling pathway; negative regulation of mRNA splicing, via spliceosome; negative regulation of RIG-I signaling pathway; negative regulation of transcription by RNA polymerase II; phosphatidylinositol 3-kinase signaling; positive regulation of apoptotic process; positive regulation of cell adhesion; positive regulation of dendritic cell chemotaxis; positive regulation of mitochondrial translation; positive regulation of neutrophil chemotaxis; positive regulation of protein kinase B signaling; positive regulation of substrate adhesion-dependent cell spreading; positive regulation of trophoblast cell migration; regulation of complement activation; RNA splicing; viral process
Disease: Combined Oxidative Phosphorylation Deficiency 33
Reference #:  Q07021 (UniProtKB)
Alt. Names/Synonyms: ASF/SF2-associated protein p32; C1q globular domain-binding protein; C1QBP; complement C1q binding protein; Complement component 1 Q subcomponent-binding protein, mitochondrial; complement component 1, q subcomponent binding protein; COXPD33; gC1Q-R; GC1q-R protein; GC1QBP; gC1qR; Glycoprotein gC1qBP; HABP1; Hyaluronan-binding protein 1; Mitochondrial matrix protein p32; p32; p33; SF2AP32; SF2P32; splicing factor SF2-associated protein
Gene Symbols: C1QBP
Molecular weight: 31,362 Da
Basal Isoelectric point: 4.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB