C1QBP

Complement component 1, q subcomponent binding protein

PDB rendering based on 1p32.

Available structures
PDB	1p32

Identifiers

Symbols

C1QBP; GC1QBP; HABP1; SF2p32; gC1Q-R; gC1qR; p32

External IDs

OMIM: 601269 MGI: 1194505 HomoloGene: 31023 GeneCards: C1QBP Gene

Gene Ontology
Molecular function	• complement component C1q binding • protein binding
Cellular component	• extracellular space • nucleus • mitochondrion • mitochondrial matrix • plasma membrane • membrane
Biological process	• immune response • blood coagulation • blood coagulation, intrinsic pathway • interspecies interaction between organisms
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
5.34 – 5.34 Mb

Chr 11:
70.79 – 70.8 Mb

PubMed search

[1]

[2]

Complement component 1 Q subcomponent-binding protein, mitochondrial is a protein that in humans is encoded by the C1QBP gene.^[1]^[2]^[3]

The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system. The protein encoded by this gene is known to bind to the globular heads of C1q molecules and inhibit C1 activation. This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein.^[3]

Interactions

C1QBP has been shown to interact with Protein kinase D1,^[4] BAT2,^[5] PRKCD,^[4] PKC alpha^[4] and Protein kinase Mζ.^[4]

References

^ Deb TB, Datta K (Mar 1996). "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". J Biol Chem 271 (4): 2206–12. doi:10.1074/jbc.271.4.2206. PMID 8567680.
^ Ghebrehiwet B, Lim BL, Peerschke EI, Willis AC, Reid KB (Jun 1994). "Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q". J Exp Med 179 (6): 1809–21. doi:10.1084/jem.179.6.1809. PMC 2191527. PMID 8195709. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2191527.
^ ^a ^b "Entrez Gene: C1QBP complement component 1, q subcomponent binding protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=708.
^ ^a ^b ^c ^d Storz, P; Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes F J (Aug. 2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. (UNITED STATES) 275 (32): 24601–7. doi:10.1074/jbc.M002964200. ISSN 0021-9258. PMID 10831594.
^ Lehner, Ben; Semple Jennifer I, Brown Stephanie E, Counsell Damian, Campbell R Duncan, Sanderson Christopher M (Jan. 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics (United States) 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819.

Krainer AR, Mayeda A, Kozak D, Binns G (1991). "Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.". Cell 66 (2): 383–94. doi:10.1016/0092-8674(91)90627-B. PMID 1830244.
Busby TF, Ingham KC (1990). "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q.". Biochemistry 29 (19): 4613–8. doi:10.1021/bi00471a016. PMID 2372546.
Fridell RA, Harding LS, Bogerd HP, Cullen BR (1995). "Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins.". Virology 209 (2): 347–57. doi:10.1006/viro.1995.1266. PMID 7778269.
Luo Y, Yu H, Peterlin BM (1994). "Cellular protein modulates effects of human immunodeficiency virus type 1 Rev.". J. Virol. 68 (6): 3850–6. PMC 236890. PMID 8189522. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=236890.
Honoré B, Madsen P, Rasmussen HH, et al. (1994). "Cloning and expression of a cDNA covering the complete coding region of the P32 subunit of human pre-mRNA splicing factor SF2.". Gene 134 (2): 283–7. doi:10.1016/0378-1119(93)90108-F. PMID 8262387.
Tange TO, Jensen TH, Kjems J (1996). "In vitro interaction between human immunodeficiency virus type 1 Rev protein and splicing factor ASF/SF2-associated protein, p32.". J. Biol. Chem. 271 (17): 10066–72. doi:10.1074/jbc.271.17.10066. PMID 8626563.
Guo N, Weremowicz S, Lynch N, et al. (1997). "Assignment of C1QBP encoding the C1q globular domain binding protein (gC1q-R) to human chromosome 17 band p13.3 by in situ hybridization.". Cytogenet. Cell Genet. 77 (3-4): 283–4. doi:10.1159/000134598. PMID 9284938.
Majumdar M, Datta K (1998). "Assignment of cDNA encoding hyaluronic acid-binding protein 1 to human chromosome 17p12-p13.". Genomics 51 (3): 476–7. doi:10.1006/geno.1998.5364. PMID 9721222.
Petersen-Mahrt SK, Estmer C, Ohrmalm C, et al. (1999). "The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation.". EMBO J. 18 (4): 1014–24. doi:10.1093/emboj/18.4.1014. PMC 1171193. PMID 10022843. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171193.
Jiang J, Zhang Y, Krainer AR, Xu RM (1999). "Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein.". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3572–7. doi:10.1073/pnas.96.7.3572. PMC 22335. PMID 10097078. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22335.
Braun L, Ghebrehiwet B, Cossart P (2000). "gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes.". EMBO J. 19 (7): 1458–66. doi:10.1093/emboj/19.7.1458. PMC 310215. PMID 10747014. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310215.
Beatch MD, Hobman TC (2000). "Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria.". J. Virol. 74 (12): 5569–76. doi:10.1128/JVI.74.12.5569-5576.2000. PMC 112044. PMID 10823864. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=112044.
Storz P, Hausser A, Link G, et al. (2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32.". J. Biol. Chem. 275 (32): 24601–7. doi:10.1074/jbc.M002964200. PMID 10831594.
Tye AJ, Ghebrehiwet B, Guo N, et al. (2001). "The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter analysis.". J. Biol. Chem. 276 (20): 17069–75. doi:10.1074/jbc.M009064200. PMID 11278463.
Schaerer MT, Kannenberg K, Hunziker P, et al. (2001). "Interaction between GABA(A) receptor beta subunits and the multifunctional protein gC1q-R.". J. Biol. Chem. 276 (28): 26597–604. doi:10.1074/jbc.M102534200. PMID 11350968.
Kobayashi M, Hanai R (2001). "M phase-specific association of human topoisomerase IIIbeta with chromosomes.". Biochem. Biophys. Res. Commun. 287 (1): 282–7. doi:10.1006/bbrc.2001.5580. PMID 11549288.
Rozanov DV, Ghebrehiwet B, Postnova TI, et al. (2002). "The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR.". J. Biol. Chem. 277 (11): 9318–25. doi:10.1074/jbc.M110711200. PMID 11773076.
Majumdar M, Meenakshi J, Goswami SK, Datta K (2002). "Hyaluronan binding protein 1 (HABP1)/C1QBP/p32 is an endogenous substrate for MAP kinase and is translocated to the nucleus upon mitogenic stimulation.". Biochem. Biophys. Res. Commun. 291 (4): 829–37. doi:10.1006/bbrc.2002.6491. PMID 11866440.

PDB gallery

1p32: CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN

C1QBP

Interactions

References

Further reading