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Q07021 (C1QBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement component 1 Q subcomponent-binding protein, mitochondrial
Alternative name(s):
ASF/SF2-associated protein p32
Glycoprotein gC1qBP
Short name=C1qBP
Hyaluronan-binding protein 1
Mitochondrial matrix protein p32
gC1q-R protein
p33
Gene names
Name:C1QBP
Synonyms:GC1QBP, HABP1, SF2P32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. Involved in replication of Rubella virus. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppresion of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. Ref.8 Ref.11 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.25 Ref.29 Ref.30 Ref.34 Ref.35 Ref.38 Ref.40 Ref.41 Ref.44 Ref.47 Ref.48 Ref.49

Subunit structure

Homotrimer; three monomers form a donut-shaped structure with an unusually asymmetric charge distribution on the surface. Interacts with CDK13, HRK, VTN, NFYB, ADRA1B, FOXC1, DDX21, DDX50, NCL, SRSF1, SRSF9 and CDKN2A isoform smARF Interacts with CD93; the association may represent a cell surface C1q receptor. Interacts with KRT1; the association represents a cell surface kininogen receptor. Interacts with CD209; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with FBL and RRP1; the respective interactions with C1QBP are competetive. Probably associates with the mitoribosome. Interacts with MAVS; the interaction occurs upon viral transfection. Interacts with PPIF. Interacts with Rubella virus capsid protein; the interaction occurs in mitochondria. Interacts with Rubella virus protease p150, Staphylococcus aureus protein A/spa, HIV-1 Tat and HCV core protein. Ref.10 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.28 Ref.29 Ref.32 Ref.33 Ref.37 Ref.38 Ref.41 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50

Subcellular location

Mitochondrion matrix. Nucleus. Cell membrane; Peripheral membrane protein; Extracellular side. Secreted. Cytoplasm. Nucleusnucleolus. Note: Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. Ref.2 Ref.8 Ref.12 Ref.13 Ref.14 Ref.22 Ref.27 Ref.28 Ref.37 Ref.38 Ref.41 Ref.47

Tissue specificity

Expressed on cell surface of peripheral blood cells (at protein level); Surface expression is reported for macrophages and monocyte-derived dendritic cells. Ref.8 Ref.27

Induction

Enhanced cell surface expression upon platelet and monocyte activation. Ref.27 Ref.30

Sequence similarities

Belongs to the MAM33 family.

Caution

The subcellular location has been matter of debate. After being reported to be exclusively localized to mitochondria, demonstrations of promiscuous associations and locations have been rather considered as artifactual due to the extremely acidic character and the use of different tagged versions of the protein (Ref.13, Ref.22). However, by now the location to multiple compartments linked to diverse functions is accepted. The N-termini of the surface and secreted forms are identical to the reported processed mitochonddrial form.

Ontologies

Keywords
   Biological processAdaptive immunity
Apoptosis
Complement pathway
Host-virus interaction
Immunity
Innate immunity
mRNA processing
mRNA splicing
Ribosome biogenesis
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
Nucleus
Secreted
   DomainTransit peptide
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Traceable author statement Ref.2. Source: ProtInc

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mature ribosome assembly

Inferred from mutant phenotype Ref.47. Source: UniProtKB

negative regulation of MDA-5 signaling pathway

Inferred from direct assay Ref.41. Source: UniProtKB

negative regulation of RIG-I signaling pathway

Inferred from direct assay Ref.41. Source: UniProtKB

negative regulation of defense response to virus

Inferred from mutant phenotype Ref.41. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from direct assay Ref.35. Source: UniProtKB

negative regulation of interleukin-12 production

Inferred from direct assay Ref.30Ref.35. Source: UniProtKB

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.29. Source: UniProtKB

phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.30. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.28. Source: UniProtKB

positive regulation of cell adhesion

Inferred from mutant phenotype Ref.44. Source: UniProtKB

positive regulation of dendritic cell chemotaxis

Inferred from mutant phenotype Ref.34. Source: UniProtKB

positive regulation of mitochondrial translation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neutrophil chemotaxis

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.30. Source: UniProtKB

positive regulation of substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.23. Source: UniProtKB

positive regulation of trophoblast cell migration

Inferred from mutant phenotype Ref.44. Source: UniProtKB

regulation of complement activation

Inferred from direct assay Ref.2. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell surface

Inferred from direct assay Ref.35. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.29. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 11290596Ref.8. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.41. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.29. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionadrenergic receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

complement component C1q binding

Inferred from direct assay Ref.2. Source: UniProtKB

hyaluronic acid binding

Inferred from direct assay Ref.9. Source: UniProtKB

kininogen binding

Inferred from direct assay Ref.8. Source: UniProtKB

mRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial ribosome binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.29. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.29. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7373Mitochondrion Ref.7 Ref.8
Chain74 – 282209Complement component 1 Q subcomponent-binding protein, mitochondrial
PRO_0000018590

Regions

Region76 – 9318C1q binding
Region168 – 21346Interation with MAVS

Amino acid modifications

Modified residue911N6-acetyllysine Ref.43
Modified residue1881Phosphotyrosine Ref.36 Ref.42
Modified residue2011Phosphoserine Ref.39

Experimental info

Mutagenesis1071G → D: Impairs HIV RNA splicing in mouse cells. Ref.25

Secondary structure

......................... 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07021 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 2F747FA73BB1314B

FASTA28231,362
        10         20         30         40         50         60 
MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR 

        70         80         90        100        110        120 
PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL 

       130        140        150        160        170        180 
VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK 

       190        200        210        220        230        240 
ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM 

       250        260        270        280 
DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a cDNA covering the complete coding region of the P32 subunit of human pre-mRNA splicing factor SF2."
Honore B., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E., Leffers H.
Gene 134:283-287(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74; 76-93 AND 208-216.
Tissue: Fibroblast.
[2]"Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular 'heads' of C1q."
Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.
J. Exp. Med. 179:1809-1821(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
[3]"The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter analysis."
Tye A.J., Ghebrehiwet B., Guo N., Sastry K.N., Chow B.K.C., Peerschke E.I.B., Lim B.L.
J. Biol. Chem. 276:17069-17075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]SeattleSNPs variation discovery resource
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Ovary.
[7]"Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators."
Krainer A.R., Mayeda A., Kozak D., Binns G.
Cell 66:383-394(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-282, PROTEIN SEQUENCE OF 74-114.
[8]"Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor."
Herwald H., Dedio J., Kellner R., Loos M., Muller-Esterl W.
J. Biol. Chem. 271:13040-13047(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 74-88, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"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."
Deb T.B., Datta K.
J. Biol. Chem. 271:2206-2212(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-282.
[10]"The binding protein for globular heads of complement C1q, gC1qR. Functional expression and characterization as a novel vitronectin binding factor."
Lim B.L., Reid K.B., Ghebrehiwet B., Peerschke E.I., Leigh L.A., Preissner K.T.
J. Biol. Chem. 271:26739-26744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VTN.
[11]"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)."
Joseph K., Ghebrehiwet B., Peerschke E.I., Reid K.B., Kaplan A.P.
Proc. Natl. Acad. Sci. U.S.A. 93:8552-8557(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The C1q-binding cell membrane proteins cC1q-R and gC1q-R are released from activated cells: subcellular distribution and immunochemical characterization."
Peterson K.L., Zhang W., Lu P.D., Keilbaugh S.A., Peerschke E.I., Ghebrehiwet B.
Clin. Immunol. Immunopathol. 84:17-26(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"p32 protein, a splicing factor 2-associated protein, is localized in mitochondrial matrix and is functionally important in maintaining oxidative phosphorylation."
Muta T., Kang D., Kitajima S., Fujiwara T., Hamasaki N.
J. Biol. Chem. 272:24363-24370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R, associate to form a complex."
Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E., Eggleton P., Reid K.B., Peerschke E.I.
J. Immunol. 159:1429-1436(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD93, SUBCELLULAR LOCATION.
[15]"C1q-mediated chemotaxis by human neutrophils: involvement of gClqR and G-protein signalling mechanisms."
Leigh L.E., Ghebrehiwet B., Perera T.P., Bird I.N., Strong P., Kishore U., Reid K.B., Eggleton P.
Biochem. J. 330:247-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells."
Joseph K., Ghebrehiwet B., Kaplan A.P.
Clin. Immunol. 92:246-255(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation."
Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C., Akusjarvi G.
EMBO J. 18:1014-1024(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SRSF1 AND SRSF9.
[18]"gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes."
Braun L., Ghebrehiwet B., Cossart P.
EMBO J. 19:1458-1466(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Staphylococcus aureus protein A recognizes platelet gC1qR/p33: a novel mechanism for staphylococcal interactions with platelets."
Nguyen T., Ghebrehiwet B., Peerschke E.I.
Infect. Immun. 68:2061-2068(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STAPHYLOCOCCUS AUREUS SPA.
[20]"Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation."
Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.
J. Clin. Invest. 106:1239-1249(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HCV CORE PROTEIN.
[21]"Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria."
Beatch M.D., Hobman T.C.
J. Virol. 74:5569-5576(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUBELLA VIRUS CAPSID PROTEIN.
[22]"Retargeting of the mitochondrial protein p32/gC1Qr to a cytoplasmic compartment and the cell surface."
van Leeuwen H.C., O'Hare P.
J. Cell Sci. 114:2115-2123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading."
Feng X., Tonnesen M.G., Peerschke E.I., Ghebrehiwet B.
J. Immunol. 168:2441-2448(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"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."
Mohan K.V., Ghebrehiwet B., Atreya C.D.
Virus Res. 85:151-161(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUBELLA VIRUS CAPSID PROTEIN.
[25]"Human p32 protein relieves a post-transcriptional block to HIV replication in murine cells."
Zheng Y.H., Yu H.F., Peterlin B.M.
Nat. Cell Biol. 5:611-618(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-107.
[26]Erratum
Zheng Y.H., Yu H.F., Peterlin B.M.
Nat. Cell Biol. 5:839-839(2003)
[27]"Activation-dependent surface expression of gC1qR/p33 on human blood platelets."
Peerschke E.I., Murphy T.K., Ghebrehiwet B.
Thromb. Haemost. 89:331-339(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[28]"Physical and functional interaction between BH3-only protein Hrk and mitochondrial pore-forming protein p32."
Sunayama J., Ando Y., Itoh N., Tomiyama A., Sakurada K., Sugiyama A., Kang D., Tashiro F., Gotoh Y., Kuchino Y., Kitanaka C.
Cell Death Differ. 11:771-781(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRK, SUBCELLULAR LOCATION.
[29]"Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro."
Chattopadhyay C., Hawke D., Kobayashi R., Maity S.N.
Nucleic Acids Res. 32:3632-3641(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NFYB.
[30]"gC1q receptor ligation selectively down-regulates human IL-12 production through activation of the phosphoinositide 3-kinase pathway."
Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.
J. Immunol. 175:4706-4714(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[31]Erratum
Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.
J. Immunol. 178:3332-3332(2007)
[32]"CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo."
Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G., Weil D., Geneviere A.M.
J. Cell. Biochem. 99:890-904(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK13.
[33]"Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32."
Berro R., Kehn K., de la Fuente C., Pumfery A., Adair R., Wade J., Colberg-Poley A.M., Hiscott J., Kashanchi F.
J. Virol. 80:3189-3204(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[34]"Chemotaxis of human monocyte-derived dendritic cells to complement component C1q is mediated by the receptors gC1qR and cC1qR."
Vegh Z., Kew R.R., Gruber B.L., Ghebrehiwet B.
Mol. Immunol. 43:1402-1407(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[35]"HCV core protein interaction with gC1q receptor inhibits Th1 differentiation of CD4+ T cells via suppression of dendritic cell IL-12 production."
Waggoner S.N., Hall C.H., Hahn Y.S.
J. Leukoc. Biol. 82:1407-1419(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[37]"The autophagic inducer smARF interacts with and is stabilized by the mitochondrial p32 protein."
Reef S., Shifman O., Oren M., Kimchi A.
Oncogene 26:6677-6683(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKN2A, SUBCELLULAR LOCATION.
[38]"Human p32 is a novel FOXC1-interacting protein that regulates FOXC1 transcriptional activity in ocular cells."
Huang L., Chi J., Berry F.B., Footz T.K., Sharp M.W., Walter M.A.
Invest. Ophthalmol. Vis. Sci. 49:5243-5249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FOXC1, SUBCELLULAR LOCATION.
[39]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[40]"Evidence for inhibitory interaction of hyaluronan-binding protein 1 (HABP1/p32/gC1qR) with Streptococcus pneumoniae hyaluronidase."
Yadav G., Prasad R.L., Jha B.K., Rai V., Bhakuni V., Datta K.
J. Biol. Chem. 284:3897-3905(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[41]"Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria."
Xu L., Xiao N., Liu F., Ren H., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAVS.
[42]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[43]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"An alternative role of C1q in cell migration and tissue remodeling: contribution to trophoblast invasion and placental development."
Agostinis C., Bulla R., Tripodo C., Gismondi A., Stabile H., Bossi F., Guarnotta C., Garlanda C., De Seta F., Spessotto P., Santoni A., Ghebrehiwet B., Girardi G., Tedesco F.
J. Immunol. 185:4420-4429(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[45]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death."
McGee A.M., Baines C.P.
Biochem. J. 433:119-125(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIF.
[47]"Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBL; RRP1; DDX21; DDX50 AND NCL.
[48]"Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore)."
Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A., Bdeir K., Cines D.B., Colman R.W.
Thromb. Haemost. 105:1053-1059(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRT1.
[49]"DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the surface of monocyte-derived immature dendritic cells."
Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R., Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.
Blood 120:1228-1236(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CD209.
[50]"Binding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifs."
Suppiah S., Mousa H.A., Tzeng W.P., Matthews J.D., Frey T.K.
J. Gen. Virol. 93:807-816(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUBELLA VIRUS PROTEASE P150.
[51]"Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein."
Jiang J., Zhang Y., Krainer A.R., Xu R.-M.
Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04636 mRNA. Translation: AAA16315.1.
X75913 mRNA. Translation: CAA53512.1.
AF338439 Genomic DNA. Translation: AAK26580.1.
BT019898 mRNA. Translation: AAV38701.1.
BT019899 mRNA. Translation: AAV38702.1.
DQ372108 Genomic DNA. Translation: ABC79624.1.
BC000435 mRNA. Translation: AAH00435.1.
BC013731 mRNA. Translation: AAH13731.1.
M69039 mRNA. Translation: AAA73055.1.
AF275902 mRNA. Translation: AAF78763.1.
PIRJT0762.
RefSeqNP_001203.1. NM_001212.3.
UniGeneHs.555866.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P32X-ray2.25A/B/C75-282[»]
3RPXX-ray2.65A/B/C96-282[»]
ProteinModelPortalQ07021.
SMRQ07021. Positions 74-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107169. 140 interactions.
DIPDIP-31164N.
IntActQ07021. 58 interactions.
MINTMINT-246803.
STRING9606.ENSP00000225698.

Protein family/group databases

TCDB9.B.103.1.1. the putative ca(2+) uniporter (gc1qr) family.

PTM databases

PhosphoSiteQ07021.

Polymorphism databases

DMDM730772.

2D gel databases

DOSAC-COBS-2DPAGEQ07021.
OGPQ07021.

Proteomic databases

PaxDbQ07021.
PRIDEQ07021.

Protocols and materials databases

DNASU708.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225698; ENSP00000225698; ENSG00000108561.
GeneID708.
KEGGhsa:708.
UCSCuc002gby.1. human.

Organism-specific databases

CTD708.
GeneCardsGC17M005336.
HGNCHGNC:1243. C1QBP.
HPAHPA026483.
MIM601269. gene.
neXtProtNX_Q07021.
PharmGKBPA25624.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295722.
HOGENOMHOG000046272.
HOVERGENHBG000914.
InParanoidQ07021.
KOK15414.
OMACACGCGC.
OrthoDBEOG7MH0ZQ.
PhylomeDBQ07021.
TreeFamTF315160.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ07021.
BgeeQ07021.
CleanExHS_C1QBP.
GenevestigatorQ07021.

Family and domain databases

Gene3D3.10.280.10. 1 hit.
InterProIPR003428. MAM33.
[Graphical view]
PfamPF02330. MAM33. 1 hit.
[Graphical view]
SUPFAMSSF54529. SSF54529. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ07021.
GeneWikiC1QBP.
GenomeRNAi708.
NextBio2880.
PMAP-CutDBQ07021.
PROQ07021.
SOURCESearch...

Entry information

Entry nameC1QBP_HUMAN
AccessionPrimary (citable) accession number: Q07021
Secondary accession number(s): Q2HXR8, Q9NNY8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM