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Q07021

- C1QBP_HUMAN

UniProt

Q07021 - C1QBP_HUMAN

Protein

Complement component 1 Q subcomponent-binding protein, mitochondrial

Gene

C1QBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    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.21 Publications

    GO - Molecular functioni

    1. adrenergic receptor binding Source: UniProtKB
    2. complement component C1q binding Source: UniProtKB
    3. hyaluronic acid binding Source: UniProtKB
    4. kininogen binding Source: UniProtKB
    5. mitochondrial ribosome binding Source: UniProtKB
    6. mRNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. transcription corepressor activity Source: UniProtKB
    9. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. blood coagulation, intrinsic pathway Source: Reactome
    4. complement activation, classical pathway Source: UniProtKB-KW
    5. immune response Source: ProtInc
    6. innate immune response Source: UniProtKB-KW
    7. mature ribosome assembly Source: UniProtKB
    8. mRNA processing Source: UniProtKB-KW
    9. negative regulation of defense response to virus Source: UniProtKB
    10. negative regulation of interferon-gamma production Source: UniProtKB
    11. negative regulation of interleukin-12 production Source: UniProtKB
    12. negative regulation of MDA-5 signaling pathway Source: UniProtKB
    13. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    14. negative regulation of RIG-I signaling pathway Source: UniProtKB
    15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. phosphatidylinositol 3-kinase signaling Source: UniProtKB
    17. positive regulation of apoptotic process Source: UniProtKB
    18. positive regulation of cell adhesion Source: UniProtKB
    19. positive regulation of dendritic cell chemotaxis Source: UniProtKB
    20. positive regulation of mitochondrial translation Source: UniProtKB
    21. positive regulation of neutrophil chemotaxis Source: UniProtKB
    22. positive regulation of protein kinase B signaling Source: UniProtKB
    23. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    24. positive regulation of trophoblast cell migration Source: UniProtKB
    25. regulation of complement activation Source: UniProtKB
    26. RNA splicing Source: UniProtKB-KW
    27. transcription, DNA-templated Source: UniProtKB-KW
    28. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Adaptive immunity, Apoptosis, Complement pathway, Host-virus interaction, Immunity, Innate immunity, mRNA processing, mRNA splicing, Ribosome biogenesis, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_326. Intrinsic Pathway.

    Protein family/group databases

    TCDBi9.B.103.1.1. the putative ca(2+) uniporter (gc1qr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:C1QBP
    Synonyms:GC1QBP, HABP1, SF2P32
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1243. C1QBP.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. extracellular space Source: Ensembl
    5. membrane Source: UniProtKB
    6. mitochondrial matrix Source: UniProtKB-SubCell
    7. mitochondrion Source: UniProtKB
    8. nucleolus Source: UniProtKB-SubCell
    9. nucleus Source: UniProtKB
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi107 – 1071G → D: Impairs HIV RNA splicing in mouse cells. 1 Publication

    Organism-specific databases

    PharmGKBiPA25624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7373Mitochondrion2 PublicationsAdd
    BLAST
    Chaini74 – 282209Complement component 1 Q subcomponent-binding protein, mitochondrialPRO_0000018590Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei91 – 911N6-acetyllysine1 Publication
    Modified residuei188 – 1881Phosphotyrosine2 Publications
    Modified residuei201 – 2011Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ07021.
    PaxDbiQ07021.
    PRIDEiQ07021.

    2D gel databases

    DOSAC-COBS-2DPAGEQ07021.
    OGPiQ07021.

    PTM databases

    PhosphoSiteiQ07021.

    Miscellaneous databases

    PMAP-CutDBQ07021.

    Expressioni

    Tissue specificityi

    Expressed on cell surface of peripheral blood cells (at protein level); Surface expression is reported for macrophages and monocyte-derived dendritic cells.2 Publications

    Inductioni

    Enhanced cell surface expression upon platelet and monocyte activation.2 Publications

    Gene expression databases

    ArrayExpressiQ07021.
    BgeeiQ07021.
    CleanExiHS_C1QBP.
    GenevestigatoriQ07021.

    Organism-specific databases

    HPAiHPA026483.

    Interactioni

    Subunit structurei

    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.19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279584EBI-347528,EBI-6377335From a different organism.
    CDK13Q14004-26EBI-347528,EBI-6375898
    CDKN2AQ8N7263EBI-347528,EBI-625922
    Cdkn2aQ643644EBI-347528,EBI-1202287From a different organism.
    F12P007482EBI-347528,EBI-6378830
    FOXC1Q129486EBI-347528,EBI-1175253
    HRKO001987EBI-347528,EBI-701322
    KNG1P010424EBI-347528,EBI-6378713
    MAVSQ7Z4345EBI-347528,EBI-995373
    PRKD1Q151399EBI-347528,EBI-1181072
    VTNP040048EBI-347528,EBI-1036653

    Protein-protein interaction databases

    BioGridi107169. 130 interactions.
    DIPiDIP-31164N.
    IntActiQ07021. 58 interactions.
    MINTiMINT-246803.
    STRINGi9606.ENSP00000225698.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi77 – 9620
    Turni106 – 1083
    Beta strandi110 – 1145
    Beta strandi117 – 1248
    Beta strandi127 – 1348
    Beta strandi168 – 1747
    Helixi175 – 1773
    Beta strandi180 – 1878
    Beta strandi205 – 2139
    Beta strandi225 – 2284
    Helixi233 – 24412
    Turni245 – 2473
    Helixi250 – 28031

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P32X-ray2.25A/B/C74-282[»]
    3RPXX-ray2.65A/B/C96-282[»]
    ProteinModelPortaliQ07021.
    SMRiQ07021. Positions 74-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07021.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni76 – 9318C1q bindingAdd
    BLAST
    Regioni168 – 21346Interaction with MAVSAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MAM33 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG295722.
    HOGENOMiHOG000046272.
    HOVERGENiHBG000914.
    InParanoidiQ07021.
    KOiK15414.
    OMAiNVNHTVD.
    OrthoDBiEOG7MH0ZQ.
    PhylomeDBiQ07021.
    TreeFamiTF315160.

    Family and domain databases

    Gene3Di3.10.280.10. 1 hit.
    InterProiIPR003428. MAM33.
    [Graphical view]
    PfamiPF02330. MAM33. 1 hit.
    [Graphical view]
    SUPFAMiSSF54529. SSF54529. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q07021-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA    50
    GSERRPGLLR PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK 100
    TLPKMSGGWE LELNGTEAKL VRKVAGEKIT VTFNINNSIP PTFDGEEEPS 150
    QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK ALVLDCHYPE DEVGQEDEAE 200
    SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM DFLADRGVDN 250
    TFADELVELS TALEHQEYIT FLEDLKSFVK SQ 282
    Length:282
    Mass (Da):31,362
    Last modified:February 1, 1995 - v1
    Checksum:i2F747FA73BB1314B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11071.1.
    PIRiJT0762.
    RefSeqiNP_001203.1. NM_001212.3.
    UniGeneiHs.555866.

    Genome annotation databases

    EnsembliENST00000225698; ENSP00000225698; ENSG00000108561.
    GeneIDi708.
    KEGGihsa:708.
    UCSCiuc002gby.1. human.

    Polymorphism databases

    DMDMi730772.

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11071.1.
    PIRi JT0762.
    RefSeqi NP_001203.1. NM_001212.3.
    UniGenei Hs.555866.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P32 X-ray 2.25 A/B/C 74-282 [» ]
    3RPX X-ray 2.65 A/B/C 96-282 [» ]
    ProteinModelPortali Q07021.
    SMRi Q07021. Positions 74-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107169. 130 interactions.
    DIPi DIP-31164N.
    IntActi Q07021. 58 interactions.
    MINTi MINT-246803.
    STRINGi 9606.ENSP00000225698.

    Protein family/group databases

    TCDBi 9.B.103.1.1. the putative ca(2+) uniporter (gc1qr) family.

    PTM databases

    PhosphoSitei Q07021.

    Polymorphism databases

    DMDMi 730772.

    2D gel databases

    DOSAC-COBS-2DPAGE Q07021.
    OGPi Q07021.

    Proteomic databases

    MaxQBi Q07021.
    PaxDbi Q07021.
    PRIDEi Q07021.

    Protocols and materials databases

    DNASUi 708.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225698 ; ENSP00000225698 ; ENSG00000108561 .
    GeneIDi 708.
    KEGGi hsa:708.
    UCSCi uc002gby.1. human.

    Organism-specific databases

    CTDi 708.
    GeneCardsi GC17M005336.
    HGNCi HGNC:1243. C1QBP.
    HPAi HPA026483.
    MIMi 601269. gene.
    neXtProti NX_Q07021.
    PharmGKBi PA25624.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295722.
    HOGENOMi HOG000046272.
    HOVERGENi HBG000914.
    InParanoidi Q07021.
    KOi K15414.
    OMAi NVNHTVD.
    OrthoDBi EOG7MH0ZQ.
    PhylomeDBi Q07021.
    TreeFami TF315160.

    Enzyme and pathway databases

    Reactomei REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    EvolutionaryTracei Q07021.
    GeneWikii C1QBP.
    GenomeRNAii 708.
    NextBioi 2880.
    PMAP-CutDB Q07021.
    PROi Q07021.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07021.
    Bgeei Q07021.
    CleanExi HS_C1QBP.
    Genevestigatori Q07021.

    Family and domain databases

    Gene3Di 3.10.280.10. 1 hit.
    InterProi IPR003428. MAM33.
    [Graphical view ]
    Pfami PF02330. MAM33. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54529. SSF54529. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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).

    Entry informationi

    Entry nameiC1QBP_HUMAN
    AccessioniPrimary (citable) accession number: Q07021
    Secondary accession number(s): Q2HXR8, Q9NNY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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 (PubMed:9305894, PubMed:11493647). 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.2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3