CPLM-011479

Genbank Nucleotide ID

Complement component 1 Q subcomponent-binding protein, mitochondrial

Protein Synonyms/Alias

ASF/SF2-associated protein p32; Glycoprotein gC1qBP; C1qBP; Hyaluronan-binding protein 1; Mitochondrial matrix protein p32; gC1q-R protein; p33

GC1QBP; HABP1; SF2P32

Homo sapiens (Human)

Position	Peptide	Type	References
91	DFLSDEIKEERKIQK	acetylation	[1, 2, 3, 4]
91	DFLSDEIKEERKIQK	ubiquitination	[4, 5, 6, 7]
104	QKHKTLPKMSGGWEL	acetylation	[3]
104	QKHKTLPKMSGGWEL	ubiquitination	[7, 8, 9]
174	NFVVEVIKNDDGKKA	ubiquitination	[5, 7]
179	VIKNDDGKKALVLDC	ubiquitination	[6, 7]
180	IKNDDGKKALVLDCH	ubiquitination	[6]
280	EDLKSFVKSQ*****	ubiquitination	[5, 7]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

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 affinty 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.

REGION 76 93 C1q binding.
REGION 168 213 Interation with MAVS.
MOD_RES 91 91 N6-acetyllysine.
MOD_RES 188 188 Phosphotyrosine.
MOD_RES 201 201 Phosphoserine.

3D-structure; Acetylation; Adaptive immunity; Apoptosis; Cell membrane; Complement pathway; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Immunity; Innate immunity; Membrane; Mitochondrion; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; Secreted; Transcription; Transcription regulation; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0009986; C:cell surface; IDA:UniProtKB.
GO:0005829; C:cytosol; IDA:UniProtKB.
GO:0005615; C:extracellular space; IEA:Compara.
GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0005886; C:plasma membrane; TAS:Reactome.
GO:0031690; F:adrenergic receptor binding; ISS:UniProtKB.
GO:0001849; F:complement component C1q binding; IDA:UniProtKB.
GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
GO:0030984; F:kininogen binding; IDA:UniProtKB.
GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO:0006955; P:immune response; TAS:ProtInc.
GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
GO:0039534; P:negative regulation of MDA-5 signaling pathway; IDA:UniProtKB.
GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO:0039536; P:negative regulation of RIG-I signaling pathway; IDA:UniProtKB.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0014065; P:phosphatidylinositol 3-kinase cascade; IMP:UniProtKB.
GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
GO:0051897; P:positive regulation of protein kinase B signaling cascade; IMP:UniProtKB.
GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO:1901165; P:positive regulation of trophoblast cell migration; IMP:UniProtKB.
GO:0030449; P:regulation of complement activation; IDA:UniProtKB.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.