C1QBP
entrez
708
canonical
uniprot
Q07021
canonical
ensembl
ENSG00000108561
resolver
ensp
ENSP00000225698
resolver
enst
ENST00000225698
resolver
genesymbol
C1QBP
resolver
genesymbol_syn
GC1QBP
resolver
genesymbol_syn
HABP1
resolver
genesymbol_syn
SF2P32
resolver
hgnc
HGNC:1243
resolver
uniprot
Q2HXR8
resolver
uniprot
Q9NNY8
resolver
uniprot_entry
C1QBP_HUMAN
resolver
uniprot_sec
Q2HXR8
resolver
uniprot_sec
Q9NNY8
resolver
amino_acid_sequence
MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ
uniprot
proteins
disease_involvement
DISEASE: Combined oxidative phosphorylation deficiency 33 (COXPD33) [MIM:617713]: An autosomal recessive disorder caused by multiple mitochondrial respiratory chain defects and impaired mitochondrial energy metabolism. Clinical manifestations are highly variable. Affected infants present with cardiomyopathy accompanied by multisystemic features involving liver, kidney, and brain. Death in infancy is observed in some patients. Children and adults present with myopathy and progressive external ophthalmoplegia. {ECO:0000269|PubMed:28942965}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing (PubMed:10022843, PubMed:10479529, PubMed:10722602, PubMed:11086025, PubMed:11859136, PubMed:15243141, PubMed:16140380, PubMed:16177118, PubMed:17881511, PubMed:18676636, PubMed:19004836, PubMed:19164550, PubMed:20810993, PubMed:21536856, PubMed:21544310, PubMed:22700724, PubMed:28942965, PubMed:8662673, PubMed:8710908, PubMed:9461517). At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades (PubMed:10479529, PubMed:11859136, PubMed:8662673, PubMed:8710908). 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 (PubMed:20810993, PubMed:8195709). In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK (PubMed:21544310). 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 (PubMed:16140380, PubMed:22700724, PubMed:9461517). Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway (PubMed:16177118). Required for protein synthesis in mitochondria (PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity (By similarity). Acts as a RNA modification reader, which specifically recognizes and binds mitochondrial RNAs modified by C5-methylcytosine (m5C) in response to stress, and promotes recruitment of the mitochondrial degradosome complex, leading to their degradation (PubMed:39019044). 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 (By similarity). Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation (PubMed:10022843, PubMed:21536856). Is required for the nuclear translocation of splicing factor U2AF1L4 (By similarity). Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF (PubMed:17486078). May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription (PubMed:15243141, PubMed:18676636). May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase (PubMed:19004836). May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells (PubMed:11086025, PubMed:17881511). Involved in regulation of antiviral response by inhibiting RIGI- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection (PubMed:19164550). Acts as a regulator of DNA repair via homologous recombination by inhibiting the activity of MRE11: interacts with unphosphorylated MRE11 and RAD50 in absence of DNA damage, preventing formation and activity of the MRN complex. Following DNA damage, dissociates from phosphorylated MRE11, allowing formation of the MRN complex (PubMed:31353207). {ECO:0000250|UniProtKB:O35658, ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:11859136, ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16140380, ECO:0000269|PubMed:16177118, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19004836, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:20810993, ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724, ECO:0000269|PubMed:28942965, ECO:0000269|PubMed:31353207, ECO:0000269|PubMed:39019044, ECO:0000269|PubMed:8195709, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.; FUNCTION: (Microbial infection) Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. {ECO:0000269|PubMed:12833064}.; FUNCTION: (Microbial infection) In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B (InlB) and Staphylococcus aureus protein A. {ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:12411480}.; FUNCTION: (Microbial infection) Involved in replication of Rubella virus. {ECO:0000269|PubMed:12034482}.
uniprot
proteins
mass_dalton
31362
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="G->D: Impairs HIVRNA splicing in mouse cells."; /evidence="ECO:0000269|PubMed:12833064
uniprot
proteins
protein_family
MAM33 family
uniprot
proteins
pubmed
10022843
uniprot
proteins
pubmed
10097078
uniprot
proteins
pubmed
10479529
uniprot
proteins
pubmed
10722602
uniprot
proteins
pubmed
10747014
uniprot
proteins
pubmed
10823864
uniprot
proteins
pubmed
11086025
uniprot
proteins
pubmed
11278463
uniprot
proteins
pubmed
11493647
uniprot
proteins
pubmed
11859136
uniprot
proteins
pubmed
12034482
uniprot
proteins
pubmed
12411480
uniprot
proteins
pubmed
12574814
uniprot
proteins
pubmed
12833064
uniprot
proteins
pubmed
15031724
uniprot
proteins
pubmed
15243141
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16140380
uniprot
proteins
pubmed
16177118
uniprot
proteins
pubmed
16537587
uniprot
proteins
pubmed
16721827
uniprot
proteins
pubmed
17486078
uniprot
proteins
pubmed
17693683
uniprot
proteins
pubmed
17881511
uniprot
proteins
pubmed
18191643
uniprot
proteins
pubmed
1830244
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18676636
uniprot
proteins
pubmed
19004836
uniprot
proteins
pubmed
19164550
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20810993
uniprot
proteins
pubmed
20950273
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21536856
uniprot
proteins
pubmed
21544310
uniprot
proteins
pubmed
22238231
uniprot
proteins
pubmed
22700724
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28942965
uniprot
proteins
pubmed
31353207
uniprot
proteins
pubmed
32958672
uniprot
proteins
pubmed
37198654
uniprot
proteins
pubmed
39019044
uniprot
proteins
pubmed
8195709
uniprot
proteins
pubmed
8262387
uniprot
proteins
pubmed
8567680
uniprot
proteins
pubmed
8662673
uniprot
proteins
pubmed
8710908
uniprot
proteins
pubmed
8900153
uniprot
proteins
pubmed
9191880
uniprot
proteins
pubmed
9233640
uniprot
proteins
pubmed
9299613
uniprot
proteins
pubmed
9305894
uniprot
proteins
pubmed
9461517
uniprot
proteins
sequence_length
282
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:9305894}. Nucleus {ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:9299613}. Nucleus, nucleolus {ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:32958672}. Cell membrane {ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11493647, ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8195709, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:9191880, ECO:0000269|PubMed:9233640}; Peripheral membrane protein {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:9191880}; Extracellular side. Secreted. Cytoplasm {ECO:0000269|PubMed:11493647, ECO:0000269|PubMed:9299613}. Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. Localizes to the nucleolus when coexpressed with POLGARF (PubMed:32958672). Interaction with POLGARF is likely to result in prevention of C1QBP maturation and redirection from mitochondria to nucleoli (PubMed:32958672). {ECO:0000269|PubMed:32958672}.
uniprot
proteins