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Protein Page:
C1QBP (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
C1QBP a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. Originally identified via its binding interactions with Splicing Factor (SF-2). Multiple, diverse binding partners of C1QBP were subsequently identified, including the globular heads of complement component C1q, hyaluronic acid, selected protein kinases, the tumor suppressor ARF, and multiple antigens of bacterial and viral origin. Overexpressed in a number of cancer cell types, and has been implicated in the Warburg effect, whereby cancer cells shift their metabolism from oxidative phosphorylation to glycolysis. Inhibits the Mitochondrial Permeability Transition (MPT) pore, possibly serving a protective function against damage from oxidative stress. Binding to C1q inhibits C1. In complex with cytokeratin-1/KRT1 is a high affinty receptor for kininogen-1/HMWK. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. The cell surface form may require docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. Belongs to the MAM33 family. Note: This description may include information from UniProtKB.
Protein type: Receptor, misc.; Motility/polarity/chemotaxis; Mitochondrial; Nucleolus
Chromosomal Location of Human Ortholog: 17p13.3
Cellular Component: cell surface; cytoplasm; cytosol; extracellular space; membrane; mitochondrial matrix; mitochondrion; nucleolus; nucleus; plasma membrane
Molecular Function: adrenergic receptor binding; complement component C1q binding; hyaluronic acid binding; kininogen binding; mRNA binding; protein binding; protein kinase C binding; transcription corepressor activity; transcription factor binding
Biological Process: apoptosis; blood coagulation; blood coagulation, intrinsic pathway; complement activation, classical pathway; immune response; innate immune response; mature ribosome assembly; mRNA processing; negative regulation of defense response to virus; negative regulation of interferon-gamma production; negative regulation of interleukin-12 production; negative regulation of nuclear mRNA splicing, via spliceosome; negative regulation of transcription from RNA polymerase II promoter; phosphoinositide 3-kinase cascade; positive regulation of apoptosis; positive regulation of cell adhesion; positive regulation of protein kinase B signaling cascade; regulation of complement activation; RNA splicing; transcription, DNA-dependent; viral reproduction
Reference #:  Q07021 (UniProtKB)
Alt. Names/Synonyms: C1q globular domain-binding protein; C1QBP; Complement component 1 Q subcomponent-binding protein, mitochondrial; complement component 1, q subcomponent binding protein; gC1Q-R; GC1q-R protein; GC1QBP; gC1qR; Glycoprotein gC1qBP; HABP1; Hyaluronan-binding protein 1; Mitochondrial matrix protein p32; p32; p33; SF2P32; splicing factor SF2-associated protein
Gene Symbols: C1QBP
Molecular weight: 31,362 Da
Basal Isoelectric point: 4.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

C1QBP

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 K80‑ac SLHTDGDkAFVDFLs
0 1 K80‑ub SLHTDGDkAFVDFLs
0 5 S87‑p kAFVDFLsDEIkEER
0 18 K91‑ac DFLsDEIkEERKIQK
0 1 K91‑ub DFLsDEIkEERKIQK
0 2 K91‑sc DFLsDEIkEERKIQK
0 1 R94 sDEIkEERKIQKHKT
0 1 R94 sDEIkEERKIQKHKT
0 1 K100 ERKIQKHKTLPkMSG
0 2 K104‑ac QKHKTLPkMSGGWEL
0 1 K104‑ub QKHKTLPkMSGGWEL
0 1 S106 HKTLPkMSGGWELEL
0 1 K119 ELNGTEAKLVRKVAG
1 0 S150 FDGEEEPSQGQKVEE
0 1 K174‑ub NFVVEVIkNDDGkkA
0 16 K179‑ac VIkNDDGkkALVLDC
0 6 K180‑ac IkNDDGkkALVLDCH
0 1 Y188‑p ALVLDCHyPEDEVGQ
0 57 S201‑p GQEDEAEsDIFsIRE
0 10 S205‑p EAEsDIFsIREVsFQ
0 1 S210‑p IFsIREVsFQstGES
0 6 S213‑p IREVsFQstGESEWK
0 1 T214‑p REVsFQstGESEWKD
  mouse

 
K77 ALHTEGDKAFVEFLT
K77 ALHTEGDKAFVEFLT
T84 KAFVEFLTDEIkEEk
K88‑ac EFLTDEIkEEkKIQK
K88 EFLTDEIKEEkKIQK
K88‑sc EFLTDEIkEEkKIQK
K91‑ac TDEIkEEkKIQKHkS
K91‑sc TDEIkEEkKIQKHkS
K97‑ac EkKIQKHkSLPkMsG
K101‑ac QKHkSLPkMsGDWEL
K101 QKHkSLPKMsGDWEL
S103‑p HkSLPkMsGDWELEV
K116‑ac EVNGTEAkLLRKVAG
S147‑p FDGEEEPsQGQKAEE
K171 NFVVEVTKTDGkkTL
K175‑ac EVTKTDGkkTLVLDC
K176‑ac VTKTDGkkTLVLDCH
Y184 TLVLDCHYPEDEIGH
S197‑p GHEDEAEsDIFsIKE
S201‑p EAEsDIFsIKEVSFQ
S206 IFsIKEVSFQATGDS
A209 IKEVSFQATGDSEWR
T210 KEVSFQATGDSEWRD
  rat

 
K78 ALHTEGDKAFVEFLT
K78 ALHTEGDKAFVEFLT
T85 KAFVEFLTDEIkEEK
K89‑ac EFLTDEIkEEKKIQK
K89 EFLTDEIKEEKKIQK
K89 EFLTDEIKEEKKIQK
K92 TDEIkEEKKIQKHKS
K92 TDEIkEEKKIQKHKS
K98 EKKIQKHKSLPkMSG
K102‑ac QKHKSLPkMSGDWEL
K102 QKHKSLPKMSGDWEL
S104 HKSLPkMSGDWELEV
K117 EVNGTEAKLLRKVAG
S148 FDGEEEPSQGQKAEE
K172 NFVVEVTKTDGkKTL
K176‑ac EVTKTDGkKTLVLDC
K177 VTKTDGkKTLVLDCH
Y185 TLVLDCHYPEDEIGH
S198 GHEDEAESDIFSIKE
S202 EAESDIFSIKEVSFQ
S207 IFSIKEVSFQTTGDS
T210 IKEVSFQTTGDSEWR
T211 KEVSFQTTGDSEWRD
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