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FLASH GENE
Symbol CPB2 contributors: mct - updated : 25-01-2016
HGNC name carboxypeptidase B2 (plasma)
HGNC id 2300
Location 13q14.13      Physical location : 46.627.322 - 46.679.211
Synonym name
  • thrombin-activable fibrinolysis inhibitor
  • carboxypeptidase B2 (plasma, carboxypeptidase U)
  • bA139H14.2 (carboxypeptidase B2 (plasma))
  • Synonym symbol(s) CPU, PCPB, TAFI
    EC.number 3.4.17.20
    DNA
    TYPE functioning gene
    STRUCTURE 51.89 kb     11 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    text structure
  • multiple initiation sites
  • no TATA
  • MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    text
  • alternatively spliced CPB2 is stored inside the cells, cannot be activated by thrombin-thrombomodulin, and does not have CPB2 activity (PMID: 23595589)
  • identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    11 - 1766 - 423 - 2013 23595589
  • variant 1 - TAFIa
  • 10 - 1655 - 385 - 2013 23595589
    10 - - - - in liver 2013 23595589
    9 - - - - in human hippocampus 2013 23595589
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    blood / hematopoieticspleen   moderately
    Digestiveliver   highly Homo sapiens
    Nervousbrain     Homo sapiens
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Lymphoid    
    Muscularstriatumskeletal  
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Blood/Hematopoieticplatelet Homo sapiens
    cell lineage
    cell lines
    fluid/secretion plasma
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES basic
    STRUCTURE
    motifs/domains
  • 22 AA signal sequence, an activation domain
  • a catalytic moiety with a zinc binding domain
  • a carboxypeptide activation peptide
  • a catalytic domain
  • secondary structure two unique flexible loops on the molecular surface, accounting for structural instability (Sanglas 2008)
    conjugated PhosphoP , MetalloP
    mono polymer monomer
    isoforms Precursor
    HOMOLOGY
    interspecies homolog to murine Cpb2
    Homologene
    FAMILY
  • zinc carboxypeptidase family
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm
    basic FUNCTION
  • cleaving C terminal basic residues
  • playing a role in the protection of the clot against fibrinolysis
  • exerts an antifibrinolytic effect by removing C-terminal lysines from partially degraded fibrin (Buelens 2008)
  • metallocarboxypeptidase (MCP) that links blood coagulation and fibrinolysis (Sanglas 2008)
  • circulating CPB2 and platelets may potentially contribute to regulating the bioactivity of leukocyte chemoattractant chemerin (RARRES2), and further extend the molecular link between blood coagulation/fibrinolysis and CMKLR1-mediated immune responses (Du 2009)
  • may contribute to hypercoagulability during pregnancy
  • is a link between coagulation and the fibrinolytic system
  • pro-carboxypeptidase, encoded by the CPB2 gene that links the coagulation cascade to fibrinolysis and inflammation
  • zymogen form of a basic carboxypeptidase (TAFIa) with both anti-fibrinolytic and anti-inflammatory properties
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS coagulation/hemostasis
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule metal binding,
  • Zn2+
  • protein
  • regulator of plasminogen activation
  • THBD is a cofactor for thrombin-mediated activation of protein C and CPB2 and thereby helps coordinate coagulation, anticoagulation, fibrinolysis, and inflammation
  • in contrast to stimulation of protein C activation, PF4 is shown here to inhibit activation of CPB2 by thrombin-THBD
  • hydrolysis of the C-terminal lysines on fibrin by CPB2 results in a down-regulation of fibrinolysis
  • thyroid hormone excess resulted in a hypofibrinolytic condition and in an enhanced CPB2-dependent prolongation of clot lysis
  • cell & other
    REGULATION
    activated by trypsin,thrombin and plasmin
    inhibited by specific carboxypeptidase B1 inhibitor
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    associated with an increased risk of a first myocardial infarction in men (Meltzer 2009)
    constitutional     --over  
    in women with polycystic ovary syndrome compared with age- and BMI-matched controls (Oral 2009)
    constitutional     --over  
    in patients with acute myocardial infarction
    constitutional     --low  
    may contribute to the development of trauma-induced coagulopathy
    constitutional     --over  
    high CPB2 levels are associated with reduced risk of early recurrent fetal loss
    constitutional     --over  
    in preeclampsia
    constitutional       loss of function
    with insufficient activation of fibrinolysis by both plasmin and neutrophil elastase promote organ dysfunction in disseminated intravascular coagulation associated with sepsis
    Susceptibility
  • to diastolic blood pressure abnormalities
  • to venous thrombosis diseases
  • Variant & Polymorphism SNP
  • GG genotype of 505G/A may increase the risk of venous thrombosis diseases
  • Candidate gene for atherothrombotic disease
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • Tafi deficiency results in accelerated fibrogenesis and increased liver damage in murine models of chronic and acute liver disease, which may be related to increased inflammation