KNG1

Gene Information
 
Gene Symbol
KNG1
 
Aliases
BDK, BK, HMWK, KNG
 
Entrez Gene ID
 
Gene Name
Kininogen 1
 
Chromosomal Location
3q27.3
 
HGNC ID
 
Summary
This gene uses alternative splicing to generate two different proteins- high molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK). HMWK is essential for blood coagulation and assembly of the kallikrein-kinin system. Also, bradykinin, a peptide causing numerous physiological effects, is released from HMWK. Bradykinin also functions as an antimicrobial peptide with antibacterial and antifungal activity. In contrast to HMWK, LMWK is not involved in blood coagulation. Three transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Nov 2014]
 
RefSeq DNA
 
RefSeq mRNA
  e!Ensembl
Gene
Transcript  
Protein

Gene Ontology (GO)

GO ID Ontology Function Evidence Reference
GO:0007162 Biological process Negative regulation of cell adhesion IDA 11970955
GO:0007204 Biological process Positive regulation of cytosolic calcium ion concentration IBA 21873635
GO:0007204 Biological process Positive regulation of cytosolic calcium ion concentration IDA 16014619
GO:0010951 Biological process Negative regulation of endopeptidase activity IBA 21873635
GO:0030195 Biological process Negative regulation of blood coagulation IBA 21873635
Protein Information
 
Protein Name
Kininogen-1, alpha-2-thiol proteinase inhibitor, bradykinin, fitzgerald factor, high molecular weight kininogen, williams-Fitzgerald-Flaujeac factor
 
Function
(1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting
 
Refseq Proteins
 
UniProt
 
PDB
 
Pfam
Pfam Accession Pfam ID
PF00031 Cystatin
Pathways
 
KEGG
 
Reactome
 

cGMP-PKG signaling pathway
Sphingolipid signaling pathway
Neuroactive ligand-receptor interaction
Complement and coagulation cascades
Inflammatory mediator regulation of TRP channels
Regulation of actin cytoskeleton
Chagas disease (American trypanosomiasis)
African trypanosomiasis
Pathways in cancer

 

Platelet degranulation
Intrinsic Pathway of Fibrin Clot Formation
Peptide ligand-binding receptors
Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
G alpha (q) signalling events
G alpha (i) signalling events
Post-translational protein phosphorylation

Interactions
 
STRING MINT IntAct
ENSP00000346484 P20794
    View interactions
     

Associated Diseases

Disease groupDisease NameReferences
Blood Disorders
Kininogen Deficiency
Cardiovascular Diseases
Hypertensive disease
Hyperemia
Angioedema
Digestive System Diseases
Liver Diseases
References
 

Overlap of proteomics biomarkers between women with pre-eclampsia and PCOS: a systematic review and biomarker database integration.

Khan Gulafshana Hafeez, Galazis Nicolas, Docheva Nikolina, Layfield Robert, Atiomo William
Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK gulafshanahafeez@hotmail.com.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| School of Life Sciences, University of Nottingham, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.
Hum Reprod. 2015 Jan;30(1):133-48. doi: 10.1093/humrep/deu268. Epub 2014 Oct 28.

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