F2 | ENSG00000180210 | NCBI 2147

Details for: F2

Gene ID: 2147

Symbol: F2

Ensembl ID: ENSG00000180210

Description: coagulation factor II, thrombin

Associated with

Cell surface interactions at the vascular wall
(R-HSA-202733)
Class a/1 (rhodopsin-like receptors)
(R-HSA-373076)
Common pathway of fibrin clot formation
(R-HSA-140875)
Complement cascade
(R-HSA-166658)
Defective f8 cleavage by thrombin
(R-HSA-9672391)
Defective factor viii causes hemophilia a
(R-HSA-9662001)
Defective factor xii causes hereditary angioedema
(R-HSA-9657688)
Defects of contact activation system (cas) and kallikrein/kinin system (kks)
(R-HSA-9651496)
Disease
(R-HSA-1643685)
Diseases of hemostasis
(R-HSA-9671793)
Formation of fibrin clot (clotting cascade)
(R-HSA-140877)
G alpha (q) signalling events
(R-HSA-416476)
Gamma-carboxylation, transport, and amino-terminal cleavage of proteins
(R-HSA-159854)
Gamma-carboxylation of protein precursors
(R-HSA-159740)
Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation
(R-HSA-163841)
Gpcr downstream signalling
(R-HSA-388396)
Gpcr ligand binding
(R-HSA-500792)
Hemostasis
(R-HSA-109582)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Intrinsic pathway of fibrin clot formation
(R-HSA-140837)
Metabolism of proteins
(R-HSA-392499)
Peptide ligand-binding receptors
(R-HSA-375276)
Platelet activation, signaling and aggregation
(R-HSA-76002)
Platelet aggregation (plug formation)
(R-HSA-76009)
Post-translational protein modification
(R-HSA-597592)
Regulation of complement cascade
(R-HSA-977606)
Regulation of insulin-like growth factor (igf) transport and uptake by insulin-like growth factor binding proteins (igfbps)
(R-HSA-381426)
Removal of aminoterminal propeptides from gamma-carboxylated proteins
(R-HSA-159782)
Signaling by gpcr
(R-HSA-372790)
Signal transduction
(R-HSA-162582)
Thrombin signalling through proteinase activated receptors (pars)
(R-HSA-456926)
Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the golgi apparatus
(R-HSA-159763)
Acute-phase response
(GO:0006953)
Antimicrobial humoral immune response mediated by antimicrobial peptide
(GO:0061844)
Blood coagulation
(GO:0007596)
Blood microparticle
(GO:0072562)
Calcium ion binding
(GO:0005509)
Cell surface receptor signaling pathway
(GO:0007166)
Collagen-containing extracellular matrix
(GO:0062023)
Cytolysis by host of symbiont cells
(GO:0051838)
Endoplasmic reticulum lumen
(GO:0005788)
External side of plasma membrane
(GO:0009897)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Fibrinolysis
(GO:0042730)
Golgi lumen
(GO:0005796)
G protein-coupled receptor signaling pathway
(GO:0007186)
Growth factor activity
(GO:0008083)
Heparin binding
(GO:0008201)
Ligand-gated ion channel signaling pathway
(GO:1990806)
Lipopolysaccharide binding
(GO:0001530)
Negative regulation of astrocyte differentiation
(GO:0048712)
Negative regulation of blood coagulation
(GO:0030195)
Negative regulation of cytokine production involved in inflammatory response
(GO:1900016)
Negative regulation of fibrinolysis
(GO:0051918)
Negative regulation of platelet activation
(GO:0010544)
Negative regulation of proteolysis
(GO:0045861)
Neutrophil-mediated killing of gram-negative bacterium
(GO:0070945)
Plasma membrane
(GO:0005886)
Platelet activation
(GO:0030168)
Positive regulation of blood coagulation
(GO:0030194)
Positive regulation of cell growth
(GO:0030307)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of collagen biosynthetic process
(GO:0032967)
Positive regulation of insulin secretion
(GO:0032024)
Positive regulation of lipid kinase activity
(GO:0090218)
Positive regulation of phosphatidylinositol 3-kinase/protein kinase b signal transduction
(GO:0051897)
Positive regulation of phospholipase c-activating g protein-coupled receptor signaling pathway
(GO:1900738)
Positive regulation of protein localization to nucleus
(GO:1900182)
Positive regulation of protein phosphorylation
(GO:0001934)
Positive regulation of reactive oxygen species metabolic process
(GO:2000379)
Positive regulation of receptor signaling pathway via jak-stat
(GO:0046427)
Positive regulation of release of sequestered calcium ion into cytosol
(GO:0051281)
Protein binding
(GO:0005515)
Proteolysis
(GO:0006508)
Receptor ligand activity
(GO:0048018)
Regulation of blood coagulation
(GO:0030193)
Regulation of cell shape
(GO:0008360)
Regulation of cytosolic calcium ion concentration
(GO:0051480)
Response to wounding
(GO:0009611)
Serine-type endopeptidase activity
(GO:0004252)
Signaling receptor binding
(GO:0005102)
Thrombospondin receptor activity
(GO:0070053)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 8.6791
Cell Significance Index: -1.3500
Cell Name: paneth cell (CL0000510)
Fold Change: 4.6636
Cell Significance Index: 48.2500
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 4.1965
Cell Significance Index: 70.6900
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 3.7829
Cell Significance Index: 440.8500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 3.0137
Cell Significance Index: 598.0800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 2.4226
Cell Significance Index: 52.4900
Cell Name: intrahepatic cholangiocyte (CL0002538)
Fold Change: 2.0299
Cell Significance Index: 7.6500
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 1.8114
Cell Significance Index: 58.0200
Cell Name: CD14-low, CD16-positive monocyte (CL0002396)
Fold Change: 1.3091
Cell Significance Index: 31.7100
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.1868
Cell Significance Index: 53.8000
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 1.1383
Cell Significance Index: 6.5600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.9313
Cell Significance Index: 177.2400
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 0.7923
Cell Significance Index: 11.7000
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.5795
Cell Significance Index: 57.3300
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 0.5651
Cell Significance Index: 12.0400
Cell Name: obsolete epithelial cell of alveolus of lung (CL0010003)
Fold Change: 0.5626
Cell Significance Index: 14.0300
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.4986
Cell Significance Index: 450.2300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.3791
Cell Significance Index: 41.2400
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.3493
Cell Significance Index: 20.9700
Cell Name: hepatic pit cell (CL2000054)
Fold Change: 0.3266
Cell Significance Index: 0.8800
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.3134
Cell Significance Index: 50.9700
Cell Name: medial ganglionic eminence derived interneuron (CL4023063)
Fold Change: 0.3062
Cell Significance Index: 4.3900
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.2016
Cell Significance Index: 13.9500
Cell Name: cholangiocyte (CL1000488)
Fold Change: 0.1510
Cell Significance Index: 1.4900
Cell Name: liver dendritic cell (CL2000055)
Fold Change: 0.1478
Cell Significance Index: 0.3900
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 0.1444
Cell Significance Index: 1.1400
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 0.1293
Cell Significance Index: 0.4500
Cell Name: inflammatory macrophage (CL0000863)
Fold Change: 0.1259
Cell Significance Index: 0.9700
Cell Name: primordial germ cell (CL0000670)
Fold Change: 0.1150
Cell Significance Index: 0.7100
Cell Name: hepatoblast (CL0005026)
Fold Change: 0.1147
Cell Significance Index: 1.9300
Cell Name: glandular epithelial cell (CL0000150)
Fold Change: 0.1056
Cell Significance Index: 0.8400
Cell Name: myeloid lineage restricted progenitor cell (CL0000839)
Fold Change: 0.0976
Cell Significance Index: 1.3700
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.0694
Cell Significance Index: 1.1900
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.0388
Cell Significance Index: 1.0400
Cell Name: Kupffer cell (CL0000091)
Fold Change: 0.0311
Cell Significance Index: 0.2900
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: 0.0309
Cell Significance Index: 0.6400
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0222
Cell Significance Index: 0.7800
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.0156
Cell Significance Index: 0.3900
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.0123
Cell Significance Index: 2.4700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.0094
Cell Significance Index: 1.6900
Cell Name: hepatocyte (CL0000182)
Fold Change: 0.0058
Cell Significance Index: 0.0800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.0045
Cell Significance Index: 0.1300
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.0040
Cell Significance Index: 1.4500
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.0037
Cell Significance Index: 0.3800
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.0005
Cell Significance Index: 0.2800
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0002
Cell Significance Index: 0.3800
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0002
Cell Significance Index: 0.3400
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0000
Cell Significance Index: -0.0200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0001
Cell Significance Index: -0.1600
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -0.0010
Cell Significance Index: -0.0100
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.0012
Cell Significance Index: -0.0300
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0013
Cell Significance Index: -0.9700
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0017
Cell Significance Index: -1.0800
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0018
Cell Significance Index: -1.0300
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0019
Cell Significance Index: -0.3200
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0028
Cell Significance Index: -1.8100
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0030
Cell Significance Index: -1.3600
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0040
Cell Significance Index: -1.1600
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.0041
Cell Significance Index: -0.2500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0058
Cell Significance Index: -1.2300
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0076
Cell Significance Index: -1.1100
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: -0.0084
Cell Significance Index: -1.1600
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.0103
Cell Significance Index: -0.6500
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: -0.0109
Cell Significance Index: -1.3400
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.0125
Cell Significance Index: -1.3000
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.0127
Cell Significance Index: -1.4600
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.0138
Cell Significance Index: -1.0600
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.0140
Cell Significance Index: -0.9400
Cell Name: proerythroblast (CL0000547)
Fold Change: -0.0154
Cell Significance Index: -0.2200
Cell Name: early lymphoid progenitor (CL0000936)
Fold Change: -0.0158
Cell Significance Index: -0.1600
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.0172
Cell Significance Index: -1.0600
Cell Name: germ cell (CL0000586)
Fold Change: -0.0172
Cell Significance Index: -0.1300
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.0174
Cell Significance Index: -0.4900
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: -0.0184
Cell Significance Index: -0.1900
Cell Name: lens fiber cell (CL0011004)
Fold Change: -0.0212
Cell Significance Index: -0.6700
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.0215
Cell Significance Index: -0.9500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.0219
Cell Significance Index: -0.8300
Cell Name: erythroid progenitor cell (CL0000038)
Fold Change: -0.0226
Cell Significance Index: -0.3000
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.0244
Cell Significance Index: -1.2700
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.0251
Cell Significance Index: -1.4100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0256
Cell Significance Index: -1.3300
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -0.0264
Cell Significance Index: -0.8400
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.0268
Cell Significance Index: -0.6900
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -0.0273
Cell Significance Index: -0.4700
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.0278
Cell Significance Index: -1.4600
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.0291
Cell Significance Index: -1.0700
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0295
Cell Significance Index: -1.3900
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.0297
Cell Significance Index: -1.2200
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0305
Cell Significance Index: -1.4200
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -0.0308
Cell Significance Index: -1.0100
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.0323
Cell Significance Index: -1.6300
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.0331
Cell Significance Index: -1.1600
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: -0.0371
Cell Significance Index: -0.4700
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -0.0372
Cell Significance Index: -0.7900
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: -0.0373
Cell Significance Index: -0.3600
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.0374
Cell Significance Index: -0.8200
Cell Name: keratinocyte (CL0000312)
Fold Change: -0.0384
Cell Significance Index: -0.9600
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: -0.0384
Cell Significance Index: -0.4300
Cell Name: cytotoxic T cell (CL0000910)
Fold Change: -0.0391
Cell Significance Index: -0.5700
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.0404
Cell Significance Index: -1.0800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** 1. **Function**: Thrombin is a serine protease that converts fibrinogen into fibrin, forming a blood clot. 2. **Expression**: The F2 gene is highly expressed in the liver, where it is converted into prothrombin, and in various other tissues, including the skin, lungs, and kidneys. 3. **Regulation**: The gene's expression is tightly regulated by various pathways, including the complement cascade, blood coagulation, and cell surface interactions at the vascular wall. 4. **Protein structure**: Thrombin is a serine protease with a molecular weight of 55 kDa and a molecular structure that includes a catalytic domain, a pro-domain, and a disintegrin domain. **Pathways and Functions** 1. **Blood coagulation**: Thrombin plays a central role in the blood coagulation cascade, converting fibrinogen into fibrin, which forms the blood clot. 2. **Cell surface interactions**: Thrombin interacts with various cell surface receptors, including the thromboxane A2 receptor, which regulates platelet activation and aggregation. 3. **Complement cascade**: Thrombin can activate the complement cascade, a group of proteins that work together to eliminate pathogens. 4. **Fibrinolysis**: Thrombin can also regulate fibrinolysis, the process of breaking down blood clots. 5. **Cell signaling**: Thrombin can regulate various cell signaling pathways, including the G protein-coupled receptor signaling pathway and the phospholipase C-activating G protein-coupled receptor signaling pathway. **Clinical Significance** 1. **Hemophilia A**: Mutations in the F2 gene can lead to hemophilia A, a bleeding disorder characterized by defective factor VIII cleavage by thrombin. 2. **Hereditary angioedema**: Mutations in the F2 gene can also lead to hereditary angioedema, a disorder characterized by defective factor XII cleavage by thrombin. 3. **Thrombosis**: Thrombin can also play a role in thrombosis, the formation of blood clots in blood vessels, which can lead to cardiovascular disease. 4. **Inflammation**: Thrombin can regulate inflammation, the body's response to injury or infection, by activating various inflammatory pathways. 5. **Cancer**: Thrombin can also play a role in cancer, by regulating cell growth and proliferation, and by promoting angiogenesis, the formation of new blood vessels. In conclusion, the F2 gene encodes for thrombin, a crucial enzyme in the blood coagulation cascade. Thrombin plays a central role in regulating blood coagulation, cell surface interactions, and cell signaling pathways. Mutations in the F2 gene can lead to various clinical disorders, including hemophilia A, hereditary angioedema, and thrombosis. Understanding the regulation of thrombin and its role in various physiological and pathological processes is essential for the development of novel therapeutic strategies for cardiovascular disease and other disorders.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Prothrombin

Genular Protein ID: 1209709366

Symbol: THRB_HUMAN

Name: Prothrombin

UniProtKB Accession Codes:

P00734 B2R7F7 B4E1A7 Q4QZ40 Q53H04 Q53H06 Q69EZ7 Q7Z7P3 Q9UCA1

Database IDs:

Citations:

PubMed ID: 2825773

Title: Nucleotide sequence of the gene for human prothrombin.

PubMed ID: 2825773

DOI: 10.1021/bi00393a033

PubMed ID: 14962227

Title: Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly.

PubMed ID: 14962227

DOI: 10.1046/j.1365-2516.2003.00838.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 6305407

Title: Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin.

PubMed ID: 6305407

DOI: 10.1021/bi00278a008

PubMed ID: 8073540

Title: Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin.

PubMed ID: 8073540

DOI: 10.1007/bf00431548

PubMed ID: 266717

Title: Amino acid sequence of human prothrombin fragments 1 and 2.

PubMed ID: 266717

DOI: 10.1073/pnas.74.5.1969

PubMed ID: 873923

Title: Primary structure of human prethrombin 2 and alpha-thrombin.

PubMed ID: 873923

DOI: 10.1016/s0021-9258(17)40144-x

PubMed ID: 6323392

Title: Mechanism of inhibition of activated protein C by protein C inhibitor.

PubMed ID: 6323392

DOI: 10.1093/oxfordjournals.jbchem.a134583

PubMed ID: 3759958

Title: Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma.

PubMed ID: 3759958

DOI: 10.1016/s0021-9258(18)69292-0

PubMed ID: 2856554

Title: Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis.

PubMed ID: 2856554

PubMed ID: 9183005

Title: Prothrombin, albumin and immunoglobulin A form covalent complexes with alpha1-microglobulin in human plasma.

PubMed ID: 9183005

DOI: 10.1111/j.1432-1033.1997.00676.x

PubMed ID: 9780208

Title: Factor Xa induces cytokine production and expression of adhesion molecules by human umbilical vein endothelial cells.

PubMed ID: 9780208

PubMed ID: 11506076

Title: Thrombophilic gene mutations and recurrent spontaneous abortion: prothrombin mutation increases the risk in the first trimester.

PubMed ID: 11506076

DOI: 10.1111/j.8755-8920.2001.460202.x

PubMed ID: 15534175

Title: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls.

PubMed ID: 15534175

DOI: 10.1001/archneur.61.11.1652

PubMed ID: 14760718

Title: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 15885491

Title: rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells.

PubMed ID: 15885491

DOI: 10.1016/j.orthres.2004.12.005

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 17244316

Title: Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study.

PubMed ID: 17244316

DOI: 10.1111/j.1524-475x.2006.00181.x

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19139490

Title: A strategy for precise and large scale identification of core fucosylated glycoproteins.

PubMed ID: 19139490

DOI: 10.1074/mcp.m800504-mcp200

PubMed ID: 19838169

Title: Enrichment of glycopeptides for glycan structure and attachment site identification.

PubMed ID: 19838169

DOI: 10.1038/nmeth.1392

PubMed ID: 22171320

Title: Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD.

PubMed ID: 22171320

DOI: 10.1074/mcp.m111.013649

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 30568593

Title: TAK-442, a Direct Factor Xa Inhibitor, Inhibits Monocyte Chemoattractant Protein 1 Production in Endothelial Cells via Involvement of Protease-Activated Receptor 1.

PubMed ID: 30568593

DOI: 10.3389/fphar.2018.01431

PubMed ID: 33732248

Title: Iripin-3, a New Salivary Protein Isolated From Ixodes ricinus Ticks, Displays Immunomodulatory and Anti-Hemostatic Properties In Vitro.

PubMed ID: 33732248

DOI: 10.3389/fimmu.2021.626200

PubMed ID: 34502392

Title: Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement.

PubMed ID: 34502392

DOI: 10.3390/ijms22179480

PubMed ID: 34265300

Title: Role of sequence and position of the cleavage sites in prothrombin activation.

PubMed ID: 34265300

DOI: 10.1016/j.jbc.2021.100955

PubMed ID: 2583108

Title: The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.

PubMed ID: 2583108

DOI: 10.1002/j.1460-2075.1989.tb08511.x

PubMed ID: 2369893

Title: Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.

PubMed ID: 2369893

DOI: 10.1002/j.1460-2075.1990.tb07410.x

PubMed ID: 2374926

Title: The structure of a complex of recombinant hirudin and human alpha-thrombin.

PubMed ID: 2374926

DOI: 10.1126/science.2374926

PubMed ID: 8251938

Title: Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms.

PubMed ID: 8251938

DOI: 10.1002/pro.5560021009

PubMed ID: 8071320

Title: Crystallographic structure of human gamma-thrombin.

PubMed ID: 8071320

DOI: 10.1016/s0021-9258(17)31746-5

PubMed ID: 9214615

Title: The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.

PubMed ID: 9214615

DOI: 10.1093/emboj/16.11.2977

PubMed ID: 10051558

Title: Unexpected crucial role of residue 225 in serine proteases.

PubMed ID: 10051558

DOI: 10.1073/pnas.96.5.1852

PubMed ID: 11493008

Title: Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate.

PubMed ID: 11493008

DOI: 10.1006/jmbi.2001.4872

PubMed ID: 16763681

Title: Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors.

PubMed ID: 16763681

DOI: 10.1039/b602585d

PubMed ID: 17685615

Title: Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin.

PubMed ID: 17685615

DOI: 10.1021/ja0735002

PubMed ID: 18291642

Title: Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.

PubMed ID: 18291642

DOI: 10.1016/j.bmcl.2008.01.098

PubMed ID: 18362344

Title: Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex.

PubMed ID: 18362344

DOI: 10.1073/pnas.0711055105

PubMed ID: 23223529

Title: Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector.

PubMed ID: 23223529

DOI: 10.1073/pnas.1211614109

PubMed ID: 28592490

Title: Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from Anopheles gambiae.

PubMed ID: 28592490

DOI: 10.1074/jbc.m117.788042

PubMed ID: 6405779

Title: Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site.

PubMed ID: 6405779

DOI: 10.1111/j.1365-2141.1983.tb02092.x

PubMed ID: 3771562

Title: Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273.

PubMed ID: 3771562

DOI: 10.1016/s0021-9258(18)66826-7

PubMed ID: 3567158

Title: Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima.

PubMed ID: 3567158

DOI: 10.1021/bi00378a020

PubMed ID: 3801671

Title: Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin.

PubMed ID: 3801671

PubMed ID: 3242619

Title: Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382.

PubMed ID: 3242619

DOI: 10.1021/bi00426a013

PubMed ID: 2719946

Title: Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity.

PubMed ID: 2719946

DOI: 10.1021/bi00431a017

PubMed ID: 1354985

Title: Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity.

PubMed ID: 1354985

DOI: 10.1021/bi00148a005

PubMed ID: 1421398

Title: Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His).

PubMed ID: 1421398

PubMed ID: 1349838

Title: Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia.

PubMed ID: 1349838

PubMed ID: 7865694

Title: Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site.

PubMed ID: 7865694

DOI: 10.1097/00001721-199410000-00025

PubMed ID: 7792730

Title: Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala.

PubMed ID: 7792730

PubMed ID: 10391209

Title: Characterization of single-nucleotide polymorphisms in coding regions of human genes.

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 22028381

Title: Quantitative detection of single amino acid polymorphisms by targeted proteomics.

PubMed ID: 22028381

DOI: 10.1093/jmcb/mjr024

Sequence Information:

Length: 622
Mass: 70037
Checksum: 8A25E1DA88208FCF
Sequence:

MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC 
VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV 
NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE 
CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA 
QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG 
DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI 
DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN 
DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP 
VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST 
RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY 
GFYTHVFRLK KWIQKVIDQF GE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: F2

Associated with

Cells (max top 100)

Other Information

Nucleotide sequence of the gene for human prothrombin. PubMed ID: 2825773

Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly. PubMed ID: 14962227

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. PubMed ID: 6305407

Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin. PubMed ID: 8073540

Amino acid sequence of human prothrombin fragments 1 and 2. PubMed ID: 266717

Primary structure of human prethrombin 2 and alpha-thrombin. PubMed ID: 873923

Mechanism of inhibition of activated protein C by protein C inhibitor. PubMed ID: 6323392

Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma. PubMed ID: 3759958

Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis. PubMed ID: 2856554

Prothrombin, albumin and immunoglobulin A form covalent complexes with alpha1-microglobulin in human plasma. PubMed ID: 9183005

Factor Xa induces cytokine production and expression of adhesion molecules by human umbilical vein endothelial cells. PubMed ID: 9780208

Thrombophilic gene mutations and recurrent spontaneous abortion: prothrombin mutation increases the risk in the first trimester. PubMed ID: 11506076

Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. PubMed ID: 15534175

Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. PubMed ID: 14760718

rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells. PubMed ID: 15885491

Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. PubMed ID: 16335952

Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study. PubMed ID: 17244316

Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. PubMed ID: 19159218

A strategy for precise and large scale identification of core fucosylated glycoproteins. PubMed ID: 19139490

Enrichment of glycopeptides for glycan structure and attachment site identification. PubMed ID: 19838169

Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. PubMed ID: 22171320

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

TAK-442, a Direct Factor Xa Inhibitor, Inhibits Monocyte Chemoattractant Protein 1 Production in Endothelial Cells via Involvement of Protease-Activated Receptor 1. PubMed ID: 30568593

Iripin-3, a New Salivary Protein Isolated From Ixodes ricinus Ticks, Displays Immunomodulatory and Anti-Hemostatic Properties In Vitro. PubMed ID: 33732248

Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement. PubMed ID: 34502392

Role of sequence and position of the cleavage sites in prothrombin activation. PubMed ID: 34265300

The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. PubMed ID: 2583108

Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition. PubMed ID: 2369893

The structure of a complex of recombinant hirudin and human alpha-thrombin. PubMed ID: 2374926

Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms. PubMed ID: 8251938

Crystallographic structure of human gamma-thrombin. PubMed ID: 8071320

The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. PubMed ID: 9214615

Unexpected crucial role of residue 225 in serine proteases. PubMed ID: 10051558

Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate. PubMed ID: 11493008

Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors. PubMed ID: 16763681

Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin. PubMed ID: 17685615

Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles. PubMed ID: 18291642

Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex. PubMed ID: 18362344

Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. PubMed ID: 23223529

Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from Anopheles gambiae. PubMed ID: 28592490

Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site. PubMed ID: 6405779

Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273. PubMed ID: 3771562

Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima. PubMed ID: 3567158

Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin. PubMed ID: 3801671

Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382. PubMed ID: 3242619

Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity. PubMed ID: 2719946

Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. PubMed ID: 1354985

Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337--&gt;Thr and Arg-388--&gt;His). PubMed ID: 1421398

Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia. PubMed ID: 1349838

Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site. PubMed ID: 7865694

Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala. PubMed ID: 7792730

Characterization of single-nucleotide polymorphisms in coding regions of human genes. PubMed ID: 10391209

Quantitative detection of single amino acid polymorphisms by targeted proteomics. PubMed ID: 22028381