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 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)
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)

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

Cell Name: hepatoblast (CL0005026)
Fold Change: 4.64
Marker Score: 15,198
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 2.3
Marker Score: 12,339
Cell Name: conventional dendritic cell (CL0000990)
Fold Change: 2.2
Marker Score: 1,517
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 2.01
Marker Score: 1,999
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 1.91
Marker Score: 8,244
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 1.83
Marker Score: 11,773
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 1.27
Marker Score: 859
Cell Name: goblet cell (CL0000160)
Fold Change: 1.15
Marker Score: 7,649
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.15
Marker Score: 4,820
Cell Name: enterocyte of colon (CL1000347)
Fold Change: 1.14
Marker Score: 1,754
Cell Name: plasma cell (CL0000786)
Fold Change: 1.08
Marker Score: 1,206
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 1.07
Marker Score: 1,149
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.06
Marker Score: 722
Cell Name: early T lineage precursor (CL0002425)
Fold Change: 1.05
Marker Score: 800
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: 1.01
Marker Score: 419
Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
Fold Change: 1
Marker Score: 71,831
Cell Name: forebrain radial glial cell (CL0013000)
Fold Change: 1
Marker Score: 48,054
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.99
Marker Score: 512
Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
Fold Change: 0.99
Marker Score: 466
Cell Name: absorptive cell (CL0000212)
Fold Change: 0.98
Marker Score: 30,409
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.95
Marker Score: 2,413
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.94
Marker Score: 434
Cell Name: transit amplifying cell (CL0009010)
Fold Change: 0.94
Marker Score: 5,352
Cell Name: B cell (CL0000236)
Fold Change: 0.93
Marker Score: 886
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.92
Marker Score: 2,741
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.91
Marker Score: 329
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.87
Marker Score: 5,296
Cell Name: mast cell (CL0000097)
Fold Change: 0.82
Marker Score: 478
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.82
Marker Score: 329
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 0.81
Marker Score: 307
Cell Name: brush cell (CL0002204)
Fold Change: 0.78
Marker Score: 710
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: 0.78
Marker Score: 1,263
Cell Name: Cajal-Retzius cell (CL0000695)
Fold Change: 0.77
Marker Score: 400
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.77
Marker Score: 12,011
Cell Name: inflammatory macrophage (CL0000863)
Fold Change: 0.77
Marker Score: 238
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 0.7
Marker Score: 180
Cell Name: precursor B cell (CL0000817)
Fold Change: 0.66
Marker Score: 436
Cell Name: Kupffer cell (CL0000091)
Fold Change: 0.62
Marker Score: 623
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.62
Marker Score: 396
Cell Name: intestinal enteroendocrine cell (CL1001516)
Fold Change: 0.59
Marker Score: 471
Cell Name: pericyte (CL0000669)
Fold Change: 0.59
Marker Score: 344
Cell Name: oocyte (CL0000023)
Fold Change: 0.56
Marker Score: 139
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: 0.55
Marker Score: 175
Cell Name: neuroendocrine cell (CL0000165)
Fold Change: 0.53
Marker Score: 206
Cell Name: common myeloid progenitor (CL0000049)
Fold Change: 0.52
Marker Score: 138
Cell Name: pro-B cell (CL0000826)
Fold Change: 0.5
Marker Score: 479
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 0.49
Marker Score: 207
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 0.46
Marker Score: 126
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.46
Marker Score: 867
Cell Name: myeloid cell (CL0000763)
Fold Change: 0.45
Marker Score: 720
Cell Name: kidney proximal convoluted tubule epithelial cell (CL1000838)
Fold Change: 0.42
Marker Score: 863
Cell Name: T cell (CL0000084)
Fold Change: 0.41
Marker Score: 703
Cell Name: cholangiocyte (CL1000488)
Fold Change: 0.39
Marker Score: 146
Cell Name: erythroblast (CL0000765)
Fold Change: 0.38
Marker Score: 238
Cell Name: fraction A pre-pro B cell (CL0002045)
Fold Change: 0.37
Marker Score: 375
Cell Name: epithelial cell of alveolus of lung (CL0010003)
Fold Change: 0.35
Marker Score: 156
Cell Name: smooth muscle myoblast (CL0000514)
Fold Change: 0.34
Marker Score: 160
Cell Name: blood vessel endothelial cell (CL0000071)
Fold Change: 0.33
Marker Score: 336
Cell Name: germ cell (CL0000586)
Fold Change: 0.33
Marker Score: 583
Cell Name: granulocyte monocyte progenitor cell (CL0000557)
Fold Change: 0.31
Marker Score: 197
Cell Name: immature innate lymphoid cell (CL0001082)
Fold Change: 0.29
Marker Score: 595
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.29
Marker Score: 209
Cell Name: cerebral cortex endothelial cell (CL1001602)
Fold Change: 0.25
Marker Score: 148
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 0.24
Marker Score: 52
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.23
Marker Score: 65
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.22
Marker Score: 75
Cell Name: oogonial cell (CL0000024)
Fold Change: 0.22
Marker Score: 313
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: 0.22
Marker Score: 130
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: 0.21
Marker Score: 77
Cell Name: plasmacytoid dendritic cell (CL0000784)
Fold Change: 0.2
Marker Score: 110
Cell Name: neuronal receptor cell (CL0000006)
Fold Change: 0.2
Marker Score: 87
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.17
Marker Score: 43
Cell Name: mature NK T cell (CL0000814)
Fold Change: 0.16
Marker Score: 76
Cell Name: renal alpha-intercalated cell (CL0005011)
Fold Change: 0.16
Marker Score: 82
Cell Name: renal beta-intercalated cell (CL0002201)
Fold Change: 0.15
Marker Score: 46
Cell Name: erythrocyte (CL0000232)
Fold Change: 0.13
Marker Score: 71
Cell Name: neutrophil (CL0000775)
Fold Change: 0.13
Marker Score: 78
Cell Name: endothelial cell (CL0000115)
Fold Change: 0.13
Marker Score: 113
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 0.12
Marker Score: 94
Cell Name: secretory cell (CL0000151)
Fold Change: 0.12
Marker Score: 219
Cell Name: astrocyte (CL0000127)
Fold Change: 0.11
Marker Score: 93
Cell Name: papillary tips cell (CL1000597)
Fold Change: 0.1
Marker Score: 20
Cell Name: innate lymphoid cell (CL0001065)
Fold Change: 0.1
Marker Score: 35
Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
Fold Change: 0.1
Marker Score: 227
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: 0.09
Marker Score: 32
Cell Name: epithelial cell (CL0000066)
Fold Change: 0.09
Marker Score: 143
Cell Name: connective tissue cell (CL0002320)
Fold Change: 0.09
Marker Score: 23
Cell Name: endothelial cell of lymphatic vessel (CL0002138)
Fold Change: 0.09
Marker Score: 55
Cell Name: parietal epithelial cell (CL1000452)
Fold Change: 0.09
Marker Score: 31
Cell Name: megakaryocyte (CL0000556)
Fold Change: 0.08
Marker Score: 47
Cell Name: glandular epithelial cell (CL0000150)
Fold Change: 0.08
Marker Score: 203
Cell Name: large intestine goblet cell (CL1000320)
Fold Change: 0.08
Marker Score: 21
Cell Name: smooth muscle cell (CL0000192)
Fold Change: 0.08
Marker Score: 52
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 0.08
Marker Score: 53
Cell Name: fibroblast (CL0000057)
Fold Change: 0.08
Marker Score: 76
Cell Name: vascular associated smooth muscle cell (CL0000359)
Fold Change: 0.08
Marker Score: 36
Cell Name: type I enteroendocrine cell (CL0002277)
Fold Change: 0.07
Marker Score: 18
Cell Name: amacrine cell (CL0000561)
Fold Change: 0.07
Marker Score: 225
Cell Name: renal principal cell (CL0005009)
Fold Change: 0.07
Marker Score: 54
Cell Name: skin fibroblast (CL0002620)
Fold Change: 0.07
Marker Score: 18

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 Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

**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: 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: 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: 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

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

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

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