Details for: SERPINC1

Gene ID: 462

Symbol: SERPINC1

Ensembl ID: ENSG00000117601

Description: serpin family C member 1

Associated with

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: hepatoblast (CL0005026)
    Fold Change: 19.6601
    Cell Significance Index: 330.6700
  • Cell Name: liver dendritic cell (CL2000055)
    Fold Change: 18.5883
    Cell Significance Index: 49.0400
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 1.9605
    Cell Significance Index: 33.0300
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: 1.3892
    Cell Significance Index: 20.5100
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.1597
    Cell Significance Index: 230.1500
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 0.9047
    Cell Significance Index: 5.2100
  • Cell Name: CD14-low, CD16-positive monocyte (CL0002396)
    Fold Change: 0.6205
    Cell Significance Index: 15.0300
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 0.5366
    Cell Significance Index: 11.6300
  • Cell Name: hepatic pit cell (CL2000054)
    Fold Change: 0.3938
    Cell Significance Index: 1.0600
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 0.3811
    Cell Significance Index: 3.7600
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.2737
    Cell Significance Index: 44.5200
  • Cell Name: intrahepatic cholangiocyte (CL0002538)
    Fold Change: 0.2655
    Cell Significance Index: 1.0000
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.2245
    Cell Significance Index: 13.4800
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 0.2065
    Cell Significance Index: 1.6300
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: 0.2035
    Cell Significance Index: 4.3400
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.1530
    Cell Significance Index: 15.1400
  • Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
    Fold Change: 0.0798
    Cell Significance Index: 0.2800
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.0614
    Cell Significance Index: 11.6900
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.0441
    Cell Significance Index: 4.8000
  • Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
    Fold Change: 0.0300
    Cell Significance Index: 0.2900
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: 0.0185
    Cell Significance Index: 0.4000
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 0.0157
    Cell Significance Index: 1.0900
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: 0.0089
    Cell Significance Index: 0.2300
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: 0.0058
    Cell Significance Index: 0.1200
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.0055
    Cell Significance Index: 3.8300
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.0021
    Cell Significance Index: 0.0600
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0024
    Cell Significance Index: -4.5200
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: -0.0043
    Cell Significance Index: -0.7800
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0046
    Cell Significance Index: -8.5000
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0059
    Cell Significance Index: -9.0800
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.0068
    Cell Significance Index: -1.9600
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -0.0068
    Cell Significance Index: -0.3400
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0069
    Cell Significance Index: -9.3600
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0070
    Cell Significance Index: -4.4200
  • Cell Name: eukaryotic cell (CL0000255)
    Fold Change: -0.0074
    Cell Significance Index: -0.3200
  • Cell Name: obsolete epithelial cell of alveolus of lung (CL0010003)
    Fold Change: -0.0081
    Cell Significance Index: -0.2000
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: -0.0082
    Cell Significance Index: -4.4800
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0091
    Cell Significance Index: -6.7200
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0105
    Cell Significance Index: -5.9000
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: -0.0106
    Cell Significance Index: -3.8000
  • Cell Name: neuron associated cell (CL0000095)
    Fold Change: -0.0107
    Cell Significance Index: -0.4400
  • Cell Name: hepatocyte (CL0000182)
    Fold Change: -0.0115
    Cell Significance Index: -0.1600
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0121
    Cell Significance Index: -5.5000
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.0150
    Cell Significance Index: -0.7800
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: -0.0166
    Cell Significance Index: -3.3200
  • Cell Name: BEST4+ enteroycte (CL4030026)
    Fold Change: -0.0173
    Cell Significance Index: -0.2600
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.0182
    Cell Significance Index: -0.5100
  • Cell Name: helper T cell (CL0000912)
    Fold Change: -0.0183
    Cell Significance Index: -0.2600
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.0222
    Cell Significance Index: -0.5600
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: -0.0224
    Cell Significance Index: -0.6100
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -0.0250
    Cell Significance Index: -0.8000
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: -0.0258
    Cell Significance Index: -0.5400
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0260
    Cell Significance Index: -3.7800
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: -0.0298
    Cell Significance Index: -3.6600
  • Cell Name: decidual cell (CL2000002)
    Fold Change: -0.0318
    Cell Significance Index: -0.5100
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.0323
    Cell Significance Index: -5.5200
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: -0.0323
    Cell Significance Index: -0.6300
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: -0.0341
    Cell Significance Index: -0.9200
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: -0.0345
    Cell Significance Index: -4.7400
  • Cell Name: natural T-regulatory cell (CL0000903)
    Fold Change: -0.0368
    Cell Significance Index: -0.3600
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -0.0373
    Cell Significance Index: -1.6900
  • Cell Name: neural progenitor cell (CL0011020)
    Fold Change: -0.0384
    Cell Significance Index: -0.3800
  • Cell Name: alpha-beta T cell (CL0000789)
    Fold Change: -0.0387
    Cell Significance Index: -0.3300
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.0408
    Cell Significance Index: -8.6000
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.0417
    Cell Significance Index: -4.8600
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.0419
    Cell Significance Index: -4.8000
  • Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
    Fold Change: -0.0462
    Cell Significance Index: -0.5100
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0463
    Cell Significance Index: -4.7300
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: -0.0467
    Cell Significance Index: -0.4700
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: -0.0468
    Cell Significance Index: -2.1800
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: -0.0476
    Cell Significance Index: -0.5200
  • Cell Name: skeletal muscle myoblast (CL0000515)
    Fold Change: -0.0478
    Cell Significance Index: -0.5200
  • Cell Name: retinal astrocyte (CL4033015)
    Fold Change: -0.0521
    Cell Significance Index: -0.5100
  • Cell Name: decidual natural killer cell, human (CL0002343)
    Fold Change: -0.0532
    Cell Significance Index: -0.5500
  • Cell Name: uterine smooth muscle cell (CL0002601)
    Fold Change: -0.0538
    Cell Significance Index: -0.5200
  • Cell Name: early lymphoid progenitor (CL0000936)
    Fold Change: -0.0542
    Cell Significance Index: -0.5500
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: -0.0542
    Cell Significance Index: -0.4700
  • Cell Name: CD8-positive, alpha-beta thymocyte (CL0000811)
    Fold Change: -0.0562
    Cell Significance Index: -0.5200
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.0574
    Cell Significance Index: -4.5500
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.0578
    Cell Significance Index: -3.6400
  • Cell Name: L5/6 near-projecting glutamatergic neuron (CL4030067)
    Fold Change: -0.0590
    Cell Significance Index: -0.3100
  • Cell Name: prostate gland microvascular endothelial cell (CL2000059)
    Fold Change: -0.0599
    Cell Significance Index: -0.4300
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.0615
    Cell Significance Index: -7.2500
  • Cell Name: peptic cell (CL0000155)
    Fold Change: -0.0619
    Cell Significance Index: -0.5500
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: -0.0676
    Cell Significance Index: -0.7700
  • Cell Name: erythroblast (CL0000765)
    Fold Change: -0.0704
    Cell Significance Index: -0.8400
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.0708
    Cell Significance Index: -4.3500
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: -0.0711
    Cell Significance Index: -0.4400
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: -0.0744
    Cell Significance Index: -0.7700
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.0753
    Cell Significance Index: -5.0600
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -0.0772
    Cell Significance Index: -5.9300
  • Cell Name: epithelial cell of esophagus (CL0002252)
    Fold Change: -0.0783
    Cell Significance Index: -0.5200
  • Cell Name: immature NK T cell (CL0000914)
    Fold Change: -0.0785
    Cell Significance Index: -1.0100
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: -0.0806
    Cell Significance Index: -0.5500
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: -0.0841
    Cell Significance Index: -0.7700
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.0845
    Cell Significance Index: -5.4500
  • Cell Name: smooth muscle cell of prostate (CL1000487)
    Fold Change: -0.0881
    Cell Significance Index: -1.0200
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: -0.0890
    Cell Significance Index: -0.5800
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: -0.0891
    Cell Significance Index: -4.6400
  • Cell Name: chondroblast (CL0000058)
    Fold Change: -0.0920
    Cell Significance Index: -0.5400

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.

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 cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

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 cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Serpin family member:** SERPINC1 belongs to the serpin family, characterized by its ability to inhibit serine proteases, such as thrombin and factor Xa, thereby regulating coagulation and fibrinolysis. 2. **Antithrombin-III:** SERPINC1 is also known as Antithrombin-III, a potent inhibitor of thrombin and factor Xa, which are essential for blood coagulation. 3. **Heparin binding:** SERPINC1 binds to heparin, a polysaccharide that enhances its anticoagulant activity. 4. **Cellular expression:** SERPINC1 is expressed in various tissues, including hepatocytes, endothelial cells, and epithelial cells, highlighting its role in multiple physiological processes. **Pathways and Functions:** 1. **Blood coagulation:** SERPINC1 regulates blood coagulation by inhibiting thrombin and factor Xa, thereby preventing excessive clot formation. 2. **Fibrinolysis:** SERPINC1 also regulates fibrinolysis by inhibiting plasminogen activators, which are essential for breaking down clots. 3. **Protein binding:** SERPINC1 binds to various proteins, including thrombin, factor Xa, heparin, and plasminogen activators, modulating their activity and function. 4. **Regulation of IGF transport:** SERPINC1 regulates the transport and uptake of insulin-like growth factor (IGF) by insulin-like growth factor binding proteins (IGFBPs), which is essential for growth and development. 5. **Endoplasmic reticulum lumen:** SERPINC1 is also involved in the regulation of protein transport and modification within the endoplasmic reticulum lumen. **Clinical Significance:** 1. **Thrombophilia:** Mutations in SERPINC1 have been associated with thrombophilia, a condition characterized by an increased risk of blood clots. 2. **Hemophilia C:** SERPINC1 is the primary cause of Hemophilia C, a rare bleeding disorder characterized by defective anticoagulant activity. 3. **Liver disease:** Alterations in SERPINC1 expression have been observed in liver disease, including cirrhosis and hepatocellular carcinoma. 4. **Cancer:** SERPINC1 has been implicated in cancer progression, including metastasis and angiogenesis, highlighting its potential as a therapeutic target. 5. **Cardiovascular disease:** SERPINC1 may play a role in cardiovascular disease, including atherosclerosis and heart failure, due to its involvement in blood coagulation and fibrinolysis. In conclusion, SERPINC1 is a multifunctional protein that plays a critical role in regulating blood coagulation, fibrinolysis, and protein binding. Its dysregulation has been implicated in various diseases, including thrombophilia, Hemophilia C, liver disease, cancer, and cardiovascular disease. Further research is needed to fully elucidate the mechanisms of SERPINC1 and its clinical significance, ultimately leading to the development of novel therapeutic strategies.

Genular Protein ID: 290456255

Symbol: ANT3_HUMAN

Name: Antithrombin-III

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 6298709

Title: Cloning and expression of the cDNA for human antithrombin III.

PubMed ID: 6298709

DOI: 10.1093/nar/10.24.8113

PubMed ID: 6572945

Title: Isolation and sequence characterization of a cDNA clone of human antithrombin III.

PubMed ID: 6572945

DOI: 10.1073/pnas.80.7.1845

PubMed ID: 8476848

Title: Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia.

PubMed ID: 8476848

DOI: 10.1021/bi00067a008

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 6305982

Title: Isolation of a cDNA clone for human antithrombin III.

PubMed ID: 6305982

DOI: 10.1016/s0021-9258(20)82077-8

PubMed ID: 3191114

Title: Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site.

PubMed ID: 3191114

DOI: 10.1021/bi00416a052

PubMed ID: 7734359

Title: Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin.

PubMed ID: 7734359

DOI: 10.1111/j.1365-2141.1995.tb08368.x

PubMed ID: 7238875

Title: The site in human antithrombin for functional proteolytic cleavage by human thrombin.

PubMed ID: 7238875

DOI: 10.1016/0014-5793(81)80255-4

PubMed ID: 6693405

Title: The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence.

PubMed ID: 6693405

DOI: 10.1016/s0021-9258(17)43548-4

PubMed ID: 15084671

Title: A proteomic analysis of human bile.

PubMed ID: 15084671

DOI: 10.1074/mcp.m400015-mcp200

PubMed ID: 14760718

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

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 15853774

Title: Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity.

PubMed ID: 15853774

DOI: 10.1042/bj20050299

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: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

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: 19838169

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

PubMed ID: 19838169

DOI: 10.1038/nmeth.1392

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

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: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 8087553

Title: Biological implications of a 3 A structure of dimeric antithrombin.

PubMed ID: 8087553

DOI: 10.1016/s0969-2126(00)00028-9

PubMed ID: 7656006

Title: The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions.

PubMed ID: 7656006

DOI: 10.1038/nsb0194-48

PubMed ID: 9067613

Title: The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site.

PubMed ID: 9067613

DOI: 10.1006/jmbi.1996.0798

PubMed ID: 9761669

Title: Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin.

PubMed ID: 9761669

DOI: 10.1006/jmbi.1998.2083

PubMed ID: 2126464

Title: Antithrombin III: structural and functional aspects.

PubMed ID: 2126464

DOI: 10.1016/0300-9084(90)90123-x

PubMed ID: 8236149

Title: Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis.

PubMed ID: 8236149

PubMed ID: 7749926

Title: What do dysfunctional serpins tell us about molecular mobility and disease?

PubMed ID: 7749926

DOI: 10.1038/nsb0295-96

PubMed ID: 8664906

Title: Molecular genetics of human antithrombin deficiency.

PubMed ID: 8664906

DOI: 10.1002/(sici)1098-1004(1996)7:1<7::aid-humu2>3.0.co;2-b

PubMed ID: 9031473

Title: Antithrombin mutation database: 2nd (1997) update.

PubMed ID: 9031473

PubMed ID: 6582486

Title: Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability.

PubMed ID: 6582486

DOI: 10.1073/pnas.81.2.289

PubMed ID: 3080419

Title: Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity.

PubMed ID: 3080419

DOI: 10.1016/s0021-9258(17)36071-4

PubMed ID: 3805013

Title: Antithrombin-III Denver, a reactive site variant.

PubMed ID: 3805013

DOI: 10.1016/s0021-9258(19)75747-0

PubMed ID: 3179438

Title: Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity.

PubMed ID: 3179438

PubMed ID: 3162733

Title: Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow.

PubMed ID: 3162733

DOI: 10.1016/s0021-9258(18)60605-2

PubMed ID: 2781509

Title: Antithrombin Chicago, amino acid substitution of arginine 393 to histidine.

PubMed ID: 2781509

DOI: 10.1016/0049-3848(89)90127-8

PubMed ID: 2365065

Title: Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution to heparin binding.

PubMed ID: 2365065

DOI: 10.1016/0014-5793(90)81530-2

PubMed ID: 1977621

Title: Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site.

PubMed ID: 1977621

DOI: 10.1016/0014-5793(90)81057-u

PubMed ID: 2229057

Title: Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine.

PubMed ID: 2229057

DOI: 10.1016/s0021-9258(17)30614-2

PubMed ID: 2013320

Title: Site-directed mutagenesis of alanine-382 of human antithrombin III.

PubMed ID: 2013320

DOI: 10.1016/0014-5793(91)80305-m

PubMed ID: 1906811

Title: Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins.

PubMed ID: 1906811

DOI: 10.1016/0014-5793(91)80809-h

PubMed ID: 1555650

Title: Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F.

PubMed ID: 1555650

DOI: 10.1016/0014-5793(92)80854-a

PubMed ID: 1547341

Title: Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with normal heparin binding and impaired serine protease reactivity.

PubMed ID: 1547341

PubMed ID: 8443391

Title: Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis.

PubMed ID: 8443391

PubMed ID: 8486379

Title: A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), identified by DNA heteroduplex detection.

PubMed ID: 8486379

DOI: 10.1006/geno.1993.1184

PubMed ID: 7981186

Title: Three novel mutations of antithrombin inducing high-molecular-mass compounds.

PubMed ID: 7981186

DOI: 10.1161/01.atv.14.12.1958

PubMed ID: 7959685

Title: Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis.

PubMed ID: 7959685

DOI: 10.1007/bf00211016

PubMed ID: 8274732

Title: Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 antithrombin deficiency and neonatal thrombosis.

PubMed ID: 8274732

PubMed ID: 7994035

Title: Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families.

PubMed ID: 7994035

PubMed ID: 7989582

Title: Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp).

PubMed ID: 7989582

DOI: 10.1172/jci117589

PubMed ID: 7878627

Title: Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6.

PubMed ID: 7878627

PubMed ID: 7832187

Title: Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin.

PubMed ID: 7832187

DOI: 10.1002/ajh.2830480104

PubMed ID: 9157604

Title: Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing type I antithrombin deficiency.

PubMed ID: 9157604

PubMed ID: 9845533

Title: Impaired cotranslational processing as a mechanism for type I antithrombin deficiency.

PubMed ID: 9845533

PubMed ID: 9759613

Title: The molecular basis of antithrombin deficiency in Belgian and Dutch families.

PubMed ID: 9759613

PubMed ID: 10361121

Title: Familial overexpression of beta-antithrombin caused by an Asn135-to-Thr substitution.

PubMed ID: 10361121

PubMed ID: 10997988

Title: Molecular bases of antithrombin deficiency in French families: identification of seven novel mutations in the antithrombin gene.

PubMed ID: 10997988

DOI: 10.1046/j.1365-2141.2000.02245.x

PubMed ID: 11794707

Title: Two novel gene mutations in type I antithrombin deficiency.

PubMed ID: 11794707

DOI: 10.1007/bf02982095

PubMed ID: 11713457

Title: Intracerebral hemorrhage associated with a novel antithrombin gene mutation in a neonate.

PubMed ID: 11713457

DOI: 10.1067/mpd.2001.118191

PubMed ID: 12353073

Title: Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin affinity.

PubMed ID: 12353073

DOI: 10.1267/THRO88030436

PubMed ID: 12595305

Title: Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerization in vivo associated with severe childhood thrombosis.

PubMed ID: 12595305

DOI: 10.1182/blood-2002-11-3391

PubMed ID: 12894857

Title: Five novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis.

PubMed ID: 12894857

DOI: 10.1007/bf02983246

PubMed ID: 15164384

Title: Molecular basis of inherited antithrombin deficiency in Portuguese families: identification of genetic alterations and screening for additional thrombotic risk factors.

PubMed ID: 15164384

DOI: 10.1002/ajh.20067

PubMed ID: 15140129

Title: Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis.

PubMed ID: 15140129

DOI: 10.1111/j.1538-7836.2004.00749.x

PubMed ID: 16908819

Title: Retinal vein occlusion associated with antithrombin deficiency secondary to a novel G9840C missense mutation.

PubMed ID: 16908819

DOI: 10.1001/archopht.124.8.1165

PubMed ID: 22758787

Title: Type II antithrombin deficiency caused by a large in-frame insertion: structural, functional and pathological relevance.

PubMed ID: 22758787

DOI: 10.1111/j.1538-7836.2012.04839.x

PubMed ID: 23910795

Title: Type II antithrombin deficiency caused by a founder mutation Pro73Leu in the Finnish population: clinical picture.

PubMed ID: 23910795

DOI: 10.1111/jth.12364

PubMed ID: 30046692

Title: Defects of splicing in antithrombin deficiency.

PubMed ID: 30046692

DOI: 10.1002/rth2.12025

Sequence Information:

  • Length: 464
  • Mass: 52602
  • Checksum: 9A4E324F00683D9D
  • Sequence:
  • MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK 
    KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA 
    MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG 
    DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN 
    ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ 
    VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG 
    FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV 
    VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK

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.