Details for: FGG

Gene ID: 2266

Gene Type:  Protein-coding  - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.

Symbol: FGG

Ensembl ID: ENSG00000171557

Description: fibrinogen gamma chain

Selected Context(s):  Overall

Cell Significance Landscape

Contexts:

Associated with

Significant Cells

Cell Significance Index (CSI) scores for the chosen context(s)

  • hepatocyte CL0000182
    CSI 29.66
    rCSI 53.09%
    PRS 87.54
  • centrilobular region hepatocyte CL0019029
    CSI 22.48
    rCSI 58.65%
    PRS 84.97
  • midzonal region hepatocyte CL0019028
    CSI 17.36
    rCSI 40.75%
    PRS 86.73
  • periportal region hepatocyte CL0019026
    CSI 15.41
    rCSI 59.94%
    PRS 86.03
  • intrahepatic cholangiocyte CL0002538
    CSI 10.6
    rCSI 25.44%
    PRS 89.24
  • Kupffer cell CL0000091
    CSI 4.74
    rCSI 10.84%
    PRS 89.52
  • cholangiocyte CL1000488
    CSI 4.38
    rCSI 26.23%
    PRS 88.46
  • hepatic stellate cell CL0000632
    CSI 4.2
    rCSI 15.75%
    PRS 83.31
  • endothelial cell of periportal hepatic sinusoid CL0019021
    CSI 3.89
    rCSI 17.84%
    PRS 90.86
  • erythrocyte CL0000232
    CSI 3.87
    rCSI 8.79%
    PRS 87.54
  • mature NK T cell CL0000814
    CSI 3.01
    rCSI 3.85%
    PRS 92.82
  • pancreatic acinar cell CL0002064
    CSI 2.67
    rCSI 3.55%
    PRS 91.85
  • intestinal epithelial cell CL0002563
    CSI 2.02
    rCSI 2.11%
    PRS 86.23
  • endothelial cell of pericentral hepatic sinusoid CL0019022
    CSI 1.9
    rCSI 5.86%
    PRS 90.93
  • monocyte CL0000576
    CSI 1.8
    rCSI 3.25%
    PRS 90.39
  • enterocyte CL0000584
    CSI 1.15
    rCSI 1.85%
    PRS 85.71
  • pancreatic ductal cell CL0002079
    CSI 0.95
    rCSI 1.85%
    PRS 90.27

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.
Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

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  • Node Color (Target Cell CSI, relative to current network):
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    • High
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  • Node Size: Proportional to Target Cell CSI magnitude
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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

## Summary [FGG](/details-gene/2266) encodes the fibrinogen gamma chain, a critical protein component of the heterohexameric fibrinogen complex. This secreted glycoprotein is synthesized primarily in the liver and circulates in the plasma. Its fundamental role is in hemostasis, where upon vascular injury, it is cleaved by thrombin to form fibrin, which polymerizes to create the insoluble fibrin matrix of a blood clot ([Link](https://pubmed.ncbi.nlm.nih.gov/6688357/)). Beyond its structural role in coagulation, functional annotations suggest [FGG](/details-gene/2266) is involved in cell adhesion, immune system processes, and signal transduction. Its expression is overwhelmingly significant in [hepatocytes](/details-cell/CL0000182), reflecting their function as the primary source of circulating fibrinogen. Defects in this gene are associated with various bleeding disorders, as documented in OMIM ([134850](https://omim.org/entry/134850)). ## Cellular Roles and Expression Landscape The expression profile of [FGG](/details-gene/2266) underscores its primary biological function as a major secretory product of the liver. **Overall**, the gene shows the highest significance scores in various subtypes of [hepatocytes](/details-cell/CL0000182), including [centrilobular region hepatocytes](/details-cell/CL0019029), [midzonal region hepatocytes](/details-cell/CL0019028), and [periportal region hepatocytes](/details-cell/CL0019026). This is consistent with the liver's role in synthesizing and secreting fibrinogen into the bloodstream. High significance is also noted in other liver-resident cells such as [intrahepatic cholangiocytes](/details-cell/CL0002538) and [Kupffer cells](/details-cell/CL0000091), which may suggest a role in local inflammatory or tissue remodeling processes within the liver microenvironment. The moderate significance in immune cells like [monocytes](/details-cell/CL0000576) could reflect either low-level synthesis or the uptake of fibrinogen complexes from the plasma. The protein's function within the circulation is further highlighted by its association with [erythrocytes](/details-cell/CL0000232), likely due to interactions within the blood plasma. The expression landscape strongly suggests that while [FGG](/details-gene/2266) is a canonical hepatic protein, its functional impact extends systemically to hemostasis and potentially to immune cell interactions. ## Pathways and Molecular Function The functional annotations for [FGG](/details-gene/2266) confirm its central role in blood coagulation and wound healing. It is a key participant in the Reactome pathways '[Hemostasis](/details-pathway/R-HSA-109582)' and the '[Common pathway of fibrin clot formation](/details-pathway/R-HSA-140875)', and the GO process '[Blood coagulation, fibrin clot formation](/details-go/GO:0072378)'. As an '[Extracellular matrix structural constituent](/details-go/GO:0005201)', it provides the scaffold for blood clots and participates in '[Platelet aggregation](/details-go/GO:0070527)'. Beyond hemostasis, the data reveal extensive involvement in immune and signaling pathways. [FGG](/details-gene/2266) is implicated in the '[Innate immune system](/details-pathway/R-HSA-168249)' and specifically in multiple '[Toll-like receptor cascades](/details-pathway/R-HSA-168898)', including those for TLR2 and TLR4. This suggests that fibrinogen, or its degradation products, may act as damage-associated molecular patterns (DAMPs) that alert the immune system to tissue injury. This is further supported by its role in processes such as '[Cellular response to interleukin-1](/details-go/GO:0071347)' and '[Cellular response to interleukin-6](/details-go/GO:0071354)'. Furthermore, its connection to '[Integrin cell surface interactions](/details-pathway/R-HSA-216083)' and downstream '[Raf/map kinase cascade](/details-pathway/R-HSA-5673001)' pathways indicates that FGG-containing matrices can initiate intracellular signaling to regulate cell adhesion, spreading, and proliferation. ## Research Directions The dual role of [FGG](/details-gene/2266) as both a structural protein for hemostasis and a signaling molecule in inflammation presents several avenues for future research. While its function in coagulation is well-established, its precise contribution to immune modulation, particularly in the context of chronic disease, remains less understood. **Proposed Hypotheses:** 1. **Fibrinogen as a pro-inflammatory mediator in liver disease:** Given its high expression in [hepatocytes](/details-cell/CL0000182) and its functional annotation in '[Toll like receptor 4 (tlr4) cascade](/details-pathway/R-HSA-166016)', we hypothesize that in states of liver injury (e.g., steatohepatitis), locally deposited FGG acts as a ligand for TLR4 on [Kupffer cells](/details-cell/CL0000091), triggering a pro-inflammatory cascade that contributes to disease progression. 2. **FGG's role in modulating hepatic stellate cell activation:** Based on its function in '[Cell-matrix adhesion](/details-go/GO:0007160)' and '[Extracellular matrix organization](/details-pathway/R-HSA-1474244)', we hypothesize that the deposition of an FGG-rich fibrin matrix in the liver following chronic injury provides a specific scaffold that promotes the activation and proliferation of [hepatic stellate cells](/details-cell/CL0000632), a key event in the development of liver fibrosis. **Experimental Approach:** To test the hypothesis that FGG drives inflammation via TLR4 on [Kupffer cells](/details-cell/CL0000091), one could perform an in vitro co-culture experiment. Primary [Kupffer cells](/details-cell/CL0000091) isolated from wild-type and TLR4-deficient mice would be cultured on plates coated with purified fibrinogen. The activation of inflammatory signaling pathways (e.g., NF-κB, MAPK) could be measured by immunoblotting, and the secretion of key cytokines such as TNF-α and IL-6 could be quantified by ELISA. A significant reduction in cytokine secretion and signaling activation in the TLR4-deficient [Kupffer cells](/details-cell/CL0000091) would support this hypothesis. **Therapeutic Potential:** As a central component of thrombosis, [FGG](/details-gene/2266) is an indirect target of existing anticoagulant therapies. However, its potential role as a pro-inflammatory signaling molecule opens new therapeutic possibilities. If FGG's interaction with immune receptors like TLR4 is confirmed to drive chronic inflammation in diseases like liver fibrosis or atherosclerosis, developing agents that specifically block this interaction could offer a novel anti-inflammatory strategy. Such a therapeutic, likely an antibody or a peptide mimetic, would aim for **inhibition** of the FGG-receptor interaction, potentially reducing inflammation without globally impairing the essential hemostatic function of fibrinogen.

Genular Protein ID: 84210600

Symbol: FIBG_HUMAN

Name: Fibrinogen gamma chain

UniProtKB Accession Codes:

P02679 A8K057 P04469 P04470 Q53Y18 Q96A14 Q96KJ3 Q9UC62 Q9UC63 Q9UCF3

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 1 CORUM 1 CPTAC 1 CTD 1 CarbonylDB 1 ChEBI 4 ChEMBL 1 ChiTaRS 1 ComplexPortal 2 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 5 EMBL 16 Ensembl 2 EvolutionaryTrace 1 ExpressionAtlas 1 GO 39 Gene3D 3 GeneCards 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 2 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 6 KEGG 1 MANE-Select 1 MIM 5 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 Orphanet 4 OrthoDB 1 PANTHER 2 PDB 45 PDBsum 45 PIR 2 PRIDE 1 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 2 Pumba 1 REPRODUCTION-2DPAGE 2 RNAct 1 Reactome 20 RefSeq 2 SIGNOR 1 SMART 2 SMR 1 STRING 1 SUPFAM 2 SignaLink 1 TreeFam 1 UCSC 1 UniLectin 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 6688357

Title: Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen.

PubMed ID: 6688357

DOI: 10.1021/bi00282a033

PubMed ID: 2990550

Title: Nucleotide sequence of the gene for the gamma chain of human fibrinogen.

PubMed ID: 2990550

DOI: 10.1021/bi00329a041

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: 8509453

Title: Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets.

PubMed ID: 8509453

DOI: 10.1083/jcb.121.6.1329

PubMed ID: 1685103

Title: Polymorphism of the human gamma chain fibrinogen gene.

PubMed ID: 1685103

DOI: 10.3109/10425179109020801

PubMed ID: 6689067

Title: Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen.

PubMed ID: 6689067

DOI: 10.1093/nar/11.21.7427

PubMed ID: 6092346

Title: Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen.

PubMed ID: 6092346

DOI: 10.1016/s0021-9258(18)90821-5

PubMed ID: 7654933

Title: Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys).

PubMed ID: 7654933

DOI: 10.1097/00001721-199505000-00002

PubMed ID: 7306501

Title: Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma').

PubMed ID: 7306501

DOI: 10.1021/bi00524a036

PubMed ID: 6575689

Title: Covalent structure of fibrinogen.

PubMed ID: 6575689

DOI: 10.1111/j.1749-6632.1983.tb23232.x

PubMed ID: 936108

Title: Disulfide bridges in NH2-terminal part of human fibrinogen.

PubMed ID: 936108

DOI: 10.1016/0049-3848(76)90245-0

PubMed ID: 6860649

Title: Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation.

PubMed ID: 6860649

DOI: 10.1021/bi00278a003

PubMed ID: 1892842

Title: Recombinant human fibrinogen and sulfation of the gamma' chain.

PubMed ID: 1892842

DOI: 10.1021/bi00103a004

PubMed ID: 11307817

Title: The amino acid sequence in fibrin responsible for high affinity thrombin binding.

PubMed ID: 11307817

PubMed ID: 6383194

Title: Fibrinogen and fibrin.

PubMed ID: 6383194

DOI: 10.1146/annurev.bi.53.070184.001211

PubMed ID: 6592597

Title: Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen.

PubMed ID: 6592597

DOI: 10.1073/pnas.81.19.5980

PubMed ID: 6451630

Title: Localization of a fibrin polymerization site.

PubMed ID: 6451630

DOI: 10.1016/s0021-9258(19)69643-2

PubMed ID: 6326808

Title: Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain.

PubMed ID: 6326808

DOI: 10.1021/bi00303a028

PubMed ID: 6325435

Title: Evidence that three adhesive proteins interact with a common recognition site on activated platelets.

PubMed ID: 6325435

DOI: 10.1016/s0021-9258(18)91019-7

PubMed ID: 3160702

Title: Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence.

PubMed ID: 3160702

DOI: 10.1016/s0021-9258(17)39297-9

PubMed ID: 6933547

Title: Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma').

PubMed ID: 6933547

DOI: 10.1073/pnas.77.9.5069

PubMed ID: 14760718

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

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

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: 18780401

Title: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.

PubMed ID: 18780401

DOI: 10.1002/pmic.200701057

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: 2143188

Title: A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule.

PubMed ID: 2143188

DOI: 10.1016/s0021-9258(18)77401-2

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: 9016719

Title: Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.

PubMed ID: 9016719

DOI: 10.1016/s0969-2126(97)00171-8

PubMed ID: 9207064

Title: The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.

PubMed ID: 9207064

DOI: 10.1073/pnas.94.14.7176

PubMed ID: 9333233

Title: Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.

PubMed ID: 9333233

DOI: 10.1038/38947

PubMed ID: 9628725

Title: Crystal structure of fragment double-D from human fibrin with two different bound ligands.

PubMed ID: 9628725

DOI: 10.1021/bi9804129

PubMed ID: 10074346

Title: Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.

PubMed ID: 10074346

DOI: 10.1021/bi982626w

PubMed ID: 19296670

Title: Crystal structure of human fibrinogen.

PubMed ID: 19296670

DOI: 10.1021/bi802205g

PubMed ID: 2496144

Title: A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi.

PubMed ID: 2496144

DOI: 10.1172/jci114056

PubMed ID: 1421174

Title: Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.

PubMed ID: 1421174

PubMed ID: 2257302

Title: Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation.

PubMed ID: 2257302

PubMed ID: 2328317

Title: Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation.

PubMed ID: 2328317

PubMed ID: 8400260

Title: Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.

PubMed ID: 8400260

PubMed ID: 2971046

Title: Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.

PubMed ID: 2971046

DOI: 10.1016/s0021-9258(18)68321-8

PubMed ID: 2819242

Title: Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization.

PubMed ID: 2819242

PubMed ID: 3708159

Title: Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization.

PubMed ID: 3708159

PubMed ID: 7841300

Title: Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution.

PubMed ID: 7841300

PubMed ID: 8080993

Title: A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.

PubMed ID: 8080993

PubMed ID: 2738036

Title: Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer.

PubMed ID: 2738036

DOI: 10.1093/oxfordjournals.jbchem.a122601

PubMed ID: 2971042

Title: Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site.

PubMed ID: 2971042

DOI: 10.1016/s0021-9258(18)68281-x

PubMed ID: 1455400

Title: Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant.

PubMed ID: 1455400

PubMed ID: 1733971

Title: Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.

PubMed ID: 1733971

DOI: 10.1016/s0021-9258(18)45943-1

PubMed ID: 8470043

Title: Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain.

PubMed ID: 8470043

PubMed ID: 3337908

Title: An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine.

PubMed ID: 3337908

PubMed ID: 2071611

Title: A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization.

PubMed ID: 2071611

DOI: 10.1016/s0021-9258(18)98861-7

PubMed ID: 3563970

Title: Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia.

PubMed ID: 3563970

PubMed ID: 2976995

Title: Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution.

PubMed ID: 2976995

PubMed ID: 11435303

Title: Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R.

PubMed ID: 11435303

DOI: 10.1182/blood.v98.2.351

PubMed ID: 10391209

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

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 11986213

Title: Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting.

PubMed ID: 11986213

DOI: 10.1182/blood.v99.10.3597

PubMed ID: 15632207

Title: Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal polymerization and fibrinogen hypercatabolism due to gamma S378P mutation.

PubMed ID: 15632207

DOI: 10.1182/blood-2004-04-1621

PubMed ID: 25427968

Title: Clinical and molecular characterisation of 21 patients affected by quantitative fibrinogen deficiency.

PubMed ID: 25427968

DOI: 10.1160/th14-07-0629

Sequence Information:

  • Length: 453
  • Mass: 51512
  • Checksum: 1787204904E0D4BB
  • Sequence:
    • MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 
GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL

Genular Protein ID: 3010825293

Symbol: A0A140VJJ6_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A140VJJ6

Database IDs:

ARBA 6 AlphaFoldDB 1 Antibodypedia 1 BioGRID-ORCS 1 CDD 1 CTD 1 DNASU 1 DisGeNET 1 EMBL 2 ExpressionAtlas 1 GO 4 Gene3D 3 InterPro 6 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 3 Pfam 2 RefSeq 1 SAM 1 SMART 2 SMR 1 SUPFAM 2 VEuPathDB 1

Sequence Information:

  • Length: 437
  • Mass: 49497
  • Checksum: 3D73A7BC1E71381B
  • Sequence:
    • MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 
GEGQQHHLGG AKQAGDV