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P02679

- FIBG_HUMAN

UniProt

P02679 - FIBG_HUMAN

Protein

Fibrinogen gamma chain

Gene

FGG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 191 (01 Oct 2014)
      Sequence version 3 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei84 – 852Cleavage; by plasmin; to break down fibrin clots
    Sitei88 – 892Cleavage; by plasmin; to break down fibrin clots
    Sitei102 – 1032Cleavage; by hementin; to prevent blood coagulation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi341 – 35515Add
    BLAST

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. receptor binding Source: BHF-UCL
    4. structural molecule activity Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell-matrix adhesion Source: BHF-UCL
    3. cellular protein complex assembly Source: BHF-UCL
    4. extracellular matrix organization Source: Reactome
    5. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
    6. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    7. platelet activation Source: Reactome
    8. platelet aggregation Source: BHF-UCL
    9. platelet degranulation Source: Reactome
    10. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    11. positive regulation of exocytosis Source: BHF-UCL
    12. positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
    13. positive regulation of peptide hormone secretion Source: BHF-UCL
    14. positive regulation of protein secretion Source: BHF-UCL
    15. positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
    16. positive regulation of vasoconstriction Source: BHF-UCL
    17. protein polymerization Source: BHF-UCL
    18. response to calcium ion Source: BHF-UCL
    19. signal transduction Source: InterPro

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_1439. Common Pathway.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibrinogen gamma chain
    Gene namesi
    Name:FGG
    ORF Names:PRO2061
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3694. FGG.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell cortex Source: Ensembl
    3. cell surface Source: BHF-UCL
    4. external side of plasma membrane Source: BHF-UCL
    5. extracellular region Source: Reactome
    6. extracellular space Source: BHF-UCL
    7. extracellular vesicular exosome Source: UniProt
    8. fibrinogen complex Source: BHF-UCL
    9. plasma membrane Source: Reactome
    10. platelet alpha granule Source: BHF-UCL
    11. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen.
    Note: The disease is caused by mutations affecting the gene represented in this entry. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi202400. phenotype.
    Orphaneti98880. Familial afibrinogenemia.
    98881. Familial dysfibrinogenemia.
    248408. Familial hypodysfibrinogenemia.
    101041. Familial hypofibrinogenemia.
    PharmGKBiPA430.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26262 PublicationsAdd
    BLAST
    Chaini27 – 453427Fibrinogen gamma chainPRO_0000009099Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 – 34Interchain (with C-35)
    Disulfide bondi35 – 35Interchain (with C-34)
    Disulfide bondi45 – 45Interchain (with C-110 in beta chain)
    Disulfide bondi49 – 49Interchain (with C-64 in alpha chain)
    Glycosylationi78 – 781N-linked (GlcNAc...) (complex)6 Publications
    Disulfide bondi161 – 161Interchain (with C-227 in beta chain)
    Disulfide bondi165 – 165Interchain (with C-180 in alpha chain)
    Disulfide bondi179 ↔ 208
    Glycosylationi334 – 3341N-linked (GlcNAc...); in variant Asahi
    Disulfide bondi352 ↔ 365
    Cross-linki424 – 424Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)
    Cross-linki432 – 432Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)
    Modified residuei444 – 4441Sulfotyrosine2 Publications
    Modified residuei448 – 4481Sulfotyrosine2 Publications

    Post-translational modificationi

    Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.1 Publication
    Sulfation of C-terminal tyrosines increases affinity for thrombin.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Sulfation

    Proteomic databases

    MaxQBiP02679.
    PaxDbiP02679.
    PeptideAtlasiP02679.
    PRIDEiP02679.

    2D gel databases

    DOSAC-COBS-2DPAGEP02679.
    OGPiP02679.
    REPRODUCTION-2DPAGEIPI00219713.
    P02679.
    SWISS-2DPAGEP02679.

    PTM databases

    PhosphoSiteiP02679.

    Miscellaneous databases

    PMAP-CutDBP02679.

    Expressioni

    Gene expression databases

    ArrayExpressiP02679.
    BgeeiP02679.
    CleanExiHS_FGG.
    GenevestigatoriP02679.

    Organism-specific databases

    HPAiHPA027529.

    Interactioni

    Subunit structurei

    Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108557. 10 interactions.
    DIPiDIP-29644N.
    IntActiP02679. 3 interactions.
    MINTiMINT-5004002.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 463
    Helixi49 – 9446
    Turni96 – 983
    Turni115 – 1184
    Turni119 – 1224
    Turni124 – 1285
    Helixi129 – 16032
    Beta strandi161 – 1633
    Beta strandi166 – 1683
    Beta strandi171 – 1788
    Helixi179 – 1846
    Beta strandi191 – 1955
    Turni198 – 2003
    Beta strandi204 – 2107
    Beta strandi212 – 2143
    Beta strandi216 – 22611
    Helixi234 – 2396
    Beta strandi241 – 2444
    Beta strandi246 – 2483
    Beta strandi252 – 2543
    Helixi256 – 2638
    Helixi265 – 2673
    Beta strandi270 – 2778
    Beta strandi279 – 2813
    Beta strandi283 – 2908
    Helixi296 – 2983
    Beta strandi301 – 3033
    Beta strandi305 – 3095
    Helixi315 – 3173
    Beta strandi322 – 3243
    Helixi327 – 3315
    Beta strandi341 – 3433
    Beta strandi346 – 3505
    Helixi352 – 3565
    Beta strandi358 – 3603
    Beta strandi363 – 3653
    Beta strandi367 – 3693
    Beta strandi370 – 3734
    Beta strandi376 – 3794
    Helixi382 – 3843
    Beta strandi385 – 3873
    Beta strandi392 – 3954
    Turni396 – 3983
    Beta strandi406 – 4149
    Helixi415 – 4173
    Beta strandi420 – 4245
    Beta strandi426 – 4338

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DUGX-ray1.80A/B424-433[»]
    1FIBX-ray2.10A169-433[»]
    1FICX-ray2.50A/B169-433[»]
    1FIDX-ray2.10A169-433[»]
    1FZAX-ray2.90C/F114-432[»]
    1FZBX-ray2.90C/F114-432[»]
    1FZCX-ray2.30C/F114-432[»]
    1FZEX-ray3.00C/F114-432[»]
    1FZFX-ray2.70C/F114-432[»]
    1FZGX-ray2.50C/F114-432[»]
    1LT9X-ray2.80C/F122-432[»]
    1LTJX-ray2.80C/F122-432[»]
    1N86X-ray3.20C/F114-433[»]
    1N8EX-ray4.50C/F114-433[»]
    1RE3X-ray2.45C/F122-432[»]
    1RE4X-ray2.70C/F122-432[»]
    1RF0X-ray2.81C/F122-432[»]
    1RF1X-ray2.53C/F122-432[»]
    2A45X-ray3.65I/L27-71[»]
    2FFDX-ray2.89C/F122-432[»]
    2FIBX-ray2.01A169-433[»]
    2H43X-ray2.70C/F115-433[»]
    2HLOX-ray2.60C/F114-433[»]
    2HODX-ray2.90C/F/I/L115-433[»]
    2HPCX-ray2.90C/F/I/L115-433[»]
    2HWLX-ray2.40P439-452[»]
    2OYHX-ray2.40C/F122-432[»]
    2OYIX-ray2.70C/F122-432[»]
    2Q9IX-ray2.80C/F114-433[»]
    2VDOX-ray2.51C426-433[»]
    2VDPX-ray2.80C428-433[»]
    2VDQX-ray2.59C426-435[»]
    2VDRX-ray2.40C428-452[»]
    2VR3X-ray1.95C/D425-436[»]
    2XNXX-ray3.30C/F/I/L114-432[»]
    2XNYX-ray7.50C/F114-432[»]
    2Y7LX-ray1.49B421-433[»]
    2Z4EX-ray2.70C/F114-433[»]
    3BVHX-ray2.60C/F128-420[»]
    3E1IX-ray2.30C/F114-432[»]
    3FIBX-ray2.10A170-418[»]
    3GHGX-ray2.90C/F/I/L27-433[»]
    3H32X-ray3.60C/F121-433[»]
    3HUSX-ray3.04C/F122-432[»]
    4B60X-ray1.83C/D421-433[»]
    ProteinModelPortaliP02679.
    SMRiP02679. Positions 28-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02679.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini170 – 416247Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni400 – 42223Gamma-chain polymerization, binding amino end of another fibrin alpha chainAdd
    BLAST
    Regioni423 – 43715Platelet aggregation and Staphylococcus clumpingAdd
    BLAST

    Domaini

    A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.

    Sequence similaritiesi

    Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal

    Phylogenomic databases

    eggNOGiNOG269667.
    HOVERGENiHBG099783.
    KOiK03905.
    OrthoDBiEOG7X9G60.
    PhylomeDBiP02679.
    TreeFamiTF336658.

    Family and domain databases

    Gene3Di3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProiIPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR012290. Fibrinogen_a/b/g_coil_dom.
    IPR020837. Fibrinogen_CS.
    [Graphical view]
    PfamiPF08702. Fib_alpha. 1 hit.
    PF00147. Fibrinogen_C. 1 hit.
    [Graphical view]
    SMARTiSM00186. FBG. 1 hit.
    [Graphical view]
    SUPFAMiSSF56496. SSF56496. 1 hit.
    PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Gamma-B (identifier: P02679-1) [UniParc]FASTAAdd to Basket

    Also known as: Gamma'

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG    50
    IADFLSTYQT KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS 100
    KPNMIDAATL KSRKMLEEIM KYEASILTHD SSIRYLQEIY NSNNQKIVNL 150
    KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ DIANKGAKQS GLYFIKPLKA 200
    NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG FGHLSPTGTT 250
    EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 300
    RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG 350
    NCAEQDGSGW WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT 400
    RWYSMKKTTM KIIPFNRLTI GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE 450
    DDL 453

    Note: Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets.

    Length:453
    Mass (Da):51,512
    Last modified:April 16, 2002 - v3
    Checksum:i1787204904E0D4BB
    GO
    Isoform Gamma-A (identifier: P02679-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         434-453: VRPEHPAETEYDSLYPEDDL → AGDV

    Show »
    Length:437
    Mass (Da):49,497
    Checksum:i3D73A7BC1E71381B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141K → I in AAB59530. (PubMed:2990550)Curated
    Sequence conflicti114 – 1141K → I in AAB59531. (PubMed:2990550)Curated
    Sequence conflicti435 – 4351R → Y AA sequence (PubMed:7306501)Curated
    Sequence conflicti448 – 4481Y → R AA sequence (PubMed:7306501)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771E → G.
    Corresponds to variant rs11551835 [ dbSNP | Ensembl ].
    VAR_049066
    Natural varianti140 – 1401Y → H.1 Publication
    Corresponds to variant rs2066870 [ dbSNP | Ensembl ].
    VAR_033930
    Natural varianti191 – 1911G → R in Milano-12. 3 Publications
    Corresponds to variant rs6063 [ dbSNP | Ensembl ].
    VAR_014170
    Natural varianti301 – 3011R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. 5 Publications
    VAR_002409
    Natural varianti301 – 3011R → H in Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 Publications
    VAR_002410
    Natural varianti318 – 3181G → V in Baltimore-1; impaired polymerization. 1 Publication
    VAR_002411
    Natural varianti334 – 3341N → I in Baltimore-3; impaired polymerization. 1 Publication
    Corresponds to variant rs121913090 [ dbSNP | Ensembl ].
    VAR_002413
    Natural varianti334 – 3341N → K in Kyoto-1; causes accelerated cleavage by plasmin. 2 Publications
    VAR_002412
    Natural varianti335 – 3351G → D in Hillsborough; prolonged thrombin clotting time. 1 Publication
    VAR_015853
    Natural varianti336 – 3361M → T in Asahi; impaired polymerization. 2 Publications
    VAR_002414
    Natural varianti345 – 3462Missing in Vlissingen; defective calcium binding and impaired polymerization. 1 Publication
    VAR_002415
    Natural varianti355 – 3551Q → R in Nagoya-1; impaired polymerization. 1 Publication
    VAR_002416
    Natural varianti356 – 3561D → V in Milano-1; impaired polymerization. 1 Publication
    VAR_002418
    Natural varianti356 – 3561D → Y in Kyoto-3; impaired polymerization. 2 Publications
    VAR_002417
    Natural varianti363 – 3631N → K in Bern-1; impaired polymerization. 1 Publication
    VAR_002419
    Natural varianti377 – 3771G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization. 1 Publication
    VAR_002420
    Natural varianti384 – 3841S → C in Milano-7; impaired polymerization. 1 Publication
    VAR_002421
    Natural varianti401 – 4011R → G in Osaka-5. 1 Publication
    VAR_002422
    Natural varianti410 – 4101M → V.1 Publication
    Corresponds to variant rs6061 [ dbSNP | Ensembl ].
    VAR_014171

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei434 – 45320VRPEH…PEDDL → AGDV in isoform Gamma-A. 5 PublicationsVSP_001537Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10014 Genomic DNA. Translation: AAB59530.1.
    M10014 Genomic DNA. Translation: AAB59531.1.
    AF118092 mRNA. Translation: AAF22036.1.
    AF350254 Genomic DNA. Translation: AAK19751.2.
    AF350254 Genomic DNA. Translation: AAK19752.2.
    AK289422 mRNA. Translation: BAF82111.1.
    AK290824 mRNA. Translation: BAF83513.1.
    BT007081 mRNA. Translation: AAP35744.1.
    CH471056 Genomic DNA. Translation: EAX04917.1.
    CH471056 Genomic DNA. Translation: EAX04919.1.
    BC007044 mRNA. Translation: AAH07044.1.
    BC021674 mRNA. Translation: AAH21674.1.
    X51473 mRNA. Translation: CAA35837.1.
    X00086 mRNA. Translation: CAA24944.1.
    K02569 Genomic DNA. Translation: AAA52430.1.
    K02569 Genomic DNA. Translation: AAA52431.1.
    CCDSiCCDS3788.1. [P02679-1]
    CCDS47153.1. [P02679-2]
    PIRiA90470. FGHUG.
    A90494. FGHUGB.
    RefSeqiNP_000500.2. NM_000509.4. [P02679-2]
    NP_068656.2. NM_021870.2. [P02679-1]
    UniGeneiHs.727584.

    Genome annotation databases

    EnsembliENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
    ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
    GeneIDi2266.
    KEGGihsa:2266.
    UCSCiuc003iog.3. human. [P02679-2]
    uc003ioj.3. human. [P02679-1]

    Polymorphism databases

    DMDMi20178280.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Fibrinogen entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10014 Genomic DNA. Translation: AAB59530.1 .
    M10014 Genomic DNA. Translation: AAB59531.1 .
    AF118092 mRNA. Translation: AAF22036.1 .
    AF350254 Genomic DNA. Translation: AAK19751.2 .
    AF350254 Genomic DNA. Translation: AAK19752.2 .
    AK289422 mRNA. Translation: BAF82111.1 .
    AK290824 mRNA. Translation: BAF83513.1 .
    BT007081 mRNA. Translation: AAP35744.1 .
    CH471056 Genomic DNA. Translation: EAX04917.1 .
    CH471056 Genomic DNA. Translation: EAX04919.1 .
    BC007044 mRNA. Translation: AAH07044.1 .
    BC021674 mRNA. Translation: AAH21674.1 .
    X51473 mRNA. Translation: CAA35837.1 .
    X00086 mRNA. Translation: CAA24944.1 .
    K02569 Genomic DNA. Translation: AAA52430.1 .
    K02569 Genomic DNA. Translation: AAA52431.1 .
    CCDSi CCDS3788.1. [P02679-1 ]
    CCDS47153.1. [P02679-2 ]
    PIRi A90470. FGHUG.
    A90494. FGHUGB.
    RefSeqi NP_000500.2. NM_000509.4. [P02679-2 ]
    NP_068656.2. NM_021870.2. [P02679-1 ]
    UniGenei Hs.727584.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUG X-ray 1.80 A/B 424-433 [» ]
    1FIB X-ray 2.10 A 169-433 [» ]
    1FIC X-ray 2.50 A/B 169-433 [» ]
    1FID X-ray 2.10 A 169-433 [» ]
    1FZA X-ray 2.90 C/F 114-432 [» ]
    1FZB X-ray 2.90 C/F 114-432 [» ]
    1FZC X-ray 2.30 C/F 114-432 [» ]
    1FZE X-ray 3.00 C/F 114-432 [» ]
    1FZF X-ray 2.70 C/F 114-432 [» ]
    1FZG X-ray 2.50 C/F 114-432 [» ]
    1LT9 X-ray 2.80 C/F 122-432 [» ]
    1LTJ X-ray 2.80 C/F 122-432 [» ]
    1N86 X-ray 3.20 C/F 114-433 [» ]
    1N8E X-ray 4.50 C/F 114-433 [» ]
    1RE3 X-ray 2.45 C/F 122-432 [» ]
    1RE4 X-ray 2.70 C/F 122-432 [» ]
    1RF0 X-ray 2.81 C/F 122-432 [» ]
    1RF1 X-ray 2.53 C/F 122-432 [» ]
    2A45 X-ray 3.65 I/L 27-71 [» ]
    2FFD X-ray 2.89 C/F 122-432 [» ]
    2FIB X-ray 2.01 A 169-433 [» ]
    2H43 X-ray 2.70 C/F 115-433 [» ]
    2HLO X-ray 2.60 C/F 114-433 [» ]
    2HOD X-ray 2.90 C/F/I/L 115-433 [» ]
    2HPC X-ray 2.90 C/F/I/L 115-433 [» ]
    2HWL X-ray 2.40 P 439-452 [» ]
    2OYH X-ray 2.40 C/F 122-432 [» ]
    2OYI X-ray 2.70 C/F 122-432 [» ]
    2Q9I X-ray 2.80 C/F 114-433 [» ]
    2VDO X-ray 2.51 C 426-433 [» ]
    2VDP X-ray 2.80 C 428-433 [» ]
    2VDQ X-ray 2.59 C 426-435 [» ]
    2VDR X-ray 2.40 C 428-452 [» ]
    2VR3 X-ray 1.95 C/D 425-436 [» ]
    2XNX X-ray 3.30 C/F/I/L 114-432 [» ]
    2XNY X-ray 7.50 C/F 114-432 [» ]
    2Y7L X-ray 1.49 B 421-433 [» ]
    2Z4E X-ray 2.70 C/F 114-433 [» ]
    3BVH X-ray 2.60 C/F 128-420 [» ]
    3E1I X-ray 2.30 C/F 114-432 [» ]
    3FIB X-ray 2.10 A 170-418 [» ]
    3GHG X-ray 2.90 C/F/I/L 27-433 [» ]
    3H32 X-ray 3.60 C/F 121-433 [» ]
    3HUS X-ray 3.04 C/F 122-432 [» ]
    4B60 X-ray 1.83 C/D 421-433 [» ]
    ProteinModelPortali P02679.
    SMRi P02679. Positions 28-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108557. 10 interactions.
    DIPi DIP-29644N.
    IntActi P02679. 3 interactions.
    MINTi MINT-5004002.

    Chemistry

    BindingDBi P02679.
    ChEMBLi CHEMBL2364709.
    DrugBanki DB00364. Sucralfate.

    PTM databases

    PhosphoSitei P02679.

    Polymorphism databases

    DMDMi 20178280.

    2D gel databases

    DOSAC-COBS-2DPAGE P02679.
    OGPi P02679.
    REPRODUCTION-2DPAGE IPI00219713.
    P02679.
    SWISS-2DPAGE P02679.

    Proteomic databases

    MaxQBi P02679.
    PaxDbi P02679.
    PeptideAtlasi P02679.
    PRIDEi P02679.

    Protocols and materials databases

    DNASUi 2266.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336098 ; ENSP00000336829 ; ENSG00000171557 . [P02679-1 ]
    ENST00000404648 ; ENSP00000384860 ; ENSG00000171557 . [P02679-2 ]
    GeneIDi 2266.
    KEGGi hsa:2266.
    UCSCi uc003iog.3. human. [P02679-2 ]
    uc003ioj.3. human. [P02679-1 ]

    Organism-specific databases

    CTDi 2266.
    GeneCardsi GC04M155525.
    HGNCi HGNC:3694. FGG.
    HPAi HPA027529.
    MIMi 134850. gene.
    202400. phenotype.
    neXtProti NX_P02679.
    Orphaneti 98880. Familial afibrinogenemia.
    98881. Familial dysfibrinogenemia.
    248408. Familial hypodysfibrinogenemia.
    101041. Familial hypofibrinogenemia.
    PharmGKBi PA430.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269667.
    HOVERGENi HBG099783.
    KOi K03905.
    OrthoDBi EOG7X9G60.
    PhylomeDBi P02679.
    TreeFami TF336658.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_1439. Common Pathway.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.

    Miscellaneous databases

    ChiTaRSi FGG. human.
    EvolutionaryTracei P02679.
    GeneWikii FGG.
    GenomeRNAii 2266.
    NextBioi 9205.
    PMAP-CutDB P02679.
    PROi P02679.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02679.
    Bgeei P02679.
    CleanExi HS_FGG.
    Genevestigatori P02679.

    Family and domain databases

    Gene3Di 3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProi IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR012290. Fibrinogen_a/b/g_coil_dom.
    IPR020837. Fibrinogen_CS.
    [Graphical view ]
    Pfami PF08702. Fib_alpha. 1 hit.
    PF00147. Fibrinogen_C. 1 hit.
    [Graphical view ]
    SMARTi SM00186. FBG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56496. SSF56496. 1 hit.
    PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen."
      Chung D.W., Chan W.-Y., Davie E.W.
      Biochemistry 22:3250-3256(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Nucleotide sequence of the gene for the gamma chain of human fibrinogen."
      Rixon M.W., Chung D.W., Davie E.W.
      Biochemistry 24:2077-2086(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
      Tissue: Liver.
    4. "Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
      Tissue: Fetal liver.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
    6. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-140 AND ARG-191.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
      Tissue: Skeletal muscle.
    9. "Human fibrinogen: sequence, sulfur bridges, glycosylation and some structural variants."
      Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.
      (In) Peeters H. (eds.); Protides of the biological fluids, Proc. 28th colloquium, pp.51-56, Pergamon Press, Oxford (1980)
      Cited for: PROTEIN SEQUENCE OF 27-437.
    10. "Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets."
      Bertagnolli M.E., Beckerle M.C.
      J. Cell Biol. 121:1329-1342(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-41.
      Tissue: Platelet.
    11. "Polymorphism of the human gamma chain fibrinogen gene."
      Marchetti L., Zanelli T., Malcovati M., Tenchini M.L.
      DNA Seq. 1:419-422(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-286.
      Tissue: Liver.
    12. "Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen."
      Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.
      Nucleic Acids Res. 11:7427-7434(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 209-270.
    13. "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."
      Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A., Crabtree G.R.
      J. Biol. Chem. 259:12826-12830(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND GAMMA-B).
    14. "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)."
      Borrell M., Gari M., Coll I., Vallve C., Tirado I., Soria J.M., Sala N., Munoz C., Oliver A., Garcia A.
      Blood Coagul. Fibrinolysis 6:198-206(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 291-310, VARIANTS BARCELONA-3/BARCELONA-4 HIS-301 AND VILLAJOYOSA CYS-301.
      Tissue: Blood.
    15. "Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma')."
      Wolfenstein-Todel C., Mosesson M.W.
      Biochemistry 20:6146-6149(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
    16. Cited for: REVIEW, DISULFIDE BONDS.
    17. "The structures of fibrinogen and fibrin."
      Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A., Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.
      (In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.); Regulatory proteolytic enzymes and their inhibitors, pp.163-172, Pergamon Press, New York (1978)
      Cited for: DISULFIDE BONDS.
    18. "Disulfide bridges in NH2-terminal part of human fibrinogen."
      Blombaeck B., Hessel B., Hogg D.
      Thromb. Res. 8:639-658(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    19. "Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation."
      Hoeprich P.D., Doolittle R.F.
      Biochemistry 22:2049-2055(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: QUATERNARY STRUCTURE, DISULFIDE BONDS.
    20. "Recombinant human fibrinogen and sulfation of the gamma' chain."
      Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W.
      Biochemistry 30:9414-9420(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION.
    21. "The amino acid sequence in fibrin responsible for high affinity thrombin binding."
      Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.
      Thromb. Haemost. 85:470-474(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-444 AND TYR-448.
    22. "Fibrinogen and fibrin."
      Doolittle R.F.
      Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
    23. "Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen."
      Horwitz B.H., Varadi A., Scheraga H.A.
      Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMERIZATION SITE.
    24. "Localization of a fibrin polymerization site."
      Olexa S.A., Budzynski A.Z.
      J. Biol. Chem. 256:3544-3549(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMERIZATION SITE.
    25. "Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain."
      Kloczewiak M., Timmons S., Lukas T.J., Hawiger J.
      Biochemistry 23:1767-1774(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PLATELET AGGREGATION SITE.
    26. "Evidence that three adhesive proteins interact with a common recognition site on activated platelets."
      Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H.
      J. Biol. Chem. 259:5388-5391(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PLATELET AGGREGATION SITE.
    27. "Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence."
      Dang C.V., Ebert R.F., Bell W.R.
      J. Biol. Chem. 260:9713-9719(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING SITE.
    28. "Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma')."
      Wolfenstein-Todel C., Mosesson M.W.
      Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
    29. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Plasma.
    30. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Plasma.
    31. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Platelet.
    32. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Milk.
    33. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Liver.
    34. Cited for: GLYCOSYLATION AT ASN-78.
    35. "A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule."
      Kirschbaum N.E., Budzynski A.Z.
      J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY HEMENTIN AND PLASMIN.
    36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen."
      Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W., Davie E.W., Stenkamp R.E., Teller D.C.
      Structure 5:125-138(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
    38. "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."
      Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W.
      Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
    39. "Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin."
      Spraggon G., Everse S.J., Doolittle R.F.
      Nature 389:455-462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 114-432.
    40. "Crystal structure of fragment double-D from human fibrin with two different bound ligands."
      Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.
      Biochemistry 37:8637-8642(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 114-432.
    41. "Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide."
      Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.
      Biochemistry 38:2941-2946(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-432.
    42. "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."
      Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M.
      J. Clin. Invest. 83:1590-1597(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASAHI THR-336.
    43. "Gene analyses of abnormal fibrinogens with a mutation in the gamma chain."
      Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M., Yoshitake S., Okuma M., Ito Y., Takeda Y., Matsuda M.
      Int. J. Hematol. 56:129-134(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356.
    44. "Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation."
      Bantia S., Mane S.M., Bell W.R., Dang C.V.
      Blood 76:2279-2283(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BALTIMORE-1 VAL-318.
    45. "Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation."
      Bantia S., Bell W.R., Dang C.V.
      Blood 75:1659-1663(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BALTIMORE-3 ILE-334.
    46. "Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization."
      Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G., Wermuth B., Furlan M.
      Blood 82:2104-2108(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BERN-1 LYS-363.
    47. "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."
      Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M.
      J. Biol. Chem. 263:13848-13856(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KYOTO-1 LYS-334.
    48. "Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization."
      Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y., Matsuda M.
      Blood 74:2681-2687(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KYOTO-3 TYR-356.
    49. "Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization."
      Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M., Beck E.A.
      Blood 67:1751-1756(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MILANO-1 VAL-356.
    50. "Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution."
      Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.
      Blood Coagul. Fibrinolysis 5:463-471(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MILANO-5 CYS-301.
    51. "A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization."
      Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.
      Blood 84:1874-1880(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MILANO-7 CYS-384.
    52. "Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer."
      Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H.
      J. Biochem. 105:10-14(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NAGOYA-1 ARG-355.
    53. "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."
      Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T., Shimonishi Y.
      J. Biol. Chem. 263:13579-13587(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OSAKA-2 CYS-301.
    54. "Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant."
      Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S.
      Thromb. Haemost. 68:534-538(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OSAKA-3 HIS-301.
    55. "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."
      Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M., Yamazumi K., Asakura S.
      J. Biol. Chem. 267:2753-2759(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OSAKA-5 GLY-401.
    56. "Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain."
      Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C., Amrani D.L.
      Thromb. Haemost. 69:217-220(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARIS-1 GLY-377 DELINS VAL-MET-CYS-GLY-GLU-ALA-LEU-PRO-MET-LEU-LYS-ASP-PRO-CYS-TYR-SER.
    57. "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."
      Yoshida N., Ota K., Moroi M., Matsuda M.
      Blood 71:480-487(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TOCHIGI CYS-301.
    58. "A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization."
      Koopman J., Haverkate F., Briet E., Lord S.T.
      J. Biol. Chem. 266:13456-13461(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
    59. "Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia."
      Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P., Nenci G.G., Berrettini M., Beck E.A.
      Thromb. Haemost. 56:401-406(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
    60. "Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution."
      Yamazumi K., Terukina S., Onohara S., Matsuda M.
      Thromb. Haemost. 60:476-480(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SAGA HIS-301.
    61. "Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R."
      Bolliger-Stucki B., Lord S.T., Furlan M.
      Blood 98:351-357(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MILANO-12 ARG-191.
    62. Cited for: VARIANTS ARG-191 AND VAL-410.
    63. "Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting."
      Mullin J.L., Brennan S.O., Ganly P.S., George P.M.
      Blood 99:3597-3601(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HILLSBOROUGH ASP-335.

    Entry informationi

    Entry nameiFIBG_HUMAN
    AccessioniPrimary (citable) accession number: P02679
    Secondary accession number(s): A8K057
    , P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 191 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The gamma-chain carries the main binding site for the platelet receptor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3