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P02671

- FIBA_HUMAN

UniProt

P02671 - FIBA_HUMAN

Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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
    Sitei35 – 362Cleavage; by thrombin; to release fibrinopeptide A
    Sitei100 – 1012Cleavage; by plasmin; to break down fibrin clots
    Sitei121 – 1222Cleavage; by hementin; to prevent blood coagulation
    Sitei123 – 1242Cleavage; by plasmin; to break down fibrin clots

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    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.
    REACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibrinogen alpha chain
    Cleaved into the following 2 chains:
    Gene namesi
    Name:FGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3661. FGA.

    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: UniProtKB
    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

    Amyloid, 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. The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
    Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti545 – 5451E → V in AMYL8.
    VAR_010731
    Natural varianti573 – 5731R → L in AMYL8. 1 Publication
    VAR_010732

    Keywords - Diseasei

    Amyloidosis, Disease mutation

    Organism-specific databases

    MIMi105200. phenotype.
    134820. gene+phenotype.
    202400. phenotype.
    Orphaneti98880. Familial afibrinogenemia.
    98881. Familial dysfibrinogenemia.
    248408. Familial hypodysfibrinogenemia.
    101041. Familial hypofibrinogenemia.
    93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
    PharmGKBiPA429.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19193 PublicationsAdd
    BLAST
    Peptidei20 – 3516Fibrinopeptide APRO_0000009021Add
    BLAST
    Chaini36 – 866831Fibrinogen alpha chainPRO_0000009022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221Phosphoserine2 Publications
    Disulfide bondi47 – 47Interchain
    Disulfide bondi55 – 55Interchain (with C-95 in beta chain)
    Disulfide bondi64 – 64Interchain (with C-49 in gamma chain)
    Disulfide bondi68 – 68Interchain (with C-106 in beta chain)
    Disulfide bondi180 – 180Interchain (with C-165 in gamma chain)
    Disulfide bondi184 – 184Interchain (with C-223 in beta chain)
    Glycosylationi320 – 3201O-linked (GalNAc...)1 Publication
    Cross-linki322 – 322Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)
    Cross-linki347 – 347Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
    Glycosylationi351 – 3511O-linked (GalNAc...)1 Publication
    Cross-linki385 – 385Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
    Modified residuei412 – 4121Phosphothreonine2 Publications
    Glycosylationi453 – 4531N-linked (GlcNAc...); in variant Caracas-2
    Disulfide bondi461 ↔ 491
    Cross-linki527 – 527Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence Analysis
    Cross-linki558 – 558Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence Analysis
    Modified residuei565 – 56514-hydroxyproline; by P4HA11 Publication
    Cross-linki575 – 575Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence Analysis
    Cross-linki581 – 581Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence Analysis
    Cross-linki599 – 599Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence Analysis
    Modified residuei609 – 6091Phosphoserine2 Publications
    Glycosylationi686 – 6861N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    The alpha chain is not glycosylated.3 Publications
    Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
    About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.
    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
    Phosphorylation sites are present in the extracellular medium.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP02671.
    PaxDbiP02671.
    PeptideAtlasiP02671.
    PRIDEiP02671.

    2D gel databases

    OGPiP02671.
    SWISS-2DPAGEP02671.

    PTM databases

    PhosphoSiteiP02671.

    Miscellaneous databases

    PMAP-CutDBP02671.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    ArrayExpressiP02671.
    BgeeiP02671.
    CleanExiHS_FGA.
    GenevestigatoriP02671.

    Organism-specific databases

    HPAiCAB016776.
    HPA051370.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APOA1P026472EBI-348571,EBI-701692

    Protein-protein interaction databases

    BioGridi108534. 20 interactions.
    DIPiDIP-29643N.
    IntActiP02671. 14 interactions.
    MINTiMINT-1033042.
    STRINGi9606.ENSP00000306361.

    Structurei

    Secondary structure

    1
    866
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni27 – 315
    Beta strandi57 – 604
    Beta strandi63 – 653
    Helixi67 – 9226
    Helixi94 – 11118
    Helixi116 – 12914
    Turni133 – 1353
    Turni139 – 1413
    Helixi142 – 17837
    Turni179 – 1835
    Beta strandi184 – 1863
    Helixi195 – 20915
    Beta strandi337 – 3437
    Beta strandi673 – 6819
    Helixi689 – 6946
    Helixi711 – 7188
    Beta strandi723 – 7297
    Beta strandi735 – 74410
    Turni747 – 7515
    Beta strandi753 – 76210
    Turni765 – 7684
    Turni771 – 7733
    Helixi775 – 7784
    Beta strandi793 – 7975
    Helixi799 – 8035
    Beta strandi810 – 8123
    Beta strandi814 – 8163
    Beta strandi823 – 8264
    Helixi829 – 8313
    Beta strandi840 – 8434
    Helixi844 – 8474
    Beta strandi854 – 8618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BBRX-ray2.30F/G/I26-35[»]
    1DM4X-ray2.50C26-35[»]
    1FZAX-ray2.90A/D130-216[»]
    1FZBX-ray2.90A/D130-216[»]
    1FZCX-ray2.30A/D130-216[»]
    1FZDX-ray2.10A/B/C/D/E/F/G/H666-866[»]
    1FZEX-ray3.00A/D130-216[»]
    1FZFX-ray2.70A/D130-216[»]
    1FZGX-ray2.50A/D130-216[»]
    1LT9X-ray2.80A/D145-210[»]
    1LTJX-ray2.80A/D145-210[»]
    1N86X-ray3.20A/D130-216[»]
    1N8EX-ray4.50A/D130-218[»]
    1RE3X-ray2.45A/D145-210[»]
    1RE4X-ray2.70A/D145-210[»]
    1RF0X-ray2.81A/D145-210[»]
    1RF1X-ray2.53A/D145-210[»]
    1YCPX-ray2.50F/N20-42[»]
    2A45X-ray3.65G/J36-92[»]
    2FFDX-ray2.89A/D145-210[»]
    2H43X-ray2.70A/D130-216[»]
    2HLOX-ray2.60A/D130-216[»]
    2HODX-ray2.90A/D/G/J130-216[»]
    2HPCX-ray2.90A/D/G/J130-216[»]
    2OYHX-ray2.40A/D145-210[»]
    2OYIX-ray2.70A/D145-210[»]
    2Q9IX-ray2.80A/D130-216[»]
    2XNXX-ray3.30A/D/G/J130-216[»]
    2XNYX-ray7.50A/D130-216[»]
    2Z4EX-ray2.70A/D130-216[»]
    3AT0X-ray2.50B332-347[»]
    3BVHX-ray2.60A/D148-209[»]
    3E1IX-ray2.30A/D130-216[»]
    3GHGX-ray2.90A/D/G/J20-581[»]
    3H32X-ray3.60A/D20-216[»]
    3HUSX-ray3.04A/D145-210[»]
    4F27X-ray1.92Q336-347[»]
    ProteinModelPortaliP02671.
    SMRiP02671. Positions 46-231, 411-524, 596-866.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02671.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini623 – 864242Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 383Alpha-chain polymerization, binding distal domain of another fibrin gamma chain

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili68 – 631564By similarityAdd
    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

    eggNOGiNOG114889.
    HOGENOMiHOG000285947.
    HOVERGENiHBG005668.
    InParanoidiP02671.
    KOiK03903.
    OMAiYKCPSGC.
    OrthoDBiEOG7X9G60.
    PhylomeDBiP02671.
    TreeFamiTF351984.

    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.
    IPR021996. Fibrinogen_aC.
    IPR020837. Fibrinogen_CS.
    [Graphical view]
    PfamiPF08702. Fib_alpha. 1 hit.
    PF12160. Fibrinogen_aC. 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 1 (identifier: P02671-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-E

    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

    MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS    50
    DWPFCSDEDW NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK 100
    DSHSLTTNIM EILRGDFSSA NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ 150
    HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC RGSCSRALAR EVDLKDYEDQ 200
    QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ LQKVPPEWKA 250
    LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 300
    GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG 350
    SPRPGSTGTW NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS 400
    GNARPNNPDW GTFEEVSGNV SPGTRREYHT EKLVTSKGDK ELRTGKEKVT 450
    SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK EVVTSEDGSD CPEAMDLGTL 500
    SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF VSETESRGSE 550
    SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 600
    YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI 650
    KLPGSSKIFS VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN 700
    DEGEGEFWLG NDYLHLLTQR GSVLRVELED WAGNEAYAEY HFRVGSEAEG 750
    YALQVSSYEG TAGDALIEGS VEEGAEYTSH NNMQFSTFDR DADQWEENCA 800
    EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG VVWVSFRGAD 850
    YSLRAVRMKI RPLVTQ 866
    Length:866
    Mass (Da):94,973
    Last modified:October 1, 1996 - v2
    Checksum:iEA73A81204D8AEC4
    GO
    Isoform 2 (identifier: P02671-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         631-644: DCDDVLQTHPSGTQ → GIHTSPLGKPSLSP
         645-866: Missing.

    Show »
    Length:644
    Mass (Da):69,757
    Checksum:iB9035F3DD864572A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771I → V in BAF83248. (PubMed:14702039)Curated
    Sequence conflicti184 – 1841C → W in AAA52426. (PubMed:6688355)Curated
    Sequence conflicti215 – 2162SR → RS AA sequence 1 PublicationCurated
    Sequence conflicti299 – 2991S → G AA sequence 1 PublicationCurated
    Sequence conflicti304 – 3041S → G AA sequence 1 PublicationCurated
    Sequence conflicti317 – 3182GT → SG AA sequence (PubMed:518846)Curated
    Isoform 2 (identifier: P02671-2)
    Sequence conflicti640 – 6445PSLSP → LPCPPRLS in AAK31372. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61I → V.1 Publication
    Corresponds to variant rs2070025 [ dbSNP | Ensembl ].
    VAR_011609
    Natural varianti26 – 261D → N in Lille-1.
    VAR_002390
    Natural varianti31 – 311G → V in Rouen-1.
    VAR_002391
    Natural varianti35 – 351R → C.
    VAR_002392
    Natural varianti35 – 351R → H.1 Publication
    VAR_002393
    Natural varianti37 – 371P → L in Kyoto-2. 1 Publication
    VAR_002394
    Natural varianti38 – 381R → G in Aarhus-1.
    VAR_002397
    Natural varianti38 – 381R → N in Munich-1; requires 2 nucleotide substitutions.
    VAR_002395
    Natural varianti38 – 381R → S in Detroit-1.
    VAR_002396
    Natural varianti39 – 391V → D in Canterbury. 1 Publication
    VAR_010730
    Natural varianti66 – 661S → T.
    VAR_002398
    Natural varianti160 – 1601R → S in Lima. 1 Publication
    VAR_002399
    Natural varianti331 – 3311T → A.3 Publications
    Corresponds to variant rs6050 [ dbSNP | Ensembl ].
    VAR_011610
    Natural varianti446 – 4461K → E.1 Publication
    Corresponds to variant rs6052 [ dbSNP | Ensembl ].
    VAR_014168
    Natural varianti453 – 4531S → N in Caracas-2. 1 Publication
    VAR_002400
    Natural varianti456 – 4561T → A.1 Publication
    Corresponds to variant rs2070031 [ dbSNP | Ensembl ].
    VAR_011611
    Natural varianti545 – 5451E → V in AMYL8.
    VAR_010731
    Natural varianti573 – 5731R → C in Dusart/Paris-5. 1 Publication
    VAR_002401
    Natural varianti573 – 5731R → L in AMYL8. 1 Publication
    VAR_010732

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei631 – 64414DCDDV…PSGTQ → GIHTSPLGKPSLSP in isoform 2. 3 PublicationsVSP_001531Add
    BLAST
    Alternative sequencei645 – 866222Missing in isoform 2. 3 PublicationsVSP_001532Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64982 Genomic DNA. Translation: AAA17056.1.
    M64982 Genomic DNA. Translation: AAA17055.1.
    M58569 Transcribed RNA. Translation: AAC97142.1.
    M58569 Transcribed RNA. Translation: AAC97143.1.
    AF361104 Genomic DNA. Translation: AAK31372.1.
    AF361104 Genomic DNA. Translation: AAK31373.1.
    AK290559 mRNA. Translation: BAF83248.1.
    CH471056 Genomic DNA. Translation: EAX04925.1.
    CH471056 Genomic DNA. Translation: EAX04926.1.
    CH471056 Genomic DNA. Translation: EAX04927.1.
    CH471056 Genomic DNA. Translation: EAX04928.1.
    BC098280 mRNA. Translation: AAH98280.1.
    BC099706 mRNA. Translation: AAH99706.1.
    BC099720 mRNA. Translation: AAH99720.1.
    BC101935 mRNA. Translation: AAI01936.1.
    J00128 mRNA. Translation: AAA52427.1.
    J00127 mRNA. Translation: AAA52426.1.
    K02272 mRNA. Translation: AAA52428.1.
    M26878 mRNA. Translation: AAA52444.1.
    CCDSiCCDS3787.1. [P02671-1]
    CCDS47152.1. [P02671-2]
    PIRiA93956. FGHUA.
    D44234.
    RefSeqiNP_000499.1. NM_000508.3. [P02671-1]
    NP_068657.1. NM_021871.2. [P02671-2]
    UniGeneiHs.351593.

    Genome annotation databases

    EnsembliENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
    ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
    GeneIDi2243.
    KEGGihsa:2243.
    UCSCiuc003iod.1. human. [P02671-1]
    uc003ioe.1. human. [P02671-2]

    Polymorphism databases

    DMDMi1706799.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Fibrinogen entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64982 Genomic DNA. Translation: AAA17056.1 .
    M64982 Genomic DNA. Translation: AAA17055.1 .
    M58569 Transcribed RNA. Translation: AAC97142.1 .
    M58569 Transcribed RNA. Translation: AAC97143.1 .
    AF361104 Genomic DNA. Translation: AAK31372.1 .
    AF361104 Genomic DNA. Translation: AAK31373.1 .
    AK290559 mRNA. Translation: BAF83248.1 .
    CH471056 Genomic DNA. Translation: EAX04925.1 .
    CH471056 Genomic DNA. Translation: EAX04926.1 .
    CH471056 Genomic DNA. Translation: EAX04927.1 .
    CH471056 Genomic DNA. Translation: EAX04928.1 .
    BC098280 mRNA. Translation: AAH98280.1 .
    BC099706 mRNA. Translation: AAH99706.1 .
    BC099720 mRNA. Translation: AAH99720.1 .
    BC101935 mRNA. Translation: AAI01936.1 .
    J00128 mRNA. Translation: AAA52427.1 .
    J00127 mRNA. Translation: AAA52426.1 .
    K02272 mRNA. Translation: AAA52428.1 .
    M26878 mRNA. Translation: AAA52444.1 .
    CCDSi CCDS3787.1. [P02671-1 ]
    CCDS47152.1. [P02671-2 ]
    PIRi A93956. FGHUA.
    D44234.
    RefSeqi NP_000499.1. NM_000508.3. [P02671-1 ]
    NP_068657.1. NM_021871.2. [P02671-2 ]
    UniGenei Hs.351593.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BBR X-ray 2.30 F/G/I 26-35 [» ]
    1DM4 X-ray 2.50 C 26-35 [» ]
    1FZA X-ray 2.90 A/D 130-216 [» ]
    1FZB X-ray 2.90 A/D 130-216 [» ]
    1FZC X-ray 2.30 A/D 130-216 [» ]
    1FZD X-ray 2.10 A/B/C/D/E/F/G/H 666-866 [» ]
    1FZE X-ray 3.00 A/D 130-216 [» ]
    1FZF X-ray 2.70 A/D 130-216 [» ]
    1FZG X-ray 2.50 A/D 130-216 [» ]
    1LT9 X-ray 2.80 A/D 145-210 [» ]
    1LTJ X-ray 2.80 A/D 145-210 [» ]
    1N86 X-ray 3.20 A/D 130-216 [» ]
    1N8E X-ray 4.50 A/D 130-218 [» ]
    1RE3 X-ray 2.45 A/D 145-210 [» ]
    1RE4 X-ray 2.70 A/D 145-210 [» ]
    1RF0 X-ray 2.81 A/D 145-210 [» ]
    1RF1 X-ray 2.53 A/D 145-210 [» ]
    1YCP X-ray 2.50 F/N 20-42 [» ]
    2A45 X-ray 3.65 G/J 36-92 [» ]
    2FFD X-ray 2.89 A/D 145-210 [» ]
    2H43 X-ray 2.70 A/D 130-216 [» ]
    2HLO X-ray 2.60 A/D 130-216 [» ]
    2HOD X-ray 2.90 A/D/G/J 130-216 [» ]
    2HPC X-ray 2.90 A/D/G/J 130-216 [» ]
    2OYH X-ray 2.40 A/D 145-210 [» ]
    2OYI X-ray 2.70 A/D 145-210 [» ]
    2Q9I X-ray 2.80 A/D 130-216 [» ]
    2XNX X-ray 3.30 A/D/G/J 130-216 [» ]
    2XNY X-ray 7.50 A/D 130-216 [» ]
    2Z4E X-ray 2.70 A/D 130-216 [» ]
    3AT0 X-ray 2.50 B 332-347 [» ]
    3BVH X-ray 2.60 A/D 148-209 [» ]
    3E1I X-ray 2.30 A/D 130-216 [» ]
    3GHG X-ray 2.90 A/D/G/J 20-581 [» ]
    3H32 X-ray 3.60 A/D 20-216 [» ]
    3HUS X-ray 3.04 A/D 145-210 [» ]
    4F27 X-ray 1.92 Q 336-347 [» ]
    ProteinModelPortali P02671.
    SMRi P02671. Positions 46-231, 411-524, 596-866.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108534. 20 interactions.
    DIPi DIP-29643N.
    IntActi P02671. 14 interactions.
    MINTi MINT-1033042.
    STRINGi 9606.ENSP00000306361.

    Chemistry

    BindingDBi P02671.
    ChEMBLi CHEMBL2364709.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00364. Sucralfate.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P02671.

    Polymorphism databases

    DMDMi 1706799.

    2D gel databases

    OGPi P02671.
    SWISS-2DPAGE P02671.

    Proteomic databases

    MaxQBi P02671.
    PaxDbi P02671.
    PeptideAtlasi P02671.
    PRIDEi P02671.

    Protocols and materials databases

    DNASUi 2243.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302053 ; ENSP00000306361 ; ENSG00000171560 . [P02671-1 ]
    ENST00000403106 ; ENSP00000385981 ; ENSG00000171560 . [P02671-2 ]
    GeneIDi 2243.
    KEGGi hsa:2243.
    UCSCi uc003iod.1. human. [P02671-1 ]
    uc003ioe.1. human. [P02671-2 ]

    Organism-specific databases

    CTDi 2243.
    GeneCardsi GC04M155504.
    HGNCi HGNC:3661. FGA.
    HPAi CAB016776.
    HPA051370.
    MIMi 105200. phenotype.
    134820. gene+phenotype.
    202400. phenotype.
    neXtProti NX_P02671.
    Orphaneti 98880. Familial afibrinogenemia.
    98881. Familial dysfibrinogenemia.
    248408. Familial hypodysfibrinogenemia.
    101041. Familial hypofibrinogenemia.
    93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
    PharmGKBi PA429.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114889.
    HOGENOMi HOG000285947.
    HOVERGENi HBG005668.
    InParanoidi P02671.
    KOi K03903.
    OMAi YKCPSGC.
    OrthoDBi EOG7X9G60.
    PhylomeDBi P02671.
    TreeFami TF351984.

    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.
    REACT_75925. Amyloids.

    Miscellaneous databases

    ChiTaRSi FGA. human.
    EvolutionaryTracei P02671.
    GeneWikii Fibrinogen_alpha_chain.
    GenomeRNAii 2243.
    NextBioi 35464018.
    PMAP-CutDB P02671.
    PROi P02671.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02671.
    Bgeei P02671.
    CleanExi HS_FGA.
    Genevestigatori P02671.

    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.
    IPR021996. Fibrinogen_aC.
    IPR020837. Fibrinogen_CS.
    [Graphical view ]
    Pfami PF08702. Fib_alpha. 1 hit.
    PF12160. Fibrinogen_aC. 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. "Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits."
      Fu Y., Weissbach L., Plant P.W., Oddoux C., Cao Y., Liang T.J., Roy S.N., Redman C.M., Grieninger G.
      Biochemistry 31:11968-11972(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
    2. "Fibrinogen DNA and protein sequences."
      Chung D.W., Grieninger G.
      (In) Ebert R.F. (eds.); Index of variant human fibrinogens, pp.13-24, CRC Press, Boca Raton (1994)
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    3. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ALA-331 AND ALA-456.
    4. "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] (ISOFORM 2), VARIANT ALA-331.
      Tissue: Heart.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2).
    7. "Nucleotide sequences of the three genes coding for human fibrinogen."
      Chung D.W., Harris J.E., Davie E.W.
      Adv. Exp. Med. Biol. 281:39-48(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1).
      Tissue: Liver.
    8. "Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications."
      Kant J.A., Lord S.T., Crabtree G.R.
      Proc. Natl. Acad. Sci. U.S.A. 80:3953-3957(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    9. "Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen."
      Rixon M.W., Chan W.-Y., Davie E.W., Chung D.W.
      Biochemistry 22:3237-3244(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
    10. "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 20-629.
    11. "Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence."
      Watt K.W.K., Cottrell B.A., Strong D.D., Doolittle R.F.
      Biochemistry 18:5410-5416(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-629, DISULFIDE BONDS.
    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 [MRNA] OF 110-156.
    13. Cited for: NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
    14. "Studies on fibrinopeptides from primates."
      Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.
      Acta Chem. Scand. 19:1788-1789(1965)
      Cited for: PROTEIN SEQUENCE OF 20-35.
    15. "Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites."
      Cottrell B.A., Strong D.D., Watt K.W.K., Doolittle R.F.
      Biochemistry 18:5405-5410(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING ACCEPTOR SITES.
    16. "Localization of the alpha-chain cross-link acceptor sites of human fibrin."
      Fretto L.J., Ferguson E.W., Steinman H.M., McKee P.A.
      J. Biol. Chem. 253:2184-2195(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING ACCEPTOR SITES.
    17. "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-686.
      Tissue: Plasma.
    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. "Fibrinogen and fibrin."
      Doolittle R.F.
      Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
    20. "Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor."
      Kimura S., Aoki N.
      J. Biol. Chem. 261:15591-15595(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
    21. Cited for: PHOSPHORYLATION.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412 AND SER-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    24. Cited for: HYDROXYLATION AT PRO-565.
    25. "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-686.
      Tissue: Liver.
    26. "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.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation."
      Zauner G., Hoffmann M., Rapp E., Koeleman C.A., Dragan I., Deelder A.M., Wuhrer M., Hensbergen P.J.
      J. Proteome Res. 11:5804-5814(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-320 AND SER-351.
    29. "The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution."
      Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.
      J. Biol. Chem. 267:7911-7920(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
    30. "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 130-216.
    31. "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 130-216.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 670-866.
    33. "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 130-216.
    34. "Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine."
      Yoshida N., Okuma M., Hirata H., Matsuda M., Yamazumi K., Asakura S.
      Blood 78:149-153(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KYOTO-2 LEU-37.
    35. "Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator."
      Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., Arocha-Pinango C.L., Rodriguez S., Nagy H., Perez-Requejo J.L., Matsuda M.
      J. Clin. Invest. 90:67-76(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LIMA SER-160.
    36. "An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation."
      Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., de Bosch N.B., Carvajal Z., Ojeda A., Arocha-Pinango C.L., Matsuda M.
      J. Biol. Chem. 266:11575-11581(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CARACAS-2 ASN-453.
    37. "Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia."
      Koopman J., Haverkate F., Grimbergen J., Lord S.T., Mosesson M.W., Diorio J.P., Siebenlist K.S., Legrand C., Soria J., Soria C., Caen J.P.
      J. Clin. Invest. 91:1637-1643(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DUSART/PARIS-5 CYS-573.
    38. "Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain."
      Benson M.D., Liepnieks J., Uemichi T., Wheeler G., Correa R.
      Nat. Genet. 3:252-255(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AMYL8 LEU-573.
    39. "Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution."
      Yamazumi K., Terukina S., Matsuda M., Kanbayashi J., Sakon M., Tsujinaka T.
      Surg. Today 23:45-50(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OSAKA IV HIS-35.
    40. "Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp)."
      Brennan S.O., Hammonds B., George P.M.
      J. Clin. Invest. 96:2854-2858(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CANTERBURY ASP-39.
    41. Cited for: VARIANTS ALA-331 AND GLU-446.

    Entry informationi

    Entry nameiFIBA_HUMAN
    AccessioniPrimary (citable) accession number: P02671
    Secondary accession number(s): A8K3E4
    , D3DP14, D3DP15, Q4QQH7, Q9BX62, Q9UCH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 190 of the entry and version 2 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

    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