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P02675

- FIBB_HUMAN

UniProt

P02675 - FIBB_HUMAN

Protein

Fibrinogen beta chain

Gene

FGB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      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
    Sitei44 – 452Cleavage; by thrombin; to release fibrinopeptide B
    Sitei152 – 1532Cleavage; by plasmin; to break down fibrin clots
    Sitei160 – 1612Cleavage; by hementin; to prevent blood coagulation
    Sitei163 – 1642Cleavage; by plasmin; to break down fibrin clots

    GO - Molecular functioni

    1. chaperone binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. 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. cellular response to interleukin-1 Source: Ensembl
    5. cellular response to leptin stimulus Source: Ensembl
    6. extracellular matrix organization Source: Reactome
    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.

    Names & Taxonomyi

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

    Organism-specific databases

    HGNCiHGNC:3662. FGB.

    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

    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.2 Publications
    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.
    PharmGKBiPA163.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 30304 PublicationsAdd
    BLAST
    Peptidei31 – 4414Fibrinopeptide B1 PublicationPRO_0000009070Add
    BLAST
    Chaini45 – 491447Fibrinogen beta chainPRO_0000009071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi95 – 95Interchain (with C-55 in alpha chain)
    Disulfide bondi106 – 106Interchain (with C-68 in alpha chain)
    Disulfide bondi110 – 110Interchain (with C-45 in gamma chain)
    Disulfide bondi223 – 223Interchain (with C-184 in alpha chain)
    Disulfide bondi227 – 227Interchain (with C-161 in gamma chain)
    Disulfide bondi231 ↔ 316
    Disulfide bondi241 ↔ 270
    Glycosylationi394 – 3941N-linked (GlcNAc...)4 Publications
    Disulfide bondi424 ↔ 437

    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP02675.
    PaxDbiP02675.
    PeptideAtlasiP02675.
    PRIDEiP02675.

    2D gel databases

    DOSAC-COBS-2DPAGEP02675.
    OGPiP02675.
    REPRODUCTION-2DPAGEIPI00298497.
    P02675.
    SWISS-2DPAGEP02675.
    UCD-2DPAGEP02675.

    PTM databases

    PhosphoSiteiP02675.

    Miscellaneous databases

    PMAP-CutDBP02675.

    Expressioni

    Gene expression databases

    ArrayExpressiP02675.
    BgeeiP02675.
    CleanExiHS_FGB.
    GenevestigatoriP02675.

    Organism-specific databases

    HPAiCAB008624.
    HPA001900.
    HPA001901.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279584EBI-1034445,EBI-6377335From a different organism.

    Protein-protein interaction databases

    BioGridi108535. 19 interactions.
    DIPiDIP-385N.
    IntActiP02675. 16 interactions.
    STRINGi9606.ENSP00000306099.

    Structurei

    Secondary structure

    1
    491
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni100 – 1023
    Helixi109 – 14537
    Helixi147 – 16721
    Helixi172 – 1809
    Turni182 – 1898
    Helixi190 – 22233
    Beta strandi224 – 2263
    Beta strandi233 – 2353
    Beta strandi238 – 2403
    Helixi241 – 2466
    Beta strandi253 – 2575
    Beta strandi261 – 2633
    Beta strandi266 – 2716
    Helixi274 – 2763
    Beta strandi279 – 28810
    Helixi296 – 3016
    Beta strandi302 – 3043
    Beta strandi306 – 3083
    Beta strandi311 – 3155
    Beta strandi321 – 3233
    Helixi326 – 3349
    Beta strandi335 – 3373
    Beta strandi339 – 3457
    Beta strandi347 – 3493
    Beta strandi351 – 36111
    Helixi364 – 3663
    Beta strandi370 – 37910
    Helixi382 – 3854
    Beta strandi388 – 3903
    Helixi392 – 3965
    Beta strandi404 – 4074
    Beta strandi408 – 4103
    Helixi420 – 4223
    Turni424 – 4285
    Beta strandi435 – 4373
    Beta strandi439 – 4413
    Beta strandi448 – 4514
    Turni454 – 4563
    Beta strandi457 – 4615
    Beta strandi464 – 4674
    Helixi468 – 4714
    Beta strandi473 – 4753
    Beta strandi478 – 4858

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FZAX-ray2.90B/E164-491[»]
    1FZBX-ray2.90B/E164-491[»]
    1FZCX-ray2.30B/E164-491[»]
    1FZEX-ray3.00B/E164-491[»]
    1FZFX-ray2.70B/E164-491[»]
    M/N/S/T45-48[»]
    1FZGX-ray2.50B/E164-491[»]
    1LT9X-ray2.80B/E179-491[»]
    1LTJX-ray2.80B/E179-491[»]
    1N86X-ray3.20B/E164-491[»]
    I/J45-51[»]
    1N8EX-ray4.50B/E164-491[»]
    1RE3X-ray2.45B/E179-491[»]
    1RE4X-ray2.70B/E179-491[»]
    1RF0X-ray2.81B/E179-491[»]
    1RF1X-ray2.53B/E179-491[»]
    2A45X-ray3.65H/K45-135[»]
    2FFDX-ray2.89B/E179-491[»]
    2H43X-ray2.70B/E164-491[»]
    2HLOX-ray2.60B/E164-491[»]
    2HODX-ray2.90B/E/H/K164-491[»]
    2HPCX-ray2.90B/E/H/K164-491[»]
    2OYHX-ray2.40B/E179-491[»]
    2OYIX-ray2.70B/E179-491[»]
    2Q9IX-ray2.80B/E164-491[»]
    2XNXX-ray3.30B/E/H/K164-491[»]
    2XNYX-ray7.50B/E164-491[»]
    2Z4EX-ray2.70B/E164-489[»]
    3BVHX-ray2.60B/E191-488[»]
    3E1IX-ray2.30B/E164-491[»]
    3GHGX-ray2.90B/E/H/K31-491[»]
    3H32X-ray3.60B/E31-488[»]
    3HUSX-ray3.04B/E179-491[»]
    ProteinModelPortaliP02675.
    SMRiP02675. Positions 88-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02675.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini232 – 488257Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 473Beta-chain polymerization, binding distal domain of another fibrin

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili157 – 22266Sequence AnalysisAdd
    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

    eggNOGiNOG277105.
    HOGENOMiHOG000059561.
    HOVERGENiHBG005707.
    InParanoidiP02675.
    KOiK03904.
    OMAiTIHNGMF.
    OrthoDBiEOG7X9G60.
    PhylomeDBiP02675.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P02675-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD    50
    KKREEAPSLR PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP 100
    DLGVLCPTGC QLQEALLQQE RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL 150
    LKDLWQKRQK QVKDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS 200
    ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE 250
    TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK 300
    QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD 350
    KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH 400
    NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG 450
    QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q 491
    Length:491
    Mass (Da):55,928
    Last modified:July 1, 1993 - v2
    Checksum:iB92FFB9976AB53C5
    GO

    Sequence cautioni

    The sequence AAH07030.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1392SQ → QS AA sequence 1 PublicationCurated
    Sequence conflicti138 – 1392SQ → QS AA sequence (PubMed:936108)Curated
    Sequence conflicti145 – 1462FQ → QF AA sequence (PubMed:420779)Curated
    Sequence conflicti145 – 1462FQ → QF AA sequence 1 PublicationCurated
    Sequence conflicti145 – 1462FQ → QF AA sequence (PubMed:936108)Curated
    Sequence conflicti192 – 1921P → A in AAA52429. (PubMed:6688356)Curated
    Sequence conflicti245 – 2451I → T in AAI07767. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21K → E.1 Publication
    Corresponds to variant rs6053 [ dbSNP | Ensembl ].
    VAR_014169
    Natural varianti39 – 10264Missing in New York-1. 1 Publication
    VAR_002402Add
    BLAST
    Natural varianti44 – 441R → C in Christchurch-2, Seattle-1 and Ijmuiden. 1 Publication
    VAR_002403
    Natural varianti45 – 451G → R in Ise. 1 Publication
    VAR_002404
    Natural varianti74 – 741R → C in Nijmegen. 1 Publication
    VAR_002405
    Natural varianti98 – 981A → T in Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 Publication
    VAR_002406
    Natural varianti100 – 1001P → S.1 Publication
    Corresponds to variant rs2227434 [ dbSNP | Ensembl ].
    VAR_013091
    Natural varianti170 – 1701N → H.1 Publication
    Corresponds to variant rs2227409 [ dbSNP | Ensembl ].
    VAR_013092
    Natural varianti196 – 1961R → C in congenital afibrinogenemia; variant Longmont. 1 Publication
    VAR_016908
    Natural varianti265 – 2651P → L.2 Publications
    Corresponds to variant rs6054 [ dbSNP | Ensembl ].
    VAR_013093
    Natural varianti365 – 3651A → T in Pontoise-2.
    VAR_002407
    Natural varianti383 – 3831L → R in congenital afibrinogenemia; abolishes fibrinogen secretion. 1 Publication
    VAR_016909
    Natural varianti430 – 4301G → D in congenital afibrinogenemia; abolishes fibrinogen secretion. 1 Publication
    VAR_016910
    Natural varianti478 – 4781R → K in Baltimore-2. 3 Publications
    Corresponds to variant rs4220 [ dbSNP | Ensembl ].
    VAR_002408

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00129 mRNA. Translation: AAA52429.1.
    J00131, J00130 Genomic DNA. Translation: AAA98115.1.
    J00132 Genomic DNA. Translation: AAA98116.1.
    J00133 mRNA. No translation available.
    M64983 Genomic DNA. Translation: AAA18024.2.
    AF388026 Genomic DNA. Translation: AAK62470.1.
    AK312972 mRNA. Translation: BAG35810.1.
    CH471056 Genomic DNA. Translation: EAX04932.1.
    BC007030 mRNA. Translation: AAH07030.1. Sequence problems.
    BC106760 mRNA. Translation: AAI06761.1.
    BC107766 mRNA. Translation: AAI07767.1.
    AH002694 Genomic DNA. Translation: AAA52445.1.
    X05018 Genomic DNA. Translation: CAA28674.1.
    CCDSiCCDS3786.1.
    PIRiB43568. FGHUB.
    RefSeqiNP_001171670.1. NM_001184741.1.
    NP_005132.2. NM_005141.4.
    UniGeneiHs.300774.

    Genome annotation databases

    EnsembliENST00000302068; ENSP00000306099; ENSG00000171564.
    GeneIDi2244.
    KEGGihsa:2244.
    UCSCiuc003ioa.4. human.

    Polymorphism databases

    DMDMi399492.

    Keywords - Coding sequence diversityi

    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
    J00129 mRNA. Translation: AAA52429.1 .
    J00131 , J00130 Genomic DNA. Translation: AAA98115.1 .
    J00132 Genomic DNA. Translation: AAA98116.1 .
    J00133 mRNA. No translation available.
    M64983 Genomic DNA. Translation: AAA18024.2 .
    AF388026 Genomic DNA. Translation: AAK62470.1 .
    AK312972 mRNA. Translation: BAG35810.1 .
    CH471056 Genomic DNA. Translation: EAX04932.1 .
    BC007030 mRNA. Translation: AAH07030.1 . Sequence problems.
    BC106760 mRNA. Translation: AAI06761.1 .
    BC107766 mRNA. Translation: AAI07767.1 .
    AH002694 Genomic DNA. Translation: AAA52445.1 .
    X05018 Genomic DNA. Translation: CAA28674.1 .
    CCDSi CCDS3786.1.
    PIRi B43568. FGHUB.
    RefSeqi NP_001171670.1. NM_001184741.1.
    NP_005132.2. NM_005141.4.
    UniGenei Hs.300774.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FZA X-ray 2.90 B/E 164-491 [» ]
    1FZB X-ray 2.90 B/E 164-491 [» ]
    1FZC X-ray 2.30 B/E 164-491 [» ]
    1FZE X-ray 3.00 B/E 164-491 [» ]
    1FZF X-ray 2.70 B/E 164-491 [» ]
    M/N/S/T 45-48 [» ]
    1FZG X-ray 2.50 B/E 164-491 [» ]
    1LT9 X-ray 2.80 B/E 179-491 [» ]
    1LTJ X-ray 2.80 B/E 179-491 [» ]
    1N86 X-ray 3.20 B/E 164-491 [» ]
    I/J 45-51 [» ]
    1N8E X-ray 4.50 B/E 164-491 [» ]
    1RE3 X-ray 2.45 B/E 179-491 [» ]
    1RE4 X-ray 2.70 B/E 179-491 [» ]
    1RF0 X-ray 2.81 B/E 179-491 [» ]
    1RF1 X-ray 2.53 B/E 179-491 [» ]
    2A45 X-ray 3.65 H/K 45-135 [» ]
    2FFD X-ray 2.89 B/E 179-491 [» ]
    2H43 X-ray 2.70 B/E 164-491 [» ]
    2HLO X-ray 2.60 B/E 164-491 [» ]
    2HOD X-ray 2.90 B/E/H/K 164-491 [» ]
    2HPC X-ray 2.90 B/E/H/K 164-491 [» ]
    2OYH X-ray 2.40 B/E 179-491 [» ]
    2OYI X-ray 2.70 B/E 179-491 [» ]
    2Q9I X-ray 2.80 B/E 164-491 [» ]
    2XNX X-ray 3.30 B/E/H/K 164-491 [» ]
    2XNY X-ray 7.50 B/E 164-491 [» ]
    2Z4E X-ray 2.70 B/E 164-489 [» ]
    3BVH X-ray 2.60 B/E 191-488 [» ]
    3E1I X-ray 2.30 B/E 164-491 [» ]
    3GHG X-ray 2.90 B/E/H/K 31-491 [» ]
    3H32 X-ray 3.60 B/E 31-488 [» ]
    3HUS X-ray 3.04 B/E 179-491 [» ]
    ProteinModelPortali P02675.
    SMRi P02675. Positions 88-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108535. 19 interactions.
    DIPi DIP-385N.
    IntActi P02675. 16 interactions.
    STRINGi 9606.ENSP00000306099.

    Chemistry

    BindingDBi P02675.
    ChEMBLi CHEMBL2364709.
    DrugBanki DB00364. Sucralfate.

    PTM databases

    PhosphoSitei P02675.

    Polymorphism databases

    DMDMi 399492.

    2D gel databases

    DOSAC-COBS-2DPAGE P02675.
    OGPi P02675.
    REPRODUCTION-2DPAGE IPI00298497.
    P02675.
    SWISS-2DPAGE P02675.
    UCD-2DPAGE P02675.

    Proteomic databases

    MaxQBi P02675.
    PaxDbi P02675.
    PeptideAtlasi P02675.
    PRIDEi P02675.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302068 ; ENSP00000306099 ; ENSG00000171564 .
    GeneIDi 2244.
    KEGGi hsa:2244.
    UCSCi uc003ioa.4. human.

    Organism-specific databases

    CTDi 2244.
    GeneCardsi GC04P155484.
    HGNCi HGNC:3662. FGB.
    HPAi CAB008624.
    HPA001900.
    HPA001901.
    MIMi 134830. gene.
    202400. phenotype.
    neXtProti NX_P02675.
    Orphaneti 98880. Familial afibrinogenemia.
    98881. Familial dysfibrinogenemia.
    248408. Familial hypodysfibrinogenemia.
    101041. Familial hypofibrinogenemia.
    PharmGKBi PA163.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277105.
    HOGENOMi HOG000059561.
    HOVERGENi HBG005707.
    InParanoidi P02675.
    KOi K03904.
    OMAi TIHNGMF.
    OrthoDBi EOG7X9G60.
    PhylomeDBi P02675.
    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 FGB. human.
    EvolutionaryTracei P02675.
    GeneWikii Fibrinogen_beta_chain.
    GenomeRNAii 2244.
    NextBioi 35459926.
    PMAP-CutDB P02675.
    PROi P02675.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02675.
    Bgeei P02675.
    CleanExi HS_FGB.
    Genevestigatori P02675.

    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 complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen."
      Chung D.W., Que B.G., Rixon M.W., Mace M. Jr., Davie E.W.
      Biochemistry 22:3244-3250(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "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 [GENOMIC DNA].
    3. "Nucleotide sequences of the three genes coding for human fibrinogen."
      Chung D.W., Harris J.E., Davie E.W.
      (In) Liu C.Y., Chien S. (eds.); Fibrinogen, thrombosis, coagulation and fibrinolysis, pp.39-48, Plenum Press, New York (1991)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-100; HIS-170; LEU-265 AND LYS-478.
    5. "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].
      Tissue: Mammary gland.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Liver.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
    9. "Characterization of the 5'-flanking region for the human fibrinogen beta gene."
      Huber P., Dalmon J., Courtois G., Laurent M., Assouline Z., Marguerie G.
      Nucleic Acids Res. 15:1615-1625(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
    10. "Amino acid sequence of the beta chain of human fibrinogen."
      Watt K.W.K., Takagi T., Doolittle R.F.
      Biochemistry 18:68-76(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-491, PYROGLUTAMATE FORMATION AT GLN-31.
    11. "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 31-491, GLYCOSYLATION AT ASN-394.
    12. "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: PROTEIN SEQUENCE OF 31-148, DISULFIDE BONDS.
    13. "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 31-44.
    14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 45-53.
      Tissue: Platelet.
    15. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 54-72; 164-178 AND 225-239, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    16. Cited for: REVIEW, DISULFIDE BONDS.
    17. "Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments."
      Gaardlund B., Hessel B., Marguerie G., Murano G., Blombaeck B.
      Eur. J. Biochem. 77:595-610(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    18. "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.
    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. "The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis."
      Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C., Argraves W.S.
      J. Biol. Chem. 270:19458-19464(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBLN1.
    21. "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-394.
      Tissue: Plasma.
    22. "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-394.
      Tissue: Platelet.
    23. "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-394.
      Tissue: Liver.
    24. "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.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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 164-491.
    27. "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 164-491.
    28. "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 164-491.
    29. "A polymorphism at B beta 448 of fibrinogen identified during structural studies of fibrinogen Baltimore II."
      Schmelzer C.H., Ebert R.F., Bell W.R.
      Thromb. Res. 52:173-177(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BALTIMORE-2 LYS-478.
    30. "A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine."
      Yoshida N., Wada H., Morita K., Hirata H., Matsuda M., Yamazumi K., Asakura S., Shirakawa S.
      Blood 77:1958-1963(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ISE ARG-45.
    31. "Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala-->Thr."
      Koopman J., Haverkate F., Lord S.T., Grimbergen J., Mannucci P.M.
      J. Clin. Invest. 90:238-244(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NAPLES THR-98.
    32. "Abnormal fibrinogens IJmuiden (B beta Arg14-->Cys) and Nijmegen (B beta Arg44-->Cys) form disulfide-linked fibrinogen-albumin complexes."
      Koopman J., Haverkate F., Grimbergen J., Engesser L., Novakova I., Kerst A.F.J.A., Lord S.T.
      Proc. Natl. Acad. Sci. U.S.A. 89:3478-3482(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IJMUIDEN CYS-44 AND NIJMEGEN CYS-74.
    33. "Characterization of fibrinogen New York 1. A dysfunctional fibrinogen with a deletion of B beta(9-72) corresponding exactly to exon 2 of the gene."
      Liu C.Y., Koehn J.A., Morgan F.J.
      J. Biol. Chem. 260:4390-4396(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NEW YORK-1 39-GLY--LEU-102 DEL.
    34. Cited for: VARIANTS GLU-2; LEU-265 AND LYS-478.
    35. "Missense mutations in the human beta fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion."
      Duga S., Asselta R., Santagostino E., Zeinali S., Simonic T., Malcovati M., Mannucci P.M., Tenchini M.L.
      Blood 95:1336-1341(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CONGENITAL AFIBRINOGENEMIA ARG-383 AND ASP-430.
    36. "The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers."
      Lounes K.C., Lefkowitz J.B., Henschen-Edman A.H., Coates A.I., Hantgan R.R., Lord S.T.
      Blood 98:661-666(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CONGENITAL AFIBRINOGENEMIA CYS-196.

    Entry informationi

    Entry nameiFIBB_HUMAN
    AccessioniPrimary (citable) accession number: P02675
    Secondary accession number(s): A0JLR9
    , B2R7G3, Q32Q65, Q3KPF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 179 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