CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001995
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibrinogen beta chain 
Protein Synonyms/Alias
 Fibrinopeptide B; Fibrinogen beta chain 
Gene Name
 FGB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
264IQPDSSVKPYRVYCDacetylation[1]
295GSVDFGRKWDPYKQGglycation[2]
353DWKGDKVKAHYGGFTglycation[2]
Reference
 [1] Acetylation and glycation of fibrinogen in vitro occur at specific lysine residues in a concentration dependent manner: a mass spectrometric and isotope labeling study.
 Svensson J, Bergman AC, Adamson U, Blombäck M, Wallén H, Jörneskog G.
 Biochem Biophys Res Commun. 2012 May 4;421(2):335-42. [PMID: 22507986]
 [2] Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes.
 Zhang Q, Tang N, Schepmoes AA, Phillips LS, Smith RD, Metz TO.
 J Proteome Res. 2008 May;7(5):2025-32. [PMID: 18396901
Functional Description
 Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. 
Sequence Annotation
 DOMAIN 232 488 Fibrinogen C-terminal.
 REGION 45 47 Beta-chain polymerization, binding distal
 MOD_RES 31 31 Pyrrolidone carboxylic acid.
 CARBOHYD 394 394 N-linked (GlcNAc...).
 DISULFID 95 95 Interchain (with C-55 in alpha chain).
 DISULFID 106 106 Interchain (with C-68 in alpha chain).
 DISULFID 110 110 Interchain (with C-45 in gamma chain).
 DISULFID 223 223 Interchain (with C-184 in alpha chain).
 DISULFID 227 227 Interchain (with C-161 in gamma chain).
 DISULFID 231 316
 DISULFID 241 270
 DISULFID 424 437  
Keyword
 3D-structure; Blood coagulation; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hemostasis; Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 491 AA 
Protein Sequence
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD KKREEAPSLR 60
PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP DLGVLCPTGC QLQEALLQQE 120
RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL LKDLWQKRQK QVKDNENVVN EYSSELEKHQ 180
LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE 240
CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK 300
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT 360
VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP 420
RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM 480
SMKIRPFFPQ Q 491 
Gene Ontology
 GO:0072562; C:blood microparticle; IEA:Compara.
 GO:0005938; C:cell cortex; IEA:Compara.
 GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
 GO:0005577; C:fibrinogen complex; TAS:ProtInc.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0051258; P:protein polymerization; IEA:InterPro.
 GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
 GO:0007165; P:signal transduction; IEA:InterPro. 
Interpro
 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. 
Pfam
 PF08702; Fib_alpha
 PF00147; Fibrinogen_C 
SMART
 SM00186; FBG 
PROSITE
 PS00514; FIBRINOGEN_C_1
 PS51406; FIBRINOGEN_C_2 
PRINTS