CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001994
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibrinogen alpha chain 
Protein Synonyms/Alias
 Fibrinopeptide A; Fibrinogen alpha chain 
Gene Name
 FGA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
148LKRKVIEKVQHIQLLglycation[1]
210QLEQVIAKDLLPSRDacetylation[2]
227HLPLIKMKPVPDLVPacetylation[2]
227HLPLIKMKPVPDLVPglycation[1]
243NFKSQLQKVPPEWKAacetylation[2]
448ELRTGKEKVTSGSTTacetylation[2]
476VIGPDGHKEVTKEVVacetylation[2]
558SGIFTNTKESSSHHPacetylation[2]
581GKSSSYSKQFTSSTSacetylation[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. 
Sequence Annotation
 DOMAIN 623 864 Fibrinogen C-terminal.
 REGION 36 38 Alpha-chain polymerization, binding
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 412 412 Phosphothreonine.
 MOD_RES 609 609 Phosphoserine.
 CARBOHYD 320 320 O-linked (GalNAc...).
 CARBOHYD 351 351 O-linked (GalNAc...).
 CARBOHYD 453 453 N-linked (GlcNAc...); in variant Caracas-
 CARBOHYD 686 686 N-linked (GlcNAc...).
 DISULFID 47 47 Interchain.
 DISULFID 55 55 Interchain (with C-95 in beta chain).
 DISULFID 64 64 Interchain (with C-49 in gamma chain).
 DISULFID 68 68 Interchain (with C-106 in beta chain).
 DISULFID 180 180 Interchain (with C-165 in gamma chain).
 DISULFID 184 184 Interchain (with C-223 in beta chain).
 DISULFID 461 491
 CROSSLNK 322 322 Isoglutamyl lysine isopeptide (Lys-Gln)
 CROSSLNK 347 347 Isoglutamyl lysine isopeptide (Gln-Lys)
 CROSSLNK 385 385 Isoglutamyl lysine isopeptide (Gln-Lys)
 CROSSLNK 527 527 Isoglutamyl lysine isopeptide (Lys-Gln)
 CROSSLNK 558 558 Isoglutamyl lysine isopeptide (Lys-Gln)
 CROSSLNK 575 575 Isoglutamyl lysine isopeptide (Lys-Gln)
 CROSSLNK 581 581 Isoglutamyl lysine isopeptide (Lys-Gln)
 CROSSLNK 599 599 Isoglutamyl lysine isopeptide (Lys-Gln)  
Keyword
 3D-structure; Alternative splicing; Amyloid; Amyloidosis; Blood coagulation; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hemostasis; Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 866 AA 
Protein Sequence
MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW 60
NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA 120
NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC 180
RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ 240
LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 300
GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW 360
NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV 420
SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK 480
EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF 540
VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 600
YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI KLPGSSKIFS 660
VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN DEGEGEFWLG NDYLHLLTQR 720
GSVLRVELED WAGNEAYAEY HFRVGSEAEG YALQVSSYEG TAGDALIEGS VEEGAEYTSH 780
NNMQFSTFDR DADQWEENCA EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG 840
VVWVSFRGAD YSLRAVRMKI RPLVTQ 866 
Gene Ontology
 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.
 IPR021996; Fibrinogen_aC.
 IPR020837; Fibrinogen_CS. 
Pfam
 PF08702; Fib_alpha
 PF12160; Fibrinogen_aC
 PF00147; Fibrinogen_C 
SMART
 SM00186; FBG 
PROSITE
 PS00514; FIBRINOGEN_C_1
 PS51406; FIBRINOGEN_C_2 
PRINTS