CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001996
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibrinogen gamma chain 
Protein Synonyms/Alias
  
Gene Name
 FGG 
Gene Synonyms/Alias
 PRO2061 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
196QSGLYFIKPLKANQQacetylation[1]
299KVGPEADKYRLTYAYacetylation[1]
411SMKKTTMKIIPFNRLglycation[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 170 416 Fibrinogen C-terminal.
 REGION 400 422 Gamma-chain polymerization, binding amino
 REGION 423 437 Platelet aggregation and Staphylococcus
 MOD_RES 444 444 Sulfotyrosine.
 MOD_RES 448 448 Sulfotyrosine.
 CARBOHYD 78 78 N-linked (GlcNAc...).
 CARBOHYD 334 334 N-linked (GlcNAc...); in variant Asahi.
 DISULFID 34 34 Interchain (with C-35).
 DISULFID 35 35 Interchain (with C-34).
 DISULFID 45 45 Interchain (with C-110 in beta chain).
 DISULFID 49 49 Interchain (with C-64 in alpha chain).
 DISULFID 161 161 Interchain (with C-227 in beta chain).
 DISULFID 165 165 Interchain (with C-180 in alpha chain).
 DISULFID 179 208
 DISULFID 352 365
 CROSSLNK 424 424 Isoglutamyl lysine isopeptide (Gln-Lys)
 CROSSLNK 432 432 Isoglutamyl lysine isopeptide (Lys-Gln)  
Keyword
 3D-structure; Alternative splicing; Blood coagulation; Calcium; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hemostasis; Isopeptide bond; Metal-binding; Polymorphism; Reference proteome; Secreted; Signal; Sulfation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 453 AA 
Protein Sequence
MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 60
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 120
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 180
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 240
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 300
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 360
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 420
GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL 453 
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 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