FIBG_HUMAN - dbPTM
FIBG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIBG_HUMAN
UniProt AC P02679
Protein Name Fibrinogen gamma chain
Gene Name FGG
Organism Homo sapiens (Human).
Sequence Length 453
Subcellular Localization Secreted .
Protein Description Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways..
Protein Sequence MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
44PhosphorylationLDERFGSYCPTTCGI
EECCCCCCCCCCCCH		11.65-
44NitrationLDERFGSYCPTTCGI
EECCCCCCCCCCCCH		11.65-
48PhosphorylationFGSYCPTTCGIADFL
CCCCCCCCCCHHHHH		8.2228857561
58PhosphorylationIADFLSTYQTKVDKD
HHHHHHHHHHHHHHH		15.71-
58NitrationIADFLSTYQTKVDKD
HHHHHHHHHHHHHHH		15.71-
68PhosphorylationKVDKDLQSLEDILHQ
HHHHHHHHHHHHHHH		40.8126091039
78N-linked_GlycosylationDILHQVENKTSEVKQ
HHHHHHHCCHHHHHH		54.7918780401
78N-linked_GlycosylationDILHQVENKTSEVKQ
HHHHHHHCCHHHHHH		54.7918780401
80PhosphorylationLHQVENKTSEVKQLI
HHHHHCCHHHHHHHH		41.5225219547
81PhosphorylationHQVENKTSEVKQLIK
HHHHCCHHHHHHHHH		41.8425219547
93PhosphorylationLIKAIQLTYNPDESS
HHHHHHCCCCCCCCC		12.6025219547
93O-linked_GlycosylationLIKAIQLTYNPDESS
HHHHHHCCCCCCCCC		12.60OGP
94NitrationIKAIQLTYNPDESSK
HHHHHCCCCCCCCCC		33.03-
94PhosphorylationIKAIQLTYNPDESSK
HHHHHCCCCCCCCCC		33.0325219547
99O-linked_GlycosylationLTYNPDESSKPNMID
CCCCCCCCCCCCCCC		51.55OGP
99PhosphorylationLTYNPDESSKPNMID
CCCCCCCCCCCCCCC		51.5528857561
100PhosphorylationTYNPDESSKPNMIDA
CCCCCCCCCCCCCCH		50.5128857561
100O-linked_GlycosylationTYNPDESSKPNMIDA
CCCCCCCCCCCCCCH		50.51OGP
109PhosphorylationPNMIDAATLKSRKML
CCCCCHHHHHHHHHH		36.1221949786
109O-linked_GlycosylationPNMIDAATLKSRKML
CCCCCHHHHHHHHHH		36.12OGP
125PhosphorylationEIMKYEASILTHDSS
HHHHHHHHHHHCHHH		13.2428857561
131PhosphorylationASILTHDSSIRYLQE
HHHHHCHHHHHHHHH		21.7628857561
132PhosphorylationSILTHDSSIRYLQEI
HHHHCHHHHHHHHHH		19.6928857561
132O-linked_GlycosylationSILTHDSSIRYLQEI
HHHHCHHHHHHHHHH		19.69OGP
135NitrationTHDSSIRYLQEIYNS
HCHHHHHHHHHHHCC		15.86-
140NitrationIRYLQEIYNSNNQKI
HHHHHHHHCCCCCEE		16.28-
140PhosphorylationIRYLQEIYNSNNQKI
HHHHHHHHCCCCCEE		16.2821253578
142PhosphorylationYLQEIYNSNNQKIVN
HHHHHHCCCCCEEEE		21.8628857561
190PhosphorylationANKGAKQSGLYFIKP
HHHCCCCCCEEEEEE		30.0228857561
193PhosphorylationGAKQSGLYFIKPLKA
CCCCCCEEEEEECCC		13.5428857561
196AcetylationQSGLYFIKPLKANQQ
CCCEEEEEECCCCCE		34.1022507986
231AcetylationLDGSVDFKKNWIQYK
CCCCCCHHHCEEEEE		40.5127178108
232AcetylationDGSVDFKKNWIQYKE
CCCCCHHHCEEEEEC		58.477672083
245PhosphorylationKEGFGHLSPTGTTEF
ECCCCCCCCCCCEEE		18.1028857561
247PhosphorylationGFGHLSPTGTTEFWL
CCCCCCCCCCEEEEE		43.7328857561
263PhosphorylationNEKIHLISTQSAIPY
CCEEEEEECCCCCCE		27.1028857561
270NitrationSTQSAIPYALRVELE
ECCCCCCEEEEEEEE		16.50-
283PhosphorylationLEDWNGRTSTADYAM
EECCCCCCCCCCEEE		31.6528857561
284PhosphorylationEDWNGRTSTADYAMF
ECCCCCCCCCCEEEE		21.9028857561
285PhosphorylationDWNGRTSTADYAMFK
CCCCCCCCCCEEEEE		23.9628857561
285O-linked_GlycosylationDWNGRTSTADYAMFK
CCCCCCCCCCEEEEE		23.96OGP
288PhosphorylationGRTSTADYAMFKVGP
CCCCCCCEEEEECCC		9.4821253578
299AcetylationKVGPEADKYRLTYAY
ECCCCHHHEEEEEEE		39.0422507986
300PhosphorylationVGPEADKYRLTYAYF
CCCCHHHEEEEEEEE		16.0521253578
300NitrationVGPEADKYRLTYAYF
CCCCHHHEEEEEEEE		16.05-
304NitrationADKYRLTYAYFAGGD
HHHEEEEEEEECCCC		12.14-
306NitrationKYRLTYAYFAGGDAG
HEEEEEEEECCCCCC		5.42-
334N-linked_GlycosylationDKFFTSHNGMQFSTW
CCCCCCCCCEEEEEE		47.61UniProtKB CARBOHYD
365S-nitrosylationSGWWMNKCHAGHLNG
CCEEECCCCCCEECC		1.9525040305
374PhosphorylationAGHLNGVYYQGGTYS
CCEECCEEECCCEEC		7.47-
375PhosphorylationGHLNGVYYQGGTYSK
CEECCEEECCCEECC		9.77-
379PhosphorylationGVYYQGGTYSKASTP
CEEECCCEECCCCCC		31.29-
380PhosphorylationVYYQGGTYSKASTPN
EEECCCEECCCCCCC		16.0821253578
382AcetylationYQGGTYSKASTPNGY
ECCCEECCCCCCCCC		35.6230585659
384PhosphorylationGGTYSKASTPNGYDN
CCEECCCCCCCCCCC		48.4028857561
389NitrationKASTPNGYDNGIIWA
CCCCCCCCCCCEEEE		16.93-
399AcetylationGIIWATWKTRWYSMK
CEEEEEECCCCEECC		24.6930585653
406AcetylationKTRWYSMKKTTMKII
CCCCEECCCCEEEEE		40.8230585665
411GlycationSMKKTTMKIIPFNRL
ECCCCEEEEEECCCE		35.08-
419O-linked_GlycosylationIIPFNRLTIGEGQQH
EEECCCEECCCCCCC		24.57OGP
444SulfationEHPAETEYDSLYPED
CCCCCCCCCCCCCCC		20.46-
444SulfationEHPAETEYDSLYPED
CCCCCCCCCCCCCCC		20.4611307817
446PhosphorylationPAETEYDSLYPEDDL
CCCCCCCCCCCCCCC		28.9727251275
448PhosphorylationETEYDSLYPEDDL--
CCCCCCCCCCCCC--		14.4511307817
448SulfationETEYDSLYPEDDL--
CCCCCCCCCCCCC--		14.4511307817
448SulfationETEYDSLYPEDDL--
CCCCCCCCCCCCC--		14.45-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
68SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIBG_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FIBG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIBA_HUMANFGAphysical
12356313
FIBB_HUMANFGBphysical
12356313
FIBG_HUMANFGGphysical
12501189
FIBG_HUMANFGGphysical
9333233
CHD9_HUMANCHD9physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
202400Congenital afibrinogenemia (CAFBN)
616004Dysfibrinogenemia, congenital (DYSFIBRIN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIBG_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
Sulfation
ReferencePubMed
"The amino acid sequence in fibrin responsible for high affinitythrombin binding.";
Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.;
Thromb. Haemost. 85:470-474(2001).
Cited for: SULFATION AT TYR-444 AND TYR-448.

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