FIBA_MOUSE - dbPTM
FIBA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIBA_MOUSE
UniProt AC E9PV24
Protein Name Fibrinogen alpha chain
Gene Name Fga {ECO:0000312|MGI:MGI:1316726}
Organism Mus musculus (Mouse).
Sequence Length 789
Subcellular Localization Secreted .
Protein Description Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. [PubMed: 7649481 In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization]
Protein Sequence MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSDGNRNPGTTGSDGTGDWGTGSPRPGSDSGNFRPANPNWGVFSEFGDSSSPATRKEYHTGKAVTSKGDKELLIGKEKVTSSGTSTTHRSCSKTITKTVTGPDGRREVVKEVITSDDGSDCGDATELDISHSFSGSLDELSERHPDLSGFFDNHFGLISPNFKEFGSKTHSDSDILTNIEDPSSHVPEFSSSSKTSTVKKQVTKTYKMADEAGSEAHREGETRNTKRGRARARPTRDCDDVLQTQTSGAQNGIFSIKPPGSSKVFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYRGTAGDALVQGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVVWVPFRGADYSLRAVRMKIRPLVGQ
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
46PhosphorylationRVVERHQSQCKDSDW
HHHHHCHHHCCCCCC
22817900
72UbiquitinationCPSGCRMKGLIDEAN
CCCCCCCCHHHHHHC
22790023
90UbiquitinationTNRINKLKNSLFDFQ
HHHHHHHHHHHHHHH
22790023
92PhosphorylationRINKLKNSLFDFQRN
HHHHHHHHHHHHHHC
22817900
103PhosphorylationFQRNNKDSNSLTRNI
HHHCCCCCCHHHHHH
23737553
105PhosphorylationRNNKDSNSLTRNIME
HCCCCCCHHHHHHHH
23737553
203UbiquitinationQDYEGHQKQLQQVIA
HHHCHHHHHHHHHHH
22790023
211UbiquitinationQLQQVIAKELLPTKD
HHHHHHHHHHCCCCC
22790023
217UbiquitinationAKELLPTKDRQYLPA
HHHHCCCCCHHHCCC
22790023
250UbiquitinationQEAPPEWKALTEMRQ
HHCCHHHHHHHHHHH
22790023
271PhosphorylationRPGKDGGSRGDSPGD
CCCCCCCCCCCCCCC
23140645
275PhosphorylationDGGSRGDSPGDSRGD
CCCCCCCCCCCCCCC
23140645
279PhosphorylationRGDSPGDSRGDSRGD
CCCCCCCCCCCCCCC
23375375
283PhosphorylationPGDSRGDSRGDFATR
CCCCCCCCCCCCCCC
27742792
295UbiquitinationATRGPGSKAENPTNP
CCCCCCCCCCCCCCC
22790023
307PhosphorylationTNPGPGGSGYWRPGN
CCCCCCCCCCCCCCC
27742792
327PhosphorylationDGNRNPGTTGSDGTG
CCCCCCCCCCCCCCC
21743459
328PhosphorylationGNRNPGTTGSDGTGD
CCCCCCCCCCCCCCC
21743459
330PhosphorylationRNPGTTGSDGTGDWG
CCCCCCCCCCCCCCC
21743459
333PhosphorylationGTTGSDGTGDWGTGS
CCCCCCCCCCCCCCC
21743459
338PhosphorylationDGTGDWGTGSPRPGS
CCCCCCCCCCCCCCC
20469934
387AcetylationAVTSKGDKELLIGKE
EECCCCCCEEEEECE
23954790
387UbiquitinationAVTSKGDKELLIGKE
EECCCCCCEEEEECE
22790023
393UbiquitinationDKELLIGKEKVTSSG
CCEEEEECEEECCCC
22790023
397PhosphorylationLIGKEKVTSSGTSTT
EEECEEECCCCCCCC
20469934
398PhosphorylationIGKEKVTSSGTSTTH
EECEEECCCCCCCCC
20469934
399PhosphorylationGKEKVTSSGTSTTHR
ECEEECCCCCCCCCC
24719451
401PhosphorylationEKVTSSGTSTTHRSC
EEECCCCCCCCCCCC
20469934
402PhosphorylationKVTSSGTSTTHRSCS
EECCCCCCCCCCCCC
20469934
414UbiquitinationSCSKTITKTVTGPDG
CCCCEEEEEEECCCC
22790023
432PhosphorylationVVKEVITSDDGSDCG
HEEEEECCCCCCCCC
29472430
436PhosphorylationVITSDDGSDCGDATE
EECCCCCCCCCCCCE
29472430
442PhosphorylationGSDCGDATELDISHS
CCCCCCCCEEECCCC
29472430
447PhosphorylationDATELDISHSFSGSL
CCCEEECCCCCCCCH
22817900
449PhosphorylationTELDISHSFSGSLDE
CEEECCCCCCCCHHH
30352176
451PhosphorylationLDISHSFSGSLDELS
EECCCCCCCCHHHHH
30352176
453PhosphorylationISHSFSGSLDELSER
CCCCCCCCHHHHHHH
29472430
458PhosphorylationSGSLDELSERHPDLS
CCCHHHHHHHCCCCC
29472430
476PhosphorylationDNHFGLISPNFKEFG
CCCCCEECCCHHHHC
24719451
485UbiquitinationNFKEFGSKTHSDSDI
CHHHHCCCCCCCCCC
22790023
490PhosphorylationGSKTHSDSDILTNIE
CCCCCCCCCCCCCCC
24719451
494PhosphorylationHSDSDILTNIEDPSS
CCCCCCCCCCCCCCC
23567750
500PhosphorylationLTNIEDPSSHVPEFS
CCCCCCCCCCCCCCC
29472430
501PhosphorylationTNIEDPSSHVPEFSS
CCCCCCCCCCCCCCC
29472430
504HydroxylationEDPSSHVPEFSSSSK
CCCCCCCCCCCCCCC
-
507PhosphorylationSSHVPEFSSSSKTST
CCCCCCCCCCCCCHH
29472430
508PhosphorylationSHVPEFSSSSKTSTV
CCCCCCCCCCCCHHH
29472430
509PhosphorylationHVPEFSSSSKTSTVK
CCCCCCCCCCCHHHH
29472430
510PhosphorylationVPEFSSSSKTSTVKK
CCCCCCCCCCHHHHH
29472430
531PhosphorylationKMADEAGSEAHREGE
HHHHHHHHHHHHCCC
27742792
539PhosphorylationEAHREGETRNTKRGR
HHHHCCCCCCCHHHC
20469934
609N-linked_GlycosylationMDGSLNFNRTWQDYK
CCCCCCCCCCHHHHH
-
615PhosphorylationFNRTWQDYKRGFGSL
CCCCHHHHHCCCCCC
28978645

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

Oops, there are no upstream regulatory protein records of FIBA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIBA_MOUSE !!

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 FIBA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FIBA_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIBA_MOUSE

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Related Literatures of Post-Translational Modification

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