FIBB_MOUSE - dbPTM
FIBB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIBB_MOUSE
UniProt AC Q8K0E8
Protein Name Fibrinogen beta chain
Gene Name Fgb
Organism Mus musculus (Mouse).
Sequence Length 481
Subcellular Localization Secreted .
Protein Description Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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. 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 immune response via both innate and T-cell mediated pathways..
Protein Sequence MRHLWLLLLLCVFSVQTQAADDDYDEPTDSLDARGHRPVDRRKEEPPSLRPAPPPISGGGYRARPAKATANQKKVERRPPDAGGCLHADTDMGVLCPTGCTLQQTLLNQERPIKSSIAELNNNIQSVSDTSSVTFQYLTLLKDMWKKKQAQVKENENVINEYSSILEDQRLYIDETVNDNIPLNLRVLRSILEDLRSKIQKLESDISAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDTSIKPYRVYCDMKTENGGWTVIQNRQDGSVDFGRKWDPYKKGFGNIATNEDAKKYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEASKYQVSVNKYKGTAGNALMDGASQLVGENRTMTIHNGMFFSTYDRDNDGWVTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGLYSWDMSKHGTDDGVVWMNWKGSWYSMRRMSMKIRPFFPQQ
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
43UbiquitinationHRPVDRRKEEPPSLR
CCCCCCCCCCCCCCC
68.29-
237UbiquitinationECEEIIRKGGETSEM
HHHHHHHCCCCCCEE
61.94-
254UbiquitinationIQPDTSIKPYRVYCD
ECCCCCCCCEEEEEE
35.45-
263UbiquitinationYRVYCDMKTENGGWT
EEEEEEEECCCCCEE
39.16-
303AcetylationIATNEDAKKYCGLPG
CCCCHHHHHHCCCCC
57.517619175
303UbiquitinationIATNEDAKKYCGLPG
CCCCHHHHHHCCCCC
57.51-
303SuccinylationIATNEDAKKYCGLPG
CCCCHHHHHHCCCCC
57.5123954790
343UbiquitinationDWKGDKVKAHYGGFT
CCCCCEEEEEECCEE
34.88-
364UbiquitinationKYQVSVNKYKGTAGN
CEEEECEECCCCHHH
46.30-
384N-linked_GlycosylationASQLVGENRTMTIHN
HHHHHCCCCEEEEEC
38.50-
386PhosphorylationQLVGENRTMTIHNGM
HHHCCCCEEEEECCE
30.1925293948
388PhosphorylationVGENRTMTIHNGMFF
HCCCCEEEEECCEEE
20.6225293948
396PhosphorylationIHNGMFFSTYDRDND
EECCEEEECEECCCC
18.1325293948
397PhosphorylationHNGMFFSTYDRDNDG
ECCEEEECEECCCCC
25.0425293948
398PhosphorylationNGMFFSTYDRDNDGW
CCEEEECEECCCCCE
14.0525293948
416UbiquitinationDPRKQCSKEDGGGWW
CCCCCCCCCCCCCCC
68.40-

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 FIBB_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIBB_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 FIBB_MOUSE !!

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

Oops, there are no PPI records of FIBB_MOUSE !!

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

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Related Literatures of Post-Translational Modification

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