FSCN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FSCN1_MOUSE
• UniProt AC: Q61553
• Protein Name: Fascin
• Gene Name: Fscn1
• Organism: Mus musculus (Mouse).
• Sequence Length: 493
• Subcellular Localization: Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Cell projection, growth cone . Cell projection, filopodium . Cell projection, invadopodium . Cell projection, microvillus . Cell junction . Colocalized with RUFY3 and F-actin at filipodia of the axonal g
• Protein Description: Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (By similarity)..
• Protein Sequence: MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVALKVGGRYLKGDHAGVLKACAETIDPASLWEY

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
2	Acetylation	------MTANGTAEA ------CCCCCCEEE	28.91	-
36	Phosphorylation	FGFKVNASASSLKKK HCCEEECCCHHHCCC	24.39	24899341
38	Phosphorylation	FKVNASASSLKKKQI CEEECCCHHHCCCEE	33.44	28418008
39	Phosphorylation	KVNASASSLKKKQIW EEECCCHHHCCCEEE	43.88	25521595
41	Acetylation	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	23806337
41	Ubiquitination	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	27667366
41	Succinylation	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	23806337
42	Ubiquitination	ASASSLKKKQIWTLE CCCHHHCCCEEEEEC	56.02	-
43	Acetylation	SASSLKKKQIWTLEQ CCHHHCCCEEEEECC	45.49	22826441
74	Ubiquitination	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	22790023
74	Acetylation	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	23806337
80	S-nitrosocysteine	DKDGNVTCEREVPDG CCCCCEEEEEECCCC	3.95	-
80	S-nitrosylation	DKDGNVTCEREVPDG CCCCCEEEEEECCCC	3.95	21278135
121	S-nitrosocysteine	GTEDRLSCFAQSVSP CCCHHHHHHEEECCH	3.76	-
121	S-nitrosylation	GTEDRLSCFAQSVSP CCCHHHHHHEEECCH	3.76	20925432
125	Phosphorylation	RLSCFAQSVSPAEKW HHHHHEEECCHHHHC	22.57	28066266
127	Phosphorylation	SCFAQSVSPAEKWSV HHHEEECCHHHHCEE	24.52	28066266
187	Phosphorylation	AFQDQRYSVQTSDHR HCCCCCEEEECCCCC	15.22	24719451
190	Phosphorylation	DQRYSVQTSDHRFLR CCCEEEECCCCCEEE	33.69	24719451
220	Ubiquitination	TLEFRSGKVAFRDCE EEEECCCCEEEECCC	31.47	27667366
230	Phosphorylation	FRDCEGRYLAPSGPS EECCCCCEECCCCCC	20.33	28978645
234	Phosphorylation	EGRYLAPSGPSGTLK CCCEECCCCCCCCEE	58.70	28978645
237	Phosphorylation	YLAPSGPSGTLKAGK EECCCCCCCCEECCC	48.19	28978645
239	Phosphorylation	APSGPSGTLKAGKAT CCCCCCCCEECCCEE	29.44	28066266
241	Ubiquitination	SGPSGTLKAGKATKV CCCCCCEECCCEEEC	55.73	22790023
260	S-nitrosylation	LFALEQSCAQVVLQA HHHHHHHHHHHHHHH	2.83	20925432
260	S-nitrosocysteine	LFALEQSCAQVVLQA HHHHHHHHHHHHHHH	2.83	-
313	Acetylation	AFRTHTGKYWTLTAT EEEECCCCEEEEEEE	38.48	22826441
341	S-nitrosylation	CYFDIEWCDRRITLR EEEEEEEECCEEEEE	1.57	20925432
341	S-nitrosocysteine	CYFDIEWCDRRITLR EEEEEEEECCEEEEE	1.57	-
353	Ubiquitination	TLRASNGKFVTAKKN EEEECCCCEEEEEEC	40.69	27667366
358	Ubiquitination	NGKFVTAKKNGQLAA CCCEEEEEECCEEEE	37.09	27667366
399	Succinylation	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	23806337
399	Acetylation	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	23806337
399	Ubiquitination	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	27667366
401	Phosphorylation	FIGCRKVTGTLDANR EECEEEEEEEEECCC	27.73	22324799
403	Phosphorylation	GCRKVTGTLDANRSS CEEEEEEEEECCCCC	16.46	22324799
464	Acetylation	DYNKVALKVGGRYLK CCCCEEEEECCEECC	29.15	22826441
464	Ubiquitination	DYNKVALKVGGRYLK CCCCEEEEECCEECC	29.15	-
471	Acetylation	KVGGRYLKGDHAGVL EECCEECCCCCHHHH	54.05	23806337
471	Ubiquitination	KVGGRYLKGDHAGVL EECCEECCCCCHHHH	54.05	-

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
39	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
39	S	Phosphorylation	Kinase	PKCG	P05129	PSP
39	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
39	S	Phosphorylation	Phosphorylation at Ser-39 inhibits actin-binding.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FSCN1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of FSCN1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.