dbPTM

FSCN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FSCN1_HUMAN
UniProt AC	Q16658
Protein Name	Fascin
Gene Name	FSCN1
Organism	Homo sapiens (Human).
Sequence Length	493
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Cell projection, filopodium . Cell projection, invadopodium . Cell projection, microvillus . Cell junction . In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol (PubMed:21706
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..
Protein Sequence	MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTANGTAEA ------CCCCCCEEE	28.91	22223895
23	Phosphorylation	LINCGNKYLTAEAFG EEECCCCEEEHHHHC	17.18	28152594
25	Phosphorylation	NCGNKYLTAEAFGFK ECCCCEEEHHHHCCE	21.25	28152594
36	Phosphorylation	FGFKVNASASSLKKK HCCEEECCCHHHCCC	24.39	30266825
38	Phosphorylation	FKVNASASSLKKKQI CEEECCCHHHCCCEE	33.44	30266825
39	Phosphorylation	KVNASASSLKKKQIW EEECCCHHHCCCEEE	43.88	23401153
41	Acetylation	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	25953088
41	Ubiquitination	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	-
41	Malonylation	NASASSLKKKQIWTL ECCCHHHCCCEEEEE	60.93	30639696
42	Ubiquitination	ASASSLKKKQIWTLE CCCHHHCCCEEEEEC	56.02	-
43	Ubiquitination	SASSLKKKQIWTLEQ CCHHHCCCEEEEECC	45.49	-
43	Malonylation	SASSLKKKQIWTLEQ CCHHHCCCEEEEECC	45.49	26320211
43	Acetylation	SASSLKKKQIWTLEQ CCHHHCCCEEEEECC	45.49	26051181
61	Glutathionylation	EAGSAAVCLRSHLGR CCCCHHHHHHHHHHH	1.93	22555962
69	Phosphorylation	LRSHLGRYLAADKDG HHHHHHHHEEECCCC	10.01	28152594
74	Acetylation	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	23954790
74	Malonylation	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	26320211
74	Ubiquitination	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	-
74	2-Hydroxyisobutyrylation	GRYLAADKDGNVTCE HHHEEECCCCCEEEE	63.91	-
79	Phosphorylation	ADKDGNVTCEREVPG ECCCCCEEEEEEECC	16.79	-
80	Glutathionylation	DKDGNVTCEREVPGP CCCCCEEEEEEECCC	3.95	22555962
111	Phosphorylation	QSEAHRRYFGGTEDR CCHHHHHHCCCCCCH	13.41	25690035
115	Phosphorylation	HRRYFGGTEDRLSCF HHHHCCCCCCHHHEE	34.78	20068231
118	Methylation	YFGGTEDRLSCFAQT HCCCCCCHHHEEEEE	23.44	-
120	Phosphorylation	GGTEDRLSCFAQTVS CCCCCHHHEEEEECC	14.21	20068231
121	Glutathionylation	GTEDRLSCFAQTVSP CCCCHHHEEEEECCH	3.76	22555962
121	S-palmitoylation	GTEDRLSCFAQTVSP CCCCHHHEEEEECCH	3.76	29575903
127	Phosphorylation	SCFAQTVSPAEKWSV HEEEEECCHHHHCEE	23.06	21815630
131	Acetylation	QTVSPAEKWSVHIAM EECCHHHHCEEEEEE	47.04	26051181
138	Sulfoxidation	KWSVHIAMHPQVNIY HCEEEEEECCCEEEE	4.72	30846556
145	Phosphorylation	MHPQVNIYSVTRKRY ECCCEEEEEEECCCE	7.59	29978859
146	Phosphorylation	HPQVNIYSVTRKRYA CCCEEEEEEECCCEE	17.14	29978859
148	Phosphorylation	QVNIYSVTRKRYAHL CEEEEEEECCCEEEC	25.24	29978859
152	Phosphorylation	YSVTRKRYAHLSARP EEEECCCEEECCCCC	11.04	28152594
186	Phosphorylation	LAFQDQRYSVQTADH HHCCCCCCEEECCCC	13.94	21406692
187	Phosphorylation	AFQDQRYSVQTADHR HCCCCCCEEECCCCC	15.22	21406692
190	Phosphorylation	DQRYSVQTADHRFLR CCCCEEECCCCCEEE	31.71	21406692
210	Phosphorylation	VARPEPATGYTLEFR EECCCCCCCEEEEEC	41.24	28152594
212	Phosphorylation	RPEPATGYTLEFRSG CCCCCCCEEEEECCC	12.09	28152594
213	Phosphorylation	PEPATGYTLEFRSGK CCCCCCEEEEECCCC	22.58	28152594
217	Methylation	TGYTLEFRSGKVAFR CCEEEEECCCCEEEE	34.81	-
218	Phosphorylation	GYTLEFRSGKVAFRD CEEEEECCCCEEEEC	48.57	27251275
220	Malonylation	TLEFRSGKVAFRDCE EEEECCCCEEEECCC	31.47	26320211
230	Phosphorylation	FRDCEGRYLAPSGPS EECCCCCEECCCCCC	20.33	28152594
234	Phosphorylation	EGRYLAPSGPSGTLK CCCEECCCCCCCCEE	58.70	23403867
237	Phosphorylation	YLAPSGPSGTLKAGK EECCCCCCCCEECCC	48.19	23403867
239	Phosphorylation	APSGPSGTLKAGKAT CCCCCCCCEECCCEE	29.44	23403867
241	2-Hydroxyisobutyrylation	SGPSGTLKAGKATKV CCCCCCEECCCEEEC	55.73	-
241	Malonylation	SGPSGTLKAGKATKV CCCCCCEECCCEEEC	55.73	26320211
241	Ubiquitination	SGPSGTLKAGKATKV CCCCCCEECCCEEEC	55.73	21906983
241	Acetylation	SGPSGTLKAGKATKV CCCCCCEECCCEEEC	55.73	26051181
247	Ubiquitination	LKAGKATKVGKDELF EECCCEEECCHHHHH	54.58	-
250	Ubiquitination	GKATKVGKDELFALE CCEEECCHHHHHHHH	51.52	-
250	Acetylation	GKATKVGKDELFALE CCEEECCHHHHHHHH	51.52	26051181
260	S-palmitoylation	LFALEQSCAQVVLQA HHHHHHHHHHHHHHH	2.83	29575903
274	Phosphorylation	AANERNVSTRQGMDL HHHHCCCCCCCCCCC	22.78	-
279	Sulfoxidation	NVSTRQGMDLSANQD CCCCCCCCCCCCCCC	3.38	30846556
282	Phosphorylation	TRQGMDLSANQDEET CCCCCCCCCCCCCCC	22.40	21406692
289	Phosphorylation	SANQDEETDQETFQL CCCCCCCCCHHEEEE	40.72	21406692
293	Phosphorylation	DEETDQETFQLEIDR CCCCCHHEEEEEEEC	15.85	21406692
302	Phosphorylation	QLEIDRDTKKCAFRT EEEEECCCCEEEEEE	33.04	21406692
303	Acetylation	LEIDRDTKKCAFRTH EEEECCCCEEEEEEC	50.58	26051181
304	Acetylation	EIDRDTKKCAFRTHT EEECCCCEEEEEECC	32.65	24471161
313	Ubiquitination	AFRTHTGKYWTLTAT EEEECCCCEEEEEEC	38.48	-
313	Acetylation	AFRTHTGKYWTLTAT EEEECCCCEEEEEEC	38.48	26051181
314	Phosphorylation	FRTHTGKYWTLTATG EEECCCCEEEEEECC	12.64	28152594
329	Phosphorylation	GVQSTASSKNASCYF CEECCCCCCCCEEEE	27.71	28857561
333	Phosphorylation	TASSKNASCYFDIEW CCCCCCCEEEEEEEE	20.81	28152594
335	Phosphorylation	SSKNASCYFDIEWRD CCCCCEEEEEEEECC	11.20	28152594
353	Methylation	TLRASNGKFVTSKKN EEEECCCEEEEECCC	40.69	-
353	Acetylation	TLRASNGKFVTSKKN EEEECCCEEEEECCC	40.69	26051181
353	Ubiquitination	TLRASNGKFVTSKKN EEEECCCEEEEECCC	40.69	-
353	"N6,N6-dimethyllysine"	TLRASNGKFVTSKKN EEEECCCEEEEECCC	40.69	-
359	Ubiquitination	GKFVTSKKNGQLAAS CEEEEECCCCEEEEE	67.11	-
397	S-nitrosylation	GEHGFIGCRKVTGTL CCCCEECEEEEEEEE	3.04	19483679
397	S-nitrosocysteine	GEHGFIGCRKVTGTL CCCCEECEEEEEEEE	3.04	-
399	Sumoylation	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	25218447
399	Sumoylation	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	-
399	Ubiquitination	HGFIGCRKVTGTLDA CCEECEEEEEEEEEC	48.50	-
401	Phosphorylation	FIGCRKVTGTLDANR EECEEEEEEEEECCC	27.73	23403867
403	Phosphorylation	GCRKVTGTLDANRSS CEEEEEEEEECCCCC	16.46	25850435
411	Phosphorylation	LDANRSSYDVFQLEF EECCCCCCEEEEEEE	19.85	21712546
426	Ubiquitination	NDGAYNIKDSTGKYW CCCCEEEECCCCCEE	41.82	-
432	Phosphorylation	IKDSTGKYWTVGSDS EECCCCCEEEECCCC	13.99	24719451
447	Phosphorylation	AVTSSGDTPVDFFFE CCCCCCCCCEEEEEE	28.83	24719451
458	Phosphorylation	FFFEFCDYNKVAIKV EEEEECCCCEEEEEE	20.33	24719451
464	Ubiquitination	DYNKVAIKVGGRYLK CCCEEEEEECCEECC	25.70	-
469	Phosphorylation	AIKVGGRYLKGDHAG EEEECCEECCCCCCC	18.95	28152594
471	Ubiquitination	KVGGRYLKGDHAGVL EECCEECCCCCCCEE	54.05	19608861
471	Acetylation	KVGGRYLKGDHAGVL EECCEECCCCCCCEE	54.05	19608861
471	2-Hydroxyisobutyrylation	KVGGRYLKGDHAGVL EECCEECCCCCCCEE	54.05	-
478	Ubiquitination	KGDHAGVLKASAETV CCCCCCEEEEECEEC	3.62	-
479	Ubiquitination	GDHAGVLKASAETVD CCCCCEEEEECEECC	37.58	21906983
484	Phosphorylation	VLKASAETVDPASLW EEEEECEECCHHHHC	29.90	-

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	P17252	GPS
39	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
39	S	Phosphorylation	Kinase	PKC	-	Uniprot
39	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
39	S	Phosphorylation		8999969
Phosphorylation at Ser-39 inhibits actin-binding.

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 FSCN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPCA_HUMAN	PRKCA	physical	14532112
ACTS_HUMAN	ACTA1	physical	8999969
SEP11_HUMAN	SEPT11	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
ASSY_HUMAN	ASS1	physical	26344197
COTL1_HUMAN	COTL1	physical	26344197
QOR_HUMAN	CRYZ	physical	26344197
FUBP1_HUMAN	FUBP1	physical	26344197
MIF_HUMAN	MIF	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
TKT_HUMAN	TKT	physical	26344197
SMUF1_HUMAN	SMURF1	physical	27879315

Drug and Disease Associations

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

Regulatory Network of FSCN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Identification of an actin binding region and a protein kinase Cphosphorylation site on human fascin."; Ono S., Yamakita Y., Yamashiro S., Matsudaira P.T., Gnarra J.R.,Obinata T., Matsumura F.; J. Biol. Chem. 272:2527-2533(1997). Cited for: PHOSPHORYLATION AT SER-39, AND MUTAGENESIS OF SER-39.	8999969 [Abstract]

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