dbPTM

COF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COF1_MOUSE
UniProt AC	P18760
Protein Name	Cofilin-1
Gene Name	Cfl1
Organism	Mus musculus (Mouse).
Sequence Length	166
Subcellular Localization	Nucleus matrix . Cytoplasm, cytoskeleton . Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side . Cell projection, lamellipodium membrane Peripheral membrane protein Cytoplasmic side . Cell projection, lamellipodium .
Protein Description	Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. [PubMed: 11809832 Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity Required for neural tube morphogenesis and neural crest cell migration]
Protein Sequence	MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPENAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVAVSD ------CCCCEEECC	18.26	19131326
3	Phosphorylation	-----MASGVAVSDG -----CCCCEEECCC	32.28	26824392
8	Phosphorylation	MASGVAVSDGVIKVF CCCCEEECCCEEEEE	20.93	27742792
13	Acetylation	AVSDGVIKVFNDMKV EECCCEEEEECCCCC	38.07	22826441
19	Succinylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	23806337
19	Acetylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	23806337
19	Malonylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	26320211
19	Ubiquitination	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	-
23	Phosphorylation	NDMKVRKSSTPEEVK CCCCCCCCCCHHHHH	28.96	25521595
24	Phosphorylation	DMKVRKSSTPEEVKK CCCCCCCCCHHHHHH	51.52	25521595
25	Phosphorylation	MKVRKSSTPEEVKKR CCCCCCCCHHHHHHH	41.64	25521595
31	Ubiquitination	STPEEVKKRKKAVLF CCHHHHHHHHCEEEE	74.71	-
33	Acetylation	PEEVKKRKKAVLFCL HHHHHHHHCEEEEEC	54.70	22826441
34	Acetylation	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	22826441
39	S-nitrosylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	24895380
39	S-nitrosocysteine	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	-
39	Glutathionylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	24333276
39	S-palmitoylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	28526873
41	Phosphorylation	KAVLFCLSEDKKNII CEEEEECCCCCCEEE	44.95	26824392
44	Ubiquitination	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	-
44	Malonylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	26320211
44	Succinylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	23806337
44	Acetylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	23806337
45	Ubiquitination	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	-
45	Acetylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	22826441
45	Malonylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	26320211
53	Acetylation	NIILEEGKEILVGDV EEEECCCCEEEECCC	44.88	22826441
63	Phosphorylation	LVGDVGQTVDDPYTT EECCCCCCCCCCCCC	21.70	22499769
68	Phosphorylation	GQTVDDPYTTFVKML CCCCCCCCCCHHEEC	25.96	22499769
69	Phosphorylation	QTVDDPYTTFVKMLP CCCCCCCCCHHEECC	21.10	22499769
70	Phosphorylation	TVDDPYTTFVKMLPD CCCCCCCCHHEECCC	22.16	22499769
73	Ubiquitination	DPYTTFVKMLPDKDC CCCCCHHEECCCCCC	30.45	-
73	Acetylation	DPYTTFVKMLPDKDC CCCCCHHEECCCCCC	30.45	23954790
78	Malonylation	FVKMLPDKDCRYALY HHEECCCCCCCHHEE	57.71	26320211
78	Acetylation	FVKMLPDKDCRYALY HHEECCCCCCCHHEE	57.71	22826441
78	Ubiquitination	FVKMLPDKDCRYALY HHEECCCCCCCHHEE	57.71	-
80	S-nitrosocysteine	KMLPDKDCRYALYDA EECCCCCCCHHEEEC	4.40	-
80	S-nitrosylation	KMLPDKDCRYALYDA EECCCCCCCHHEEEC	4.40	24926564
80	Glutathionylation	KMLPDKDCRYALYDA EECCCCCCCHHEEEC	4.40	24333276
82	Phosphorylation	LPDKDCRYALYDATY CCCCCCCHHEEECCC	13.80	30550596
85	Phosphorylation	KDCRYALYDATYETK CCCCHHEEECCCCCC	8.72	20116462
88	Phosphorylation	RYALYDATYETKESK CHHEEECCCCCCCCC	20.99	25263469
89	Phosphorylation	YALYDATYETKESKK HHEEECCCCCCCCCC	24.26	25263469
91	Phosphorylation	LYDATYETKESKKED EEECCCCCCCCCCCC	29.69	24899341
92	Ubiquitination	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	-
92	Malonylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	26320211
92	Acetylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	23806337
92	Succinylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	23806337
95	Ubiquitination	TYETKESKKEDLVFI CCCCCCCCCCCEEEE	62.36	-
96	Acetylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	129421
112	Ubiquitination	APENAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
114	Succinylation	ENAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	23806337
114	Ubiquitination	ENAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
114	Acetylation	ENAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	23806337
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCEEEECCHHHH	9.27	20116462
119	Phosphorylation	KSKMIYASSKDAIKK CCCEEEECCHHHHHH	22.43	22499769
120	Phosphorylation	SKMIYASSKDAIKKK CCEEEECCHHHHHHH	26.78	22499769
121	Ubiquitination	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	-
121	Succinylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	23806337
121	Acetylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	23806337
127	Acetylation	SKDAIKKKLTGIKHE CHHHHHHHHHCCCHH	46.40	22826441
129	Phosphorylation	DAIKKKLTGIKHELQ HHHHHHHHCCCHHHH	45.82	19060867
132	Acetylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	22826441
139	S-nitrosylation	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	24926564
139	S-nitrosocysteine	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	-
139	Glutathionylation	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	24333276
140	Phosphorylation	HELQANCYEEVKDRC HHHHHCHHHHHHHHC	18.22	26824392
144	Malonylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	26320211
144	Acetylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	23806337
144	Succinylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	23806337
144	Ubiquitination	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	-
148	Phosphorylation	EEVKDRCTLAEKLGG HHHHHHCHHHHHHCC	29.87	19854140
152	Acetylation	DRCTLAEKLGGSAVI HHCHHHHHHCCCEEE	46.99	22826441
156	Phosphorylation	LAEKLGGSAVISLEG HHHHHCCCEEEEECC	19.98	26824392
160	Phosphorylation	LGGSAVISLEGKPL- HCCCEEEEECCEEC-	17.48	26643407
164	Ubiquitination	AVISLEGKPL----- EEEEECCEEC-----	33.50	-

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
3	S	Phosphorylation	Kinase	TESK1	Q63572	PSP
25	T	Phosphorylation	Kinase	ERK2	P63085	PSP
25	T	Phosphorylation	Kinase	ERK1	Q63844	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
3	S	Phosphorylation	16452087
Inactivated by phosphorylation on Ser-3.
3	S	Phosphorylation	16452087
Phosphorylated on Ser-3 in resting cells.
24	S	Phosphorylation	25107909
The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal (By similarity).

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 COF1_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of COF1_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,AND MASS SPECTROMETRY.	16452087 [Abstract]
Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-8, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,AND MASS SPECTROMETRY.	16452087 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-140, AND MASSSPECTROMETRY.	17947660 [Abstract]

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