dbPTM

COF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COF2_MOUSE
UniProt AC	P45591
Protein Name	Cofilin-2
Gene Name	Cfl2
Organism	Mus musculus (Mouse).
Sequence Length	166
Subcellular Localization	Nucleus matrix. Cytoplasm, cytoskeleton. Colocalizes with CSPR3 in the Z line of sarcomeres.
Protein Description	Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere..
Protein Sequence	MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGSVVVSLEGKPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVTVND ------CCCCCEECH	18.26	16452087
3	Phosphorylation	-----MASGVTVNDE -----CCCCCEECHH	32.28	23527152
6	Phosphorylation	--MASGVTVNDEVIK --CCCCCEECHHHHH	19.67	25619855
19	Acetylation	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	132829
19	Ubiquitination	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	-
23	Phosphorylation	NDMKVRKSSTQEEIK CCCCCCCCCCHHHHH	28.22	23684622
24	Phosphorylation	DMKVRKSSTQEEIKK CCCCCCCCCHHHHHH	36.83	23684622
25	Phosphorylation	MKVRKSSTQEEIKKR CCCCCCCCHHHHHHH	47.28	22210690
34	Acetylation	EEIKKRKKAVLFCLS HHHHHHHCEEEEEEC	48.00	22826441
39	S-nitrosylation	RKKAVLFCLSDDKRQ HHCEEEEEECCCCCE	2.88	21278135
39	S-nitrosocysteine	RKKAVLFCLSDDKRQ HHCEEEEEECCCCCE	2.88	-
44	Acetylation	LFCLSDDKRQIIVEE EEEECCCCCEEHHHH	51.71	22826441
44	Ubiquitination	LFCLSDDKRQIIVEE EEEECCCCCEEHHHH	51.71	22790023
82	Phosphorylation	LPLNDCRYALYDATY EECCCHHHHEEECCC	13.80	25367039
85	Phosphorylation	NDCRYALYDATYETK CCHHHHEEECCCCCC	8.72	20116462
88	Phosphorylation	RYALYDATYETKESK HHHEEECCCCCCCCC	20.99	25263469
89	Phosphorylation	YALYDATYETKESKK HHEEECCCCCCCCCC	24.26	25263469
91	Phosphorylation	LYDATYETKESKKED EEECCCCCCCCCCCC	29.69	24899341
92	Ubiquitination	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	-
92	Acetylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	22648313
95	Ubiquitination	TYETKESKKEDLVFI CCCCCCCCCCCEEEE	62.36	-
108	Phosphorylation	FIFWAPESAPLKSKM EEEECCCCCCCCCCE	33.84	-
112	Ubiquitination	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	22790023
114	Ubiquitination	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCEEEECCHHHH	9.27	20116462
119	Phosphorylation	KSKMIYASSKDAIKK CCCEEEECCHHHHHH	22.43	22499769
120	Phosphorylation	SKMIYASSKDAIKKK CCEEEECCHHHHHHH	26.78	22499769
121	Acetylation	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	8273347
121	Ubiquitination	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	-
144	Acetylation	VNGLDDIKDRSTLGE ECCCCCCCCCCCHHH	54.83	23954790
144	Ubiquitination	VNGLDDIKDRSTLGE ECCCCCCCCCCCHHH	54.83	22790023
147	Phosphorylation	LDDIKDRSTLGEKLG CCCCCCCCCHHHHHC	37.81	21454597

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 COF2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
24	S	Phosphorylation		-
The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal.

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 COF2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of COF2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of COF2_MOUSE

Related Literatures of Post-Translational Modification

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 THR-6, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASSSPECTROMETRY.	18034455 [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-89, AND MASSSPECTROMETRY.	17947660 [Abstract]

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