dbPTM

COF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COF2_HUMAN
UniProt AC	Q9Y281
Protein Name	Cofilin-2
Gene Name	CFL2
Organism	Homo sapiens (Human).
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. Its F-actin depolymerization activity is regulated by association with CSPR3. [PubMed: 19752190 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 (By similarity]
Protein Sequence	MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVTVND ------CCCCCEECH	18.26	20068231
3	Phosphorylation	-----MASGVTVNDE -----CCCCCEECHH	32.28	29255136
6	Phosphorylation	--MASGVTVNDEVIK --CCCCCEECHHHHH	19.67	20639409
13	Ubiquitination	TVNDEVIKVFNDMKV EECHHHHHHHCCCCC	46.05	21890473
19	Sumoylation	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	-
19	Ubiquitination	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	21890473
19	Acetylation	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	132827
19	Sumoylation	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	-
19	Methylation	IKVFNDMKVRKSSTQ HHHHCCCCCCCCCCH	41.57	-
23	Phosphorylation	NDMKVRKSSTQEEIK CCCCCCCCCCHHHHH	28.22	26437602
24	Phosphorylation	DMKVRKSSTQEEIKK CCCCCCCCCHHHHHH	36.83	22798277
25	Phosphorylation	MKVRKSSTQEEIKKR CCCCCCCCHHHHHHH	47.28	26437602
41	Phosphorylation	KAVLFCLSDDKRQII CEEEEEECCCCCEEH	44.97	21815630
44	Acetylation	LFCLSDDKRQIIVEE EEEECCCCCEEHHHH	51.71	26051181
44	Malonylation	LFCLSDDKRQIIVEE EEEECCCCCEEHHHH	51.71	26320211
68	Phosphorylation	GDTVEDPYTSFVKLL CCCCCCCCCCCEEEE	27.60	-
73	Ubiquitination	DPYTSFVKLLPLNDC CCCCCCEEEEECCCH	42.15	-
82	Phosphorylation	LPLNDCRYALYDATY EECCCHHHHEEECCC	13.80	21712546
85	Phosphorylation	NDCRYALYDATYETK CCHHHHEEECCCCCC	8.72	27273156
88	Phosphorylation	RYALYDATYETKESK HHHEEECCCCCCCCC	20.99	27273156
89	Phosphorylation	YALYDATYETKESKK HHEEECCCCCCCCCC	24.26	25159151
91	Phosphorylation	LYDATYETKESKKED EEECCCCCCCCCCCC	29.69	27273156
92	Ubiquitination	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	21890473
92	Acetylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	22648311
94	Phosphorylation	ATYETKESKKEDLVF CCCCCCCCCCCCEEE	51.05	26356563
95	Ubiquitination	TYETKESKKEDLVFI CCCCCCCCCCCEEEE	62.36	-
96	Methylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	-
96	Acetylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	129575
96	Trimethylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	-
96	Ubiquitination	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	21890473
108	Phosphorylation	FIFWAPESAPLKSKM EEEECCCCCCCCCCE	33.84	28450419
112	Sumoylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
112	Sumoylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
112	Ubiquitination	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	21890473
113	Phosphorylation	PESAPLKSKMIYASS CCCCCCCCCEEEECC	34.83	28270605
114	Sumoylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
114	Sumoylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
114	Acetylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	22648305
114	Ubiquitination	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	21890473
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCEEEECCHHHH	9.27	27273156
119	Phosphorylation	KSKMIYASSKDAIKK CCCEEEECCHHHHHH	22.43	26356563
120	Phosphorylation	SKMIYASSKDAIKKK CCEEEECCHHHHHHH	26.78	26356563
121	Sumoylation	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	-
121	Ubiquitination	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	-
121	Sumoylation	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	-
121	Acetylation	KMIYASSKDAIKKKF CEEEECCHHHHHHHH	49.00	8273343
125	Acetylation	ASSKDAIKKKFTGIK ECCHHHHHHHHCCCC	52.19	8273353
129	Phosphorylation	DAIKKKFTGIKHEWQ HHHHHHHCCCCEEEE	47.04	-
144	Ubiquitination	VNGLDDIKDRSTLGE ECCCCCCCCCCCHHH	54.83	21890473
160	Phosphorylation	LGGNVVVSLEGKPL- HCCEEEEEECCEEC-	14.75	-

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	LIMK1	P53667	PhosphoELM
24	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IPYR_HUMAN	PPA1	physical	22939629
COF2_HUMAN	CFL2	physical	25416956
CAP2_HUMAN	CAP2	physical	25416956
DEST_HUMAN	DSTN	physical	25416956
POTE1_HUMAN	POT1	physical	25416956
GABT_HUMAN	ABAT	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
AL4A1_HUMAN	ALDH4A1	physical	26344197
CATA_HUMAN	CAT	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LDH6A_HUMAN	LDHAL6A	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
NDKB_HUMAN	NME2	physical	26344197
ACTB_HUMAN	ACTB	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610687	Nemaline myopathy 7 (NEM7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of COF2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-92, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASSSPECTROMETRY.	15951569 [Abstract]

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