##gff-version 3
P18760	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|Ref.3,ECO:0007744|PubMed:19131326;Dbxref=PMID:19131326	
P18760	UniProtKB	Chain	2	166	.	.	.	ID=PRO_0000214900;Note=Cofilin-1	
P18760	UniProtKB	Domain	4	153	.	.	.	Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
P18760	UniProtKB	Motif	30	34	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P18760	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30550596,ECO:0000269|Ref.3,ECO:0007744|PubMed:19131326;Dbxref=PMID:19131326,PMID:30550596	
P18760	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:25107909,ECO:0000269|PubMed:30550596,ECO:0007744|PubMed:16452087,ECO:0007744|PubMed:19131326;Dbxref=PMID:16452087,PMID:19131326,PMID:25107909,PMID:30550596	
P18760	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19131326;Dbxref=PMID:19131326	
P18760	UniProtKB	Modified residue	13	13	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30550596;Dbxref=PMID:30550596	
P18760	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17947660;Dbxref=PMID:17947660	
P18760	UniProtKB	Modified residue	73	73	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30550596;Dbxref=PMID:30550596	
P18760	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:15592455,ECO:0007744|PubMed:17947660;Dbxref=PMID:15592455,PMID:17947660	
P18760	UniProtKB	Modified residue	144	144	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30550596,ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079,PMID:30550596	
P18760	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23528	
P18760	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Decreases abundance and increases disorganization of zygotic subcortical F-actin%2C disrupts centralization of the mitotic spindle and leads to asymmetric two-cell embryos. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25208553;Dbxref=PMID:25208553	
P18760	UniProtKB	Mutagenesis	3	3	.	.	.	Note=No effect on zygotic subcortical F-actin abundance and centralization of the mitotic spindle. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25208553;Dbxref=PMID:25208553