##gff-version 3
P31001	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02542	
P31001	UniProtKB	Chain	2	469	.	.	.	ID=PRO_0000063773;Note=Desmin	
P31001	UniProtKB	Domain	107	415	.	.	.	Note=IF rod;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01188	
P31001	UniProtKB	Region	2	108	.	.	.	Note=Head	
P31001	UniProtKB	Region	109	140	.	.	.	Note=Coil 1A	
P31001	UniProtKB	Region	141	150	.	.	.	Note=Linker 1	
P31001	UniProtKB	Region	151	251	.	.	.	Note=Coil 1B	
P31001	UniProtKB	Region	252	267	.	.	.	Note=Linker 12	
P31001	UniProtKB	Region	267	414	.	.	.	Note=Interaction with NEB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17661	
P31001	UniProtKB	Region	268	286	.	.	.	Note=Coil 2A	
P31001	UniProtKB	Region	287	294	.	.	.	Note=Linker 2	
P31001	UniProtKB	Region	295	411	.	.	.	Note=Coil 2B	
P31001	UniProtKB	Region	412	469	.	.	.	Note=Tail	
P31001	UniProtKB	Region	437	452	.	.	.	Note=Interaction with CRYAB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17661	
P31001	UniProtKB	Site	353	353	.	.	.	Note=Stutter	
P31001	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17661	
P31001	UniProtKB	Modified residue	16	16	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
P31001	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphothreonine%3B by AURKB and ROCK1;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P31001	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P31001	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:27565725,ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079,PMID:27565725	
P31001	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P31001	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:27565725,ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079,PMID:27565725	
P31001	UniProtKB	Modified residue	37	37	.	.	.	Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
P31001	UniProtKB	Modified residue	37	37	.	.	.	Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
P31001	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48675	
P31001	UniProtKB	Modified residue	58	58	.	.	.	Note=ADP-ribosylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48675	
P31001	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079	
P31001	UniProtKB	Modified residue	70	70	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
P31001	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphothreonine%3B by ROCK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphothreonine%3B by ROCK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17661	
P31001	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48675	
P31001	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48675	
P31001	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48675	
P31001	UniProtKB	Modified residue	423	423	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P31001	UniProtKB	Mutagenesis	7	7	.	.	.	Note=Reduced phosphorylation. Almost complete loss of phosphorylation%3B when associated with A-28 and A-32. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Reduced phosphorylation. Almost complete loss of phosphorylation%3B when associated with A-7 and A-32. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Reduced phosphorylation and formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis. Almost complete loss of phosphorylation%3B when associated with A-7 and A-28. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis%3B when associated with A-60 and A-76. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Mutagenesis	60	60	.	.	.	Note=Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis%3B when associated with A-76. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis%3B when associated with A-32 and A-76. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis%3B when associated with A-60. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis%3B when associated with A-32 and A-60. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27565725;Dbxref=PMID:27565725	
P31001	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Increases protein decay. forms subsarcolemmal aggregates. Changes the subcellular localization and turnover of its direct%2C extrasarcomeric binding partners. Knockin mice develop age-dependent desmin-positive protein aggregation pathology%2C skeletal muscle weakness%2C dilated cardiomyopathy%2C as well as cardiac arrhythmias and conduction defects. Knockin mice exhibit altered axial myofibrillar lattice arrangement in fast- and slow-twitch muscle fibers%2C increased axial stiffness and stretch-induced vulnerability in soleus muscle fiber bundles%2C reduced Ca(2+)-sensitivity in heterozygous fiber bundles and increased Ca(2+)-sensitivity in homozygous fiber bundles. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25394388;Dbxref=PMID:25394388