##gff-version 3
Q61644	UniProtKB	Chain	1	441	.	.	.	ID=PRO_0000161793;Note=Protein kinase C and casein kinase substrate in neurons protein 1	
Q61644	UniProtKB	Domain	10	280	.	.	.	Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077	
Q61644	UniProtKB	Domain	382	441	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
Q61644	UniProtKB	Region	297	380	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q61644	UniProtKB	Coiled coil	23	272	.	.	.	.	
Q61644	UniProtKB	Compositional bias	306	320	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q61644	UniProtKB	Compositional bias	327	359	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q61644	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0W5	
Q61644	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0W5	
Q61644	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0W5	
Q61644	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q61644	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q61644	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0W5	
Q61644	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q61644	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0W5	
Q61644	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18034455;Dbxref=PMID:18034455	
Q61644	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q61644	UniProtKB	Modified residue	427	427	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q61644	UniProtKB	Mutagenesis	122	123	.	.	.	Note=Increases membrane tubulation. IM->FF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404169;Dbxref=PMID:20404169	
Q61644	UniProtKB	Mutagenesis	122	123	.	.	.	Note=Abolishes membrane tubulation. No effect on phospholipid binding. IM->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404169;Dbxref=PMID:20404169	
Q61644	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Abolishes membrane tubulation%3B when associated with E-130. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404169;Dbxref=PMID:20404169	
Q61644	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Abolishes membrane tubulation%3B when associated with E-127. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404169;Dbxref=PMID:20404169	
Q61644	UniProtKB	Mutagenesis	145	148	.	.	.	Note=Abolishes membrane tubulation. KKMK->EEME;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404169;Dbxref=PMID:20404169	
Q61644	UniProtKB	Mutagenesis	400	400	.	.	.	Note=Impairs interaction with DNM1. E->R	
Q61644	UniProtKB	Mutagenesis	434	434	.	.	.	Note=Abolishes interaction with DNM1%2C MAPT%2C SYNJ1 and WASL. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11082044,ECO:0000269|PubMed:20404169,ECO:0000269|PubMed:23035120;Dbxref=PMID:11082044,PMID:20404169,PMID:23035120	
Q61644	UniProtKB	Turn	19	22	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	23	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	75	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	106	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Helix	127	175	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	182	253	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	255	257	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	260	274	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Helix	277	288	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3V	
Q61644	UniProtKB	Beta strand	386	389	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Beta strand	396	400	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Beta strand	408	411	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Beta strand	417	424	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Beta strand	430	434	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W	
Q61644	UniProtKB	Helix	435	437	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X3W