2K7N

Solution structure of the PPIL1 bound to a fragment of SKIP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000398	biological_process	mRNA splicing, via spliceosome
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005681	cellular_component	spliceosomal complex
A	0006397	biological_process	mRNA processing
A	0006457	biological_process	protein folding
A	0008380	biological_process	RNA splicing
A	0016018	molecular_function	cyclosporin A binding
A	0016853	molecular_function	isomerase activity
A	0071007	cellular_component	U2-type catalytic step 2 spliceosome
A	0071013	cellular_component	catalytic step 2 spliceosome
A	0097718	molecular_function	disordered domain specific binding
A	1990403	biological_process	embryonic brain development

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngTkFHRIIkdFMiQGG

Chain	Residue	Details
A	TYR48-GLY65

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:16595688

Chain	Residue	Details
A	HIS54
A	THR70
A	ALA99
A	GLY109
A	THR119
A	LYS125

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER149

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