2F9D

2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000387	biological_process	spliceosomal snRNP assembly
A	0000388	biological_process	spliceosome conformational change to release U4 (or U4atac) and U1 (or U11)
A	0000398	biological_process	mRNA splicing, via spliceosome
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0003729	molecular_function	mRNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005681	cellular_component	spliceosomal complex
A	0005684	cellular_component	U2-type spliceosomal complex
A	0005689	cellular_component	U12-type spliceosomal complex
A	0006397	biological_process	mRNA processing
A	0008380	biological_process	RNA splicing
A	1903241	biological_process	U2-type prespliceosome assembly
B	0000387	biological_process	spliceosomal snRNP assembly
B	0000388	biological_process	spliceosome conformational change to release U4 (or U4atac) and U1 (or U11)
B	0000398	biological_process	mRNA splicing, via spliceosome
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0003729	molecular_function	mRNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005681	cellular_component	spliceosomal complex
B	0005684	cellular_component	U2-type spliceosomal complex
B	0005689	cellular_component	U12-type spliceosomal complex
B	0006397	biological_process	mRNA processing
B	0008380	biological_process	RNA splicing
B	1903241	biological_process	U2-type prespliceosome assembly
P	0000245	biological_process	spliceosomal complex assembly
P	0003729	molecular_function	mRNA binding
Q	0000245	biological_process	spliceosomal complex assembly
Q	0003729	molecular_function	mRNA binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	150
Details	Domain: {"description":"RRM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00176","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	26
Details	Region: {"description":"Interaction with pre-mRNA branch site"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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