3BAP

Crystal Structure of the 25 kDa Subunit of Human Cleavage Factor Im

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003682	molecular_function	chromatin 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	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005847	cellular_component	mRNA cleavage and polyadenylation specificity factor complex
A	0005849	cellular_component	mRNA cleavage factor complex
A	0006397	biological_process	mRNA processing
A	0010608	biological_process	post-transcriptional regulation of gene expression
A	0016604	cellular_component	nuclear body
A	0030154	biological_process	cell differentiation
A	0031124	biological_process	mRNA 3'-end processing
A	0034451	cellular_component	centriolar satellite
A	0035925	molecular_function	mRNA 3'-UTR AU-rich region binding
A	0042382	cellular_component	paraspeckles
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042826	molecular_function	histone deacetylase binding
A	0051262	biological_process	protein tetramerization
A	0051290	biological_process	protein heterotetramerization
A	0110104	biological_process	mRNA alternative polyadenylation
A	0180010	biological_process	co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
A	1900365	biological_process	obsolete positive regulation of mRNA polyadenylation
A	2000738	biological_process	positive regulation of stem cell differentiation
A	2000975	biological_process	positive regulation of pro-B cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 2

Chain	Residue
A	GLU81
A	LYS105
A	LEU106
A	LYS172
A	ILE211
A	HOH237
A	HOH317

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Interaction with RNA => ECO:0000269|PubMed:20479262, ECO:0000312|PDB:3MDG, ECO:0000312|PDB:3MDI

Chain	Residue	Details
A	GLU55
A	ARG63

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|Ref.6

Chain	Residue	Details
A	SER2

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315

Chain	Residue	Details
A	ARG15

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17172643, ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS23

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS29
A	LYS56

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR40

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