Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9ASQ

Human Drosha, DGCR8 and SRSF3 in complex with Pri-let-7f1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001530	molecular_function	lipopolysaccharide binding
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0004525	molecular_function	ribonuclease III activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006364	biological_process	rRNA processing
A	0006396	biological_process	RNA processing
A	0010468	biological_process	regulation of gene expression
A	0010586	biological_process	miRNA metabolic process
A	0010628	biological_process	positive regulation of gene expression
A	0014069	cellular_component	postsynaptic density
A	0016787	molecular_function	hydrolase activity
A	0017151	molecular_function	DEAD/H-box RNA helicase binding
A	0031047	biological_process	regulatory ncRNA-mediated gene silencing
A	0031053	biological_process	primary miRNA processing
A	0031054	biological_process	pre-miRNA processing
A	0035196	biological_process	miRNA processing
A	0042254	biological_process	ribosome biogenesis
A	0042803	molecular_function	protein homodimerization activity
A	0045589	biological_process	regulation of regulatory T cell differentiation
A	0046332	molecular_function	SMAD binding
A	0046872	molecular_function	metal ion binding
A	0050727	biological_process	regulation of inflammatory response
A	0050829	biological_process	defense response to Gram-negative bacterium
A	0050830	biological_process	defense response to Gram-positive bacterium
A	0070412	molecular_function	R-SMAD binding
A	0070877	cellular_component	microprocessor complex
A	0070878	molecular_function	primary miRNA binding
A	0098978	cellular_component	glutamatergic synapse
A	2000628	biological_process	regulation of miRNA metabolic process
B	0003723	molecular_function	RNA binding
B	0003725	molecular_function	double-stranded RNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006974	biological_process	DNA damage response
B	0014069	cellular_component	postsynaptic density
B	0016604	cellular_component	nuclear body
B	0020037	molecular_function	heme binding
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0031053	biological_process	primary miRNA processing
B	0035861	cellular_component	site of double-strand break
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0070877	cellular_component	microprocessor complex
B	0070878	molecular_function	primary miRNA binding
B	0072091	biological_process	regulation of stem cell proliferation
B	0098978	cellular_component	glutamatergic synapse
B	0140517	molecular_function	protein-RNA adaptor activity
B	2000633	biological_process	positive regulation of pre-miRNA processing
C	0003723	molecular_function	RNA binding
C	0003725	molecular_function	double-stranded RNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006974	biological_process	DNA damage response
C	0014069	cellular_component	postsynaptic density
C	0016604	cellular_component	nuclear body
C	0020037	molecular_function	heme binding
C	0030674	molecular_function	protein-macromolecule adaptor activity
C	0031053	biological_process	primary miRNA processing
C	0035861	cellular_component	site of double-strand break
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0070877	cellular_component	microprocessor complex
C	0070878	molecular_function	primary miRNA binding
C	0072091	biological_process	regulation of stem cell proliferation
C	0098978	cellular_component	glutamatergic synapse
C	0140517	molecular_function	protein-RNA adaptor activity
C	2000633	biological_process	positive regulation of pre-miRNA processing
H	0003676	molecular_function	nucleic acid binding
H	0003723	molecular_function	RNA binding
H	0003729	molecular_function	mRNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005654	cellular_component	nucleoplasm
H	0005737	cellular_component	cytoplasm
H	0006397	biological_process	mRNA processing
H	0006406	biological_process	mRNA export from nucleus
H	0008380	biological_process	RNA splicing
H	0016607	cellular_component	nuclear speck
H	0031053	biological_process	primary miRNA processing
H	0036002	molecular_function	pre-mRNA binding
H	0043274	molecular_function	phospholipase binding
H	0045292	biological_process	mRNA cis splicing, via spliceosome
H	0048024	biological_process	regulation of mRNA splicing, via spliceosome
H	0051028	biological_process	mRNA transport
H	0070878	molecular_function	primary miRNA binding
H	0160134	molecular_function	protein-RNA sequence-specific adaptor activity
H	1990825	molecular_function	sequence-specific mRNA binding
H	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PROSITE/UniProt

site_id	PS00517
Number of Residues	9
Details	RNASE_3_1 Ribonuclease III family signature. ERLEFLGDA

Chain	Residue	Details
A	GLU966-ALA974
A	GLN1144-SER1152

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
H	MET1
C	CYS352
A	THR586
A	GLU598
A	GLU646
A	LEU713
A	GLU717
A	LEU1063

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
H	SER5
B	SER92
C	SER35
C	SER92

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
H	LYS23
C	SER95

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332

Chain	Residue	Details
B	SER271
C	SER271

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER275
C	SER275

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q9EQM6

Chain	Residue	Details
B	THR279
C	THR279

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
B	THR371
C	THR371

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER373
C	SER373

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER377
C	SER377

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine; by ATM => ECO:0000269\|PubMed:34188037

Chain	Residue	Details
B	SER677
C	SER677

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
B	LYS424
C	LYS424

site_id	SWS_FT_FI12
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25755297

Chain	Residue	Details
B	LYS707
C	LYS707

site_id	SWS_FT_FI13
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
B	LYS500
C	LYS500

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)