Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XWU

CRYSTAL STRUCTURE OF IMPORTIN 13 - UBC9 COMPLEX

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000795	cellular_component	synaptonemal complex
A	0001221	molecular_function	transcription coregulator binding
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005643	cellular_component	nuclear pore
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0007059	biological_process	chromosome segregation
A	0007084	biological_process	mitotic nuclear membrane reassembly
A	0008134	molecular_function	transcription factor binding
A	0016604	cellular_component	nuclear body
A	0016605	cellular_component	PML body
A	0016740	molecular_function	transferase activity
A	0016925	biological_process	protein sumoylation
A	0019789	molecular_function	SUMO transferase activity
A	0019899	molecular_function	enzyme binding
A	0030335	biological_process	positive regulation of cell migration
A	0036211	biological_process	protein modification process
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043398	molecular_function	HLH domain binding
A	0044388	molecular_function	small protein activating enzyme binding
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050804	biological_process	modulation of chemical synaptic transmission
A	0051168	biological_process	nuclear export
A	0051301	biological_process	cell division
A	0061656	molecular_function	SUMO conjugating enzyme activity
A	0071535	molecular_function	RING-like zinc finger domain binding
A	0098685	cellular_component	Schaffer collateral - CA1 synapse
A	0098978	cellular_component	glutamatergic synapse
A	0099523	cellular_component	presynaptic cytosol
A	0099524	cellular_component	postsynaptic cytosol
A	0106068	cellular_component	SUMO ligase complex
A	1990234	cellular_component	transferase complex
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006606	biological_process	protein import into nucleus
B	0006886	biological_process	intracellular protein transport
B	0015031	biological_process	protein transport
B	0031267	molecular_function	small GTPase binding

Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL

Chain	Residue	Details
A	PHE82-LEU97

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	153
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Region: {"description":"Interaction with SUMO1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Site: {"description":"Interaction with RANBP2"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Substrate binding"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"22509284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	30
Details	Repeat: {"description":"HEAT 1","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	66
Details	Domain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	32
Details	Repeat: {"description":"HEAT 2","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	40
Details	Repeat: {"description":"HEAT 3","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	37
Details	Repeat: {"description":"HEAT 5","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	32
Details	Repeat: {"description":"HEAT 6","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	49
Details	Repeat: {"description":"HEAT 7","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	42
Details	Repeat: {"description":"HEAT 8","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	63
Details	Repeat: {"description":"HEAT 9","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	35
Details	Repeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	34
Details	Repeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	38
Details	Repeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	45
Details	Repeat: {"description":"HEAT 14","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	40
Details	Repeat: {"description":"HEAT 15","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	34
Details	Repeat: {"description":"HEAT 16","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	42
Details	Repeat: {"description":"HEAT 17","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	30
Details	Repeat: {"description":"HEAT 18","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	33
Details	Repeat: {"description":"HEAT 19","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	34
Details	Repeat: {"description":"HEAT 20","evidences":[{"source":"PubMed","id":"20122403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)