Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PX9

The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000166	molecular_function	nucleotide binding
B	0000795	cellular_component	synaptonemal complex
B	0001221	molecular_function	transcription coregulator binding
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005635	cellular_component	nuclear envelope
B	0005643	cellular_component	nuclear pore
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0007059	biological_process	chromosome segregation
B	0007084	biological_process	mitotic nuclear membrane reassembly
B	0008134	molecular_function	transcription factor binding
B	0016604	cellular_component	nuclear body
B	0016605	cellular_component	PML body
B	0016740	molecular_function	transferase activity
B	0016925	biological_process	protein sumoylation
B	0019789	molecular_function	SUMO transferase activity
B	0019899	molecular_function	enzyme binding
B	0030335	biological_process	positive regulation of cell migration
B	0036211	biological_process	protein modification process
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0043398	molecular_function	HLH domain binding
B	0044388	molecular_function	small protein activating enzyme binding
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050804	biological_process	modulation of chemical synaptic transmission
B	0051168	biological_process	nuclear export
B	0051301	biological_process	cell division
B	0061656	molecular_function	SUMO conjugating enzyme activity
B	0071535	molecular_function	RING-like zinc finger domain binding
B	0098685	cellular_component	Schaffer collateral - CA1 synapse
B	0098978	cellular_component	glutamatergic synapse
B	0099523	cellular_component	presynaptic cytosol
B	0099524	cellular_component	postsynaptic cytosol
B	0106068	cellular_component	SUMO ligase complex
B	1990234	cellular_component	transferase complex

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
B	PHE82-LEU97

site_id	PS00865
Number of Residues	9
Details	UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP

Chain	Residue	Details
A	PRO171-PRO179

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	29
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164921","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
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_FI8
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","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 SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}

Chain

Residue

Details

site_id	SWS_FT_FI11
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_FI12
Number of Residues	5
Details	Region: {"description":"Interaction with SUMO1"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Site: {"description":"Interaction with RANBP2"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Site: {"description":"Substrate binding"}

Chain

Residue

Details

site_id	SWS_FT_FI16
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_FI17
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_FI18
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_FI19
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_FI20
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_FI21
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

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