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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9IF6

Crystal structure of human SUMO E1 with large unit cell parameters in the P1 21 1 space group.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008047molecular_functionenzyme activator activity
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0016567biological_processprotein ubiquitination
A0016925biological_processprotein sumoylation
A0019948molecular_functionSUMO activating enzyme activity
A0031510cellular_componentSUMO activating enzyme complex
A0033235biological_processpositive regulation of protein sumoylation
A0036211biological_processprotein modification process
A0043008molecular_functionATP-dependent protein binding
A0044388molecular_functionsmall protein activating enzyme binding
A0046982molecular_functionprotein heterodimerization activity
A1903749biological_processpositive regulation of protein localization to mitochondrion
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0016925biological_processprotein sumoylation
B0019948molecular_functionSUMO activating enzyme activity
B0031510cellular_componentSUMO activating enzyme complex
B0032183molecular_functionSUMO binding
B0032446biological_processprotein modification by small protein conjugation
B0033235biological_processpositive regulation of protein sumoylation
B0044388molecular_functionsmall protein activating enzyme binding
B0044390molecular_functionubiquitin-like protein conjugating enzyme binding
B0046982molecular_functionprotein heterodimerization activity
C0004839molecular_functionubiquitin activating enzyme activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008047molecular_functionenzyme activator activity
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0016567biological_processprotein ubiquitination
C0016925biological_processprotein sumoylation
C0019948molecular_functionSUMO activating enzyme activity
C0031510cellular_componentSUMO activating enzyme complex
C0033235biological_processpositive regulation of protein sumoylation
C0036211biological_processprotein modification process
C0043008molecular_functionATP-dependent protein binding
C0044388molecular_functionsmall protein activating enzyme binding
C0046982molecular_functionprotein heterodimerization activity
C1903749biological_processpositive regulation of protein localization to mitochondrion
D0000287molecular_functionmagnesium ion binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0008641molecular_functionubiquitin-like modifier activating enzyme activity
D0016925biological_processprotein sumoylation
D0019948molecular_functionSUMO activating enzyme activity
D0031510cellular_componentSUMO activating enzyme complex
D0032183molecular_functionSUMO binding
D0032446biological_processprotein modification by small protein conjugation
D0033235biological_processpositive regulation of protein sumoylation
D0044388molecular_functionsmall protein activating enzyme binding
D0044390molecular_functionubiquitin-like protein conjugating enzyme binding
D0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00536
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ
ChainResidueDetails
BLYS404-GLN412
site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP
ChainResidueDetails
BPRO171-PRO179
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive 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"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}
ChainResidueDetails

257179

PDB entries from 2026-07-29

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