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1Y8Q

SUMO E1 ACTIVATING ENZYME SAE1-SAE2-MG-ATP COMPLEX

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
A0016874molecular_functionligase activity
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
A1903955biological_processobsolete positive regulation of protein targeting to mitochondrion
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0016740molecular_functiontransferase activity
B0016925biological_processprotein sumoylation
B0019948molecular_functionSUMO activating enzyme activity
B0031510cellular_componentSUMO activating enzyme complex
B0032183molecular_functionSUMO binding
B0033235biological_processpositive regulation of protein sumoylation
B0044388molecular_functionsmall protein activating enzyme binding
B0044390molecular_functionubiquitin-like protein conjugating enzyme binding
B0046872molecular_functionmetal ion 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
C0016874molecular_functionligase activity
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
C1903955biological_processobsolete positive regulation of protein targeting to mitochondrion
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0008641molecular_functionubiquitin-like modifier activating enzyme activity
D0016740molecular_functiontransferase activity
D0016925biological_processprotein sumoylation
D0019948molecular_functionSUMO activating enzyme activity
D0031510cellular_componentSUMO activating enzyme complex
D0032183molecular_functionSUMO binding
D0033235biological_processpositive regulation of protein sumoylation
D0044388molecular_functionsmall protein activating enzyme binding
D0044390molecular_functionubiquitin-like protein conjugating enzyme binding
D0046872molecular_functionmetal ion binding
D0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 641
ChainResidue
DASP117
DATP801
DHOH851
DHOH903
DHOH991

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 641
ChainResidue
BHOH1065
BASP117
BATP802
BHOH935
BHOH978

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 642
ChainResidue
DCYS158
DCYS161
DCYS441
DCYS444

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 642
ChainResidue
BCYS158
BCYS161
BCYS441
BCYS444

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP D 801
ChainResidue
CARG21
DGLY26
DGLY27
DASP48
DLEU49
DASP50
DASN56
DARG59
DGLN60
DLYS72
DASP94
DSER95
DILE96
DLEU116
DASP117
DLYS346
DMG641
DHOH837
DHOH842
DHOH851
DHOH866
DHOH903
DHOH908
DHOH991

site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ATP B 802
ChainResidue
AARG21
BGLY26
BGLY27
BASP48
BLEU49
BASP50
BASN56
BARG59
BGLN60
BLYS72
BASP94
BSER95
BILE96
BMET97
BLEU116
BASP117
BASN118
BALA121
BLYS346
BMG641
BHOH818
BHOH829
BHOH839
BHOH875
BHOH879
BHOH918
BHOH935
BHOH978
BHOH1065

Functional Information from PROSITE/UniProt
site_idPS00536
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ
ChainResidueDetails
BLYS404-GLN412

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

250059

PDB entries from 2026-03-04

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