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3KYC

Human SUMO E1 complex with a SUMO1-AMP mimic

Functional Information from GO Data
ChainGOidnamespacecontents
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
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
A0032446biological_processprotein modification by small protein conjugation
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_processpositive regulation of protein targeting 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
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
D0001741cellular_componentXY body
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006281biological_processDNA repair
D0006355biological_processregulation of DNA-templated transcription
D0008076cellular_componentvoltage-gated potassium channel complex
D0008134molecular_functiontranscription factor binding
D0010621biological_processnegative regulation of transcription by transcription factor localization
D0015459molecular_functionpotassium channel regulator activity
D0016604cellular_componentnuclear body
D0016605cellular_componentPML body
D0016607cellular_componentnuclear speck
D0016925biological_processprotein sumoylation
D0019899molecular_functionenzyme binding
D0030578biological_processPML body organization
D0031334biological_processpositive regulation of protein-containing complex assembly
D0031386molecular_functionprotein tag activity
D0031625molecular_functionubiquitin protein ligase binding
D0031647biological_processregulation of protein stability
D0031965cellular_componentnuclear membrane
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0032880biological_processregulation of protein localization
D0034605biological_processcellular response to heat
D0042308biological_processnegative regulation of protein import into nucleus
D0043392biological_processnegative regulation of DNA binding
D0043433biological_processnegative regulation of DNA-binding transcription factor activity
D0044388molecular_functionsmall protein activating enzyme binding
D0044389molecular_functionubiquitin-like protein ligase binding
D0045759biological_processnegative regulation of action potential
D0045892biological_processnegative regulation of DNA-templated transcription
D0050821biological_processprotein stabilization
D0060021biological_processroof of mouth development
D0071276biological_processcellular response to cadmium ion
D0086004biological_processregulation of cardiac muscle cell contraction
D0090204biological_processprotein localization to nuclear pore
D0097165cellular_componentnuclear stress granule
D1902260biological_processnegative regulation of delayed rectifier potassium channel activity
D1903169biological_processregulation of calcium ion transmembrane transport
D1990381molecular_functionubiquitin-specific protease binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 641
ChainResidue
BCYS158
BCYS161
BCYS441
BCYS444

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE JZU D 98
ChainResidue
BGLN60
BLYS72
BASP94
BSER95
BILE96
BMET97
BALA115
BLEU116
BASP117
BASN118
BALA121
DGLY97
DHOH101
DHOH191
BGLY26
BGLY27
BASP48
BLEU49
BASP50

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 Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU10132, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921
ChainResidueDetails
BCYS173

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15660128
ChainResidueDetails
BGLY24
BASP48
BASN56
BLYS72
BSER95
BASP117

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BCYS158
BCYS161
BCYS441
BCYS444

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER207

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS271

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER507
DGLY97

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER592

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q9Z1F9
ChainResidueDetails
BLYS613

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
ChainResidueDetails
BLYS164
DLYS39
DLYS45
DLYS46

site_idSWS_FT_FI10
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
ChainResidueDetails
DLYS25
BLYS190
BLYS275
BLYS611
BLYS617
BLYS623

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS236

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS257
BLYS420

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
ChainResidueDetails
BLYS271
BLYS613

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS371
BLYS540

222624

PDB entries from 2024-07-17

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