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2ASQ

Solution Structure of SUMO-1 in Complex with a SUMO-binding Motif (SBM)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001741cellular_componentXY body
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005940cellular_componentseptin ring
A0006281biological_processDNA repair
A0006355biological_processregulation of DNA-templated transcription
A0008076cellular_componentvoltage-gated potassium channel complex
A0008134molecular_functiontranscription factor binding
A0010621biological_processnegative regulation of transcription by transcription factor localization
A0015459molecular_functionpotassium channel regulator activity
A0016020cellular_componentmembrane
A0016604cellular_componentnuclear body
A0016605cellular_componentPML body
A0016607cellular_componentnuclear speck
A0016925biological_processprotein sumoylation
A0019899molecular_functionenzyme binding
A0030578biological_processPML body organization
A0031334biological_processpositive regulation of protein-containing complex assembly
A0031386molecular_functionprotein tag activity
A0031625molecular_functionubiquitin protein ligase binding
A0031647biological_processregulation of protein stability
A0031965cellular_componentnuclear membrane
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032880biological_processregulation of protein localization
A0034605biological_processcellular response to heat
A0042308biological_processnegative regulation of protein import into nucleus
A0043392biological_processnegative regulation of DNA binding
A0043433biological_processnegative regulation of DNA-binding transcription factor activity
A0044388molecular_functionsmall protein activating enzyme binding
A0044389molecular_functionubiquitin-like protein ligase binding
A0045759biological_processnegative regulation of action potential
A0045892biological_processnegative regulation of DNA-templated transcription
A0050821biological_processprotein stabilization
A0060021biological_processroof of mouth development
A0071276biological_processcellular response to cadmium ion
A0086004biological_processregulation of cardiac muscle cell contraction
A0090204biological_processprotein localization to nuclear pore
A0097165cellular_componentnuclear stress granule
A1902260biological_processnegative regulation of delayed rectifier potassium channel activity
A1903169biological_processregulation of calcium ion transmembrane transport
A1990381molecular_functionubiquitin-specific protease binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER11
BSER12
BSER13

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18707152, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER9

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER32

site_idSWS_FT_FI5
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS7

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000269|PubMed:27068747
ChainResidueDetails
AGLY97

site_idSWS_FT_FI7
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS16

site_idSWS_FT_FI8
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS17

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS23
ALYS39
ALYS45
ALYS46

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
ChainResidueDetails
ALYS25

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS37

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PDB entries from 2024-04-17

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