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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2N1A

Docked structure between SUMO1 and ZZ-domain from CBP

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
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
A0098978cellular_componentglutamatergic synapse
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A0141109molecular_functiontransporter activator activity
A1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
A1902260biological_processnegative regulation of delayed rectifier potassium channel activity
A1903169biological_processregulation of calcium ion transmembrane transport
A1990381molecular_functionubiquitin-specific protease binding
B0004402molecular_functionhistone acetyltransferase activity
B0006355biological_processregulation of DNA-templated transcription
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BCYS209
BCYS212
BCYS231
BCYS234
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS222
BCYS225
BHIS240
BHIS242
Functional Information from PROSITE/UniProt
site_idPS01357
Number of Residues26
DetailsZF_ZZ_1 Zinc finger ZZ-type signature. CneCkhhvet..RWhCtv...CeDYdLCinC
ChainResidueDetails
BCYS209-CYS234
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsPropeptide: {"featureId":"PRO_0000035940","evidences":[{"source":"PubMed","id":"15487983","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues77
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsRegion: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Interaction with PIAS2"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18707152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"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"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"27068747","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
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_FI13
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsCross-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"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues48
DetailsZinc finger: {"description":"ZZ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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