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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7UN3

Complex of UBE2O with NAP1L1 and ubiquitylated uL2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002181biological_processcytoplasmic translation
A0003723molecular_functionRNA binding
A0003735molecular_functionstructural constituent of ribosome
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005840cellular_componentribosome
A0005925cellular_componentfocal adhesion
A0006412biological_processtranslation
A0006513biological_processprotein monoubiquitination
A0014069cellular_componentpostsynaptic density
A0015934cellular_componentlarge ribosomal subunit
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0019843molecular_functionrRNA binding
A0022625cellular_componentcytosolic large ribosomal subunit
A0022626cellular_componentcytosolic ribosome
A0030513biological_processpositive regulation of BMP signaling pathway
A0042147biological_processretrograde transport, endosome to Golgi
A0045202cellular_componentsynapse
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070534biological_processprotein K63-linked ubiquitination
A0098794cellular_componentpostsynapse
A1990904cellular_componentribonucleoprotein complex
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006260biological_processDNA replication
B0006334biological_processnucleosome assembly
B0007399biological_processnervous system development
B0008284biological_processpositive regulation of cell population proliferation
B0016020cellular_componentmembrane
B0042393molecular_functionhistone binding
B0042470cellular_componentmelanosome
B0050769biological_processpositive regulation of neurogenesis
B0140713molecular_functionhistone chaperone activity
B2000179biological_processpositive regulation of neural precursor cell proliferation
C0000785cellular_componentchromatin
C0003682molecular_functionchromatin binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006260biological_processDNA replication
C0006334biological_processnucleosome assembly
C0007399biological_processnervous system development
C0008284biological_processpositive regulation of cell population proliferation
C0016020cellular_componentmembrane
C0042393molecular_functionhistone binding
C0042470cellular_componentmelanosome
C0050769biological_processpositive regulation of neurogenesis
C0140713molecular_functionhistone chaperone activity
C2000179biological_processpositive regulation of neural precursor cell proliferation
D0000166molecular_functionnucleotide binding
D0002181biological_processcytoplasmic translation
D0003723molecular_functionRNA binding
D0003735molecular_functionstructural constituent of ribosome
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005840cellular_componentribosome
D0005925cellular_componentfocal adhesion
D0006412biological_processtranslation
D0006513biological_processprotein monoubiquitination
D0014069cellular_componentpostsynaptic density
D0015934cellular_componentlarge ribosomal subunit
D0016020cellular_componentmembrane
D0016567biological_processprotein ubiquitination
D0016604cellular_componentnuclear body
D0016740molecular_functiontransferase activity
D0019843molecular_functionrRNA binding
D0022625cellular_componentcytosolic large ribosomal subunit
D0022626cellular_componentcytosolic ribosome
D0030513biological_processpositive regulation of BMP signaling pathway
D0042147biological_processretrograde transport, endosome to Golgi
D0045202cellular_componentsynapse
D0061630molecular_functionubiquitin protein ligase activity
D0061631molecular_functionubiquitin conjugating enzyme activity
D0070534biological_processprotein K63-linked ubiquitination
D0098794cellular_componentpostsynapse
D1990904cellular_componentribonucleoprotein complex
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
DLYS27-ASP52
site_idPS00467
Number of Residues12
DetailsRIBOSOMAL_L2 Ribosomal protein L2 signature. PrvRGVAmNPvE
ChainResidueDetails
DPRO275-GLU286
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25474007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues12
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
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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