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8P83

Cryo-EM structure of full-length human UBR5 (homotetramer)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0000785cellular_componentchromatin
A0003723molecular_functionRNA binding
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0010628biological_processpositive regulation of gene expression
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0032991cellular_componentprotein-containing complex
A0033696biological_processheterochromatin boundary formation
A0034450molecular_functionubiquitin-ubiquitin ligase activity
A0035519biological_processprotein K29-linked ubiquitination
A0042307biological_processpositive regulation of protein import into nucleus
A0043130molecular_functionubiquitin binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045879biological_processnegative regulation of smoothened signaling pathway
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050847biological_processprogesterone receptor signaling pathway
A0061630molecular_functionubiquitin protein ligase activity
A0070936biological_processprotein K48-linked ubiquitination
A0070979biological_processprotein K11-linked ubiquitination
A0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
A0071630biological_processnuclear protein quality control by the ubiquitin-proteasome system
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A0140455biological_processcytoplasm protein quality control
A0140861biological_processDNA repair-dependent chromatin remodeling
A0141198biological_processprotein branched polyubiquitination
B0000209biological_processprotein polyubiquitination
B0000785cellular_componentchromatin
B0003723molecular_functionRNA binding
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0008270molecular_functionzinc ion binding
B0010628biological_processpositive regulation of gene expression
B0016020cellular_componentmembrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0032991cellular_componentprotein-containing complex
B0033696biological_processheterochromatin boundary formation
B0034450molecular_functionubiquitin-ubiquitin ligase activity
B0035519biological_processprotein K29-linked ubiquitination
B0042307biological_processpositive regulation of protein import into nucleus
B0043130molecular_functionubiquitin binding
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0045879biological_processnegative regulation of smoothened signaling pathway
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050847biological_processprogesterone receptor signaling pathway
B0061630molecular_functionubiquitin protein ligase activity
B0070936biological_processprotein K48-linked ubiquitination
B0070979biological_processprotein K11-linked ubiquitination
B0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
B0071630biological_processnuclear protein quality control by the ubiquitin-proteasome system
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
B0140455biological_processcytoplasm protein quality control
B0140861biological_processDNA repair-dependent chromatin remodeling
B0141198biological_processprotein branched polyubiquitination
C0000209biological_processprotein polyubiquitination
C0000785cellular_componentchromatin
C0003723molecular_functionRNA binding
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006281biological_processDNA repair
C0006974biological_processDNA damage response
C0008270molecular_functionzinc ion binding
C0010628biological_processpositive regulation of gene expression
C0016020cellular_componentmembrane
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0032991cellular_componentprotein-containing complex
C0033696biological_processheterochromatin boundary formation
C0034450molecular_functionubiquitin-ubiquitin ligase activity
C0035519biological_processprotein K29-linked ubiquitination
C0042307biological_processpositive regulation of protein import into nucleus
C0043130molecular_functionubiquitin binding
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0045879biological_processnegative regulation of smoothened signaling pathway
C0046872molecular_functionmetal ion binding
C0048471cellular_componentperinuclear region of cytoplasm
C0050847biological_processprogesterone receptor signaling pathway
C0061630molecular_functionubiquitin protein ligase activity
C0070936biological_processprotein K48-linked ubiquitination
C0070979biological_processprotein K11-linked ubiquitination
C0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
C0071630biological_processnuclear protein quality control by the ubiquitin-proteasome system
C0090263biological_processpositive regulation of canonical Wnt signaling pathway
C0140455biological_processcytoplasm protein quality control
C0140861biological_processDNA repair-dependent chromatin remodeling
C0141198biological_processprotein branched polyubiquitination
D0000209biological_processprotein polyubiquitination
D0000785cellular_componentchromatin
D0003723molecular_functionRNA binding
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006281biological_processDNA repair
D0006974biological_processDNA damage response
D0008270molecular_functionzinc ion binding
D0010628biological_processpositive regulation of gene expression
D0016020cellular_componentmembrane
D0016567biological_processprotein ubiquitination
D0016740molecular_functiontransferase activity
D0032991cellular_componentprotein-containing complex
D0033696biological_processheterochromatin boundary formation
D0034450molecular_functionubiquitin-ubiquitin ligase activity
D0035519biological_processprotein K29-linked ubiquitination
D0042307biological_processpositive regulation of protein import into nucleus
D0043130molecular_functionubiquitin binding
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0045879biological_processnegative regulation of smoothened signaling pathway
D0046872molecular_functionmetal ion binding
D0048471cellular_componentperinuclear region of cytoplasm
D0050847biological_processprogesterone receptor signaling pathway
D0061630molecular_functionubiquitin protein ligase activity
D0070936biological_processprotein K48-linked ubiquitination
D0070979biological_processprotein K11-linked ubiquitination
D0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
D0071630biological_processnuclear protein quality control by the ubiquitin-proteasome system
D0090263biological_processpositive regulation of canonical Wnt signaling pathway
D0140455biological_processcytoplasm protein quality control
D0140861biological_processDNA repair-dependent chromatin remodeling
D0141198biological_processprotein branched polyubiquitination
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues272
DetailsZN_FING: UBR-type => ECO:0000255|PROSITE-ProRule:PRU00508
ChainResidueDetails
AASP1177-ALA1245
BASP1177-ALA1245
CASP1177-ALA1245
DASP1177-ALA1245

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00104, ECO:0000305|PubMed:11287654, ECO:0000305|PubMed:23027739, ECO:0000305|PubMed:28689657, ECO:0000305|PubMed:37040767, ECO:0000305|PubMed:37478862, ECO:0000305|PubMed:37620400
ChainResidueDetails
ACYS2768
BCYS2768
CCYS2768
DCYS2768

site_idSWS_FT_FI3
Number of Residues44
DetailsBINDING: BINDING => ECO:0000269|PubMed:37040767, ECO:0000269|PubMed:37409633, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:37620400, ECO:0007744|PDB:8BJA, ECO:0007744|PDB:8C06, ECO:0007744|PDB:8D4X, ECO:0007744|PDB:8E0Q, ECO:0007744|PDB:8EWI, ECO:0007744|PDB:8P82
ChainResidueDetails
ACYS1179
ACYS1234
ACYS1240
BCYS1179
BCYS1196
BCYS1199
BCYS1208
BCYS1211
BCYS1215
BHIS1216
BHIS1219
ACYS1196
BCYS1232
BCYS1234
BCYS1240
CCYS1179
CCYS1196
CCYS1199
CCYS1208
CCYS1211
CCYS1215
CHIS1216
ACYS1199
CHIS1219
CCYS1232
CCYS1234
CCYS1240
DCYS1179
DCYS1196
DCYS1199
DCYS1208
DCYS1211
DCYS1215
ACYS1208
DHIS1216
DHIS1219
DCYS1232
DCYS1234
DCYS1240
ACYS1211
ACYS1215
AHIS1216
AHIS1219
ACYS1232

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330
ChainResidueDetails
ATHR2
BTHR2
CTHR2
DTHR2

site_idSWS_FT_FI5
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER110
CSER578
CSER612
CSER808
DSER110
DSER578
DSER612
DSER808
ASER578
ASER612
ASER808
BSER110
BSER578
BSER612
BSER808
CSER110

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER327
BSER327
CSER327
DSER327

site_idSWS_FT_FI7
Number of Residues56
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388
ChainResidueDetails
ASER352
ASER2026
ASER2028
ASER2076
ASER2289
ASER2484
BSER352
BSER928
BSER1018
BSER1227
BSER1355
ASER928
BSER1375
BSER1481
BSER1741
BSER1780
BSER2026
BSER2028
BSER2076
BSER2289
BSER2484
CSER352
ASER1018
CSER928
CSER1018
CSER1227
CSER1355
CSER1375
CSER1481
CSER1741
CSER1780
CSER2026
CSER2028
ASER1227
CSER2076
CSER2289
CSER2484
DSER352
DSER928
DSER1018
DSER1227
DSER1355
DSER1375
DSER1481
ASER1355
DSER1741
DSER1780
DSER2026
DSER2028
DSER2076
DSER2289
DSER2484
ASER1375
ASER1481
ASER1741
ASER1780

site_idSWS_FT_FI8
Number of Residues24
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21924388
ChainResidueDetails
ATHR637
BTHR1736
BTHR2030
BTHR2213
CTHR637
CTHR1115
CTHR1135
CTHR1736
CTHR2030
CTHR2213
DTHR637
ATHR1115
DTHR1115
DTHR1135
DTHR1736
DTHR2030
DTHR2213
ATHR1135
ATHR1736
ATHR2030
ATHR2213
BTHR637
BTHR1115
BTHR1135

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1308
BSER1308
CSER1308
DSER1308

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1549
BSER1549
CSER1549
DSER1549

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR1746
BTYR1746
CTYR1746
DTYR1746

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR1969
BTHR1969
CTHR1969
DTHR1969

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1990
BSER1990
CSER1990
DSER1990

site_idSWS_FT_FI14
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2241
ASER2469
BSER2241
BSER2469
CSER2241
CSER2469
DSER2241
DSER2469

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2486
BSER2486
CSER2486
DSER2486

226707

PDB entries from 2024-10-30

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