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8BJA

Structure of the human UBR5 Dimer.

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues136
DetailsZN_FING: UBR-type => ECO:0000255|PROSITE-ProRule:PRU00508
ChainResidueDetails
BASP1177-ALA1245
AASP1177-ALA1245

site_idSWS_FT_FI2
Number of Residues2
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
BCYS2768
ACYS2768

site_idSWS_FT_FI3
Number of Residues22
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
BCYS1179
BCYS1234
BCYS1240
ACYS1179
ACYS1196
ACYS1199
ACYS1208
ACYS1211
ACYS1215
AHIS1216
AHIS1219
BCYS1196
ACYS1232
ACYS1234
ACYS1240
BCYS1199
BCYS1208
BCYS1211
BCYS1215
BHIS1216
BHIS1219
BCYS1232

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330
ChainResidueDetails
BTHR2
ATHR2

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER110
BSER578
BSER612
BSER808
ASER110
ASER578
ASER612
ASER808

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER327
ASER327

site_idSWS_FT_FI7
Number of Residues28
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388
ChainResidueDetails
BSER352
BSER2026
BSER2028
BSER2076
BSER2289
BSER2484
ASER352
ASER928
ASER1018
ASER1227
ASER1355
BSER928
ASER1375
ASER1481
ASER1741
ASER1780
ASER2026
ASER2028
ASER2076
ASER2289
ASER2484
BSER1018
BSER1227
BSER1355
BSER1375
BSER1481
BSER1741
BSER1780

site_idSWS_FT_FI8
Number of Residues12
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21924388
ChainResidueDetails
BTHR637
ATHR1736
ATHR2030
ATHR2213
BTHR1115
BTHR1135
BTHR1736
BTHR2030
BTHR2213
ATHR637
ATHR1115
ATHR1135

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER1308
ASER1308

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER1549
ASER1549

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
BTYR1746
ATYR1746

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21924388, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR1969
ATHR1969

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER1990
ASER1990

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER2241
BSER2469
ASER2241
ASER2469

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER2486
ASER2486

223166

PDB entries from 2024-07-31

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