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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9AZM

In situ human ribosome (Focused on 40S with SERBP1 CTD)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
SD0000977molecular_functionRNA polymerase II transcription regulatory region sequence-specific DNA binding
SD0002181biological_processcytoplasmic translation
SD0003677molecular_functionDNA binding
SD0003684molecular_functiondamaged DNA binding
SD0003723molecular_functionRNA binding
SD0003729molecular_functionmRNA binding
SD0003735molecular_functionstructural constituent of ribosome
SD0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
SD0004520molecular_functionDNA endonuclease activity
SD0005515molecular_functionprotein binding
SD0005634cellular_componentnucleus
SD0005654cellular_componentnucleoplasm
SD0005730cellular_componentnucleolus
SD0005737cellular_componentcytoplasm
SD0005739cellular_componentmitochondrion
SD0005743cellular_componentmitochondrial inner membrane
SD0005759cellular_componentmitochondrial matrix
SD0005783cellular_componentendoplasmic reticulum
SD0005819cellular_componentspindle
SD0005829cellular_componentcytosol
SD0005840cellular_componentribosome
SD0005856cellular_componentcytoskeleton
SD0005886cellular_componentplasma membrane
SD0005925cellular_componentfocal adhesion
SD0006281biological_processDNA repair
SD0006284biological_processbase-excision repair
SD0006412biological_processtranslation
SD0006413biological_processtranslational initiation
SD0006417biological_processregulation of translation
SD0006915biological_processapoptotic process
SD0006974biological_processDNA damage response
SD0007059biological_processchromosome segregation
SD0008017molecular_functionmicrotubule binding
SD0010628biological_processpositive regulation of gene expression
SD0014069cellular_componentpostsynaptic density
SD0015631molecular_functiontubulin binding
SD0016020cellular_componentmembrane
SD0016829molecular_functionlyase activity
SD0017148biological_processnegative regulation of translation
SD0019104molecular_functionDNA N-glycosylase activity
SD0019899molecular_functionenzyme binding
SD0019900molecular_functionkinase binding
SD0019901molecular_functionprotein kinase binding
SD0022626cellular_componentcytosolic ribosome
SD0022627cellular_componentcytosolic small ribosomal subunit
SD0030544molecular_functionHsp70 protein binding
SD0031116biological_processpositive regulation of microtubule polymerization
SD0031334biological_processpositive regulation of protein-containing complex assembly
SD0031397biological_processnegative regulation of protein ubiquitination
SD0032079biological_processpositive regulation of endodeoxyribonuclease activity
SD0032357molecular_functionoxidized purine DNA binding
SD0032358molecular_functionoxidized pyrimidine DNA binding
SD0032587cellular_componentruffle membrane
SD0032743biological_processpositive regulation of interleukin-2 production
SD0034614biological_processcellular response to reactive oxygen species
SD0042104biological_processpositive regulation of activated T cell proliferation
SD0042981biological_processregulation of apoptotic process
SD0044390molecular_functionubiquitin-like protein conjugating enzyme binding
SD0044877molecular_functionprotein-containing complex binding
SD0045202cellular_componentsynapse
SD0045738biological_processnegative regulation of DNA repair
SD0045739biological_processpositive regulation of DNA repair
SD0050862biological_processpositive regulation of T cell receptor signaling pathway
SD0051018molecular_functionprotein kinase A binding
SD0051092biological_processpositive regulation of NF-kappaB transcription factor activity
SD0051225biological_processspindle assembly
SD0051301biological_processcell division
SD0051536molecular_functioniron-sulfur cluster binding
SD0051879molecular_functionHsp90 protein binding
SD0061481biological_processresponse to TNF agonist
SD0070062cellular_componentextracellular exosome
SD0070181molecular_functionsmall ribosomal subunit rRNA binding
SD0070301biological_processcellular response to hydrogen peroxide
SD0071159cellular_componentNF-kappaB complex
SD0071356biological_processcellular response to tumor necrosis factor
SD0072686cellular_componentmitotic spindle
SD0097100molecular_functionsupercoiled DNA binding
SD0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
SD0140297molecular_functionDNA-binding transcription factor binding
SD1901224biological_processpositive regulation of non-canonical NF-kappaB signal transduction
SD1902231biological_processpositive regulation of intrinsic apoptotic signaling pathway in response to DNA damage
SD1905053biological_processpositive regulation of base-excision repair
SD1990904cellular_componentribonucleoprotein complex
SD2001235biological_processpositive regulation of apoptotic signaling pathway
SF0002181biological_processcytoplasmic translation
SF0003723molecular_functionRNA binding
SF0003729molecular_functionmRNA binding
SF0003735molecular_functionstructural constituent of ribosome
SF0005515molecular_functionprotein binding
SF0005634cellular_componentnucleus
SF0005654cellular_componentnucleoplasm
SF0005730cellular_componentnucleolus
SF0005737cellular_componentcytoplasm
SF0005829cellular_componentcytosol
SF0005840cellular_componentribosome
SF0005925cellular_componentfocal adhesion
SF0006412biological_processtranslation
SF0006413biological_processtranslational initiation
SF0006450biological_processregulation of translational fidelity
SF0016020cellular_componentmembrane
SF0019843molecular_functionrRNA binding
SF0022626cellular_componentcytosolic ribosome
SF0022627cellular_componentcytosolic small ribosomal subunit
SF0032040cellular_componentsmall-subunit processome
SF0042274biological_processribosomal small subunit biogenesis
SF0045202cellular_componentsynapse
SF0070062cellular_componentextracellular exosome
SF1990904cellular_componentribonucleoprotein complex
SM0002181biological_processcytoplasmic translation
SM0003723molecular_functionRNA binding
SM0003735molecular_functionstructural constituent of ribosome
SM0005515molecular_functionprotein binding
SM0005634cellular_componentnucleus
SM0005654cellular_componentnucleoplasm
SM0005730cellular_componentnucleolus
SM0005737cellular_componentcytoplasm
SM0005794cellular_componentGolgi apparatus
SM0005829cellular_componentcytosol
SM0005840cellular_componentribosome
SM0006412biological_processtranslation
SM0016020cellular_componentmembrane
SM0022626cellular_componentcytosolic ribosome
SM0022627cellular_componentcytosolic small ribosomal subunit
SM0032040cellular_componentsmall-subunit processome
SM0042274biological_processribosomal small subunit biogenesis
SM0090263biological_processpositive regulation of canonical Wnt signaling pathway
SM1990145biological_processmaintenance of translational fidelity
SM1990904cellular_componentribonucleoprotein complex
SQ0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
SQ0002181biological_processcytoplasmic translation
SQ0003723molecular_functionRNA binding
SQ0003735molecular_functionstructural constituent of ribosome
SQ0005515molecular_functionprotein binding
SQ0005634cellular_componentnucleus
SQ0005654cellular_componentnucleoplasm
SQ0005730cellular_componentnucleolus
SQ0005737cellular_componentcytoplasm
SQ0005829cellular_componentcytosol
SQ0005840cellular_componentribosome
SQ0005925cellular_componentfocal adhesion
SQ0006364biological_processrRNA processing
SQ0006412biological_processtranslation
SQ0015935cellular_componentsmall ribosomal subunit
SQ0016020cellular_componentmembrane
SQ0022626cellular_componentcytosolic ribosome
SQ0022627cellular_componentcytosolic small ribosomal subunit
SQ0032040cellular_componentsmall-subunit processome
SQ0042274biological_processribosomal small subunit biogenesis
SQ0045202cellular_componentsynapse
SQ0070062cellular_componentextracellular exosome
SQ1990830biological_processcellular response to leukemia inhibitory factor
SQ1990904cellular_componentribonucleoprotein complex
SS0002181biological_processcytoplasmic translation
SS0003723molecular_functionRNA binding
SS0003735molecular_functionstructural constituent of ribosome
SS0005515molecular_functionprotein binding
SS0005634cellular_componentnucleus
SS0005654cellular_componentnucleoplasm
SS0005737cellular_componentcytoplasm
SS0005829cellular_componentcytosol
SS0005840cellular_componentribosome
SS0005925cellular_componentfocal adhesion
SS0006412biological_processtranslation
SS0014069cellular_componentpostsynaptic density
SS0015935cellular_componentsmall ribosomal subunit
SS0016020cellular_componentmembrane
SS0019843molecular_functionrRNA binding
SS0022626cellular_componentcytosolic ribosome
SS0022627cellular_componentcytosolic small ribosomal subunit
SS0045202cellular_componentsynapse
SS0070062cellular_componentextracellular exosome
SS1990904cellular_componentribonucleoprotein complex
ST0000028biological_processribosomal small subunit assembly
ST0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
ST0002181biological_processcytoplasmic translation
ST0002548biological_processmonocyte chemotaxis
ST0003723molecular_functionRNA binding
ST0003735molecular_functionstructural constituent of ribosome
ST0005515molecular_functionprotein binding
ST0005634cellular_componentnucleus
ST0005654cellular_componentnucleoplasm
ST0005730cellular_componentnucleolus
ST0005737cellular_componentcytoplasm
ST0005829cellular_componentcytosol
ST0005840cellular_componentribosome
ST0005925cellular_componentfocal adhesion
ST0006364biological_processrRNA processing
ST0006412biological_processtranslation
ST0007000biological_processnucleolus organization
ST0014069cellular_componentpostsynaptic density
ST0016020cellular_componentmembrane
ST0017134molecular_functionfibroblast growth factor binding
ST0019901molecular_functionprotein kinase binding
ST0022626cellular_componentcytosolic ribosome
ST0022627cellular_componentcytosolic small ribosomal subunit
ST0030218biological_processerythrocyte differentiation
ST0030490biological_processmaturation of SSU-rRNA
ST0031640biological_processkilling of cells of another organism
ST0032040cellular_componentsmall-subunit processome
ST0042274biological_processribosomal small subunit biogenesis
ST0042802molecular_functionidentical protein binding
ST0050829biological_processdefense response to Gram-negative bacterium
ST0060265biological_processpositive regulation of respiratory burst involved in inflammatory response
ST0060266biological_processnegative regulation of respiratory burst involved in inflammatory response
ST0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
ST0070062cellular_componentextracellular exosome
ST1990904cellular_componentribonucleoprotein complex
Sc0000028biological_processribosomal small subunit assembly
Sc0002181biological_processcytoplasmic translation
Sc0003723molecular_functionRNA binding
Sc0003735molecular_functionstructural constituent of ribosome
Sc0005515molecular_functionprotein binding
Sc0005634cellular_componentnucleus
Sc0005654cellular_componentnucleoplasm
Sc0005730cellular_componentnucleolus
Sc0005737cellular_componentcytoplasm
Sc0005783cellular_componentendoplasmic reticulum
Sc0005791cellular_componentrough endoplasmic reticulum
Sc0005829cellular_componentcytosol
Sc0005840cellular_componentribosome
Sc0006364biological_processrRNA processing
Sc0006412biological_processtranslation
Sc0015935cellular_componentsmall ribosomal subunit
Sc0022626cellular_componentcytosolic ribosome
Sc0022627cellular_componentcytosolic small ribosomal subunit
Sc0030490biological_processmaturation of SSU-rRNA
Sc0032040cellular_componentsmall-subunit processome
Sc0042254biological_processribosome biogenesis
Sc0042274biological_processribosomal small subunit biogenesis
Sc0045202cellular_componentsynapse
Sc0070062cellular_componentextracellular exosome
Sc0098556cellular_componentcytoplasmic side of rough endoplasmic reticulum membrane
Sc1990904cellular_componentribonucleoprotein complex
Sd0002181biological_processcytoplasmic translation
Sd0003735molecular_functionstructural constituent of ribosome
Sd0005654cellular_componentnucleoplasm
Sd0005737cellular_componentcytoplasm
Sd0005783cellular_componentendoplasmic reticulum
Sd0005791cellular_componentrough endoplasmic reticulum
Sd0005829cellular_componentcytosol
Sd0005840cellular_componentribosome
Sd0005925cellular_componentfocal adhesion
Sd0006412biological_processtranslation
Sd0008270molecular_functionzinc ion binding
Sd0015935cellular_componentsmall ribosomal subunit
Sd0022626cellular_componentcytosolic ribosome
Sd0022627cellular_componentcytosolic small ribosomal subunit
Sd0046872molecular_functionmetal ion binding
Sd0070062cellular_componentextracellular exosome
Sd0098556cellular_componentcytoplasmic side of rough endoplasmic reticulum membrane
Sd1990904cellular_componentribonucleoprotein complex
Sg0001891cellular_componentphagocytic cup
Sg0001934biological_processpositive regulation of protein phosphorylation
Sg0002181biological_processcytoplasmic translation
Sg0003723molecular_functionRNA binding
Sg0005080molecular_functionprotein kinase C binding
Sg0005102molecular_functionsignaling receptor binding
Sg0005515molecular_functionprotein binding
Sg0005634cellular_componentnucleus
Sg0005654cellular_componentnucleoplasm
Sg0005737cellular_componentcytoplasm
Sg0005739cellular_componentmitochondrion
Sg0005829cellular_componentcytosol
Sg0005840cellular_componentribosome
Sg0005886cellular_componentplasma membrane
Sg0006412biological_processtranslation
Sg0006417biological_processregulation of translation
Sg0006915biological_processapoptotic process
Sg0007369biological_processgastrulation
Sg0008047molecular_functionenzyme activator activity
Sg0008200molecular_functionion channel inhibitor activity
Sg0008656molecular_functioncysteine-type endopeptidase activator activity involved in apoptotic process
Sg0010629biological_processnegative regulation of gene expression
Sg0015935cellular_componentsmall ribosomal subunit
Sg0016020cellular_componentmembrane
Sg0016567biological_processprotein ubiquitination
Sg0017148biological_processnegative regulation of translation
Sg0019899molecular_functionenzyme binding
Sg0019903molecular_functionprotein phosphatase binding
Sg0022627cellular_componentcytosolic small ribosomal subunit
Sg0030178biological_processnegative regulation of Wnt signaling pathway
Sg0030291molecular_functionprotein serine/threonine kinase inhibitor activity
Sg0030292molecular_functionprotein tyrosine kinase inhibitor activity
Sg0030308biological_processnegative regulation of cell growth
Sg0030332molecular_functioncyclin binding
Sg0030335biological_processpositive regulation of cell migration
Sg0030425cellular_componentdendrite
Sg0030496cellular_componentmidbody
Sg0030971molecular_functionreceptor tyrosine kinase binding
Sg0031334biological_processpositive regulation of protein-containing complex assembly
Sg0032091biological_processnegative regulation of protein binding
Sg0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Sg0032880biological_processregulation of protein localization
Sg0035591molecular_functionsignaling adaptor activity
Sg0042169molecular_functionSH2 domain binding
Sg0042802molecular_functionidentical protein binding
Sg0042803molecular_functionprotein homodimerization activity
Sg0042995cellular_componentcell projection
Sg0042998biological_processpositive regulation of Golgi to plasma membrane protein transport
Sg0043005cellular_componentneuron projection
Sg0043022molecular_functionribosome binding
Sg0043025cellular_componentneuronal cell body
Sg0043065biological_processpositive regulation of apoptotic process
Sg0043204cellular_componentperikaryon
Sg0043473biological_processpigmentation
Sg0043547biological_processpositive regulation of GTPase activity
Sg0044297cellular_componentcell body
Sg0045296molecular_functioncadherin binding
Sg0045879biological_processnegative regulation of smoothened signaling pathway
Sg0048471cellular_componentperinuclear region of cytoplasm
Sg0048511biological_processrhythmic process
Sg0050765biological_processnegative regulation of phagocytosis
Sg0051302biological_processregulation of cell division
Sg0051434molecular_functionBH3 domain binding
Sg0051726biological_processregulation of cell cycle
Sg0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Sg0051901biological_processpositive regulation of mitochondrial depolarization
Sg0060090molecular_functionmolecular adaptor activity
Sg0070062cellular_componentextracellular exosome
Sg0071333biological_processcellular response to glucose stimulus
Sg0071363biological_processcellular response to growth factor stimulus
Sg0072344biological_processrescue of stalled ribosome
Sg0106070biological_processregulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
Sg1900102biological_processnegative regulation of endoplasmic reticulum unfolded protein response
Sg1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
Sg1990630cellular_componentIRE1-RACK1-PP2A complex
Sg1990904cellular_componentribonucleoprotein complex
Sg2000114biological_processregulation of establishment of cell polarity
Sg2000543biological_processpositive regulation of gastrulation
Sg2001125biological_processnegative regulation of translational frameshifting
Sg2001244biological_processpositive regulation of intrinsic apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00052
Number of Residues27
DetailsRIBOSOMAL_S7 Ribosomal protein S7 signature. ErLtnsMMmhgrnnGKKlmtvrIVkhA
ChainResidueDetails
SFGLU70-ALA96
site_idPS00323
Number of Residues25
DetailsRIBOSOMAL_S19 Ribosomal protein S19 signature. NGKtfnqveIkpemIGhyLGEFsiT
ChainResidueDetails
SPASN98-THR122
site_idPS00360
Number of Residues19
DetailsRIBOSOMAL_S9 Ribosomal protein S9 signature. GGGhvAQiyAirqSiSKAL
ChainResidueDetails
SQGLY74-LEU92
site_idPS00361
Number of Residues16
DetailsRIBOSOMAL_S10 Ribosomal protein S10 signature. AkekNLkvkGPVrMPT
ChainResidueDetails
SUALA43-THR58
site_idPS00527
Number of Residues23
DetailsRIBOSOMAL_S14 Ribosomal protein S14 signature. RvCsnrhglirkyg.LNMCRqCFR
ChainResidueDetails
SdARG22-ARG44
site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKsmkfvdGlMihSgdpVnyyVDtavrhvlLrqGvlG
ChainResidueDetails
SDALA147-GLY183
site_idPS00628
Number of Residues20
DetailsRIBOSOMAL_S19E Ribosomal protein S19e signature. PshfsrgSksVaRrVLQaLE
ChainResidueDetails
STPRO89-GLU108
site_idPS00646
Number of Residues14
DetailsRIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHfwGlrVRGQ
ChainResidueDetails
SSARG121-GLN134
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ALSGswDgTLRLWDL
ChainResidueDetails
SgALA78-LEU92
SgILE120-THR134
SgILE165-LEU179
SgCYS207-LEU221
site_idPS00961
Number of Residues9
DetailsRIBOSOMAL_S28E Ribosomal protein S28e signature. ESEREARrL
ChainResidueDetails
ScGLU60-LEU68
site_idPS01189
Number of Residues19
DetailsRIBOSOMAL_S12E Ribosomal protein S12e signature. ALQevLktAlihDGLarGI
ChainResidueDetails
SMALA17-ILE35
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CY58","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues71
DetailsDomain: {"description":"KH type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Murray L.","Brunton V.G.","Frame M.C.","Calvo F.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by MAPK","evidences":[{"source":"PubMed","id":"15950189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"Asymmetric dimethylarginine; by PRMT1","evidences":[{"source":"PubMed","id":"19460357","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB","evidences":[{"source":"PubMed","id":"20605787","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62908","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by IKKB","evidences":[{"source":"PubMed","id":"21399639","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21871177","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16807684","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28065601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28132843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31981475","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32011234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34348161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34469731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues5
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P63325","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
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_FI23
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Boulahbel H.","Gottlieb E."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60867","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FLX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LKS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LKS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues31
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues30
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues30
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues32
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues30
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues29
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues30
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Kanor S.","Tissot J.-D.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"19423701","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"11279199","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P63323","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62852","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62852","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues23
DetailsZinc finger: {"description":"C4-type"}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"36638793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"32129764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36638793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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