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6WKR

PRC2-AEBP2-JARID2 bound to H2AK119ub1 nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0001222molecular_functiontranscription corepressor binding
A0001739cellular_componentsex chromatin
A0003682molecular_functionchromatin binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005677cellular_componentchromatin silencing complex
A0005730cellular_componentnucleolus
A0006325biological_processchromatin organization
A0006351biological_processDNA-templated transcription
A0008047molecular_functionenzyme activator activity
A0008270molecular_functionzinc ion binding
A0016586cellular_componentRSC-type complex
A0016604cellular_componentnuclear body
A0031490molecular_functionchromatin DNA binding
A0031507biological_processheterochromatin formation
A0031519cellular_componentPcG protein complex
A0032993cellular_componentprotein-DNA complex
A0035098cellular_componentESC/E(Z) complex
A0043565molecular_functionsequence-specific DNA binding
A0045596biological_processnegative regulation of cell differentiation
A0046872molecular_functionmetal ion binding
A0062072molecular_functionhistone H3K9me2/3 reader activity
A0106222molecular_functionlncRNA binding
A0140718biological_processfacultative heterochromatin formation
A1990841molecular_functionpromoter-specific chromatin binding
A1990904cellular_componentribonucleoprotein complex
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000781cellular_componentchromosome, telomeric region
C0000785cellular_componentchromatin
C0000792cellular_componentheterochromatin
C0000976molecular_functiontranscription cis-regulatory region binding
C0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
C0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
C0001222molecular_functiontranscription corepressor binding
C0003677molecular_functionDNA binding
C0003682molecular_functionchromatin binding
C0003714molecular_functiontranscription corepressor activity
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005677cellular_componentchromatin silencing complex
C0005694cellular_componentchromosome
C0005721cellular_componentpericentric heterochromatin
C0006325biological_processchromatin organization
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0006355biological_processregulation of DNA-templated transcription
C0008168molecular_functionmethyltransferase activity
C0008284biological_processpositive regulation of cell population proliferation
C0010629biological_processnegative regulation of gene expression
C0010718biological_processpositive regulation of epithelial to mesenchymal transition
C0016279molecular_functionprotein-lysine N-methyltransferase activity
C0016740molecular_functiontransferase activity
C0021766biological_processhippocampus development
C0030183biological_processB cell differentiation
C0030335biological_processpositive regulation of cell migration
C0031048biological_processregulatory ncRNA-mediated heterochromatin formation
C0031490molecular_functionchromatin DNA binding
C0031491molecular_functionnucleosome binding
C0031507biological_processheterochromatin formation
C0031509biological_processsubtelomeric heterochromatin formation
C0031519cellular_componentPcG protein complex
C0032259biological_processmethylation
C0032355biological_processresponse to estradiol
C0035098cellular_componentESC/E(Z) complex
C0042054molecular_functionhistone methyltransferase activity
C0042393molecular_functionhistone binding
C0042752biological_processregulation of circadian rhythm
C0043021molecular_functionribonucleoprotein complex binding
C0043406biological_processpositive regulation of MAP kinase activity
C0043547biological_processpositive regulation of GTPase activity
C0043565molecular_functionsequence-specific DNA binding
C0045120cellular_componentpronucleus
C0045202cellular_componentsynapse
C0045814biological_processnegative regulation of gene expression, epigenetic
C0045892biological_processnegative regulation of DNA-templated transcription
C0046976molecular_functionhistone H3K27 methyltransferase activity
C0048387biological_processnegative regulation of retinoic acid receptor signaling pathway
C0048468biological_processcell development
C0048511biological_processrhythmic process
C0051932biological_processsynaptic transmission, GABAergic
C0070878molecular_functionprimary miRNA binding
C0071902biological_processpositive regulation of protein serine/threonine kinase activity
C0090183biological_processregulation of kidney development
C0106222molecular_functionlncRNA binding
C0140718biological_processfacultative heterochromatin formation
C0140938molecular_functionhistone H3 methyltransferase activity
C0140951molecular_functionhistone H3K27 trimethyltransferase activity
C1900006biological_processpositive regulation of dendrite development
C1900016biological_processnegative regulation of cytokine production involved in inflammatory response
C1902808biological_processpositive regulation of cell cycle G1/S phase transition
C1990841molecular_functionpromoter-specific chromatin binding
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005694cellular_componentchromosome
I0030527molecular_functionstructural constituent of chromatin
I0031492molecular_functionnucleosomal DNA binding
I0031507biological_processheterochromatin formation
I0046982molecular_functionprotein heterodimerization activity
J0000786cellular_componentnucleosome
J0003677molecular_functionDNA binding
J0005515molecular_functionprotein binding
J0005634cellular_componentnucleus
J0005694cellular_componentchromosome
J0006334biological_processnucleosome assembly
J0030527molecular_functionstructural constituent of chromatin
J0031507biological_processheterochromatin formation
J0046982molecular_functionprotein heterodimerization activity
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0005634cellular_componentnucleus
K0005694cellular_componentchromosome
K0030527molecular_functionstructural constituent of chromatin
K0031507biological_processheterochromatin formation
K0046982molecular_functionprotein heterodimerization activity
L0000122biological_processnegative regulation of transcription by RNA polymerase II
L0001222molecular_functiontranscription corepressor binding
L0001739cellular_componentsex chromatin
L0003682molecular_functionchromatin binding
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005654cellular_componentnucleoplasm
L0005677cellular_componentchromatin silencing complex
L0005694cellular_componentchromosome
L0006325biological_processchromatin organization
L0006351biological_processDNA-templated transcription
L0008047molecular_functionenzyme activator activity
L0021510biological_processspinal cord development
L0031491molecular_functionnucleosome binding
L0031507biological_processheterochromatin formation
L0035098cellular_componentESC/E(Z) complex
L0042802molecular_functionidentical protein binding
L0045120cellular_componentpronucleus
L0045892biological_processnegative regulation of DNA-templated transcription
L0140718biological_processfacultative heterochromatin formation
L1990841molecular_functionpromoter-specific chromatin binding
M0000786cellular_componentnucleosome
M0002227biological_processinnate immune response in mucosa
M0003677molecular_functionDNA binding
M0005515molecular_functionprotein binding
M0005615cellular_componentextracellular space
M0005634cellular_componentnucleus
M0005694cellular_componentchromosome
M0006325biological_processchromatin organization
M0019731biological_processantibacterial humoral response
M0030527molecular_functionstructural constituent of chromatin
M0031507biological_processheterochromatin formation
M0046982molecular_functionprotein heterodimerization activity
M0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
N0000118cellular_componenthistone deacetylase complex
N0000122biological_processnegative regulation of transcription by RNA polymerase II
N0000781cellular_componentchromosome, telomeric region
N0000785cellular_componentchromatin
N0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0006260biological_processDNA replication
N0006281biological_processDNA repair
N0006325biological_processchromatin organization
N0006334biological_processnucleosome assembly
N0006335biological_processDNA replication-dependent chromatin assembly
N0006338biological_processchromatin remodeling
N0006351biological_processDNA-templated transcription
N0006355biological_processregulation of DNA-templated transcription
N0006974biological_processDNA damage response
N0007420biological_processbrain development
N0008094molecular_functionATP-dependent activity, acting on DNA
N0008285biological_processnegative regulation of cell population proliferation
N0016581cellular_componentNuRD complex
N0016589cellular_componentNURF complex
N0030336biological_processnegative regulation of cell migration
N0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
N0031492molecular_functionnucleosomal DNA binding
N0031507biological_processheterochromatin formation
N0032991cellular_componentprotein-containing complex
N0033186cellular_componentCAF-1 complex
N0035098cellular_componentESC/E(Z) complex
N0042393molecular_functionhistone binding
N0042659biological_processregulation of cell fate specification
N0042826molecular_functionhistone deacetylase binding
N0045892biological_processnegative regulation of DNA-templated transcription
N0045893biological_processpositive regulation of DNA-templated transcription
N0045944biological_processpositive regulation of transcription by RNA polymerase II
N0070822cellular_componentSin3-type complex
N1902455biological_processnegative regulation of stem cell population maintenance
N1902459biological_processpositive regulation of stem cell population maintenance
N2000736biological_processregulation of stem cell differentiation
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0030527molecular_functionstructural constituent of chromatin
O0031492molecular_functionnucleosomal DNA binding
O0031507biological_processheterochromatin formation
O0046982molecular_functionprotein heterodimerization activity
Q0000786cellular_componentnucleosome
Q0003677molecular_functionDNA binding
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005694cellular_componentchromosome
Q0006334biological_processnucleosome assembly
Q0030527molecular_functionstructural constituent of chromatin
Q0031507biological_processheterochromatin formation
Q0046982molecular_functionprotein heterodimerization activity
R0000786cellular_componentnucleosome
R0003677molecular_functionDNA binding
R0005634cellular_componentnucleus
R0005694cellular_componentchromosome
R0030527molecular_functionstructural constituent of chromatin
R0031507biological_processheterochromatin formation
R0046982molecular_functionprotein heterodimerization activity
S0000786cellular_componentnucleosome
S0002227biological_processinnate immune response in mucosa
S0003677molecular_functionDNA binding
S0005515molecular_functionprotein binding
S0005615cellular_componentextracellular space
S0005634cellular_componentnucleus
S0005694cellular_componentchromosome
S0006325biological_processchromatin organization
S0019731biological_processantibacterial humoral response
S0030527molecular_functionstructural constituent of chromatin
S0031507biological_processheterochromatin formation
S0046982molecular_functionprotein heterodimerization activity
S0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 801
ChainResidue
APRO510
AALA513

site_idAC2
Number of Residues13
Detailsbinding site for residue SAH C 801
ChainResidue
CPHE665
CASN688
CHIS689
CTYR736
CVAL737
CILE739
CVAL621
CALA622
CGLY623
CTRP624
CMET662
CCYS663
CSER664

site_idAC3
Number of Residues3
Detailsbinding site for residue ZN P 301
ChainResidue
PCYS94
PHIS110
PMET111

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues24
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. CcwdqCqacFnsspdladHirsi.H
ChainResidueDetails
PCYS55-HIS78
PCYS122-HIS144
ACYS450-HIS471

site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
KALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
JGLY14-HIS18

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
TLYS27-ASP52

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ILYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
MARG89-GLY111

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI
ChainResidueDetails
NLEU193-ILE207
NLEU289-LEU303
NLEU333-LEU347
LLEU206-ILE220

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
IPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsZinc finger: {"description":"C2H2-type"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsRegion: {"description":"VEFS-box"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Breakpoint for translocation to form JAZF1-SUZ12 oncogene"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
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_FI7
Number of Residues43
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues43
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues41
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues37
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues40
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues33
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues360
DetailsRegion: {"description":"Interaction with EZH2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues294
DetailsRegion: {"description":"Required for interaction with the matrix protein MA of HIV-1"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"20974918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues49
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues47
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues45
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues56
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues32
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues102
DetailsDomain: {"description":"CXC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00970","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues115
DetailsDomain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues29
DetailsRegion: {"description":"Interaction with EED","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"16224021","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","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"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"24474760","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues25
DetailsZinc finger: {"description":"C2H2-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 2; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues71
DetailsRegion: {"description":"Interaction with SUZ12","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues5
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues1
DetailsModified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI47
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI48
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI49
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI50
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI51
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI52
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI53
Number of Residues5
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI54
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI55
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI56
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI57
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI58
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI59
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI60
Number of Residues4
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI61
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI62
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI63
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI64
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI65
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI66
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI67
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI68
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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