Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8T9G

Automethylated PRC2 dimer bound to nucleosome

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0030527	molecular_function	structural constituent of chromatin
A	0031492	molecular_function	nucleosomal DNA binding
A	0031507	biological_process	heterochromatin formation
A	0046982	molecular_function	protein heterodimerization activity
C	0006338	biological_process	chromatin remodeling
C	0042054	molecular_function	histone methyltransferase activity
C	0046976	molecular_function	histone H3K27 methyltransferase activity
F	0000122	biological_process	negative regulation of transcription by RNA polymerase II
F	0001222	molecular_function	transcription corepressor binding
F	0001739	cellular_component	sex chromatin
F	0003682	molecular_function	chromatin binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005677	cellular_component	chromatin silencing complex
F	0005694	cellular_component	chromosome
F	0006325	biological_process	chromatin organization
F	0006351	biological_process	DNA-templated transcription
F	0008047	molecular_function	enzyme activator activity
F	0021510	biological_process	spinal cord development
F	0031491	molecular_function	nucleosome binding
F	0031507	biological_process	heterochromatin formation
F	0035098	cellular_component	ESC/E(Z) complex
F	0042802	molecular_function	identical protein binding
F	0045120	cellular_component	pronucleus
F	0045892	biological_process	negative regulation of DNA-templated transcription
F	0140718	biological_process	facultative heterochromatin formation
F	1990841	molecular_function	promoter-specific chromatin binding
I	0006338	biological_process	chromatin remodeling
I	0042054	molecular_function	histone methyltransferase activity
I	0046976	molecular_function	histone H3K27 methyltransferase activity
J	0000786	cellular_component	nucleosome
J	0003677	molecular_function	DNA binding
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005694	cellular_component	chromosome
J	0006334	biological_process	nucleosome assembly
J	0030527	molecular_function	structural constituent of chromatin
J	0031507	biological_process	heterochromatin formation
J	0046982	molecular_function	protein heterodimerization activity
K	0000122	biological_process	negative regulation of transcription by RNA polymerase II
K	0001222	molecular_function	transcription corepressor binding
K	0001739	cellular_component	sex chromatin
K	0003682	molecular_function	chromatin binding
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005677	cellular_component	chromatin silencing complex
K	0005694	cellular_component	chromosome
K	0006325	biological_process	chromatin organization
K	0006351	biological_process	DNA-templated transcription
K	0008047	molecular_function	enzyme activator activity
K	0021510	biological_process	spinal cord development
K	0031491	molecular_function	nucleosome binding
K	0031507	biological_process	heterochromatin formation
K	0035098	cellular_component	ESC/E(Z) complex
K	0042802	molecular_function	identical protein binding
K	0045120	cellular_component	pronucleus
K	0045892	biological_process	negative regulation of DNA-templated transcription
K	0140718	biological_process	facultative heterochromatin formation
K	1990841	molecular_function	promoter-specific chromatin binding
L	0000118	cellular_component	histone deacetylase complex
L	0000122	biological_process	negative regulation of transcription by RNA polymerase II
L	0000781	cellular_component	chromosome, telomeric region
L	0000785	cellular_component	chromatin
L	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0005654	cellular_component	nucleoplasm
L	0006260	biological_process	DNA replication
L	0006281	biological_process	DNA repair
L	0006325	biological_process	chromatin organization
L	0006334	biological_process	nucleosome assembly
L	0006335	biological_process	DNA replication-dependent chromatin assembly
L	0006338	biological_process	chromatin remodeling
L	0006351	biological_process	DNA-templated transcription
L	0006355	biological_process	regulation of DNA-templated transcription
L	0006974	biological_process	DNA damage response
L	0007420	biological_process	brain development
L	0008094	molecular_function	ATP-dependent activity, acting on DNA
L	0008285	biological_process	negative regulation of cell population proliferation
L	0016581	cellular_component	NuRD complex
L	0016589	cellular_component	NURF complex
L	0030336	biological_process	negative regulation of cell migration
L	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
L	0031492	molecular_function	nucleosomal DNA binding
L	0031507	biological_process	heterochromatin formation
L	0032991	cellular_component	protein-containing complex
L	0033186	cellular_component	CAF-1 complex
L	0035098	cellular_component	ESC/E(Z) complex
L	0042393	molecular_function	histone binding
L	0042659	biological_process	regulation of cell fate specification
L	0042826	molecular_function	histone deacetylase binding
L	0045892	biological_process	negative regulation of DNA-templated transcription
L	0045893	biological_process	positive regulation of DNA-templated transcription
L	0045944	biological_process	positive regulation of transcription by RNA polymerase II
L	0070822	cellular_component	Sin3-type complex
L	1902455	biological_process	negative regulation of stem cell population maintenance
L	1902459	biological_process	positive regulation of stem cell population maintenance
L	2000736	biological_process	regulation of stem cell differentiation
O	0000118	cellular_component	histone deacetylase complex
O	0000122	biological_process	negative regulation of transcription by RNA polymerase II
O	0000781	cellular_component	chromosome, telomeric region
O	0000785	cellular_component	chromatin
O	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005654	cellular_component	nucleoplasm
O	0006260	biological_process	DNA replication
O	0006281	biological_process	DNA repair
O	0006325	biological_process	chromatin organization
O	0006334	biological_process	nucleosome assembly
O	0006335	biological_process	DNA replication-dependent chromatin assembly
O	0006338	biological_process	chromatin remodeling
O	0006351	biological_process	DNA-templated transcription
O	0006355	biological_process	regulation of DNA-templated transcription
O	0006974	biological_process	DNA damage response
O	0007420	biological_process	brain development
O	0008094	molecular_function	ATP-dependent activity, acting on DNA
O	0008285	biological_process	negative regulation of cell population proliferation
O	0016581	cellular_component	NuRD complex
O	0016589	cellular_component	NURF complex
O	0030336	biological_process	negative regulation of cell migration
O	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
O	0031492	molecular_function	nucleosomal DNA binding
O	0031507	biological_process	heterochromatin formation
O	0032991	cellular_component	protein-containing complex
O	0033186	cellular_component	CAF-1 complex
O	0035098	cellular_component	ESC/E(Z) complex
O	0042393	molecular_function	histone binding
O	0042659	biological_process	regulation of cell fate specification
O	0042826	molecular_function	histone deacetylase binding
O	0045892	biological_process	negative regulation of DNA-templated transcription
O	0045893	biological_process	positive regulation of DNA-templated transcription
O	0045944	biological_process	positive regulation of transcription by RNA polymerase II
O	0070822	cellular_component	Sin3-type complex
O	1902455	biological_process	negative regulation of stem cell population maintenance
O	1902459	biological_process	positive regulation of stem cell population maintenance
O	2000736	biological_process	regulation of stem cell differentiation
R	0000786	cellular_component	nucleosome
R	0003677	molecular_function	DNA binding
R	0005634	cellular_component	nucleus
R	0005694	cellular_component	chromosome
R	0030527	molecular_function	structural constituent of chromatin
R	0031507	biological_process	heterochromatin formation
R	0046982	molecular_function	protein heterodimerization activity
S	0000786	cellular_component	nucleosome
S	0002227	biological_process	innate immune response in mucosa
S	0003677	molecular_function	DNA binding
S	0005515	molecular_function	protein binding
S	0005615	cellular_component	extracellular space
S	0005634	cellular_component	nucleus
S	0005694	cellular_component	chromosome
S	0006325	biological_process	chromatin organization
S	0019731	biological_process	antibacterial humoral response
S	0030527	molecular_function	structural constituent of chromatin
S	0031507	biological_process	heterochromatin formation
S	0046982	molecular_function	protein heterodimerization activity
S	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
U	0000786	cellular_component	nucleosome
U	0003677	molecular_function	DNA binding
U	0005634	cellular_component	nucleus
U	0005694	cellular_component	chromosome
U	0030527	molecular_function	structural constituent of chromatin
U	0031507	biological_process	heterochromatin formation
U	0046982	molecular_function	protein heterodimerization activity
V	0000786	cellular_component	nucleosome
V	0002227	biological_process	innate immune response in mucosa
V	0003677	molecular_function	DNA binding
V	0005515	molecular_function	protein binding
V	0005615	cellular_component	extracellular space
V	0005634	cellular_component	nucleus
V	0005694	cellular_component	chromosome
V	0006325	biological_process	chromatin organization
V	0019731	biological_process	antibacterial humoral response
V	0030527	molecular_function	structural constituent of chromatin
V	0031507	biological_process	heterochromatin formation
V	0046982	molecular_function	protein heterodimerization activity
V	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
W	0000786	cellular_component	nucleosome
W	0003677	molecular_function	DNA binding
W	0005515	molecular_function	protein binding
W	0005634	cellular_component	nucleus
W	0005654	cellular_component	nucleoplasm
W	0005694	cellular_component	chromosome
W	0030527	molecular_function	structural constituent of chromatin
W	0031492	molecular_function	nucleosomal DNA binding
W	0031507	biological_process	heterochromatin formation
W	0046982	molecular_function	protein heterodimerization activity
X	0000786	cellular_component	nucleosome
X	0003677	molecular_function	DNA binding
X	0005515	molecular_function	protein binding
X	0005634	cellular_component	nucleus
X	0005694	cellular_component	chromosome
X	0006334	biological_process	nucleosome assembly
X	0030527	molecular_function	structural constituent of chromatin
X	0031507	biological_process	heterochromatin formation
X	0046982	molecular_function	protein heterodimerization activity

Functional Information from PROSITE/UniProt

site_id	PS00028
Number of Residues	24
Details	ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. CcwdqCqacFnsspdladHirsi.H

Chain	Residue	Details
M	CYS55-HIS78
M	CYS122-HIS144
B	CYS450-HIS471

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
R	ALA21-VAL27

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
J	GLY14-HIS18

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
A	LYS14-LEU20

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
S	ARG89-GLY111

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSVskDhALRLWNI

Chain	Residue	Details
F	LEU206-ILE220
L	LEU193-ILE207
L	LEU289-LEU303
L	LEU333-LEU347

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	46
Details	Zinc finger: {"description":"C2H2-type"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	152
Details	Region: {"description":"VEFS-box"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Breakpoint for translocation to form JAZF1-SUZ12 oncogene"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	230
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	58
Details	Region: {"description":"Interaction with EED","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"16224021","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"24474760","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	102
Details	Domain: {"description":"CXC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00970","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	86
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	86
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	80
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	82
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	74
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	80
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	66
Details	Repeat: {"description":"WD 7"}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	720
Details	Region: {"description":"Interaction with EZH2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	588
Details	Region: {"description":"Required for interaction with the matrix protein MA of HIV-1"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"20974918","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	98
Details	Repeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	94
Details	Repeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	90
Details	Repeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	86
Details	Repeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	112
Details	Repeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	64
Details	Repeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	4
Details	Cross-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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	142
Details	Region: {"description":"Interaction with SUZ12","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	5
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	5
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI56
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI57
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	4
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI60
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI61
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI62
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI63
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI64
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI65
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI66
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI67
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)