8XRJ

RNA polymerase II elongation complex with upstream nucleosome extracted from human nuclei

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	0005576	cellular_component	extracellular region
a	0005634	cellular_component	nucleus
a	0005654	cellular_component	nucleoplasm
a	0005694	cellular_component	chromosome
a	0006325	biological_process	chromatin organization
a	0006334	biological_process	nucleosome assembly
a	0016020	cellular_component	membrane
a	0030527	molecular_function	structural constituent of chromatin
a	0032200	biological_process	telomere organization
a	0032991	cellular_component	protein-containing complex
a	0040029	biological_process	epigenetic regulation of gene expression
a	0045296	molecular_function	cadherin binding
a	0070062	cellular_component	extracellular exosome
A	0000287	molecular_function	magnesium ion binding
A	0000428	cellular_component	DNA-directed RNA polymerase complex
A	0000974	cellular_component	Prp19 complex
A	0001172	biological_process	RNA-templated transcription
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003723	molecular_function	RNA binding
A	0003899	molecular_function	DNA-directed RNA polymerase activity
A	0003968	molecular_function	RNA-directed RNA polymerase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005665	cellular_component	RNA polymerase II, core complex
A	0005694	cellular_component	chromosome
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0006353	biological_process	DNA-templated transcription termination
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006366	biological_process	transcription by RNA polymerase II
A	0006368	biological_process	transcription elongation by RNA polymerase II
A	0008270	molecular_function	zinc ion binding
A	0010628	biological_process	positive regulation of gene expression
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0016787	molecular_function	hydrolase activity
A	0019900	molecular_function	kinase binding
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0033120	biological_process	positive regulation of RNA splicing
A	0034062	molecular_function	5'-3' RNA polymerase activity
A	0042789	biological_process	mRNA transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0050436	molecular_function	microfibril binding
A	1990841	molecular_function	promoter-specific chromatin binding
b	0000781	cellular_component	chromosome, telomeric region
b	0000786	cellular_component	nucleosome
b	0003677	molecular_function	DNA binding
b	0003723	molecular_function	RNA binding
b	0005515	molecular_function	protein binding
b	0005576	cellular_component	extracellular region
b	0005634	cellular_component	nucleus
b	0005654	cellular_component	nucleoplasm
b	0005694	cellular_component	chromosome
b	0006325	biological_process	chromatin organization
b	0006334	biological_process	nucleosome assembly
b	0016020	cellular_component	membrane
b	0030527	molecular_function	structural constituent of chromatin
b	0032200	biological_process	telomere organization
b	0032991	cellular_component	protein-containing complex
b	0043505	cellular_component	CENP-A containing nucleosome
b	0045653	biological_process	negative regulation of megakaryocyte differentiation
b	0061644	biological_process	protein localization to CENP-A containing chromatin
b	0070062	cellular_component	extracellular exosome
B	0000428	cellular_component	DNA-directed RNA polymerase complex
B	0000781	cellular_component	chromosome, telomeric region
B	0001172	biological_process	RNA-templated transcription
B	0003677	molecular_function	DNA binding
B	0003682	molecular_function	chromatin binding
B	0003723	molecular_function	RNA binding
B	0003899	molecular_function	DNA-directed RNA polymerase activity
B	0003968	molecular_function	RNA-directed RNA polymerase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005665	cellular_component	RNA polymerase II, core complex
B	0006366	biological_process	transcription by RNA polymerase II
B	0008270	molecular_function	zinc ion binding
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0016787	molecular_function	hydrolase activity
B	0034062	molecular_function	5'-3' RNA polymerase activity
B	0046872	molecular_function	metal ion binding
c	0000786	cellular_component	nucleosome
c	0003677	molecular_function	DNA binding
c	0005515	molecular_function	protein binding
c	0005634	cellular_component	nucleus
c	0005694	cellular_component	chromosome
c	0006325	biological_process	chromatin organization
c	0008285	biological_process	negative regulation of cell population proliferation
c	0030527	molecular_function	structural constituent of chromatin
c	0031507	biological_process	heterochromatin formation
c	0043505	cellular_component	CENP-A containing nucleosome
c	0061644	biological_process	protein localization to CENP-A containing chromatin
c	0070062	cellular_component	extracellular exosome
C	0000428	cellular_component	DNA-directed RNA polymerase complex
C	0003899	molecular_function	DNA-directed RNA polymerase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005665	cellular_component	RNA polymerase II, core complex
C	0005829	cellular_component	cytosol
C	0006366	biological_process	transcription by RNA polymerase II
d	0000786	cellular_component	nucleosome
d	0001530	molecular_function	lipopolysaccharide binding
d	0002227	biological_process	innate immune response in mucosa
d	0003677	molecular_function	DNA binding
d	0005515	molecular_function	protein binding
d	0005615	cellular_component	extracellular space
d	0005634	cellular_component	nucleus
d	0005654	cellular_component	nucleoplasm
d	0005694	cellular_component	chromosome
d	0005829	cellular_component	cytosol
d	0005886	cellular_component	plasma membrane
d	0006325	biological_process	chromatin organization
d	0006334	biological_process	nucleosome assembly
d	0010804	biological_process	negative regulation of tumor necrosis factor-mediated signaling pathway
d	0019731	biological_process	antibacterial humoral response
d	0030527	molecular_function	structural constituent of chromatin
d	0031640	biological_process	killing of cells of another organism
d	0042742	biological_process	defense response to bacterium
d	0043505	cellular_component	CENP-A containing nucleosome
d	0050829	biological_process	defense response to Gram-negative bacterium
d	0050830	biological_process	defense response to Gram-positive bacterium
d	0061644	biological_process	protein localization to CENP-A containing chromatin
d	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
D	0000428	cellular_component	DNA-directed RNA polymerase complex
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005665	cellular_component	RNA polymerase II, core complex
D	0005829	cellular_component	cytosol
D	0006366	biological_process	transcription by RNA polymerase II
D	0006367	biological_process	transcription initiation at RNA polymerase II promoter
D	0016607	cellular_component	nuclear speck
D	0031369	molecular_function	translation initiation factor binding
e	0000786	cellular_component	nucleosome
e	0003677	molecular_function	DNA binding
e	0005515	molecular_function	protein binding
e	0005576	cellular_component	extracellular region
e	0005634	cellular_component	nucleus
e	0005654	cellular_component	nucleoplasm
e	0005694	cellular_component	chromosome
e	0006325	biological_process	chromatin organization
e	0006334	biological_process	nucleosome assembly
e	0016020	cellular_component	membrane
e	0030527	molecular_function	structural constituent of chromatin
e	0032200	biological_process	telomere organization
e	0032991	cellular_component	protein-containing complex
e	0040029	biological_process	epigenetic regulation of gene expression
e	0045296	molecular_function	cadherin binding
e	0070062	cellular_component	extracellular exosome
E	0000428	cellular_component	DNA-directed RNA polymerase complex
E	0003899	molecular_function	DNA-directed RNA polymerase activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005665	cellular_component	RNA polymerase II, core complex
E	0005666	cellular_component	RNA polymerase III complex
E	0005730	cellular_component	nucleolus
E	0005736	cellular_component	RNA polymerase I complex
E	0005829	cellular_component	cytosol
E	0006362	biological_process	transcription elongation by RNA polymerase I
E	0006366	biological_process	transcription by RNA polymerase II
E	0042797	biological_process	tRNA transcription by RNA polymerase III
E	0050821	biological_process	protein stabilization
E	1990062	cellular_component	RPAP3/R2TP/prefoldin-like complex
f	0000781	cellular_component	chromosome, telomeric region
f	0000786	cellular_component	nucleosome
f	0003677	molecular_function	DNA binding
f	0003723	molecular_function	RNA binding
f	0005515	molecular_function	protein binding
f	0005576	cellular_component	extracellular region
f	0005634	cellular_component	nucleus
f	0005654	cellular_component	nucleoplasm
f	0005694	cellular_component	chromosome
f	0006325	biological_process	chromatin organization
f	0006334	biological_process	nucleosome assembly
f	0016020	cellular_component	membrane
f	0030527	molecular_function	structural constituent of chromatin
f	0032200	biological_process	telomere organization
f	0032991	cellular_component	protein-containing complex
f	0043505	cellular_component	CENP-A containing nucleosome
f	0045653	biological_process	negative regulation of megakaryocyte differentiation
f	0061644	biological_process	protein localization to CENP-A containing chromatin
f	0070062	cellular_component	extracellular exosome
F	0000428	cellular_component	DNA-directed RNA polymerase complex
F	0001650	cellular_component	fibrillar center
F	0003899	molecular_function	DNA-directed RNA polymerase activity
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005665	cellular_component	RNA polymerase II, core complex
F	0005666	cellular_component	RNA polymerase III complex
F	0005730	cellular_component	nucleolus
F	0005736	cellular_component	RNA polymerase I complex
F	0005829	cellular_component	cytosol
F	0006360	biological_process	transcription by RNA polymerase I
F	0006366	biological_process	transcription by RNA polymerase II
F	0042797	biological_process	tRNA transcription by RNA polymerase III
g	0000786	cellular_component	nucleosome
g	0003677	molecular_function	DNA binding
g	0005515	molecular_function	protein binding
g	0005634	cellular_component	nucleus
g	0005694	cellular_component	chromosome
g	0006325	biological_process	chromatin organization
g	0008285	biological_process	negative regulation of cell population proliferation
g	0030527	molecular_function	structural constituent of chromatin
g	0031507	biological_process	heterochromatin formation
g	0043505	cellular_component	CENP-A containing nucleosome
g	0061644	biological_process	protein localization to CENP-A containing chromatin
g	0070062	cellular_component	extracellular exosome
G	0000428	cellular_component	DNA-directed RNA polymerase complex
G	0000932	cellular_component	P-body
G	0000956	biological_process	nuclear-transcribed mRNA catabolic process
G	0003697	molecular_function	single-stranded DNA binding
G	0003723	molecular_function	RNA binding
G	0003727	molecular_function	single-stranded RNA binding
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005654	cellular_component	nucleoplasm
G	0005665	cellular_component	RNA polymerase II, core complex
G	0006366	biological_process	transcription by RNA polymerase II
G	0006367	biological_process	transcription initiation at RNA polymerase II promoter
G	0031369	molecular_function	translation initiation factor binding
G	0045948	biological_process	positive regulation of translational initiation
G	0060213	biological_process	positive regulation of nuclear-transcribed mRNA poly(A) tail shortening
h	0000786	cellular_component	nucleosome
h	0001530	molecular_function	lipopolysaccharide binding
h	0002227	biological_process	innate immune response in mucosa
h	0003677	molecular_function	DNA binding
h	0005515	molecular_function	protein binding
h	0005615	cellular_component	extracellular space
h	0005634	cellular_component	nucleus
h	0005654	cellular_component	nucleoplasm
h	0005694	cellular_component	chromosome
h	0005829	cellular_component	cytosol
h	0005886	cellular_component	plasma membrane
h	0006325	biological_process	chromatin organization
h	0006334	biological_process	nucleosome assembly
h	0010804	biological_process	negative regulation of tumor necrosis factor-mediated signaling pathway
h	0019731	biological_process	antibacterial humoral response
h	0030527	molecular_function	structural constituent of chromatin
h	0031640	biological_process	killing of cells of another organism
h	0042742	biological_process	defense response to bacterium
h	0043505	cellular_component	CENP-A containing nucleosome
h	0050829	biological_process	defense response to Gram-negative bacterium
h	0050830	biological_process	defense response to Gram-positive bacterium
h	0061644	biological_process	protein localization to CENP-A containing chromatin
h	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
H	0000428	cellular_component	DNA-directed RNA polymerase complex
H	0003677	molecular_function	DNA binding
H	0003697	molecular_function	single-stranded DNA binding
H	0003899	molecular_function	DNA-directed RNA polymerase activity
H	0005634	cellular_component	nucleus
H	0005654	cellular_component	nucleoplasm
H	0005665	cellular_component	RNA polymerase II, core complex
H	0005666	cellular_component	RNA polymerase III complex
H	0005730	cellular_component	nucleolus
H	0005736	cellular_component	RNA polymerase I complex
H	0005829	cellular_component	cytosol
H	0006366	biological_process	transcription by RNA polymerase II
H	0032993	cellular_component	protein-DNA complex
I	0000428	cellular_component	DNA-directed RNA polymerase complex
I	0001193	biological_process	maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II
I	0003899	molecular_function	DNA-directed RNA polymerase activity
I	0005515	molecular_function	protein binding
I	0005634	cellular_component	nucleus
I	0005654	cellular_component	nucleoplasm
I	0005665	cellular_component	RNA polymerase II, core complex
I	0005730	cellular_component	nucleolus
I	0006283	biological_process	transcription-coupled nucleotide-excision repair
I	0006366	biological_process	transcription by RNA polymerase II
I	0006367	biological_process	transcription initiation at RNA polymerase II promoter
I	0008270	molecular_function	zinc ion binding
I	0046872	molecular_function	metal ion binding
J	0000428	cellular_component	DNA-directed RNA polymerase complex
J	0003899	molecular_function	DNA-directed RNA polymerase activity
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005654	cellular_component	nucleoplasm
J	0005665	cellular_component	RNA polymerase II, core complex
J	0005666	cellular_component	RNA polymerase III complex
J	0005730	cellular_component	nucleolus
J	0005736	cellular_component	RNA polymerase I complex
J	0005829	cellular_component	cytosol
J	0006356	biological_process	regulation of transcription by RNA polymerase I
J	0006360	biological_process	transcription by RNA polymerase I
J	0006366	biological_process	transcription by RNA polymerase II
J	0008270	molecular_function	zinc ion binding
J	0042797	biological_process	tRNA transcription by RNA polymerase III
J	0046872	molecular_function	metal ion binding
K	0000428	cellular_component	DNA-directed RNA polymerase complex
K	0003899	molecular_function	DNA-directed RNA polymerase activity
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005665	cellular_component	RNA polymerase II, core complex
K	0006366	biological_process	transcription by RNA polymerase II
K	0030275	molecular_function	LRR domain binding
L	0000428	cellular_component	DNA-directed RNA polymerase complex
L	0003899	molecular_function	DNA-directed RNA polymerase activity
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0005654	cellular_component	nucleoplasm
L	0005665	cellular_component	RNA polymerase II, core complex
L	0005666	cellular_component	RNA polymerase III complex
L	0005730	cellular_component	nucleolus
L	0005736	cellular_component	RNA polymerase I complex
L	0005829	cellular_component	cytosol
L	0006356	biological_process	regulation of transcription by RNA polymerase I
L	0006366	biological_process	transcription by RNA polymerase II
L	0006383	biological_process	transcription by RNA polymerase III
L	0008270	molecular_function	zinc ion binding
L	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DNDPNDYVEqdDI

Chain	Residue	Details
C	ASP136-ILE148

---

site_id	PS00115
Number of Residues	7
Details	RNA_POL_II_REPEAT Eukaryotic RNA polymerase II heptapeptide repeat. YSPTSPA

Chain	Residue	Details
A	TYR1593-ALA1599
A	TYR1671-SER1677
A	TYR1678-SER1684
A	TYR1685-SER1691
A	TYR1692-SER1698
A	TYR1699-SER1705
A	TYR1706-SER1712
A	TYR1713-SER1719
A	TYR1720-SER1726
A	TYR1727-SER1733
A	TYR1734-SER1740
A	TYR1615-SER1621
A	TYR1741-ASN1747
A	TYR1748-ASN1754
A	TYR1755-SER1761
A	TYR1762-SER1768
A	TYR1769-ASN1775
A	TYR1776-ASN1782
A	TYR1783-SER1789
A	TYR1790-SER1796
A	TYR1797-SER1803
A	TYR1818-SER1824
A	TYR1622-SER1628
A	TYR1825-SER1831
A	TYR1839-SER1845
A	TYR1853-LYS1859
A	TYR1860-LYS1866
A	TYR1867-LYS1873
A	TYR1874-THR1880
A	TYR1888-THR1894
A	TYR1902-LYS1908
A	TYR1909-THR1915
A	TYR1916-LYS1922
A	TYR1629-ASN1635
A	TYR1923-THR1929
A	TYR1930-LYS1936
A	TYR1947-THR1953
A	TYR1636-SER1642
A	TYR1643-SER1649
A	TYR1650-SER1656
A	TYR1657-SER1663
A	TYR1664-SER1670

---

site_id	PS01154
Number of Residues	32
Details	RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. InkEdHTLgNiIksqLlkdpqVlfagYkvpHP

Chain	Residue	Details
K	ILE35-PRO66

---

site_id	PS00446
Number of Residues	41
Details	RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSIRRvfiaevpiiAidwVqidaNsSvlhDEfIAhRLGLIP

Chain	Residue	Details
C	ASN32-PRO72

---

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

Chain	Residue	Details
a	LYS14-LEU20

---

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

Chain	Residue	Details
a	PRO66-ILE74

---

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YVCTAPH

Chain	Residue	Details
I	TYR112-HIS118

---

site_id	PS00466
Number of Residues	38
Details	ZF_TFIIS_1 Zinc finger TFIIS-type signature. CqkCghkeavffqSHSARaEDAmrlyyvCtaph.CghrW

Chain	Residue	Details
I	CYS86-TRP123

---

site_id	PS01030
Number of Residues	27
Details	RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCQECNNMLypkedkenrillyaCrnC

Chain	Residue	Details
I	PHE16-CYS42

---

site_id	PS01111
Number of Residues	15
Details	RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARvLGtRAlQ

Chain	Residue	Details
F	THR58-GLN72

---

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

Chain	Residue	Details
b	GLY14-HIS18

---

site_id	PS01166
Number of Residues	13
Details	RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT

Chain	Residue	Details
B	GLY932-THR944

---

site_id	PS01112
Number of Residues	10
Details	RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IIPVrCFTCG

Chain	Residue	Details
J	ILE2-GLY11

---

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

Chain	Residue	Details
d	ARG92-GLY114

---

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

Chain	Residue	Details
c	ALA21-VAL27

---

site_id	PS01110
Number of Residues	14
Details	RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPEHvvMtkEE

Chain	Residue	Details
E	HIS142-GLU155

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	41
Details	Region: {"description":"Bridging helix","evidences":[{"source":"UniProtKB","id":"G3MZY8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"G3MZY8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	21
Details	Zinc finger: {"description":"C4-type","evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IYD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A5PJW8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	23
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
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_FI14
Number of Residues	24
Details	Region: {"description":"Non-specific ssDNA binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	25
Details	Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	42
Details	Zinc finger: {"description":"TFIIS-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10145","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33674783","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D58","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DN3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI21
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33674783","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DN3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI23
Number of Residues	20
Details	Zinc finger: {"description":"C4-type","evidences":[{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33674783","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DN3","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D58","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI24
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33674783","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DN3","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D58","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI25
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI26
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558764","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558766","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D58","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI27
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193682","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33558766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33674783","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DN3","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5IY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D58","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI28
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI29
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI31
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI33
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI34
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI35
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI36
Number of Residues	4
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI37
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27436229","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI38
Number of Residues	2
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"17267393","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI39
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21724829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI40
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI41
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI42
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI43
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI44
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"PubMed","id":"30886146","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI45
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"19818714","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI46
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI47
Number of Residues	2
Details	Modified residue: {"description":"N6-crotonyllysine; alternate","evidences":[{"source":"PubMed","id":"21925322","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI48
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI49
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"source":"PubMed","id":"24352239","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI50
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22713238","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22980979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI51
Number of Residues	2
Details	Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI52
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI53
Number of Residues	4
Details	Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI54
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI55
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI56
Number of Residues	2
Details	Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI57
Number of Residues	4
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI58
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI59
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_FI60
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"21726816","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI61
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"16307923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713563","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---