Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9S3G

State 1 MAP3 RNA Pol II activated elongation complex with SETD2 and upstream hexasome

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000428	cellular_component	DNA-directed RNA polymerase complex
A	0001172	biological_process	RNA-templated transcription
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003899	molecular_function	DNA-directed RNA polymerase activity
A	0003968	molecular_function	RNA-directed RNA polymerase activity
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005737	cellular_component	cytoplasm
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000428	cellular_component	DNA-directed RNA polymerase complex
B	0000781	cellular_component	chromosome, telomeric region
B	0001172	biological_process	RNA-templated transcription
B	0003682	molecular_function	chromatin binding
B	0003899	molecular_function	DNA-directed RNA polymerase activity
B	0003968	molecular_function	RNA-directed RNA polymerase activity
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005665	cellular_component	RNA polymerase II, core complex
B	0006354	biological_process	DNA-templated transcription elongation
B	0006366	biological_process	transcription by RNA polymerase II
B	0006367	biological_process	transcription initiation at RNA polymerase II promoter
B	0006368	biological_process	transcription elongation by RNA polymerase II
B	0008270	molecular_function	zinc ion binding
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	0000428	cellular_component	DNA-directed RNA polymerase complex
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005665	cellular_component	RNA polymerase II, core complex
C	0006366	biological_process	transcription by RNA polymerase II
C	0006367	biological_process	transcription initiation at RNA polymerase II promoter
C	0006368	biological_process	transcription elongation by RNA polymerase II
C	0046872	molecular_function	metal ion binding
E	0000428	cellular_component	DNA-directed RNA polymerase complex
E	0003899	molecular_function	DNA-directed RNA polymerase activity
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	0005736	cellular_component	RNA polymerase I complex
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
F	0000428	cellular_component	DNA-directed RNA polymerase complex
F	0001650	cellular_component	fibrillar center
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	0005736	cellular_component	RNA polymerase I complex
F	0006362	biological_process	transcription elongation by RNA polymerase I
F	0006366	biological_process	transcription by RNA polymerase II
F	0006367	biological_process	transcription initiation at RNA polymerase II promoter
F	0006368	biological_process	transcription elongation by RNA polymerase II
F	0006383	biological_process	transcription by RNA polymerase III
F	0006384	biological_process	transcription initiation at RNA polymerase III promoter
F	0006386	biological_process	termination of RNA polymerase III transcription
G	0000428	cellular_component	DNA-directed RNA polymerase complex
G	0005634	cellular_component	nucleus
G	0006352	biological_process	DNA-templated transcription initiation
H	0000428	cellular_component	DNA-directed RNA polymerase complex
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	0005736	cellular_component	RNA polymerase I complex
H	0006351	biological_process	DNA-templated transcription
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	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	0006368	biological_process	transcription elongation by RNA polymerase II
I	0008270	molecular_function	zinc ion binding
I	0046872	molecular_function	metal ion binding
J	0000428	cellular_component	DNA-directed RNA polymerase complex
J	0005634	cellular_component	nucleus
J	0005665	cellular_component	RNA polymerase II, core complex
J	0008270	molecular_function	zinc ion binding
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	0005634	cellular_component	nucleus
K	0005665	cellular_component	RNA polymerase II, core complex
K	0006366	biological_process	transcription by RNA polymerase II
L	0000428	cellular_component	DNA-directed RNA polymerase complex
L	0001650	cellular_component	fibrillar center
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	0006362	biological_process	transcription elongation by RNA polymerase I
L	0006366	biological_process	transcription by RNA polymerase II
L	0006367	biological_process	transcription initiation at RNA polymerase II promoter
L	0006368	biological_process	transcription elongation by RNA polymerase II
L	0006383	biological_process	transcription by RNA polymerase III
L	0006384	biological_process	transcription initiation at RNA polymerase III promoter
L	0006386	biological_process	termination of RNA polymerase III transcription
L	0008270	molecular_function	zinc ion binding
L	0046872	molecular_function	metal ion binding
M	0003723	molecular_function	RNA binding
M	0005515	molecular_function	protein binding
M	0005634	cellular_component	nucleus
M	0005654	cellular_component	nucleoplasm
M	0006351	biological_process	DNA-templated transcription
M	0006368	biological_process	transcription elongation by RNA polymerase II
M	0006397	biological_process	mRNA processing
M	0008023	cellular_component	transcription elongation factor complex
M	0008380	biological_process	RNA splicing
M	0031491	molecular_function	nucleosome binding
M	0034728	biological_process	nucleosome organization
M	0042393	molecular_function	histone binding
M	0045191	biological_process	regulation of isotype switching
M	0051028	biological_process	mRNA transport
M	0051147	biological_process	regulation of muscle cell differentiation
M	0140673	biological_process	transcription elongation-coupled chromatin remodeling
Q	0000122	biological_process	negative regulation of transcription by RNA polymerase II
Q	0000791	cellular_component	euchromatin
Q	0000993	molecular_function	RNA polymerase II complex binding
Q	0001711	biological_process	endodermal cell fate commitment
Q	0005515	molecular_function	protein binding
Q	0005634	cellular_component	nucleus
Q	0005654	cellular_component	nucleoplasm
Q	0006325	biological_process	chromatin organization
Q	0006351	biological_process	DNA-templated transcription
Q	0006357	biological_process	regulation of transcription by RNA polymerase II
Q	0006368	biological_process	transcription elongation by RNA polymerase II
Q	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
Q	0016055	biological_process	Wnt signaling pathway
Q	0016593	cellular_component	Cdc73/Paf1 complex
Q	0016607	cellular_component	nuclear speck
Q	0019827	biological_process	stem cell population maintenance
Q	0042169	molecular_function	SH2 domain binding
Q	0045638	biological_process	negative regulation of myeloid cell differentiation
Q	0045944	biological_process	positive regulation of transcription by RNA polymerase II
Q	0070102	biological_process	interleukin-6-mediated signaling pathway
Q	0071222	biological_process	cellular response to lipopolysaccharide
R	0000122	biological_process	negative regulation of transcription by RNA polymerase II
R	0001711	biological_process	endodermal cell fate commitment
R	0003677	molecular_function	DNA binding
R	0003697	molecular_function	single-stranded DNA binding
R	0003723	molecular_function	RNA binding
R	0005515	molecular_function	protein binding
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005730	cellular_component	nucleolus
R	0006325	biological_process	chromatin organization
R	0006351	biological_process	DNA-templated transcription
R	0006368	biological_process	transcription elongation by RNA polymerase II
R	0016055	biological_process	Wnt signaling pathway
R	0016593	cellular_component	Cdc73/Paf1 complex
R	0019827	biological_process	stem cell population maintenance
S	0003677	molecular_function	DNA binding
S	0003711	molecular_function	transcription elongation factor activity
S	0005515	molecular_function	protein binding
S	0005634	cellular_component	nucleus
S	0005654	cellular_component	nucleoplasm
S	0005669	cellular_component	transcription factor TFIID complex
S	0006351	biological_process	DNA-templated transcription
S	0006368	biological_process	transcription elongation by RNA polymerase II
S	0008270	molecular_function	zinc ion binding
S	0046872	molecular_function	metal ion binding
U	0001650	cellular_component	fibrillar center
U	0001711	biological_process	endodermal cell fate commitment
U	0005515	molecular_function	protein binding
U	0005634	cellular_component	nucleus
U	0005654	cellular_component	nucleoplasm
U	0006351	biological_process	DNA-templated transcription
U	0006368	biological_process	transcription elongation by RNA polymerase II
U	0016055	biological_process	Wnt signaling pathway
U	0016593	cellular_component	Cdc73/Paf1 complex
U	0019827	biological_process	stem cell population maintenance
U	0031124	biological_process	mRNA 3'-end processing
U	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
U	0045638	biological_process	negative regulation of myeloid cell differentiation
U	0045944	biological_process	positive regulation of transcription by RNA polymerase II
U	1990269	molecular_function	RNA polymerase II C-terminal domain phosphoserine binding
V	0000122	biological_process	negative regulation of transcription by RNA polymerase II
V	0000993	molecular_function	RNA polymerase II complex binding
V	0001650	cellular_component	fibrillar center
V	0001711	biological_process	endodermal cell fate commitment
V	0003682	molecular_function	chromatin binding
V	0005515	molecular_function	protein binding
V	0005634	cellular_component	nucleus
V	0005654	cellular_component	nucleoplasm
V	0005737	cellular_component	cytoplasm
V	0006351	biological_process	DNA-templated transcription
V	0006368	biological_process	transcription elongation by RNA polymerase II
V	0016020	cellular_component	membrane
V	0016055	biological_process	Wnt signaling pathway
V	0016593	cellular_component	Cdc73/Paf1 complex
V	0019827	biological_process	stem cell population maintenance
V	0031124	biological_process	mRNA 3'-end processing
V	0034504	biological_process	protein localization to nucleus
V	0045638	biological_process	negative regulation of myeloid cell differentiation
V	0045944	biological_process	positive regulation of transcription by RNA polymerase II
V	0071222	biological_process	cellular response to lipopolysaccharide
V	1902808	biological_process	positive regulation of cell cycle G1/S phase transition
W	0000791	cellular_component	euchromatin
W	0000956	biological_process	nuclear-transcribed mRNA catabolic process
W	0005515	molecular_function	protein binding
W	0005634	cellular_component	nucleus
W	0005654	cellular_component	nucleoplasm
W	0005737	cellular_component	cytoplasm
W	0005829	cellular_component	cytosol
W	0006351	biological_process	DNA-templated transcription
W	0006368	biological_process	transcription elongation by RNA polymerase II
W	0016055	biological_process	Wnt signaling pathway
W	0016593	cellular_component	Cdc73/Paf1 complex
W	0045638	biological_process	negative regulation of myeloid cell differentiation
W	0055087	cellular_component	Ski complex
W	0070478	biological_process	nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay
W	0072344	biological_process	rescue of stalled ribosome
X	0000122	biological_process	negative regulation of transcription by RNA polymerase II
X	0000781	cellular_component	chromosome, telomeric region
X	0000993	molecular_function	RNA polymerase II complex binding
X	0001711	biological_process	endodermal cell fate commitment
X	0005515	molecular_function	protein binding
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0006351	biological_process	DNA-templated transcription
X	0006368	biological_process	transcription elongation by RNA polymerase II
X	0008285	biological_process	negative regulation of cell population proliferation
X	0016055	biological_process	Wnt signaling pathway
X	0016593	cellular_component	Cdc73/Paf1 complex
X	0019827	biological_process	stem cell population maintenance
X	0030177	biological_process	positive regulation of Wnt signaling pathway
X	0031124	biological_process	mRNA 3'-end processing
X	0031442	biological_process	positive regulation of mRNA 3'-end processing
X	0031648	biological_process	protein destabilization
X	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
X	0045638	biological_process	negative regulation of myeloid cell differentiation
X	0045944	biological_process	positive regulation of transcription by RNA polymerase II
X	0048147	biological_process	negative regulation of fibroblast proliferation
X	0050680	biological_process	negative regulation of epithelial cell proliferation
X	0071222	biological_process	cellular response to lipopolysaccharide
X	1902808	biological_process	positive regulation of cell cycle G1/S phase transition
X	2000134	biological_process	negative regulation of G1/S transition of mitotic cell cycle
Y	0000122	biological_process	negative regulation of transcription by RNA polymerase II
Y	0000993	molecular_function	RNA polymerase II complex binding
Y	0005634	cellular_component	nucleus
Y	0006351	biological_process	DNA-templated transcription
Y	0006368	biological_process	transcription elongation by RNA polymerase II
Y	0008270	molecular_function	zinc ion binding
Y	0032044	cellular_component	DSIF complex
Y	0032785	biological_process	negative regulation of DNA-templated transcription, elongation
Y	0032786	biological_process	positive regulation of DNA-templated transcription, elongation
Y	0034243	biological_process	regulation of transcription elongation by RNA polymerase II
Y	0045944	biological_process	positive regulation of transcription by RNA polymerase II
Y	0046872	molecular_function	metal ion binding
Y	0046982	molecular_function	protein heterodimerization activity
Y	0140870	molecular_function	RNA polymerase inhibitor activity
Y	0160239	biological_process	transcription pausing by RNA polymerase II
Z	0000122	biological_process	negative regulation of transcription by RNA polymerase II
Z	0003723	molecular_function	RNA binding
Z	0003729	molecular_function	mRNA binding
Z	0005515	molecular_function	protein binding
Z	0005634	cellular_component	nucleus
Z	0005654	cellular_component	nucleoplasm
Z	0006351	biological_process	DNA-templated transcription
Z	0006368	biological_process	transcription elongation by RNA polymerase II
Z	0016239	biological_process	positive regulation of macroautophagy
Z	0019899	molecular_function	enzyme binding
Z	0032044	cellular_component	DSIF complex
Z	0032785	biological_process	negative regulation of DNA-templated transcription, elongation
Z	0032786	biological_process	positive regulation of DNA-templated transcription, elongation
Z	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
Z	0034243	biological_process	regulation of transcription elongation by RNA polymerase II
Z	0045944	biological_process	positive regulation of transcription by RNA polymerase II
Z	0046982	molecular_function	protein heterodimerization activity
Z	0140870	molecular_function	RNA polymerase inhibitor activity
Z	0160239	biological_process	transcription pausing by RNA polymerase II
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	0030527	molecular_function	structural constituent of chromatin
a	0031492	molecular_function	nucleosomal DNA binding
a	0031507	biological_process	heterochromatin formation
a	0070062	cellular_component	extracellular exosome
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	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
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	0030527	molecular_function	structural constituent of chromatin
e	0031492	molecular_function	nucleosomal DNA binding
e	0031507	biological_process	heterochromatin formation
e	0070062	cellular_component	extracellular exosome
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	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
g	0000786	cellular_component	nucleosome
g	0003677	molecular_function	DNA binding
g	0005515	molecular_function	protein binding
g	0005634	cellular_component	nucleus
g	0005654	cellular_component	nucleoplasm
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	0061644	biological_process	protein localization to CENP-A containing chromatin
g	0070062	cellular_component	extracellular exosome
h	0000786	cellular_component	nucleosome
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	0006325	biological_process	chromatin organization
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	0050829	biological_process	defense response to Gram-negative bacterium
h	0050830	biological_process	defense response to Gram-positive bacterium
h	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
j	0003723	molecular_function	RNA binding
j	0005634	cellular_component	nucleus
j	0005654	cellular_component	nucleoplasm
j	0005694	cellular_component	chromosome
j	0006260	biological_process	DNA replication
j	0006281	biological_process	DNA repair
j	0006334	biological_process	nucleosome assembly
j	0006337	biological_process	nucleosome disassembly
j	0006351	biological_process	DNA-templated transcription
j	0006366	biological_process	transcription by RNA polymerase II
j	0006974	biological_process	DNA damage response
j	0008023	cellular_component	transcription elongation factor complex
j	0031491	molecular_function	nucleosome binding
j	0032784	biological_process	regulation of DNA-templated transcription elongation
j	0032786	biological_process	positive regulation of DNA-templated transcription, elongation
j	0035101	cellular_component	FACT complex
k	0003677	molecular_function	DNA binding
k	0003682	molecular_function	chromatin binding
k	0003723	molecular_function	RNA binding
k	0005515	molecular_function	protein binding
k	0005634	cellular_component	nucleus
k	0005654	cellular_component	nucleoplasm
k	0005694	cellular_component	chromosome
k	0005730	cellular_component	nucleolus
k	0006260	biological_process	DNA replication
k	0006281	biological_process	DNA repair
k	0006334	biological_process	nucleosome assembly
k	0006337	biological_process	nucleosome disassembly
k	0006351	biological_process	DNA-templated transcription
k	0006974	biological_process	DNA damage response
k	0031491	molecular_function	nucleosome binding
k	0035101	cellular_component	FACT complex
k	0042393	molecular_function	histone binding
k	1902275	biological_process	regulation of chromatin organization

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ASP136-ILE148

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

Chain	Residue	Details
g	ALA22-VAL28

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

Chain	Residue	Details
b	GLY15-HIS19

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	TYR1832-LYS1838
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	TYR1629-ASN1635
A	TYR1916-LYS1922
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	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YVCTAPH

Chain	Residue	Details
I	TYR112-HIS118

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

Chain	Residue	Details
a	LYS15-LEU21

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

Chain	Residue	Details
h	ARG93-GLY115

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	PS00466
Number of Residues	36
Details	ZF_TFIIS_1 Zinc finger TFIIS-type signature. CgkCkkknctytqVQTRSaDEPmttfvvCne...CgnrW

Chain	Residue	Details
S	CYS263-TRP298
I	CYS86-TRP123

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

Chain	Residue	Details
W	ALA79-LEU93

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

Chain	Residue	Details
a	PRO67-ILE75

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

Chain	Residue	Details
E	HIS142-GLU155

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	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	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	PS01159
Number of Residues	26
Details	WW_DOMAIN_1 WW/rsp5/WWP domain signature. WktardpegkiyYYhvitrq.TQWDPP

Chain	Residue	Details
O	TRP2395-PRO2420

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

Chain	Residue	Details
B	GLY932-THR944

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI9
Number of Residues	45
Details	Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
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_FI11
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10145","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	34
Details	Repeat: {"description":"TPR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	33
Details	Repeat: {"description":"TPR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	33
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	33
Details	Repeat: {"description":"TPR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	33
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	33
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	33
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	32
Details	Repeat: {"description":"TPR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	33
Details	Repeat: {"description":"TPR 9"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	33
Details	Repeat: {"description":"TPR 10"}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	33
Details	Repeat: {"description":"TPR 11"}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	32
Details	Repeat: {"description":"TPR 12"}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	33
Details	Repeat: {"description":"TPR 13"}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	33
Details	Repeat: {"description":"TPR 14"}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	33
Details	Repeat: {"description":"TPR 15"}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	33
Details	Repeat: {"description":"TPR 16"}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	43
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	39
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	39
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	41
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	39
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	39
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	33
Details	Repeat: {"description":"WD 7"}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Modified residue: {"description":"N-acetylthreonine; in WD repeat-containing protein 61, N-terminally processed","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	38
Details	Region: {"description":"Interaction with SUPT5H","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P63272","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P63272","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	33
Details	Domain: {"description":"KOW 1"}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	31
Details	Domain: {"description":"KOW 2"}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	31
Details	Domain: {"description":"KOW 3"}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	33
Details	Domain: {"description":"KOW 4"}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	33
Details	Domain: {"description":"KOW 5"}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O55201","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	11
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
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_FI56
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_FI57
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI60
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_FI61
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_FI62
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"21076176","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI63
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_FI64
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_FI65
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_FI66
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_FI67
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI68
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI69
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_FI70
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_FI71
Number of Residues	5
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_FI72
Number of Residues	1
Details	Modified residue: {"description":"N6-crotonyllysine; alternate","evidences":[{"source":"PubMed","id":"21925322","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI73
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI74
Number of Residues	1
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"source":"PubMed","id":"24352239","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI75
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_FI76
Number of Residues	1
Details	Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI77
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q8CGP1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI78
Number of Residues	2
Details	Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI79
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI80
Number of Residues	1
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI81
Number of Residues	1
Details	Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI82
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI83
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI84
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI85
Number of Residues	1
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_FI86
Number of Residues	2
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

site_id	SWS_FT_FI87
Number of Residues	15
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI88
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI89
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI90
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"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_FI91
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI92
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI93
Number of Residues	5
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_FI94
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI95
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Vousden K.H.","Lukashchuk N."]}},{"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_FI96
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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