Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XRE

Structure of the p53/RNA polymerase II assembly

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
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	0006351	biological_process	DNA-templated transcription
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	0006367	biological_process	transcription initiation at RNA polymerase II promoter
A	0006368	biological_process	transcription elongation by RNA polymerase II
A	0006369	biological_process	termination of RNA polymerase II transcription
A	0008270	molecular_function	zinc ion binding
A	0010628	biological_process	positive regulation of gene expression
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	0050436	molecular_function	microfibril binding
A	1990841	molecular_function	promoter-specific chromatin binding
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	0006351	biological_process	DNA-templated transcription
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	0016020	cellular_component	membrane
B	0032549	molecular_function	ribonucleoside binding
B	0034062	molecular_function	5'-3' RNA polymerase activity
C	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
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	0046983	molecular_function	protein dimerization activity
D	0000166	molecular_function	nucleotide binding
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	0006352	biological_process	DNA-templated transcription initiation
D	0006366	biological_process	transcription by RNA polymerase II
D	0006367	biological_process	transcription initiation at RNA polymerase II promoter
D	0006368	biological_process	transcription elongation by RNA polymerase II
D	0016607	cellular_component	nuclear speck
D	0030880	cellular_component	RNA polymerase complex
D	0031369	molecular_function	translation initiation factor binding
E	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
E	0006361	biological_process	transcription initiation at RNA polymerase I promoter
E	0006362	biological_process	transcription elongation by RNA polymerase I
E	0006363	biological_process	termination of RNA polymerase I transcription
E	0006366	biological_process	transcription by RNA polymerase II
E	0006367	biological_process	transcription initiation at RNA polymerase II promoter
E	0006368	biological_process	transcription elongation by RNA polymerase II
E	0006383	biological_process	transcription by RNA polymerase III
E	0006384	biological_process	transcription initiation at RNA polymerase III promoter
E	0006386	biological_process	termination of RNA polymerase III transcription
E	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
E	0042797	biological_process	tRNA transcription by RNA polymerase III
E	0050821	biological_process	protein stabilization
F	0001650	cellular_component	fibrillar center
F	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
F	0006360	biological_process	transcription by RNA polymerase I
F	0006361	biological_process	transcription initiation at RNA polymerase I promoter
F	0006362	biological_process	transcription elongation by RNA polymerase I
F	0006363	biological_process	termination of RNA polymerase I transcription
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
F	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
F	0042797	biological_process	tRNA transcription by RNA polymerase III
G	0000932	cellular_component	P-body
G	0000956	biological_process	nuclear-transcribed mRNA catabolic process
G	0003676	molecular_function	nucleic acid binding
G	0003697	molecular_function	single-stranded DNA 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	0006351	biological_process	DNA-templated transcription
G	0006352	biological_process	DNA-templated transcription initiation
G	0006366	biological_process	transcription by RNA polymerase II
G	0006367	biological_process	transcription initiation at RNA polymerase II promoter
G	0006368	biological_process	transcription elongation by RNA polymerase II
G	0031369	molecular_function	translation initiation factor binding
G	0045948	biological_process	positive regulation of translational initiation
G	0055029	cellular_component	nuclear DNA-directed RNA polymerase complex
G	0060213	biological_process	positive regulation of nuclear-transcribed mRNA poly(A) tail shortening
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	0006351	biological_process	DNA-templated transcription
H	0006361	biological_process	transcription initiation at RNA polymerase I promoter
H	0006362	biological_process	transcription elongation by RNA polymerase I
H	0006363	biological_process	termination of RNA polymerase I transcription
H	0006366	biological_process	transcription by RNA polymerase II
H	0006367	biological_process	transcription initiation at RNA polymerase II promoter
H	0006368	biological_process	transcription elongation by RNA polymerase II
H	0006383	biological_process	transcription by RNA polymerase III
H	0006384	biological_process	transcription initiation at RNA polymerase III promoter
H	0006386	biological_process	termination of RNA polymerase III transcription
H	0032993	cellular_component	protein-DNA complex
H	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
I	0001193	biological_process	maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II
I	0003676	molecular_function	nucleic acid binding
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	0006351	biological_process	DNA-templated transcription
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
J	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
J	0006356	biological_process	regulation of transcription by RNA polymerase I
J	0006360	biological_process	transcription by RNA polymerase I
J	0006361	biological_process	transcription initiation at RNA polymerase I promoter
J	0006362	biological_process	transcription elongation by RNA polymerase I
J	0006363	biological_process	termination of RNA polymerase I transcription
J	0006366	biological_process	transcription by RNA polymerase II
J	0006367	biological_process	transcription initiation at RNA polymerase II promoter
J	0006368	biological_process	transcription elongation by RNA polymerase II
J	0006383	biological_process	transcription by RNA polymerase III
J	0006384	biological_process	transcription initiation at RNA polymerase III promoter
J	0006386	biological_process	termination of RNA polymerase III transcription
J	0008270	molecular_function	zinc ion binding
J	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
J	0042797	biological_process	tRNA transcription by RNA polymerase III
K	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
K	0006366	biological_process	transcription by RNA polymerase II
K	0006367	biological_process	transcription initiation at RNA polymerase II promoter
K	0006368	biological_process	transcription elongation by RNA polymerase II
K	0030275	molecular_function	LRR domain binding
K	0046983	molecular_function	protein dimerization activity
L	0001650	cellular_component	fibrillar center
L	0003677	molecular_function	DNA binding
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	0006351	biological_process	DNA-templated transcription
L	0006356	biological_process	regulation of transcription by RNA polymerase I
L	0006361	biological_process	transcription initiation at RNA polymerase I promoter
L	0006362	biological_process	transcription elongation by RNA polymerase I
L	0006363	biological_process	termination of RNA polymerase I transcription
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	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
M	0000122	biological_process	negative regulation of transcription by RNA polymerase II
M	0000785	cellular_component	chromatin
M	0000976	molecular_function	transcription cis-regulatory region binding
M	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
M	0000981	molecular_function	DNA-binding transcription factor activity, RNA polymerase II-specific
M	0000987	molecular_function	cis-regulatory region sequence-specific DNA binding
M	0001046	molecular_function	core promoter sequence-specific DNA binding
M	0001094	molecular_function	TFIID-class transcription factor complex binding
M	0001223	molecular_function	transcription coactivator binding
M	0001227	molecular_function	DNA-binding transcription repressor activity, RNA polymerase II-specific
M	0001228	molecular_function	DNA-binding transcription activator activity, RNA polymerase II-specific
M	0002020	molecular_function	protease binding
M	0002039	molecular_function	p53 binding
M	0002244	biological_process	hematopoietic progenitor cell differentiation
M	0003677	molecular_function	DNA binding
M	0003682	molecular_function	chromatin binding
M	0003700	molecular_function	DNA-binding transcription factor activity
M	0003730	molecular_function	mRNA 3'-UTR binding
M	0005507	molecular_function	copper ion binding
M	0005515	molecular_function	protein binding
M	0005634	cellular_component	nucleus
M	0005654	cellular_component	nucleoplasm
M	0005667	cellular_component	transcription regulator complex
M	0005730	cellular_component	nucleolus
M	0005737	cellular_component	cytoplasm
M	0005739	cellular_component	mitochondrion
M	0005759	cellular_component	mitochondrial matrix
M	0005783	cellular_component	endoplasmic reticulum
M	0005813	cellular_component	centrosome
M	0005829	cellular_component	cytosol
M	0006289	biological_process	nucleotide-excision repair
M	0006355	biological_process	regulation of DNA-templated transcription
M	0006357	biological_process	regulation of transcription by RNA polymerase II
M	0006914	biological_process	autophagy
M	0006915	biological_process	apoptotic process
M	0006974	biological_process	DNA damage response
M	0006979	biological_process	response to oxidative stress
M	0006983	biological_process	ER overload response
M	0007265	biological_process	Ras protein signal transduction
M	0007623	biological_process	circadian rhythm
M	0008104	biological_process	intracellular protein localization
M	0008270	molecular_function	zinc ion binding
M	0008285	biological_process	negative regulation of cell population proliferation
M	0008340	biological_process	determination of adult lifespan
M	0009299	biological_process	mRNA transcription
M	0009410	biological_process	response to xenobiotic stimulus
M	0009411	biological_process	response to UV
M	0010212	biological_process	response to ionizing radiation
M	0010332	biological_process	response to gamma radiation
M	0010628	biological_process	positive regulation of gene expression
M	0016032	biological_process	viral process
M	0016363	cellular_component	nuclear matrix
M	0016604	cellular_component	nuclear body
M	0016605	cellular_component	PML body
M	0019899	molecular_function	enzyme binding
M	0030308	biological_process	negative regulation of cell growth
M	0030330	biological_process	DNA damage response, signal transduction by p53 class mediator
M	0030971	molecular_function	receptor tyrosine kinase binding
M	0031571	biological_process	mitotic G1 DNA damage checkpoint signaling
M	0031625	molecular_function	ubiquitin protein ligase binding
M	0032211	biological_process	negative regulation of telomere maintenance via telomerase
M	0032991	cellular_component	protein-containing complex
M	0033209	biological_process	tumor necrosis factor-mediated signaling pathway
M	0034644	biological_process	cellular response to UV
M	0036310	molecular_function	ATP-dependent DNA/DNA annealing activity
M	0042149	biological_process	cellular response to glucose starvation
M	0042771	biological_process	intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
M	0042802	molecular_function	identical protein binding
M	0042826	molecular_function	histone deacetylase binding
M	0042981	biological_process	regulation of apoptotic process
M	0043065	biological_process	positive regulation of apoptotic process
M	0043066	biological_process	negative regulation of apoptotic process
M	0043153	biological_process	entrainment of circadian clock by photoperiod
M	0043621	molecular_function	obsolete protein self-association
M	0045815	biological_process	transcription initiation-coupled chromatin remodeling
M	0045892	biological_process	negative regulation of DNA-templated transcription
M	0045893	biological_process	positive regulation of DNA-templated transcription
M	0045899	biological_process	positive regulation of RNA polymerase II transcription preinitiation complex assembly
M	0045944	biological_process	positive regulation of transcription by RNA polymerase II
M	0046677	biological_process	response to antibiotic
M	0046982	molecular_function	protein heterodimerization activity
M	0048147	biological_process	negative regulation of fibroblast proliferation
M	0048512	biological_process	circadian behavior
M	0048539	biological_process	bone marrow development
M	0051053	biological_process	negative regulation of DNA metabolic process
M	0051087	molecular_function	protein-folding chaperone binding
M	0051097	biological_process	negative regulation of helicase activity
M	0051262	biological_process	protein tetramerization
M	0051721	molecular_function	protein phosphatase 2A binding
M	0051726	biological_process	regulation of cell cycle
M	0060218	biological_process	hematopoietic stem cell differentiation
M	0060333	biological_process	type II interferon-mediated signaling pathway
M	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
M	0062100	biological_process	positive regulation of programmed necrotic cell death
M	0065003	biological_process	protein-containing complex assembly
M	0070059	biological_process	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
M	0070245	biological_process	positive regulation of thymocyte apoptotic process
M	0071456	biological_process	cellular response to hypoxia
M	0071466	biological_process	cellular response to xenobiotic stimulus
M	0071479	biological_process	cellular response to ionizing radiation
M	0071480	biological_process	cellular response to gamma radiation
M	0071889	molecular_function	14-3-3 protein binding
M	0072331	biological_process	signal transduction by p53 class mediator
M	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator
M	0072717	biological_process	cellular response to actinomycin D
M	0090200	biological_process	positive regulation of release of cytochrome c from mitochondria
M	0090398	biological_process	cellular senescence
M	0090399	biological_process	replicative senescence
M	0090403	biological_process	oxidative stress-induced premature senescence
M	0097190	biological_process	apoptotic signaling pathway
M	0097193	biological_process	intrinsic apoptotic signaling pathway
M	0097252	biological_process	oligodendrocyte apoptotic process
M	0097371	molecular_function	MDM2/MDM4 family protein binding
M	0097718	molecular_function	disordered domain specific binding
M	0140296	molecular_function	general transcription initiation factor binding
M	0140677	molecular_function	molecular function activator activity
M	0140693	molecular_function	molecular condensate scaffold activity
M	1900119	biological_process	positive regulation of execution phase of apoptosis
M	1902749	biological_process	regulation of cell cycle G2/M phase transition
M	1902895	biological_process	positive regulation of miRNA transcription
M	1903451	biological_process	negative regulation of G1 to G0 transition
M	1905856	biological_process	negative regulation of pentose-phosphate shunt
M	1990841	molecular_function	promoter-specific chromatin binding
M	2000379	biological_process	positive regulation of reactive oxygen species metabolic process
M	2000774	biological_process	positive regulation of cellular senescence
M	2001242	biological_process	regulation of intrinsic apoptotic signaling pathway
M	2001244	biological_process	positive regulation of intrinsic apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 2001

Chain	Residue
A	ASP495
A	ASP497
A	ASP499

site_id	AC2
Number of Residues	3
Details	binding site for residue ZN A 2002

Chain	Residue
A	PRO82
A	GLY83
B	MET1125

site_id	AC3
Number of Residues	3
Details	binding site for residue ZN A 2003

Chain	Residue
A	PHE112
A	TYR187
A	GLU211

site_id	AC4
Number of Residues	2
Details	binding site for residue ZN A 2004

Chain	Residue
A	GLU30
B	CYS1122

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 1201

Chain	Residue
B	GLU959
B	GLY960
C	ALA180
J	CYS10

site_id	AC6
Number of Residues	1
Details	binding site for residue ZN C 301

Chain	Residue
C	THR89

site_id	AC7
Number of Residues	2
Details	binding site for residue ZN I 201

Chain	Residue
I	ARG40
I	ASN41

site_id	AC8
Number of Residues	3
Details	binding site for residue ZN I 202

Chain	Residue
I	HIS91
I	LYS92
I	CYS114

site_id	AC9
Number of Residues	2
Details	binding site for residue ZN L 101

Chain	Residue
L	CYS36
L	CYS39

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

Chain	Residue	Details
I	TYR112-HIS118

site_id	PS00348
Number of Residues	13
Details	P53 p53 family signature. MCNSSCMGGMNRR

Chain	Residue	Details
M	MET237-ARG249

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	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	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	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_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	41
Details	Region: {"description":"Trigger loop","evidences":[{"source":"UniProtKB","id":"G3MZY8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"G3MZY8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04050","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); by NEDD4","evidences":[{"source":"PubMed","id":"32142649","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32142654","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
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_FI10
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A5PJW8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
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_FI12
Number of Residues	66
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
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_FI16
Number of Residues	24
Details	Region: {"description":"Non-specific ssDNA binding"}

Chain

Residue

Details

site_id	SWS_FT_FI17
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_FI18
Number of Residues	25
Details	Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
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_FI20
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_FI21
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_FI22
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_FI23
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_FI24
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_FI25
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_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":"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_FI27
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_FI28
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_FI29
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_FI30
Number of Residues	190
Details	DNA binding: {"evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	200
Details	Region: {"description":"Required for interaction with ZNF385A","evidences":[{"source":"PubMed","id":"17719541","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	123
Details	Region: {"description":"Required for interaction with FBXO42","evidences":[{"source":"PubMed","id":"19509332","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	176
Details	Region: {"description":"Interaction with AXIN1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	7
Details	Region: {"description":"Interaction with the 53BP2 SH3 domain"}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	38
Details	Region: {"description":"Interaction with E4F1","evidences":[{"source":"PubMed","id":"10644996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	7
Details	Region: {"description":"Interaction with DNA"}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	8
Details	Motif: {"description":"TADI"}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	8
Details	Motif: {"description":"TADII"}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	16
Details	Motif: {"description":"Bipartite nuclear localization signal"}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	11
Details	Motif: {"description":"Nuclear export signal"}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	17
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14534297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17015838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18650397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19515728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20142040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	1
Details	Site: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM","evidences":[{"source":"PubMed","id":"10570149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11554766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15866171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17108107","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17967874","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21317932","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28842590","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CK1, VRK1 and VRK2","evidences":[{"source":"PubMed","id":"10606744","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10951572","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16704422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527692","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CHEK2, CK1 and PLK3","evidences":[{"source":"PubMed","id":"10570149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11447225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11551930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12810724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20041275","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK5 and CDK7","evidences":[{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9372954","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by MAPKAPK5","evidences":[{"source":"PubMed","id":"17254968","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG","evidences":[{"source":"PubMed","id":"11740489","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11780126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16377624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17349958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by TAF1 and GRK5","evidences":[{"source":"PubMed","id":"15053879","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20124405","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	2
Details	Modified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"38653238","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"12724314","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by AURKA, CDK1 and CDK2","evidences":[{"source":"PubMed","id":"10884347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14702041","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI56
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P02340","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI57
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"19011621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	2
Details	Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"19011621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21597459","evidenceCode":"ECO:0000269"}]}

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)","evidences":[{"source":"PubMed","id":"19033443","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI61
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19536131","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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