Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7TRF

Human telomerase catalytic core RNP with H2A/H2B

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000333	cellular_component	telomerase catalytic core complex
A	0000722	biological_process	telomere maintenance via recombination
A	0000723	biological_process	telomere maintenance
A	0000781	cellular_component	chromosome, telomeric region
A	0000783	cellular_component	nuclear telomere cap complex
A	0001172	biological_process	RNA-templated transcription
A	0001223	molecular_function	transcription coactivator binding
A	0003677	molecular_function	DNA binding
A	0003720	molecular_function	telomerase activity
A	0003723	molecular_function	RNA binding
A	0003964	molecular_function	RNA-directed DNA 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	0005697	cellular_component	telomerase holoenzyme complex
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006278	biological_process	RNA-templated DNA biosynthetic process
A	0006606	biological_process	protein import into nucleus
A	0007004	biological_process	telomere maintenance via telomerase
A	0007005	biological_process	mitochondrion organization
A	0007507	biological_process	heart development
A	0016605	cellular_component	PML body
A	0016607	cellular_component	nuclear speck
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0022616	biological_process	DNA strand elongation
A	0030177	biological_process	positive regulation of Wnt signaling pathway
A	0030422	biological_process	siRNA processing
A	0031379	cellular_component	RNA-directed RNA polymerase complex
A	0031647	biological_process	regulation of protein stability
A	0034061	molecular_function	DNA polymerase activity
A	0042162	molecular_function	telomeric DNA binding
A	0042635	biological_process	positive regulation of hair cycle
A	0042645	cellular_component	mitochondrial nucleoid
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043066	biological_process	negative regulation of apoptotic process
A	0043524	biological_process	negative regulation of neuron apoptotic process
A	0045766	biological_process	positive regulation of angiogenesis
A	0046686	biological_process	response to cadmium ion
A	0046872	molecular_function	metal ion binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0070034	molecular_function	telomerase RNA binding
A	0070200	biological_process	establishment of protein localization to telomere
A	0071456	biological_process	cellular response to hypoxia
A	0071897	biological_process	DNA biosynthetic process
A	0090399	biological_process	replicative senescence
A	0098680	molecular_function	template-free RNA nucleotidyltransferase activity
A	0140745	biological_process	siRNA transcription
A	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
A	1902895	biological_process	positive regulation of miRNA transcription
A	1903620	biological_process	positive regulation of transdifferentiation
A	1904707	biological_process	positive regulation of vascular associated smooth muscle cell proliferation
A	1904751	biological_process	positive regulation of protein localization to nucleolus
A	1904754	biological_process	positive regulation of vascular associated smooth muscle cell migration
A	1990572	cellular_component	TERT-RMRP complex
A	1990904	cellular_component	ribonucleoprotein complex
A	2000352	biological_process	negative regulation of endothelial cell apoptotic process
A	2000648	biological_process	positive regulation of stem cell proliferation
A	2000773	biological_process	negative regulation of cellular senescence
A	2001240	biological_process	negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005634	cellular_component	nucleus
E	0005694	cellular_component	chromosome
E	0030527	molecular_function	structural constituent of chromatin
E	0031507	biological_process	heterochromatin formation
E	0046982	molecular_function	protein heterodimerization activity
E	0070062	cellular_component	extracellular exosome
F	0000786	cellular_component	nucleosome
F	0002227	biological_process	innate immune response in mucosa
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005615	cellular_component	extracellular space
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	0019731	biological_process	antibacterial humoral response
F	0030527	molecular_function	structural constituent of chromatin
F	0042742	biological_process	defense response to bacterium
F	0042802	molecular_function	identical protein binding
F	0046982	molecular_function	protein heterodimerization activity
F	0050830	biological_process	defense response to Gram-positive bacterium
F	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
F	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	ALA22-VAL28

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

Chain	Residue	Details
F	ARG93-GLY115

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q6ZWY9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-isonicotinyllysine; alternate","evidences":[{"source":"PubMed","id":"34545082","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
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_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"PubMed","id":"34961760","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"22121020","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
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"},{"source":"PubMed","id":"22121020","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Region: {"description":"Required for regulating specificity for telomeric DNA and for processivity for primer elongation"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	14
Details	Region: {"description":"Required for oligomerization"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Region: {"description":"Primer grip sequence"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	196
Details	Region: {"description":"CTE"}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	5
Details	Motif: {"description":"TFLY; involved in RNA binding","evidences":[{"source":"UniProtKB","id":"Q4KTA7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00405","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Site: {"description":"Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Site: {"description":"Required for nucleotide incorporation and primer extension rate"}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by DYRK2","evidences":[{"source":"PubMed","id":"23362280","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"12808100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829466","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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