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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7TRF

Human telomerase catalytic core RNP with H2A/H2B

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000333cellular_componenttelomerase catalytic core complex
A0000722biological_processtelomere maintenance via recombination
A0000723biological_processtelomere maintenance
A0000781cellular_componentchromosome, telomeric region
A0000783cellular_componentnuclear telomere cap complex
A0001172biological_processRNA-templated transcription
A0001223molecular_functiontranscription coactivator binding
A0003677molecular_functionDNA binding
A0003720molecular_functiontelomerase activity
A0003723molecular_functionRNA binding
A0003964molecular_functionRNA-directed DNA polymerase activity
A0003968molecular_functionRNA-directed RNA polymerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005697cellular_componenttelomerase holoenzyme complex
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006278biological_processRNA-templated DNA biosynthetic process
A0006606biological_processprotein import into nucleus
A0007004biological_processtelomere maintenance via telomerase
A0007005biological_processmitochondrion organization
A0007507biological_processheart development
A0016605cellular_componentPML body
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0022616biological_processDNA strand elongation
A0030177biological_processpositive regulation of Wnt signaling pathway
A0030422biological_processsiRNA processing
A0031379cellular_componentRNA-directed RNA polymerase complex
A0031647biological_processregulation of protein stability
A0034061molecular_functionDNA polymerase activity
A0042162molecular_functiontelomeric DNA binding
A0042635biological_processpositive regulation of hair cycle
A0042645cellular_componentmitochondrial nucleoid
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043066biological_processnegative regulation of apoptotic process
A0043524biological_processnegative regulation of neuron apoptotic process
A0045766biological_processpositive regulation of angiogenesis
A0046326biological_processpositive regulation of D-glucose import
A0046686biological_processresponse to cadmium ion
A0046872molecular_functionmetal ion binding
A0051087molecular_functionprotein-folding chaperone binding
A0070034molecular_functiontelomerase RNA binding
A0070200biological_processestablishment of protein localization to telomere
A0071456biological_processcellular response to hypoxia
A0071897biological_processDNA biosynthetic process
A0090399biological_processreplicative senescence
A0098680molecular_functiontemplate-free RNA nucleotidyltransferase
A0140745biological_processsiRNA transcription
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
A1902895biological_processpositive regulation of miRNA transcription
A1903620biological_processpositive regulation of transdifferentiation
A1904707biological_processpositive regulation of vascular associated smooth muscle cell proliferation
A1904751biological_processpositive regulation of protein localization to nucleolus
A1904754biological_processpositive regulation of vascular associated smooth muscle cell migration
A1990572cellular_componentTERT-RMRP complex
A1990904cellular_componentribonucleoprotein complex
A2000352biological_processnegative regulation of endothelial cell apoptotic process
A2000648biological_processpositive regulation of stem cell proliferation
A2000773biological_processnegative regulation of cellular senescence
A2001240biological_processnegative regulation of extrinsic apoptotic signaling pathway in absence of ligand
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031507biological_processheterochromatin formation
E0046982molecular_functionprotein heterodimerization activity
E0070062cellular_componentextracellular exosome
F0000786cellular_componentnucleosome
F0002227biological_processinnate immune response in mucosa
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005615cellular_componentextracellular space
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0005829cellular_componentcytosol
F0006334biological_processnucleosome assembly
F0019731biological_processantibacterial humoral response
F0030527molecular_functionstructural constituent of chromatin
F0042742biological_processdefense response to bacterium
F0042802molecular_functionidentical protein binding
F0046982molecular_functionprotein heterodimerization activity
F0050830biological_processdefense response to Gram-positive bacterium
F0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
F0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
EALA22-VAL28
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
FARG93-GLY115
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q6ZWY9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"22121020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsCross-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"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsRegion: {"description":"Required for regulating specificity for telomeric DNA and for processivity for primer elongation"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues14
DetailsRegion: {"description":"Required for oligomerization"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsRegion: {"description":"Primer grip sequence"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues196
DetailsRegion: {"description":"CTE"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues5
DetailsMotif: {"description":"TFLY; involved in RNA binding","evidences":[{"source":"UniProtKB","id":"Q4KTA7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00405","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsSite: {"description":"Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsSite: {"description":"Required for nucleotide incorporation and primer extension rate"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by DYRK2","evidences":[{"source":"PubMed","id":"23362280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"12808100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829466","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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