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7V99

catalytic core of human telomerase holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000333cellular_componenttelomerase catalytic core complex
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
A0003721molecular_functiontelomerase RNA reverse transcriptase activity
A0003723molecular_functionRNA binding
A0003964molecular_functionRNA-directed DNA polymerase activity
A0003968molecular_functionRNA-dependent RNA polymerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005697cellular_componenttelomerase holoenzyme complex
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006278biological_processRNA-templated DNA biosynthetic process
A0007004biological_processtelomere maintenance via telomerase
A0007005biological_processmitochondrion organization
A0010629biological_processnegative regulation of gene expression
A0016605cellular_componentPML body
A0016607cellular_componentnuclear speck
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
A0032092biological_processpositive regulation of protein binding
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
A0043231cellular_componentintracellular membrane-bounded organelle
A0043524biological_processnegative regulation of neuron apoptotic process
A0045766biological_processpositive regulation of angiogenesis
A0046326biological_processpositive regulation of glucose import
A0046686biological_processresponse to cadmium ion
A0046872molecular_functionmetal ion binding
A0051000biological_processpositive regulation of nitric-oxide synthase activity
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
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005694cellular_componentchromosome
K0006325biological_processchromatin organization
K0008285biological_processnegative regulation of cell population proliferation
K0030527molecular_functionstructural constituent of chromatin
K0031492molecular_functionnucleosomal DNA binding
K0031507biological_processheterochromatin formation
K0043229cellular_componentintracellular organelle
K0043505cellular_componentCENP-A containing nucleosome
K0046982molecular_functionprotein heterodimerization activity
K0061644biological_processprotein localization to CENP-A containing chromatin
K0070062cellular_componentextracellular exosome
L0000786cellular_componentnucleosome
L0002227biological_processinnate immune response in mucosa
L0003674molecular_functionmolecular_function
L0003677molecular_functionDNA binding
L0005515molecular_functionprotein binding
L0005615cellular_componentextracellular space
L0005634cellular_componentnucleus
L0005654cellular_componentnucleoplasm
L0005694cellular_componentchromosome
L0005829cellular_componentcytosol
L0019731biological_processantibacterial humoral response
L0030527molecular_functionstructural constituent of chromatin
L0031640biological_processkilling of cells of another organism
L0042742biological_processdefense response to bacterium
L0043229cellular_componentintracellular organelle
L0046982molecular_functionprotein heterodimerization activity
L0050829biological_processdefense response to Gram-negative bacterium
L0050830biological_processdefense response to Gram-positive bacterium
L0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
KALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
LARG92-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527
ChainResidueDetails
LPRO1
AASP868
AASP869

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: ADP-ribosyl glutamic acid => ECO:0000269|PubMed:27530147
ChainResidueDetails
LGLU2

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
LLYS5
LLYS11
LLYS15
LLYS16
LLYS20
LLYS23
LLYS43
LLYS85

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:34874266
ChainResidueDetails
LSER6
KLYS95

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
LLYS12

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
ChainResidueDetails
LSER14

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
LLYS24
KLYS75

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
LLYS34
LLYS116
LLYS120

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
LGLU35
KLYS119
KLYS125

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q8CGP1
ChainResidueDetails
LSER36

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
LLYS46
LLYS108

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
LLYS57
KLYS119

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
LARG79

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
LARG86
LARG92

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
LTHR115

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
LSER112

site_idSWS_FT_FI17
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
LLYS5

site_idSWS_FT_FI18
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
ChainResidueDetails
LLYS120

site_idSWS_FT_FI19
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
LLYS20

site_idSWS_FT_FI20
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
LLYS34

222926

PDB entries from 2024-07-24

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