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Information on EC 2.7.7.19 - polynucleotide adenylyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8NDF8
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2.7.7.19 polynucleotide adenylyltransferaseIUBMB Comments
Also acts slowly with CTP. Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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Word Map
- 2.7.7.19
-
polyadenylation
- polymerases
- pre-mrnas
- phosphorylase
-
exosome
-
rna-binding
- vaccinia
- trna
-
oligoa
- helicase
-
tramp
-
aauaaa
-
deadenylation
-
polya-binding
- pnpase
-
dna-dependent
-
meiotic
-
noncanonical
-
exonuclease
-
3'-terminal
- cordycepin
-
oligoadenylation
- exoribonucleases
- polyu
- drug development
-
endoribonuclease
- medicine
- snornas
-
non-templated
-
cca-adding
- hfq
-
polya-specific
-
deadenylase
- biotechnology
-
polya-tailed
-
snrnp
-
pabpn1
-
degradosome
-
exonucleolytic
- 3'-deoxyadenosine
-
pancreatitis-associated
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
poly(a) polymerase, pap i, fam46c, gld-2, star-pap, fam46a, poly(a) polymerase i, pap ii, papd5, mtpap, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate:ribonucleic acid adenylyltransferase
-
-
-
-
AMP polynucleotidylexotransferase
-
-
-
-
ATP-polynucleotide adenylyltransferase
-
-
-
-
ATP:polynucleotidylexotransferase
-
-
-
-
Cid1
-
putative cytoplasmic PAP, in addition to having PAP activity, Cid1 possesses substantial poly(U) polymerase activity
FAM46B
FAM46C
Hs2
-
contains two PAP-associated domains and two nucleotidyl transferase motifs
neo-PAP
-
-
-
-
NTP polymerase
-
-
-
-
nucleotidyltransferase, polyadenylate
-
-
-
-
PAP
PAP I
-
-
-
-
PAPalpha
PAPgamma
poly(A) hydrolase
-
-
-
-
poly(A) polymerase
poly(A) polymerase gamma
poly(A) synthetase
-
-
-
-
polyadenylate nucleotidyltransferase
-
-
-
-
polyadenylate polymerase
polyadenylate synthetase
-
-
-
-
polyadenylic acid polymerase
-
-
-
-
polyadenylic polymerase
-
-
-
-
RNA adenylating enzyme
-
-
-
-
RNA formation factors, PF1
-
-
-
-
Star-PAP
terminal riboadenylate transferase
-
-
-
-
PAP
-
-
-
-
poly(A) polymerase
-
-
-
-
polyadenylate polymerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:polynucleotide adenylyltransferase
Also acts slowly with CTP. Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY
9026-30-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(A)15 + n ATP
(A)15+n + n diphosphate
in the presence of ATP, the incorporation of several nucleotides into the RNA substrate is observed
-
-
?
ATP + miR-21-5p
?
enzyme isoform PAPD5 adenylates the 3'-end of miR-21-5p, marking it for 3'-to-5'-trimming by the poly(A) specific ribonuclease PARN
-
-
?
ATP + yeast tRNAiMet
diphosphate + ?
in vitro-synthesized yeast tRNAiMet, but not the native tRNA is substrate
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
-
isoform PAPD7 displays strong nucleotidyl transferase activity
-
?
UTP + RNA
diphosphate + RNA(U)n
-
recombinant Cid1 shows a preference for UTP over ATP, the poly(U) polymerase activity of recombinant Cid1 out-competes its PAP activity under physiologically relevant conditions
-
-
?
ATP + RNA
?
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Hs2 complexes have very little PAP activity, Hs2 also displays efficient poly(U) polymerase activity
-
-
?
additional information
?
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
?
additional information
?
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
additional information
?
-
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + miR-21-5p
?
enzyme isoform PAPD5 adenylates the 3'-end of miR-21-5p, marking it for 3'-to-5'-trimming by the poly(A) specific ribonuclease PARN
-
-
?
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
?
ATP + RNA
?
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
Mg2+
-
NE PAP I (isoenzyme from cytoplasmic fraction) and S100 PAP (isoenzyme from nuclear fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
4 mM used in assay conditions. When Mg2+ is replaced by Mn2+, the protein becomes more potent in catalyzing polyadenylation
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mn2+
-
NE PAP I (isoenzyme from nuclear fraction) and S100 PAP (isoenzyme from cytoplasmic fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
neomycin B
-
an increase in pH releases the neomycin B inhibitory effect on PAPgamma
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
-
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
mainly localizes to the nucleus, but is excluded from the nucleolus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme depletion not only reduces GLUT1 poly(A) tail length, but also GLUT1 protein. Enzyme depletion impairs glucose deprivation-induced GLUT1 up-regulation
metabolism
the enzyme is involved in non-templated 3'-adenylation of miRNAs
physiological function
enzyme-mediated translational control of GLUT1 mRNA is dependent of an RNA binding protein, CPEB1, and its binding elements in the 3_UTR. Through regulating GLUT1 level, the enzyme affects glucose uptake into cells and lactate levels. The enzyme affects glucose-dependent cellular phenotypes such as migration and invasion in glioblastoma cells
malfunction
metabolism
-
nuclear enzyme isoforms regulate transcript abundance genome-wide. Isoform Star-PAP-specific polyadenylation site usage regulates the expression of the eukaryotic translation initiation factor EIF4A1, the tumor suppressor gene PTEN and the long non-coding RNANEAT1. Isoform Star-PAP-mediated alternative polyadenylation of PTEN is essential for DNA damage-induced increase of PTEN protein levels
physiological function
malfunction
enzyme knock-out is lethal. Knock-down of enzyme induces apoptosis and restricts protein synthesis
physiological function
depletion of isoform Gld2 promotes rather than inhibits p53 mRNA polyadenylation/translation, induces premature senescence and enhances the stability of cytoplasmic polyadenylation element binding protein CPEB mRNA. TheCPEB 3' untranslated region contains two miR-122 binding sites, which when deleted, elevate mRNA translation. miR-122 is present in primary fibroblasts and destabilizes by Gld2 depletion
physiological function
isoform GLD4 regulates p53 polyadenylation/translation in a cytoplasmic polyadenylation element binding protein CPEB dependent manner
physiological function
-
a terminal poly(A) tail is important for a subset of intron excision events that follow cleavage and polyadenylation. In these cases, splicing is promoted by the nuclear poly(A) binding protein, PABPN1, and poly(A) polymerase, PAP. Poly(A) polymerase is needed for efficient splicing. Inefficient polyadenylation is associated with impaired recruitment of splicing factors to affected introns, which are consequently degraded by the exosome
physiological function
inactivation of PAP-dependent hyperadenylation in cells leads to the upregulation of various ncRNAs, including snoRNA host genes, primary miRNA transcripts, and promoter upstream antisense RNAs. mRNAs with retained introns are susceptible to PABPN1 and PAPalpha/gamma-mediated decay. Transcripts are targeted for degradation due to inefficient export, a consequence of reduced intron number or incomplete splicing. A genetically-encoded poly(A) tail is sufficient to drive decay. Treatment with transcription inhibitors uncouples polyadenylation from decay, leading to runaway hyperadenylation of nuclear decay targets
physiological function
processing of the common precursor releases an incomplete tRNATyr lacking the 3'-adenosine which has to be added before addition of the CCA end and subsequent aminoacylation. Mitochondrial poly(A) polymerase mtPAP is responsible for this A addition. Complete repair can be reconstituted in vitro with three enzymes: mtPAP frequently adds more than one A to the 3'-end of the truncated tRNA, and either the mitochondrial deadenylase PDE12 or the endonuclease RNase Z trims the oligo(A) tail to a single A before CCA addition
physiological function
autophagy receptor NDP52 and the enzyme form an autophagy receptor complex, which enhances autophagic elimination of damaged mitochondria
physiological function
ectopic enzyme expression inhibits proliferation as well as colony-forming ability of breast cancer cells. By regulating the expression of BCL2-interacting killer, the enzyme induces apoptosis of breast cancer cells through the mitochondrial pathway
physiological function
the enzyme acts as an onco-suppressor with the specificity for B-lymphocyte lineage from which multiple myeloma originates. The enzyme controls survival and proliferation of multiple myeloma cells
physiological function
the enzyme is indispensable for the viability of human embryonic stem cells
physiological function
the enzyme regulates gene expression and probably plays a critical role during cell differentiation. Isoform FAM46C is a causal driver of multiple myeloma
physiological function
the enzyme regulates gene expression and probably plays a critical role during cell differentiation. The enzyme gene may be involved in the development of major malignancies including lung, colorectal, hepatocellular, head and neck, urothelial, endometrial and renal papillary carcinomas and melanoma
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAPD5_HUMAN
572
0
63267
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
50000 - 60000
58000
63000
75000
50000 - 60000
-
enzymes NE PAP I and II, S100 PAP, sucrose density gradient sedimentation
58000
-
nuclear Mg2+- and Mn2+-stimulated enzyme, glycerol density gradient sedimentation
63000
-
cytoplasmic Mn2+-dependent enzyme, glycerol density gradient sedimentation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
dimerization is required for the catalytic activity of isoform PAPD1
additional information
-
dimerization is required for the catalytic activity of isoform PAPD1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform PAPgamma bound to cordycepin triphosphate (3?dATP) and Ca2+, to 2.8 A resolution. One 3'-dATP and one Ca2+ are present in the active site of each PAP molecule. Strictly conserved catalytic residues Asp112 and Asp114 interact with Ca2+, which also ligates three non-bridging oxygens of the alpha, beta and gamma phosphates of 3'-dATP. PAPgamma closely resembles its PAPalpha ortholog
mutant D325A, to 3.1 A resolution. The overall structure of the palm and fingers domains is similar to that in the canonical poly(A) polymerases. The active site is located at the interface between the two domains, with a large pocket that can accommodate the substrates. The structure reveals a domain in the N-terminal region of PAPD1, with a backbone-fold that is similar to that of RNP-type RNA binding domains. This domain, together with a beta-arm insertion in the palm domain, contributes to dimerization of PAPD1. The crystal structure reveals a dimer, formed by the two molecules in the asymmetric unit
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K560E
mutation in the C-terminal basic motif. About 20% of wild-type activity
D124A
the mutant shows strongly reduced activity compared to the wild type enzyme
D126A
the mutant shows strongly reduced activity compared to the wild type enzyme
D325A
mutation of one of the conserved Asp residues in the active site, complete loss of activity. The mutant protein gives better quality crystals than the wild-type enzyme
E200A
the mutant shows strongly reduced activity compared to the wild type enzyme
G107A
the mutant shows strongly reduced activity compared to the wild type enzyme
H259A/K260A/I261A/H294A/F295A/P297A
mutations simultaneously disrupt both areas of contact in the dimer interface, mutant is a stable monomer in solution, complete loss of activity
H294A/F295A/P297A
mutation in helix alphaE, mutant exists in a monomer-dimer equilibrium
S108A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y221A/F222A
mutation in helix alphaB, mutant exists in a monomer-dimer equilibrium
additional information
additional information
deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
-
deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
-
hmtPAP knockdown mutant cells show decreased steady state levels of mtDNA-encoded proteins as well as deficient mitochondrial activities such as oxygen consumption rate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
-
by BD TALON Resin (zco, clontechClontech) or nickel-nitrilotriacetic acid-agarose (Qiagen)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PAPgamma(1-683C), a C-terminally truncated version of full length human PAPgamma with the same catalytic efficiency is expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is highly expressed in human pre-implantation embryos and pluripotent stem cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
use as prognostic factor for early recurrence and death in breast cancer patients
medicine
-
PAP activity is used to measure the effects of anticancer drugs etoposide and cordycepin in two epithelial cancer cell lines, HeLa (human epithelioid cervix carcinoma) and MCF-7 (human breast cancer). MCF-7 is found to express significantly more PAP than the cervical cancer cell line, HeLa. Treatment of HeLa cells with etoposide (0.034 mM) leads to a continuous increase in PAP activity levels during the 2 h of exposure. Important differential modulations in both PAP enzyme activity and isoforms are observed, occurring earlier than chromatin condensation and cleavage, in both epithelial cancer cell lines tested. Treatment of HeLa cells with cordycepin (0.067 mM) leads to a continuous increase in PAP activity and isoform levels after 4 h of exposure. In the case of MCF-7 cells, treatment with 0.067 mM cordycepin leads to a decrease in both PAP II enzyme activity and phosphorylated PAP isoforms after 4 h of exposure. Thus high PAP activity levels in breast cancer cells may be an independent unfavorable prognostic factor contributing to the malignant phenotype of cells. The differentiated modulations of PAP in the two epithelial cancer cell lines correlate to changes in the cell cycle, suggesting that in this case PAP II follows the cell cycle despite the course of apoptosis. Thus in these two epithelial cell lines PAP modulations follow cell cycle progression rather than apoptosis
medicine
the enzyme possesses tumor-suppressing activity and sensitizes breast cancer cells to chemotherapy drugs. In breast cancer patients, high levels of enzyme correlate with an improved prognosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edmonds, M.
Poly(A) adding enzymes
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
15
217-244
1982
Bos taurus, Cricetulus griseus, Coturnix sp., Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Vaccinia virus
-
Nevins, J.R.; Joklik, W.K.
Isolation and partial characterization of the poly(A) polymerases from HeLa cells infected with vaccinia virus
J. Biol. Chem.
252
6939-6947
1977
Homo sapiens, Vaccinia virus
Ryner, L.C.; Takagaki, Y.; Manley, J.L.
Multiple forms of poly(A) polymerases purified from HeLa cells function in specific mRNA 3-end formation
Mol. Cell. Biol.
9
4229-4238
1989
Homo sapiens
Takagaki, Y.; Ryner, L.C.; Manley, J.L.
Separation and characterization of a poly(A) polymerase and a cleavage/specificity factor required for pre-mRNA polyadenylation
Cell
52
731-742
1988
Homo sapiens
Christofori, G.; Keller, W.
Poly(A) polymerase purified from HeLa cell nuclear extract is required for both cleavage and polyadenylation of pre-mRNA in vitro
Mol. Cell. Biol.
9
193-203
1989
Homo sapiens
Blakesley, R.W.; Boezi, J.A.
A kinetic and structural characterization of adenosine-5-triphosphate: ribonucleic acid adenylyltransferase from Pseudomonas putida
Biochim. Biophys. Acta
414
133-145
1975
Homo sapiens, Pseudomonas putida
Brakel, C.; Kates, J.R.
Poly(A) polymerase from vaccinia virus-infected cells. I. Partial purification and characterization
J. Virol.
14
715-723
1974
Homo sapiens
Scorilas, A.; Talieri, M.; Ardavanis, A.; Courtis, N.; Dimitriadis, E.; Yotis, J.; Tsiapalis, C.M.; Trangas, T.
Polyadenylate polymerase enzymatic activity in mammary tumor cytosols: a new independent prognostic marker in primary breast cancer
Cancer Res.
60
5427-5433
2000
Homo sapiens
Kyriakopoulou, C.; Tsiapalis, C.M.; Havredaki, M.
Biochemical and immunological identification and enrichment of poly(A) polymerase from human thymus
Mol. Cell. Biochem.
154
9-16
1996
Homo sapiens
Topalian, S.L.; Kaneko, S.; Gonzales, M.I.; Bond, G.L.; Ward, Y.; Manley, J.L.
Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors
Mol. Cell. Biol.
21
5614-5623
2001
Homo sapiens (Q9BWT3), Homo sapiens
Thomadaki, H.; Tsiapalis, C.M.; Scorilas, A.
Polyadenylate polymerase modulations in human epithelioid cervix and breast cancer cell lines, treated with etoposide or cordycepin, follow cell cycle rather than apoptosis induction
Biol. Chem.
386
471-480
2005
Homo sapiens
Nagaike, T.; Suzuki, T.; Katoh, T.; Ueda, T.
Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
J. Biol. Chem.
280
19721-19727
2005
Homo sapiens
Tomecki, R.; Dmochowska, A.; Gewartowski, K.; Dziembowski, A.; Stepien, P.P.
Identification of a novel human nuclear-encoded mitochondrial poly(A) polymerase
Nucleic Acids Res.
32
6001-6014
2004
Homo sapiens (Q9NVV4), Homo sapiens
Rouhana, L.; Wang, L.; Buter, N.; Kwak, J.E.; Schiltz, C.A.; Gonzalez, T.; Kelley, A.E.; Landry, C.F.; Wickens, M.
Vertebrate GLD2 poly(A) polymerases in the germline and the brain
RNA
11
1117-1130
2005
Homo sapiens, Mus musculus, Xenopus laevis
Slomovic, S.; Portnoy, V.; Yehudai-Resheff, S.; Bronshtein, E.; Schuster, G.
Polynucleotide phosphorylase and the archaeal exosome as poly(A)-polymerases
Biochim. Biophys. Acta
1779
247-255
2008
Homo sapiens
Thuresson, A.; Kirsebom, L.A.; Virtanen, A.
Inhibition of poly(A) polymerase by aminoglycosides
Biochimie
89
1221-1227
2007
Homo sapiens
Rissland, O.S.; Mikulasova, A.; Norbury, C.J.
Efficient RNA polyuridylation by noncanonical poly(A) polymerases
Mol. Cell. Biol.
27
3612-3624
2007
Homo sapiens
Bai, Y.; Srivastava, S.K.; Chang, J.H.; Manley, J.L.; Tong, L.
Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase
Mol. Cell
41
311-320
2011
Homo sapiens (Q9NVV4), Homo sapiens
Burns, D.M.; DAmbrogio, A.; Nottrott, S.; Richter, J.D.
CPEB and two poly(A) polymerases control miR-122 stability and p53 mRNA translation
Nature
473
105-108
2011
Homo sapiens (Q6PIY7), Homo sapiens
Rammelt, C.; Bilen, B.; Zavolan, M.; Keller, W.
PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif
RNA
17
1737-1746
2011
Homo sapiens (Q8NDF8), Homo sapiens
Ogami, K.; Cho, R.; Hoshino, S.
Molecular cloning and characterization of a novel isoform of the non-canonical poly(A) polymerase PAPD7
Biochem. Biophys. Res. Commun.
432
135-140
2013
Homo sapiens (Q5XG87)
Yang, Q.; Nausch, L.W.; Martin, G.; Keller, W.; Doublie, S.
Crystal structure of human poly(A) polymerase gamma reveals a conserved catalytic core for canonical poly(A) polymerases
J. Mol. Biol.
426
43-50
2014
Homo sapiens (Q9BWT3), Homo sapiens
Muniz, L.; Davidson, L.; West, S.
Poly(A) polymerase and the nuclear poly(A) binding protein, PABPN1, coordinate the splicing and degradation of a subset of human pre-mRNAs
Mol. Cell. Biol.
35
2218-2230
2015
Homo sapiens
Fiedler, M.; Rossmanith, W.; Wahle, E.; Rammelt, C.
Mitochondrial poly(A) polymerase is involved in tRNA repair
Nucleic Acids Res.
43
9937-9949
2015
Homo sapiens (Q9NVV4)
Bresson, S.M.; Conrad, N.K.
The human nuclear poly(a)-binding protein promotes RNA hyperadenylation and decay
PLoS Genet.
9
e1003893
2013
Homo sapiens (P51003), Homo sapiens (Q9BWT3)
Yu, C.; Gong, Y.; Zhou, H.; Wang, M.; Kong, L.; Liu, J.; An, T.; Zhu, H.; Li, Y.
Star-PAP, a poly(A) polymerase, functions as a tumor suppressor in an orthotopic human breast cancer model
Cell Death Dis.
8
e2582
2017
Homo sapiens (Q9H6E5), Homo sapiens
Furuya, N.; Kakuta, S.; Sumiyoshi, K.; Ando, M.; Nonaka, R.; Suzuki, A.; Kazuno, S.; Saiki, S.; Hattori, N.
NDP52 interacts with mitochondrial RNA poly(A) polymerase to promote mitophagy
EMBO Rep.
19
e46363
2018
Homo sapiens (Q9NVV4)
Mroczek, S.; Chlebowska, J.; Kulinski, T.M.; Gewartowska, O.; Gruchota, J.; Cysewski, D.; Liudkovska, V.; Borsuk, E.; Nowis, D.; Dziembowski, A.
The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in multiple myeloma
Nat. Commun.
8
619
2017
Mus musculus (Q5SSF7), Mus musculus, Homo sapiens (Q5VWP2)
Kuchta, K.; Muszewska, A.; Knizewski, L.; Steczkiewicz, K.; Wyrwicz, L.S.; Pawlowski, K.; Rychlewski, L.; Ginalski, K.
FAM46 proteins are novel eukaryotic non-canonical poly(A) polymerases
Nucleic Acids Res.
44
3534-3548
2016
Homo sapiens (Q5VWP2), Homo sapiens (Q8NEK8), Homo sapiens (Q96A09), Homo sapiens (Q96IP4), Homo sapiens
Shin, J.; Paek, K.; Ivshina, M.; Stackpole, E.; Richter, J.
Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic polyadenylation and carbohydrate metabolism
Nucleic Acids Res.
45
6793-6804
2017
Homo sapiens (Q8NDF8)
Li, W.; Li, W.; Laishram, R.S.; Hoque, M.; Ji, Z.; Tian, B.; Anderson, R.A.
Distinct regulation of alternative polyadenylation and gene expression by nuclear poly(A) polymerases
Nucleic Acids Res.
45
8930-8942
2017
Homo sapiens
Hu, J.L.; Liang, H.; Zhang, H.; Yang, M.Z.; Sun, W.; Zhang, P.; Luo, L.; Feng, J.X.; Bai, H.; Liu, F.; Zhang, T.; Yang, J.Y.; Gao, Q.; Long, Y.; Ma, X.Y.; Chen, Y.; Zhong, Q.; Yu, B.; Liao, S.; Wang, Y.; Zhao, Y.; Zeng, M.S.; Cao, N.; Wang, J.; Chen, W.; Yang, H.T.; Gao, S.
FAM46B is a prokaryotic-like cytoplasmic poly(A) polymerase essential in human embryonic stem cells
Nucleic Acids Res.
48
2733-2748
2020
Xenopus tropicalis (F7E7M3), Homo sapiens (Q96A09), Homo sapiens
Newie, I.; Sokilde, R.; Persson, H.; Jacomasso, T.; Gorbatenko, A.; Borg, A.; de Hoon, M.; Pedersen, S.F.; Rovira, C.
HER2-encoded mir-4728 forms a receptor-independent circuit with miR-21-5p through the non-canonical poly(A) polymerase PAPD5
Sci. Rep.
6
35664
2016
Homo sapiens (Q8NDF8), Homo sapiens
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