Product: Rpb1 CTD Antibody
Catalog: AF7773
Description: Rabbit polyclonal antibody to Rpb1 CTD
Application: WB
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Horse, Sheep, Dog, Xenopus
Mol.Wt.: 270kDa; 217kD(Calculated).
Uniprot: P24928
RRID: AB_2844137

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Dog(100%), Xenopus(89%)
Clonality:
Polyclonal
Specificity:
Rpb1 CTD Antibody detects endogenous levels of total Rpb1 CTD.
RRID:
AB_2844137
Cite Format: Affinity Biosciences Cat# AF7773, RRID:AB_2844137.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

DNA directed RNA polymerase II subunit RPB1; hRPB220; hsRPB1; POLR2; POLR2A; POLRA; polymerase (RNA) II (DNA directed) polypeptide A, 220kDa; RNA polymerase II subunit 1; RNA polymerase II subunit B1; RP02; RPB220; RPBh1; RpIILS; RPO21; RPOL2; SUA8;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Sequence:
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
89
Zebrafish
0
Chicken
0
Rabbit
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P24928 As Substrate

Site PTM Type Enzyme
Phosphorylation
M1 Acetylation
S8 Phosphorylation
S27 Phosphorylation
K32 Ubiquitination
S35 Phosphorylation
T37 Phosphorylation
K42 Ubiquitination
T46 Phosphorylation
T47 Phosphorylation
K92 Ubiquitination
K116 Ubiquitination
S121 Phosphorylation
K125 Ubiquitination
K127 Ubiquitination
K134 Acetylation
K139 Acetylation
Y145 Phosphorylation
K149 Ubiquitination
K151 Ubiquitination
K163 Ubiquitination
T176 Phosphorylation
K177 Ubiquitination
K179 Ubiquitination
K203 Ubiquitination
K213 Sumoylation
K213 Ubiquitination
S217 Phosphorylation
K226 Ubiquitination
S269 Phosphorylation
K279 Ubiquitination
K285 Acetylation
K285 Ubiquitination
K331 Ubiquitination
T368 Phosphorylation
K417 Ubiquitination
R426 Methylation
K434 Ubiquitination
K445 Ubiquitination
K466 Ubiquitination
S530 Phosphorylation
T543 Phosphorylation
T549 Phosphorylation
K581 Ubiquitination
T587 Phosphorylation
S607 Phosphorylation
T608 Phosphorylation
Y618 Phosphorylation
K619 Ubiquitination
K642 Ubiquitination
K643 Ubiquitination
K697 Ubiquitination
T698 Phosphorylation
Y699 Phosphorylation
K707 Sumoylation
K707 Ubiquitination
K708 Methylation
K710 Acetylation
K710 Sumoylation
K710 Ubiquitination
K719 Ubiquitination
T732 Phosphorylation
T736 Phosphorylation
K751 Ubiquitination
K758 Ubiquitination
Y763 Phosphorylation
K767 Methylation
K767 Ubiquitination
S768 Phosphorylation
S772 Phosphorylation
K775 Ubiquitination
S777 Phosphorylation
K778 Ubiquitination
K796 Ubiquitination
K803 Methylation
K803 Ubiquitination
K812 Ubiquitination
K853 Ubiquitination
K866 Ubiquitination
K874 Ubiquitination
K910 Ubiquitination
K914 Ubiquitination
K918 Ubiquitination
K919 Ubiquitination
K940 Ubiquitination
K976 Ubiquitination
K992 Ubiquitination
K1008 Ubiquitination
K1014 Ubiquitination
K1019 Ubiquitination
K1125 Ubiquitination
K1132 Ubiquitination
K1155 Ubiquitination
K1225 Sumoylation
K1225 Ubiquitination
K1234 Ubiquitination
K1254 Ubiquitination
K1268 Ubiquitination
K1278 Ubiquitination
K1317 Ubiquitination
K1319 Ubiquitination
K1350 Ubiquitination
Y1383 Phosphorylation
T1406 Phosphorylation
T1415 Phosphorylation
T1424 Phosphorylation
T1525 Phosphorylation
T1540 Phosphorylation
R1603 Methylation
Y1615 Phosphorylation
S1616 Phosphorylation P50613 (CDK7) , Q13627 (DYRK1A) , Q14004 (CDK13) , Q9NYV4 (CDK12) , O60885 (BRD4) , P78527 (PRKDC) , P50750 (CDK9)
T1618 O-Glycosylation
T1618 Phosphorylation P50750 (CDK9)
S1619 Phosphorylation P27361 (MAPK3) , Q9NYV4 (CDK12) , P49336 (CDK8) , Q14004 (CDK13) , P50750 (CDK9) , Q13627 (DYRK1A) , P28482 (MAPK1) , P50613 (CDK7)
S1621 Phosphorylation P50750 (CDK9) , P78527 (PRKDC) , P50613 (CDK7)
S1623 Phosphorylation P50750 (CDK9)
S1626 Phosphorylation P27361 (MAPK3) , P50613 (CDK7) , P28482 (MAPK1)
S1644 Phosphorylation P50750 (CDK9)
S1647 Phosphorylation P28482 (MAPK1) , P50613 (CDK7) , P27361 (MAPK3)
S1651 Phosphorylation P50750 (CDK9)
S1654 Phosphorylation P27361 (MAPK3) , P28482 (MAPK1) , P50613 (CDK7)
S1665 Phosphorylation P50750 (CDK9)
S1668 Phosphorylation P27361 (MAPK3) , P50613 (CDK7) , P28482 (MAPK1)
S1672 Phosphorylation P50750 (CDK9)
S1675 Phosphorylation P50613 (CDK7) , P28482 (MAPK1) , P27361 (MAPK3)
S1693 Phosphorylation P50750 (CDK9)
S1696 Phosphorylation P28482 (MAPK1) , P50613 (CDK7) , P27361 (MAPK3)
S1714 Phosphorylation P50750 (CDK9)
S1717 Phosphorylation P50613 (CDK7) , P27361 (MAPK3) , P28482 (MAPK1)
S1721 Phosphorylation P50750 (CDK9)
S1724 Phosphorylation P50613 (CDK7) , P28482 (MAPK1) , P27361 (MAPK3)
S1735 Phosphorylation P50750 (CDK9)
S1738 Phosphorylation P27361 (MAPK3) , P50613 (CDK7) , P28482 (MAPK1)
S1763 Phosphorylation P50750 (CDK9)
S1766 Phosphorylation P50613 (CDK7) , P28482 (MAPK1) , P27361 (MAPK3)
S1784 Phosphorylation P50750 (CDK9)
S1787 Phosphorylation P50613 (CDK7) , P27361 (MAPK3) , P28482 (MAPK1)
R1810 Methylation
Y1811 Phosphorylation
T1812 Phosphorylation
S1815 Phosphorylation
Y1818 Phosphorylation
T1819 Phosphorylation
S1821 Phosphorylation
S1822 Phosphorylation
S1824 Phosphorylation
Y1825 Phosphorylation
S1826 Phosphorylation
S1828 Phosphorylation
S1829 Phosphorylation
S1831 Phosphorylation
Y1832 Phosphorylation
S1833 Phosphorylation
S1836 Phosphorylation
Y1839 Phosphorylation
T1840 Phosphorylation
T1842 Phosphorylation
S1843 Phosphorylation
S1845 Phosphorylation
Y1846 Phosphorylation
S1847 Phosphorylation
S1849 Phosphorylation
S1850 Phosphorylation
Y1853 Phosphorylation
T1854 Phosphorylation
T1856 Phosphorylation
S1857 Phosphorylation
K1859 Methylation
Y1860 Phosphorylation
S1861 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
T1863 Phosphorylation
S1864 Phosphorylation P50613 (CDK7) , P27361 (MAPK3) , P28482 (MAPK1)
K1866 Acetylation
K1866 Methylation
Y1867 Phosphorylation
S1868 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
T1870 Phosphorylation
S1871 Phosphorylation P28482 (MAPK1) , P27361 (MAPK3) , P50613 (CDK7)
K1873 Methylation
Y1874 Phosphorylation
S1875 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
T1877 Phosphorylation
S1878 Phosphorylation P28482 (MAPK1) , P50613 (CDK7) , Q9NYV4 (CDK12) , P50750 (CDK9) , P27361 (MAPK3)
T1880 Phosphorylation
Y1881 Phosphorylation
S1882 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9) , P24941 (CDK2)
T1884 Phosphorylation P24941 (CDK2)
T1885 Phosphorylation P24941 (CDK2)
K1887 Acetylation
K1887 Methylation
Y1888 Phosphorylation
S1889 Phosphorylation P50750 (CDK9) , Q9NYV4 (CDK12)
T1891 Phosphorylation
S1892 Phosphorylation P28482 (MAPK1) , P50613 (CDK7) , P27361 (MAPK3)
T1894 Phosphorylation
Y1895 Phosphorylation
S1896 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
T1898 Phosphorylation
S1899 Phosphorylation P27361 (MAPK3) , P50613 (CDK7) , P28482 (MAPK1)
Y1902 Phosphorylation
T1903 Phosphorylation
T1905 Phosphorylation
S1906 Phosphorylation
Y1909 Phosphorylation
S1910 Phosphorylation P50750 (CDK9) , Q9NYV4 (CDK12)
T1912 Phosphorylation
S1913 Phosphorylation P27361 (MAPK3) , P50613 (CDK7) , P28482 (MAPK1)
T1915 Phosphorylation P24941 (CDK2)
Y1916 Phosphorylation
S1917 Phosphorylation P50750 (CDK9) , Q9NYV4 (CDK12) , P24941 (CDK2)
T1919 Phosphorylation
S1920 Phosphorylation P06493 (CDK1) , P28482 (MAPK1) , P27361 (MAPK3) , P50613 (CDK7)
K1922 Acetylation
K1922 Methylation
Y1923 Phosphorylation
S1924 Phosphorylation P50750 (CDK9) , Q9NYV4 (CDK12)
T1926 Phosphorylation
S1927 Phosphorylation P28482 (MAPK1) , P27361 (MAPK3)
T1929 Phosphorylation
Y1930 Phosphorylation
S1931 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
T1933 Phosphorylation
S1934 Phosphorylation P27361 (MAPK3) , P06493 (CDK1) , P28482 (MAPK1) , P50613 (CDK7)
K1936 Acetylation
K1936 Methylation
S1941 Phosphorylation P50750 (CDK9) , Q9NYV4 (CDK12)
S1944 Phosphorylation P50613 (CDK7) , P28482 (MAPK1) , P27361 (MAPK3)
S1948 Phosphorylation Q9NYV4 (CDK12) , P50750 (CDK9)
S1951 Phosphorylation P50613 (CDK7) , P27361 (MAPK3) , P28482 (MAPK1)
S1962 Phosphorylation
S1966 Phosphorylation

Research Backgrounds

Function:

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression (By similarity).

(Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.

PTMs:

The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.

Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. Regulates initiation or early elongation steps of transcription specially for inducible genes.

Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.

Ubiquitinated by WWP2 leading to proteasomal degradation (By similarity). Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery.

Subcellular Location:

Nucleus. Cytoplasm.
Note: Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX. Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2. Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1 and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2. Interacts with FUS. Interacts with MCM3AP isoform GANP.

(Microbial infection) Interacts with herpes simplex virus 1 protein ICP22; this interaction causes loss of CTD 'Ser-2' phosphorylation from pol II engaged in transcription.

Family&Domains:

The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.

Belongs to the RNA polymerase beta' chain family.

Research Fields

· Genetic Information Processing > Transcription > RNA polymerase.

· Human Diseases > Neurodegenerative diseases > Huntington's disease.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Metabolism > Nucleotide metabolism > Purine metabolism.

· Metabolism > Nucleotide metabolism > Pyrimidine metabolism.

· Metabolism > Global and overview maps > Metabolic pathways.

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