PAPD5_HUMAN
ID PAPD5_HUMAN Reviewed; 572 AA.
AC Q8NDF8; B4DV38; Q9NW67; Q9Y6C0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Terminal nucleotidyltransferase 4B {ECO:0000305};
DE AltName: Full=Non-canonical poly(A) RNA polymerase PAPD5 {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:21788334};
DE AltName: Full=PAP-associated domain-containing protein 5;
DE AltName: Full=Terminal guanylyltransferase {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:30026317};
DE AltName: Full=Terminal uridylyltransferase 3;
DE Short=TUTase 3;
DE AltName: Full=Topoisomerase-related function protein 4-2;
DE Short=TRF4-2 {ECO:0000303|PubMed:21788334};
GN Name=TENT4B {ECO:0000312|HGNC:HGNC:30758};
GN Synonyms=GLD4 {ECO:0000303|PubMed:28383716},
GN PAPD5 {ECO:0000312|HGNC:HGNC:30758}, TRF4-2 {ECO:0000303|PubMed:21788334},
GN TUT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC TISSUE=Embryo, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-538 (ISOFORM 3), AND IDENTIFICATION.
RX PubMed=10066793; DOI=10.1074/jbc.274.11.7302;
RA Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A.,
RA Christman M.F.;
RT "The topoisomerase-related function gene TRF4 affects cellular sensitivity
RT to the antitumor agent camptothecin.";
RL J. Biol. Chem. 274:7302-7308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-572 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION IN A TRAMP-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21855801; DOI=10.1016/j.molcel.2011.06.028;
RA Lubas M., Christensen M.S., Kristiansen M.S., Domanski M., Falkenby L.G.,
RA Lykke-Andersen S., Andersen J.S., Dziembowski A., Jensen T.H.;
RT "Interaction profiling identifies the human nuclear exosome targeting
RT complex.";
RL Mol. Cell 43:624-637(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21788334; DOI=10.1261/rna.2787011;
RA Rammelt C., Bilen B., Zavolan M., Keller W.;
RT "PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding
RT motif.";
RL RNA 17:1737-1746(2011).
RN [9]
RP REVIEW ON RNA EXOSOMES.
RX PubMed=22817747; DOI=10.1042/bst20120061;
RA Sloan K.E., Schneider C., Watkins N.J.;
RT "Comparison of the yeast and human nuclear exosome complexes.";
RL Biochem. Soc. Trans. 40:850-855(2012).
RN [10]
RP FUNCTION.
RX PubMed=22442037; DOI=10.1261/rna.032292.112;
RA Berndt H., Harnisch C., Rammelt C., Stoehr N., Zirkel A., Dohm J.C.,
RA Himmelbauer H., Tavanez J.P., Huettelmaier S., Wahle E.;
RT "Maturation of mammalian H/ACA box snoRNAs: PAPD5-dependent adenylation and
RT PARN-dependent trimming.";
RL RNA 18:958-972(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23376078; DOI=10.1016/j.bbrc.2013.01.072;
RA Ogami K., Cho R., Hoshino S.;
RT "Molecular cloning and characterization of a novel isoform of the non-
RT canonical poly(A) polymerase PAPD7.";
RL Biochem. Biophys. Res. Commun. 432:135-140(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION.
RX PubMed=25049417; DOI=10.1073/pnas.1317751111;
RA Boele J., Persson H., Shin J.W., Ishizu Y., Newie I.S., Soekilde R.,
RA Hawkins S.M., Coarfa C., Ikeda K., Takayama K., Horie-Inoue K., Ando Y.,
RA Burroughs A.M., Sasaki C., Suzuki C., Sakai M., Aoki S., Ogawa A.,
RA Hasegawa A., Lizio M., Kaida K., Teusink B., Carninci P., Suzuki H.,
RA Inoue S., Gunaratne P.H., Rovira C., Hayashizaki Y., de Hoon M.J.;
RT "PAPD5-mediated 3' adenylation and subsequent degradation of miR-21 is
RT disrupted in proliferative disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11467-11472(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-470; LYS-497; LYS-512 AND
RP LYS-526, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151 (ISOFORM 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CPEB1.
RX PubMed=28383716; DOI=10.1093/nar/gkx239;
RA Shin J., Paek K.Y., Ivshina M., Stackpole E.E., Richter J.D.;
RT "Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic
RT polyadenylation and carbohydrate metabolism.";
RL Nucleic Acids Res. 45:6793-6804(2017).
RN [16]
RP FUNCTION.
RX PubMed=30026317; DOI=10.1126/science.aam5794;
RA Lim J., Kim D., Lee Y.S., Ha M., Lee M., Yeo J., Chang H., Song J., Ahn K.,
RA Kim V.N.;
RT "Mixed tailing by TENT4A and TENT4B shields mRNA from rapid
RT deadenylation.";
RL Science 361:701-704(2018).
CC -!- FUNCTION: Terminal nucleotidyltransferase that catalyzes preferentially
CC the transfert of ATP and GTP on RNA 3' poly(A) tail creating a
CC heterogeneous 3' poly(A) tail leading to mRNAs stabilization by
CC protecting mRNAs from active deadenylation (PubMed:21788334,
CC PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like
CC complex which has a poly(A) RNA polymerase activity and is involved in
CC a post-transcriptional quality control mechanism. Polyadenylation with
CC short oligo(A) tails is required for the degradative activity of the
CC exosome on several of its nuclear RNA substrates. Doesn't need a
CC cofactor for polyadenylation activity (in vitro) (PubMed:21788334,
CC PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs
CC involved in carbohydrate metabolism, including the glucose transporter
CC SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent
CC histone mRNA degradation, probably through terminal uridylation of
CC mature histone mRNAs. May play a role in sister chromatid cohesion
CC (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21
CC followed by its 3'-to-5' trimming by the exoribonuclease PARN leading
CC to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box
CC snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the
CC exoribonuclease PARN which enhances snoRNA stability and maturation
CC (PubMed:22442037). {ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:21788334, ECO:0000269|PubMed:21855801,
CC ECO:0000269|PubMed:22442037, ECO:0000269|PubMed:25049417,
CC ECO:0000269|PubMed:28383716, ECO:0000269|PubMed:30026317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:21788334};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes (PubMed:21855801). Interacts with CPEB1; the
CC interaction is required for TENT4B-mediated translational control
CC (PubMed:28383716). {ECO:0000269|PubMed:21855801,
CC ECO:0000269|PubMed:28383716}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:21788334}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:21855801, ECO:0000269|PubMed:23376078}. Cytoplasm
CC {ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:28383716}.
CC Note=Predominantly expressed in the cytoplasm (PubMed:18172165).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8NDF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDF8-2; Sequence=VSP_012734, VSP_012736;
CC Name=3;
CC IsoId=Q8NDF8-3; Sequence=VSP_012735, VSP_012737;
CC Name=4;
CC IsoId=Q8NDF8-4; Sequence=VSP_012732, VSP_012733;
CC Name=5;
CC IsoId=Q8NDF8-5; Sequence=VSP_046989, VSP_046990, VSP_012735;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have DNA polymerase activity.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45199.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91518.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001141; BAA91518.1; ALT_INIT; mRNA.
DR EMBL; AK097589; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK300918; BAG62550.1; -; mRNA.
DR EMBL; AC007597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF089897; AAD45199.1; ALT_INIT; mRNA.
DR EMBL; AL833922; CAD38778.1; -; mRNA.
DR CCDS; CCDS54006.1; -. [Q8NDF8-5]
DR RefSeq; NP_001035374.2; NM_001040284.2. [Q8NDF8-5]
DR RefSeq; NP_001035375.2; NM_001040285.2.
DR AlphaFoldDB; Q8NDF8; -.
DR SMR; Q8NDF8; -.
DR BioGRID; 122126; 170.
DR DIP; DIP-59183N; -.
DR ELM; Q8NDF8; -.
DR IntAct; Q8NDF8; 18.
DR MINT; Q8NDF8; -.
DR ChEMBL; CHEMBL4680036; -.
DR GlyGen; Q8NDF8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NDF8; -.
DR PhosphoSitePlus; Q8NDF8; -.
DR BioMuta; PAPD5; -.
DR DMDM; 59800139; -.
DR EPD; Q8NDF8; -.
DR jPOST; Q8NDF8; -.
DR MassIVE; Q8NDF8; -.
DR MaxQB; Q8NDF8; -.
DR PaxDb; Q8NDF8; -.
DR PeptideAtlas; Q8NDF8; -.
DR PRIDE; Q8NDF8; -.
DR ProteomicsDB; 5240; -.
DR ProteomicsDB; 73020; -. [Q8NDF8-1]
DR ProteomicsDB; 73021; -. [Q8NDF8-2]
DR ProteomicsDB; 73022; -. [Q8NDF8-3]
DR ProteomicsDB; 73023; -. [Q8NDF8-4]
DR Antibodypedia; 28218; 155 antibodies from 26 providers.
DR DNASU; 64282; -.
DR Ensembl; ENST00000436909.8; ENSP00000396995.3; ENSG00000121274.14. [Q8NDF8-5]
DR GeneID; 64282; -.
DR KEGG; hsa:64282; -.
DR UCSC; uc010vgo.3; human. [Q8NDF8-1]
DR CTD; 64282; -.
DR DisGeNET; 64282; -.
DR GeneCards; TENT4B; -.
DR HGNC; HGNC:30758; TENT4B.
DR HPA; ENSG00000121274; Low tissue specificity.
DR MIM; 605540; gene.
DR neXtProt; NX_Q8NDF8; -.
DR OpenTargets; ENSG00000121274; -.
DR PharmGKB; PA134949693; -.
DR VEuPathDB; HostDB:ENSG00000121274; -.
DR eggNOG; KOG1906; Eukaryota.
DR GeneTree; ENSGT00940000158301; -.
DR HOGENOM; CLU_013572_3_2_1; -.
DR InParanoid; Q8NDF8; -.
DR OrthoDB; 1016712at2759; -.
DR PhylomeDB; Q8NDF8; -.
DR TreeFam; TF313939; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q8NDF8; -.
DR SignaLink; Q8NDF8; -.
DR BioGRID-ORCS; 64282; 58 hits in 1083 CRISPR screens.
DR ChiTaRS; PAPD5; human.
DR GenomeRNAi; 64282; -.
DR Pharos; Q8NDF8; Tbio.
DR PRO; PR:Q8NDF8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NDF8; protein.
DR Bgee; ENSG00000121274; Expressed in ileal mucosa and 196 other tissues.
DR ExpressionAtlas; Q8NDF8; baseline and differential.
DR Genevisible; Q8NDF8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031499; C:TRAMP complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0070568; F:guanylyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0010587; P:miRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0043629; P:ncRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0043630; P:ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process; IMP:BHF-UCL.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IMP:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0071050; P:sno(s)RNA polyadenylation; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR040136; TENT4B.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 2.
DR PANTHER; PTHR23092:SF51; PTHR23092:SF51; 2.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; DNA-binding;
KW DNA-directed DNA polymerase; Isopeptide bond; Magnesium; Manganese;
KW Metal-binding; Mitosis; mRNA processing; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; rRNA processing; Transferase;
KW Ubl conjugation.
FT CHAIN 1..572
FT /note="Terminal nucleotidyltransferase 4B"
FT /id="PRO_0000120310"
FT DOMAIN 308..368
FT /note="PAP-associated"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 557..563
FT /note="Basic, involved in binding of the RNA primer"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MRPRPRSAPGKPRRRSRARLRSSRTPSGGASGGGGSSSSSSTATGGS
FT GSSTGSPGGAASAPAPAPAGM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046989"
FT VAR_SEQ 85
FT /note="A -> ASTYGLNYSLLQP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046990"
FT VAR_SEQ 368..370
FT /note="NDV -> IEI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012732"
FT VAR_SEQ 371..572
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012733"
FT VAR_SEQ 444
FT /note="G -> GNGVTLIVDTQQLDKCNNNLSEENEALGKCRSKTSESLSKHSSNSSS
FT G (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10066793,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_012735"
FT VAR_SEQ 445..465
FT /note="PVSSSSATQSSSSDVDSDATP -> NETLHQVQCRPLLPHSPALVT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012734"
FT VAR_SEQ 466..572
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012736"
FT VAR_SEQ 539..572
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10066793"
FT /id="VSP_012737"
FT CROSSLNK Q8NDF8-5:151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63267 MW; D205C0DE961DA701 CRC64;
MYRSGERLLG SHALPAEQRD FLPLETTNNN NNHHQPGAWA RRAGSSASSP PSASSSPHPS
AAVPAADPAD SASGSSNKRK RDNKASGGRA AGGGRADGGG VVYSGTPWKR RNYNQGVVGL
HEEISDFYEY MSPRPEEEKM RMEVVNRIES VIKELWPSAD VQIFGSFKTG LYLPTSDIDL
VVFGKWENLP LWTLEEALRK HKVADEDSVK VLDKATVPII KLTDSFTEVK VDISFNVQNG
VRAADLIKDF TKKYPVLPYL VLVLKQFLLQ RDLNEVFTGG IGSYSLFLMA VSFLQLHPRE
DACIPNTNYG VLLIEFFELY GRHFNYLKTG IRIKDGGSYV AKDEVQKNML DGYRPSMLYI
EDPLQPGNDV GRSSYGAMQV KQAFDYAYVV LSHAVSPIAK YYPNNETESI LGRIIRVTDE
VATYRDWISK QWGLKNRPEP SCNGPVSSSS ATQSSSSDVD SDATPCKTPK QLLCRPSTGN
RVGSQDVSLE SSQAVGKMQS TQTTNTSNST NKSQHGSARL FRSSSKGFQG TTQTSHGSLM
TNKQHQGKSN NQYYHGKKRK HKRDAPLSDL CR
