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Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)

 TUT4_HUMAN              Reviewed;        1644 AA.
Q5TAX3; A2RRP0; B7Z8J5; D3DQ35; Q12764; Q5TAX2; Q5TAX4; Q86XZ3;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
13-FEB-2019, entry version 133.
RecName: Full=Terminal uridylyltransferase 4 {ECO:0000305};
Short=TUTase 4;
EC=2.7.7.52 {ECO:0000269|PubMed:19703396};
AltName: Full=Zinc finger CCHC domain-containing protein 11;
Name=TUT4 {ECO:0000312|HGNC:HGNC:28981};
Synonyms=KIAA0191, ZCCHC11 {ECO:0000312|HGNC:HGNC:28981};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1644.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[6]
FUNCTION, INTERACTION WITH T2BP, AND SUBCELLULAR LOCATION.
PubMed=16643855; DOI=10.1016/j.bbrc.2006.04.006;
Minoda Y., Saeki K., Aki D., Takaki H., Sanada T., Koga K.,
Kobayashi T., Takaesu G., Yoshimura A.;
"A novel Zinc finger protein, ZCCHC11, interacts with TIFA and
modulates TLR signaling.";
Biochem. Biophys. Res. Commun. 344:1023-1030(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
LIN28A, AND MUTAGENESIS OF ASP-1011.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INTERACTION WITH LIN28A.
PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
"Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
mechanisms.";
Cell 147:1066-1079(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-156, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-1011.
PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J.,
Kim V.N.;
"Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
Cell 159:1365-1376(2014).
[14]
FUNCTION.
PubMed=25979828; DOI=10.15252/embj.201590931;
Kim B., Ha M., Loeff L., Chang H., Simanshu D.K., Li S., Fareh M.,
Patel D.J., Joo C., Kim V.N.;
"TUT7 controls the fate of precursor microRNAs by using three
different uridylation mechanisms.";
EMBO J. 34:1801-1815(2015).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MOV10, AND
MUTAGENESIS OF ASP-1011.
PubMed=30122351; DOI=10.1016/j.cell.2018.07.022;
Warkocki Z., Krawczyk P.S., Adamska D., Bijata K., Garcia-Perez J.L.,
Dziembowski A.;
"Uridylation by TUT4/7 Restricts Retrotransposition of Human LINE-
1s.";
Cell 0:0-0(2018).
-!- FUNCTION: Uridylyltransferase that mediates the terminal
uridylation of mRNAs with short (less than 25 nucleotides) poly(A)
tails, hence facilitating global mRNA decay (PubMed:25480299).
Essential for both oocyte maturation and fertility. Through 3'
terminal uridylation of mRNA, sculpts, with TUT7, the maternal
transcriptome by eliminating transcripts during oocyte growth (By
similarity). Involved in microRNA (miRNA)-induced gene silencing
through uridylation of deadenylated miRNA targets. Also functions
as an integral regulator of microRNA biogenesis using 3 different
uridylation mechanisms (PubMed:25979828). Acts as a suppressor of
miRNA biogenesis by mediating the terminal uridylation of some
miRNA precursors, including that of let-7 (pre-let-7), miR107,
miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer
and undergo degradation. Degradation of pre-let-7 contributes to
the maintenance of embryonic stem (ES) cell pluripotency (By
similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA
that targets IL6 transcript. This abrogates the silencing of IL6
transcript, hence promoting cytokine expression (PubMed:19703396).
In the absence of LIN28A, TUT7 and TUT4 monouridylate group II
pre-miRNAs, which includes most of pre-let7 members, that shapes
an optimal 3' end overhang for efficient processing
(PubMed:25979828). Adds oligo-U tails to truncated pre-miRNAS with
a 5' overhang which may promote rapid degradation of non-
functional pre-miRNA species (PubMed:25979828). May also suppress
Toll-like receptor-induced NF-kappa-B activation via binding to
T2BP (PubMed:16643855). Does not play a role in replication-
dependent histone mRNA degradation (PubMed:18172165). Due to
functional redundancy between TUT4 and TUT7, the identification of
the specific role of each of these proteins is difficult
(PubMed:25979828, PubMed:25480299, PubMed:16643855,
PubMed:19703396, PubMed:18172165) (By similarity). TUT4 and TUT7
restrict retrotransposition of long interspersed element-1 (LINE-
1) in cooperation with MOV10 counteracting the RNA chaperonne
activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm
which inhibits initiation of reverse transcription once in the
nucleus, whereas uridylation by TUT4 destabilizes mRNAs in
cytoplasmic ribonucleoprotein granules (PubMed:30122351).
{ECO:0000250|UniProtKB:B2RX14, ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299, ECO:0000269|PubMed:25979828,
ECO:0000269|PubMed:30122351}.
-!- CATALYTIC ACTIVITY:
Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine
ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:11128,
Rhea:RHEA-COMP:14648, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
ChEBI:CHEBI:83400, ChEBI:CHEBI:140627; EC=2.7.7.52;
Evidence={ECO:0000269|PubMed:19703396};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with LIN28A in the presence of pre-let-7 RNA
(PubMed:19703396, PubMed:22118463). Interacts with T2BP
(PubMed:16643855). Interacts with MOV10; the interaction IS RNA-
dependent (PubMed:30122351). {ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463,
ECO:0000269|PubMed:30122351}.
-!- INTERACTION:
Q96CG3:TIFA; NbExp=2; IntAct=EBI-1606425, EBI-740711;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16643855}.
Cytoplasm {ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:25480299}.
Cytoplasm, Cytoplasmic ribonucleoprotein granule
{ECO:0000269|PubMed:30122351}. Note=Mainly cytoplasmic
(PubMed:19703396, PubMed:25480299). Translocates into the
cytoplasm following treatment of the cell with LPS
(PubMed:16643855). Co-enriched in cytoplasmic foci with MOV10
(PubMed:30122351). {ECO:0000269|PubMed:30122351}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5TAX3-1; Sequence=Displayed;
Name=2;
IsoId=Q5TAX3-2; Sequence=VSP_038135, VSP_038136;
Note=No experimental confirmation available.;
-!- DOMAIN: Utilizes two multidomain functional modules during the
switch from monouridylation to oligouridylation. The catalytic
module (containing the 3 CCHC-type Zinc finger domains) is
essential for both activites while the Lin28-interacting module
(LIM) at the N-termail part is indispensable for oligouridylation.
{ECO:0000250|UniProtKB:B2RX14}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
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EMBL; AK303532; BAH13981.1; -; mRNA.
EMBL; AL138849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06778.1; -; Genomic_DNA.
EMBL; CH471059; EAX06780.1; -; Genomic_DNA.
EMBL; BC131734; AAI31735.1; -; mRNA.
EMBL; D83776; BAA12105.1; -; mRNA.
CCDS; CCDS30716.1; -. [Q5TAX3-1]
RefSeq; NP_001009881.1; NM_001009881.2.
RefSeq; NP_056084.1; NM_015269.2. [Q5TAX3-1]
UniGene; Hs.655407; -.
ProteinModelPortal; Q5TAX3; -.
SMR; Q5TAX3; -.
BioGrid; 116909; 24.
IntAct; Q5TAX3; 7.
STRING; 9606.ENSP00000257177; -.
iPTMnet; Q5TAX3; -.
PhosphoSitePlus; Q5TAX3; -.
BioMuta; ZCCHC11; -.
DMDM; 116242850; -.
EPD; Q5TAX3; -.
jPOST; Q5TAX3; -.
MaxQB; Q5TAX3; -.
PaxDb; Q5TAX3; -.
PeptideAtlas; Q5TAX3; -.
PRIDE; Q5TAX3; -.
ProteomicsDB; 64876; -.
ProteomicsDB; 64877; -. [Q5TAX3-2]
DNASU; 23318; -.
Ensembl; ENST00000371544; ENSP00000360599; ENSG00000134744. [Q5TAX3-1]
GeneID; 23318; -.
KEGG; hsa:23318; -.
UCSC; uc001ctx.3; human. [Q5TAX3-1]
CTD; 23318; -.
DisGeNET; 23318; -.
EuPathDB; HostDB:ENSG00000134744.13; -.
GeneCards; TUT4; -.
HGNC; HGNC:28981; TUT4.
HPA; HPA027412; -.
HPA; HPA027973; -.
MIM; 613692; gene.
neXtProt; NX_Q5TAX3; -.
OpenTargets; ENSG00000134744; -.
PharmGKB; PA134918178; -.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00940000156988; -.
InParanoid; Q5TAX3; -.
KO; K13291; -.
OrthoDB; 803033at2759; -.
PhylomeDB; Q5TAX3; -.
TreeFam; TF315661; -.
BRENDA; 2.7.7.52; 2681.
Reactome; R-HSA-429947; Deadenylation of mRNA.
ChiTaRS; ZCCHC11; human.
GenomeRNAi; 23318; -.
PRO; PR:Q5TAX3; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134744; Expressed in 221 organ(s), highest expression level in kidney.
ExpressionAtlas; Q5TAX3; baseline and differential.
Genevisible; Q5TAX3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:UniProtKB.
GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IDA:UniProtKB.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
GO; GO:0071076; P:RNA 3' uridylation; ISS:UniProtKB.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 2.
Pfam; PF00098; zf-CCHC; 2.
SMART; SM00343; ZnF_C2HC; 3.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50158; ZF_CCHC; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Magnesium;
Manganese; Metal-binding; Methylation; Nucleotidyltransferase;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
RNA-mediated gene silencing; Transferase; Zinc; Zinc-finger.
CHAIN 1 1644 Terminal uridylyltransferase 4.
/FTId=PRO_0000150970.
DOMAIN 628 678 PAP-associated 1.
DOMAIN 1184 1237 PAP-associated 2.
ZN_FING 304 334 Matrin-type. {ECO:0000255|PROSITE-
ProRule:PRU00130}.
ZN_FING 913 930 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1293 1310 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1357 1374 CCHC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 901 1634 Sufficient for monouridylation activity.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 998 1001 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1008 1011 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1121 1125 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
COMPBIAS 1398 1483 Gln-rich.
COMPBIAS 1424 1598 Pro-rich.
METAL 1009 1009 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 1011 1011 Magnesium or manganese; catalytic.
{ECO:0000250}.
BINDING 1081 1081 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1103 1103 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1237 1237 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:B2RX14}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1624 1624 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:B2RX14}.
VAR_SEQ 685 719 RSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKST -> LQ
PGRQEWKLCLKKKKKNSVKYTFIYEIQVSLFVI (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038135.
VAR_SEQ 720 1644 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038136.
VARIANT 796 796 D -> Y (in dbSNP:rs12127732).
/FTId=VAR_028402.
MUTAGEN 1011 1011 D->A: Loss of nucleotidyltransferase
activity and stabilization of pre-let-7
miRNAs. Abolishes inhibition of LIRE1
retrotransposition.
{ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299,
ECO:0000269|PubMed:30122351}.
CONFLICT 1313 1313 S -> SS (in Ref. 4; AAI31735).
{ECO:0000305}.
SEQUENCE 1644 AA; 185166 MW; B7C88D7DCF0F3356 CRC64;
MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP NRNSSKKNKQ
NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK FPNSPVKAEK ATISQAKSEK
ATSLQAKAEK SPKSPNSVKA EKASSYQMKS EKVPSSPAEA EKGPSLLLKD MRQKTELQQI
GKKIPSSFTS VDKVNIEAVG GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS
KMKNDESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT
NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA HLAALSVAVI
ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG SSLTRFALKS SDVNIDIKFP
PKMNHPDLLI KVLGILKKNV LYVDVESDFH AKVPVVVCRD RKSGLLCRVS AGNDMACLTT
DLLTALGKIE PVFIPLVLAF RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC
LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK
TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV ICVRIQDILT
RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF RAAYRYFACP QTKGGNKSTV
DFKKREKGKI SNKKPVKSNN MATNGCILLG ETTEKINAER EQPVQCDEMD CTSQRCIIDN
NNLLVNELDF ADHGQDSSSL STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK
SPDPDKSTGT DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF
DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI LDLVCKRCFD
ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK NGFGFRDSDL DICMTLEGHE
NAEKLNCKEI IENLAKILKR HPGLRNILPI TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH
NTRMLATYAA IDPRVQYLGY TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI
PVLQEIFDGK QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF
DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF IMKAFINGRK
LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK IGHYMKDCPK RKSLLFRLKK
KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ
RNSSVAAAQL VRNLVNAQQV AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS
AAITQPSSQP GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI
PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH WPRTVAPNSL
VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG LHQNFMHQGN ARFQPNKPFY
TQDRCATRRC RERCPHPPRG NVSE


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP1689: Porphyrin and chlorophyll metabolism
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism

Related Genes :
[TUT4 KIAA0191 ZCCHC11] Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)
[Tut4 Kiaa0191 Zcchc11] Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)
[TUT7 HS2 KIAA1711 ZCCHC6] Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 6)
[Tut7 Kiaa1711 Zcchc6] Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 6)
[cid1 SPAC19D5.03] Terminal uridylyltransferase cid1 (TUTase cid1) (EC 2.7.7.19) (EC 2.7.7.52) (Caffeine-induced death protein 1) (Poly(A) polymerase cid1) (PAP) (Poly(U) polymerase cid1) (PUP)
[TENT4A PAPD7 POLS TRF4] Terminal nucleotidyltransferase 4A (DNA polymerase sigma) (LAK-1) (Non-canonical poly(A) RNA polymerase PAPD7) (EC 2.7.7.19) (PAP-associated domain-containing protein 7) (TRAMP-like complex polyadenylate polymerase) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 5) (TUTase 5) (Topoisomerase-related function protein 4-1) (TRF4-1)
[TENT4B GLD4 PAPD5 TRF4-2 TUT3] Terminal nucleotidyltransferase 4A (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal nucleotidyltransferase 4B) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)
[Tent4b Papd5] Terminal nucleotidyltransferase 4A (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal nucleotidyltransferase 4B) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)
[TUT1 RBM21] Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Tut1 Rbm21] Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
[TENT2 GLD2 PAPD4] Poly(A) RNA polymerase GLD2 (hGLD-2) (EC 2.7.7.19) (PAP-associated domain-containing protein 4) (Terminal nucleotidyltransferase 2) (Terminal uridylyltransferase 2) (TUTase 2)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[TY3B-I YILWTy3-1 POL YIL082W-A] Transposon Ty3-I Gag-Pol polyprotein (Gag3-Pol3) (Transposon Ty3-2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA) (p24); Spacer peptide p3; Nucleocapsid protein p11 (NC); Ty3 protease (PR) (EC 3.4.23.-) (p16); Spacer peptide J; Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (p55); Integrase p52 (IN); Integrase p49 (IN)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[Tut1 Rbm21] Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
[] Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3; Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.47) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Nucleocapsid protein p7 (NC); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[TUT1 RBM21] Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
[pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-Pol (NC-pol); Protease (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[TUT1 RBM21 PANDA_014931] Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

Bibliography :