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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.
25-OCT-2017, entry version 125.
RecName: Full=Terminal uridylyltransferase 4;
Short=TUTase 4;
EC=2.7.7.52;
AltName: Full=Zinc finger CCHC domain-containing protein 11;
Name=ZCCHC11; Synonyms=KIAA0191, TUT4;
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).
-!- 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).
Involved in microRNA (miRNA)-induced gene silencing through
uridylation of deadenylated miRNA targets. Also 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). Does not bind RNA directly, but
recruited to RNA targets by RNA-binding protein LIN28A. 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 (By similarity). May also suppress
Toll-like receptor-induced NF-kappa-B activation via binding to
T2BP. Does not play a role in replication-dependent histone mRNA
degradation. Due to functional redundancy between ZCCHC6 and
ZCCHC11, the identification of the specific role of each of these
proteins is difficult. {ECO:0000250|UniProtKB:B2RX14,
ECO:0000269|PubMed:16643855, ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
{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.
Interacts with T2BP. {ECO:0000269|PubMed:16643855,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463}.
-!- 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}.
Note=Mainly cytoplasmic (PubMed:19703396, PubMed:25480299).
Translocates into the cytoplasm following treatment of the cell
with LPS (PubMed:16643855).
-!- 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.;
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI23477.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AK303532; BAH13981.1; -; mRNA.
EMBL; AL138849; CAI23476.1; -; Genomic_DNA.
EMBL; AL138849; CAI23477.1; ALT_SEQ; Genomic_DNA.
EMBL; AL138849; CAI23478.1; -; 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; 12.
IntAct; Q5TAX3; 7.
STRING; 9606.ENSP00000257177; -.
iPTMnet; Q5TAX3; -.
PhosphoSitePlus; Q5TAX3; -.
BioMuta; ZCCHC11; -.
DMDM; 116242850; -.
EPD; Q5TAX3; -.
MaxQB; Q5TAX3; -.
PaxDb; Q5TAX3; -.
PeptideAtlas; Q5TAX3; -.
PRIDE; Q5TAX3; -.
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; ZCCHC11; -.
HGNC; HGNC:28981; ZCCHC11.
HPA; HPA027412; -.
HPA; HPA027973; -.
MIM; 613692; gene.
neXtProt; NX_Q5TAX3; -.
OpenTargets; ENSG00000134744; -.
PharmGKB; PA134918178; -.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00550000074490; -.
InParanoid; Q5TAX3; -.
KO; K13291; -.
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; -.
CleanEx; HS_ZCCHC11; -.
ExpressionAtlas; Q5TAX3; baseline and differential.
Genevisible; Q5TAX3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0003723; F:RNA binding; IDA: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; ISS:UniProtKB.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
Gene3D; 4.10.60.10; -; 3.
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 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}.
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}.
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. {ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:25480299}.
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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Catalog number Product name Quantity
EIAAB44557 Kiaa0191,Mouse,Mus musculus,Terminal uridylyltransferase 4,Tut4,TUTase 4,Zcchc11,Zinc finger CCHC domain-containing protein 11
EIAAB44559 Kiaa1711,Mouse,Mus musculus,Terminal uridylyltransferase 7,Tut7,TUTase 7,Zcchc6,Zinc finger CCHC domain-containing protein 6
EIAAB44560 Homo sapiens,HS2,Human,KIAA1711,Terminal uridylyltransferase 7,TUT7,TUTase 7,ZCCHC6,Zinc finger CCHC domain-containing protein 6
EIAAB44558 Homo sapiens,Human,KIAA0191,Terminal uridylyltransferase 4,TUT4,TUTase 4,ZCCHC11,Zinc finger CCHC domain-containing protein 11
EIAAB29836 Homo sapiens,Human,PAP-associated domain-containing protein 5,PAPD5,Terminal uridylyltransferase 3,Topoisomerase-related function protein 4-2,TRF4-2,TUTase 3
EIAAB29834 Homo sapiens,Human,mtPAP,MTPAP,PAP,PAP-associated domain-containing protein 1,PAPD1,Poly(A) RNA polymerase, mitochondrial,Polynucleotide adenylyltransferase,Terminal uridylyltransferase 1,TUTase 1
EIAAB46924 Homo sapiens,Human,SIZN1,Smad-interacting zinc finger protein 1,ZCCHC12,Zinc finger CCHC domain-containing protein 12
EIAAB46926 Mouse,Mus musculus,Sizn1,Smad-interacting zinc finger protein 1,Zcchc12,Zinc finger CCHC domain-containing protein 12
79-636 Zinc finger CCHC domain containing protein 10 Antibody 0.1 mg
E7054h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7164h Human Zinc Finger, CCHC Domain Containing Protein 96T
E3599h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7704h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7556h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7244h Human Zinc Finger, CCHC Domain Containing Protein 96T
E6750h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7345h Human Zinc Finger, CCHC Domain Containing Protein 96T
E7089h Human Zinc Finger, CCHC Domain Containing Protein 96T
E6761h Human Zinc Finger, CCHC Domain Containing Protein 96T
E4834h Human Zinc Finger, CCHC Domain Containing Protein 96T
E8028h Human Zinc Finger, CCHC Domain Containing Protein 96T
EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
E1986Rb Mouse ELISA Kit FOR Zinc finger CCHC domain-containing protein 4 96T
CSB-EL026388RA Rat Zinc finger CCHC domain-containing protein 7(ZCCHC7) ELISA kit 96T
I3166 Zinc finger CCHC domain-containing protein 12 (ZCCHC12), Rat, ELISA Kit 96T


 

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