Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Deadenylating nuclease) (Deadenylation nuclease) (Polyadenylate-specific ribonuclease)

 PARN_HUMAN              Reviewed;         639 AA.
O95453; B2RCB3; B4DDG8; B4DSB0; B4DWR4; B4E1H6;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 163.
RecName: Full=Poly(A)-specific ribonuclease PARN;
EC=3.1.13.4;
AltName: Full=Deadenylating nuclease;
AltName: Full=Deadenylation nuclease;
AltName: Full=Polyadenylate-specific ribonuclease;
Name=PARN; Synonyms=DAN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9736620; DOI=10.1093/emboj/17.18.5427;
Koerner C.G., Wormington M., Muckenthaler M., Schneider S., Dehlin E.,
Wahle E.;
"The deadenylating nuclease (DAN) is involved in poly(A) tail removal
during the meiotic maturation of Xenopus oocytes.";
EMBO J. 17:5427-5437(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Adrenal gland, Brain, Esophagus, and Placenta;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[6]
TISSUE SPECIFICITY.
PubMed=10640832;
Buiting K., Koerner C., Ulrich B., Wahle E., Horsthemke B.;
"The human gene for the poly(A)-specific ribonuclease (PARN) maps to
16p13 and has a truncated copy in the Prader-Willi/Angelman syndrome
region on 15q11-->q13.";
Cytogenet. Cell Genet. 87:125-131(1999).
[7]
ENZYME ACTIVITY, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10801819; DOI=10.1074/jbc.M001705200;
Martinez J., Ren Y.-G., Thuresson A.-C., Hellman U., Aastroem J.,
Virtanen A.;
"A 54-kDa fragment of the Poly(A)-specific ribonuclease is an
oligomeric, processive, and cap-interacting Poly(A)-specific 3'
exonuclease.";
J. Biol. Chem. 275:24222-24230(2000).
[8]
FUNCTION.
PubMed=10882133; DOI=10.1016/S1097-2765(00)80442-6;
Gao M., Fritz D.T., Ford L.P., Wilusz J.;
"Interaction between a poly(A)-specific ribonuclease and the 5' cap
influences mRNA deadenylation rates in vitro.";
Mol. Cell 5:479-488(2000).
[9]
FUNCTION, AND COFACTOR.
PubMed=11359775; DOI=10.1074/jbc.M102270200;
Martinez J., Ren Y.-G., Nilsson P., Ehrenberg M., Virtanen A.;
"The mRNA cap structure stimulates rate of poly(A) removal and
amplifies processivity of degradation.";
J. Biol. Chem. 276:27923-27929(2001).
[10]
MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
PubMed=11742007; DOI=10.1074/jbc.M111515200;
Ren Y.-G., Martinez J., Virtanen A.;
"Identification of the active site of poly(A)-specific ribonuclease by
site-directed mutagenesis and Fe(2+)-mediated cleavage.";
J. Biol. Chem. 277:5982-5987(2002).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[12]
IDENTIFICATION IN A MRNA DECAY COMPLEX WITH RENT1; RENT2 AND RENT3B.
PubMed=14527413; DOI=10.1016/S1097-2765(03)00349-6;
Lejeune F., Li X., Maquat L.E.;
"Nonsense-mediated mRNA decay in mammalian cells involves decapping,
deadenylating, and exonucleolytic activities.";
Mol. Cell 12:675-687(2003).
[13]
FUNCTION, AND MUTAGENESIS OF ASP-28; GLU-30 AND ASP-382.
PubMed=12748283; DOI=10.1128/MCB.23.11.3798-3812.2003;
Lai W.S., Kennington E.A., Blackshear P.J.;
"Tristetraprolin and its family members can promote the cell-free
deadenylation of AU-rich element-containing mRNAs by poly(A)
ribonuclease.";
Mol. Cell. Biol. 23:3798-3812(2003).
[14]
FUNCTION, AND INTERACTION WITH KHSRP.
PubMed=15175153; DOI=10.1016/j.molcel.2004.05.002;
Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M.,
Chen C.-Y.;
"A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA
turnover by recruiting the degradation machinery.";
Mol. Cell 14:571-583(2004).
[15]
COFACTOR, AND MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
PubMed=15358788; DOI=10.1074/jbc.M403858200;
Ren Y.-G., Kirsebom L.A., Virtanen A.;
"Coordination of divalent metal ions in the active site of poly(A)-
specific ribonuclease.";
J. Biol. Chem. 279:48702-48706(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-557, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
INTERACTION WITH CELF1.
PubMed=16601207; DOI=10.1261/rna.59606;
Moraes K.C., Wilusz C.J., Wilusz J.;
"CUG-BP binds to RNA substrates and recruits PARN deadenylase.";
RNA 12:1084-1091(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-499, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION AT SER-557 BY MAPKAPK2, AND PHOSPHORYLATION AT
SER-557.
PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,
van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,
Yaffe M.B.;
"DNA damage activates a spatially distinct late cytoplasmic cell-cycle
checkpoint network controlled by MK2-mediated RNA stabilization.";
Mol. Cell 40:34-49(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-619; SER-628
AND THR-631, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
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).
[25]
INTERACTION WITH ZC3HAV1.
PubMed=21876179; DOI=10.1073/pnas.1101676108;
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L.,
Zheng Y.T., Gao G.;
"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
targeting multiply spliced viral mRNAs for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-619 AND
SER-623, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22442037; DOI=10.1261/rna.032292.112;
Berndt H., Harnisch C., Rammelt C., Stoehr N., Zirkel A., Dohm J.C.,
Himmelbauer H., Tavanez J.P., Huettelmaier S., Wahle E.;
"Maturation of mammalian H/ACA box snoRNAs: PAPD5-dependent
adenylation and PARN-dependent trimming.";
RNA 18:958-972(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-530;
SER-557; SER-619 AND SER-623, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
FUNCTION.
PubMed=25049417; DOI=10.1073/pnas.1317751111;
Boele J., Persson H., Shin J.W., Ishizu Y., Newie I.S., Soekilde R.,
Hawkins S.M., Coarfa C., Ikeda K., Takayama K., Horie-Inoue K.,
Ando Y., Burroughs A.M., Sasaki C., Suzuki C., Sakai M., Aoki S.,
Ogawa A., Hasegawa A., Lizio M., Kaida K., Teusink B., Carninci P.,
Suzuki H., Inoue S., Gunaratne P.H., Rovira C., Hayashizaki Y.,
de Hoon M.J.;
"PAPD5-mediated 3' adenylation and subsequent degradation of miR-21 is
disrupted in proliferative disease.";
Proc. Natl. Acad. Sci. U.S.A. 111:11467-11472(2014).
[31]
INVOLVEMENT IN DKCB6, AND VARIANT DKCB6 VAL-383.
PubMed=25893599; DOI=10.1172/JCI78963;
Tummala H., Walne A., Collopy L., Cardoso S., de la Fuente J.,
Lawson S., Powell J., Cooper N., Foster A., Mohammed S., Plagnol V.,
Vulliamy T., Dokal I.;
"Poly(A)-specific ribonuclease deficiency impacts telomere biology and
causes dyskeratosis congenita.";
J. Clin. Invest. 125:2151-2160(2015).
[32]
INVOLVEMENT IN PFBMFT4, AND VARIANT PFBMFT4 ARG-421.
PubMed=25848748; DOI=10.1038/ng.3278;
Stuart B.D., Choi J., Zaidi S., Xing C., Holohan B., Chen R., Choi M.,
Dharwadkar P., Torres F., Girod C.E., Weissler J., Fitzgerald J.,
Kershaw C., Klesney-Tait J., Mageto Y., Shay J.W., Ji W., Bilguvar K.,
Mane S., Lifton R.P., Garcia C.K.;
"Exome sequencing links mutations in PARN and RTEL1 with familial
pulmonary fibrosis and telomere shortening.";
Nat. Genet. 47:512-517(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-430 IN COMPLEX WITH DNA,
MUTAGENESIS OF PHE-31; ILE-34; ILE-113; PHE-123 AND HIS-377, AND
SUBUNIT.
PubMed=16281054; DOI=10.1038/sj.emboj.7600869;
Wu M., Reuter M., Lilie H., Liu Y., Wahle E., Song H.;
"Structural insight into poly(A) binding and catalytic mechanism of
human PARN.";
EMBO J. 24:4082-4093(2005).
-!- FUNCTION: 3'-exoribonuclease that has a preference for poly(A)
tails of mRNAs, thereby efficiently degrading poly(A) tails.
Exonucleolytic degradation of the poly(A) tail is often the first
step in the decay of eukaryotic mRNAs and is also used to silence
certain maternal mRNAs translationally during oocyte maturation
and early embryonic development. Interacts with both the 3'-end
poly(A) tail and the 5'-end cap structure during degradation, the
interaction with the cap structure being required for an efficient
degradation of poly(A) tails. Involved in nonsense-mediated mRNA
decay, a critical process of selective degradation of mRNAs that
contain premature stop codons. Also involved in degradation of
inherently unstable mRNAs that contain AU-rich elements (AREs) in
their 3'-UTR, possibly via its interaction with KHSRP. Probably
mediates the removal of poly(A) tails of AREs mRNAs, which
constitutes the first step of destabilization (PubMed:10882133,
PubMed:11359775, PubMed:12748283, PubMed:15175153,
PubMed:9736620). Also able to recognize and trim poly(A) tails of
microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar
RNAs) leading to microRNAs degradation or snoRNA increased
stability (PubMed:25049417, PubMed:22442037).
{ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775,
ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153,
ECO:0000269|PubMed:22442037, ECO:0000269|PubMed:25049417,
ECO:0000269|PubMed:9736620}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage of poly(A) to 5'-AMP.
{ECO:0000269|PubMed:10801819, ECO:0000269|PubMed:9736620}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11359775,
ECO:0000269|PubMed:15358788};
Note=Divalent metal cations. Mg(2+) is the most probable.
{ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:15358788};
-!- SUBUNIT: Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found
in a mRNA decay complex with RENT1, RENT2 and RENT3B. Interacts
with ZC3HAV1 in an RNA-independent manner.
{ECO:0000269|PubMed:10801819, ECO:0000269|PubMed:14527413,
ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:16281054,
ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:21876179}.
-!- INTERACTION:
Q99728:BARD1; NbExp=4; IntAct=EBI-372832, EBI-473181;
P33240:CSTF2; NbExp=5; IntAct=EBI-372832, EBI-711360;
Q09161:NCBP1; NbExp=2; IntAct=EBI-372832, EBI-464743;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9736620}.
Cytoplasm {ECO:0000269|PubMed:9736620}. Nucleus, nucleolus
{ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22442037}.
Note=Some nuclear fraction is nucleolar.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95453-1; Sequence=Displayed;
Name=2;
IsoId=O95453-2; Sequence=VSP_042846;
Note=No experimental confirmation available. Non canonical
splice junctions.;
Name=3;
IsoId=O95453-3; Sequence=VSP_042847;
Name=4;
IsoId=O95453-4; Sequence=VSP_057269;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10640832,
ECO:0000269|PubMed:9736620}.
-!- PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA
degradation after genotoxic stress. {ECO:0000269|PubMed:20932473}.
-!- DISEASE: Dyskeratosis congenita, autosomal recessive, 6 (DKCB6)
[MIM:616353]: A form of dyskeratosis congenita, a rare multisystem
disorder caused by defective telomere maintenance. It is
characterized by progressive bone marrow failure, and the clinical
triad of reticulated skin hyperpigmentation, nail dystrophy, and
mucosal leukoplakia. Common but variable features include
premature graying, aplastic anemia, low platelets, osteoporosis,
pulmonary fibrosis, and liver fibrosis among others. Early
mortality is often associated with bone marrow failure,
infections, fatal pulmonary complications, or malignancy.
{ECO:0000269|PubMed:25893599}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere-
related, 4 (PFBMFT4) [MIM:616371]: A disease associated with
shortened telomeres. Pulmonary fibrosis is the most common
manifestation. Other manifestations include aplastic anemia due to
bone marrow failure, hepatic fibrosis, and increased cancer risk,
particularly myelodysplastic syndrome and acute myeloid leukemia.
Phenotype, age at onset, and severity are determined by telomere
length. {ECO:0000269|PubMed:25848748}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ005698; CAA06683.1; -; mRNA.
EMBL; AK293189; BAG56729.1; -; mRNA.
EMBL; AK299653; BAG61572.1; -; mRNA.
EMBL; AK301648; BAG63126.1; -; mRNA.
EMBL; AK315020; BAG37510.1; -; mRNA.
EMBL; AC009167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85110.1; -; Genomic_DNA.
EMBL; BC050029; AAH50029.1; -; mRNA.
CCDS; CCDS45419.1; -. [O95453-1]
CCDS; CCDS45420.1; -. [O95453-2]
CCDS; CCDS58425.1; -. [O95453-3]
RefSeq; NP_001127949.1; NM_001134477.2. [O95453-2]
RefSeq; NP_001229921.1; NM_001242992.1. [O95453-3]
RefSeq; NP_002573.1; NM_002582.3. [O95453-1]
UniGene; Hs.253197; -.
PDB; 2A1R; X-ray; 2.60 A; A/B=1-430.
PDB; 2A1S; X-ray; 2.60 A; A/B/C/D=1-430.
PDB; 3CTR; X-ray; 2.10 A; A=445-540.
PDBsum; 2A1R; -.
PDBsum; 2A1S; -.
PDBsum; 3CTR; -.
ProteinModelPortal; O95453; -.
SMR; O95453; -.
BioGrid; 111107; 29.
CORUM; O95453; -.
DIP; DIP-31124N; -.
IntAct; O95453; 9.
MINT; O95453; -.
STRING; 9606.ENSP00000387911; -.
BindingDB; O95453; -.
ChEMBL; CHEMBL3616362; -.
iPTMnet; O95453; -.
PhosphoSitePlus; O95453; -.
SwissPalm; O95453; -.
BioMuta; PARN; -.
SWISS-2DPAGE; O95453; -.
EPD; O95453; -.
MaxQB; O95453; -.
PaxDb; O95453; -.
PeptideAtlas; O95453; -.
PRIDE; O95453; -.
ProteomicsDB; 50886; -.
ProteomicsDB; 50887; -. [O95453-2]
ProteomicsDB; 50888; -. [O95453-3]
DNASU; 2987; -.
DNASU; 5073; -.
Ensembl; ENST00000341484; ENSP00000345456; ENSG00000140694. [O95453-2]
Ensembl; ENST00000420015; ENSP00000410525; ENSG00000140694. [O95453-3]
Ensembl; ENST00000437198; ENSP00000387911; ENSG00000140694. [O95453-1]
Ensembl; ENST00000539279; ENSP00000444381; ENSG00000140694. [O95453-4]
Ensembl; ENST00000615183; ENSP00000478668; ENSG00000274829. [O95453-1]
Ensembl; ENST00000618929; ENSP00000484279; ENSG00000274829. [O95453-3]
Ensembl; ENST00000631868; ENSP00000488554; ENSG00000274829. [O95453-4]
Ensembl; ENST00000634004; ENSP00000487634; ENSG00000274829. [O95453-2]
GeneID; 5073; -.
KEGG; hsa:5073; -.
UCSC; uc010uzc.3; human. [O95453-1]
CTD; 5073; -.
DisGeNET; 5073; -.
EuPathDB; HostDB:ENSG00000140694.16; -.
GeneCards; PARN; -.
HGNC; HGNC:8609; PARN.
HPA; CAB011673; -.
HPA; HPA006314; -.
HPA; HPA012010; -.
MalaCards; PARN; -.
MIM; 604212; gene.
MIM; 616353; phenotype.
MIM; 616371; phenotype.
neXtProt; NX_O95453; -.
OpenTargets; ENSG00000140694; -.
PharmGKB; PA29072; -.
PharmGKB; PA32949; -.
eggNOG; KOG1990; Eukaryota.
eggNOG; ENOG410XS9D; LUCA.
GeneTree; ENSGT00530000063673; -.
HOGENOM; HOG000007285; -.
HOVERGEN; HBG053512; -.
InParanoid; O95453; -.
KO; K01148; -.
OMA; SPNTSKC; -.
OrthoDB; EOG091G04CM; -.
PhylomeDB; O95453; -.
TreeFam; TF314502; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-429947; Deadenylation of mRNA.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
SIGNOR; O95453; -.
ChiTaRS; PARN; human.
EvolutionaryTrace; O95453; -.
GeneWiki; PARN; -.
GeneWiki; Poly(A)-specific_ribonuclease; -.
GenomeRNAi; 5073; -.
PRO; PR:O95453; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140694; -.
CleanEx; HS_PARN; -.
ExpressionAtlas; O95453; baseline and differential.
Genevisible; O95453; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0043169; F:cation binding; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; TAS:ProtInc.
GO; GO:0004518; F:nuclease activity; TAS:ProtInc.
GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
GO; GO:0000495; P:box H/ACA snoRNA 3'-end processing; IDA:UniProtKB.
GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
GO; GO:0010587; P:miRNA catabolic process; IDA:UniProtKB.
GO; GO:0110008; P:ncRNA deadenylation; IMP:BHF-UCL.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IDA:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
GO; GO:0009451; P:RNA modification; TAS:ProtInc.
GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IMP:BHF-UCL.
GO; GO:0090669; P:telomerase RNA stabilization; IMP:BHF-UCL.
CDD; cd02637; R3H_PARN; 1.
Gene3D; 3.30.1370.50; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034042; PARN_R3H.
InterPro; IPR014789; PolyA-riboNase_RNA_binding.
InterPro; IPR001374; R3H_dom.
InterPro; IPR036867; R3H_dom_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR006941; RNase_CAF1.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF04857; CAF1; 1.
Pfam; PF01424; R3H; 1.
Pfam; PF08675; RNA_bind; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF54928; SSF54928; 1.
SUPFAM; SSF82708; SSF82708; 1.
PROSITE; PS51061; R3H; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Disease mutation; Dyskeratosis congenita; Exonuclease;
Hydrolase; Magnesium; Metal-binding; Nonsense-mediated mRNA decay;
Nuclease; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
CHAIN 1 639 Poly(A)-specific ribonuclease PARN.
/FTId=PRO_0000212851.
DOMAIN 178 245 R3H. {ECO:0000255|PROSITE-
ProRule:PRU00382}.
METAL 28 28 Divalent metal cation; catalytic.
{ECO:0000305}.
METAL 30 30 Divalent metal cation; catalytic.
{ECO:0000305}.
METAL 292 292 Divalent metal cation; catalytic.
{ECO:0000305}.
METAL 382 382 Divalent metal cation; catalytic.
{ECO:0000305}.
SITE 326 326 Interaction with poly(A).
{ECO:0000269|PubMed:16281054}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 557 557 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:20932473}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDG3}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDG3}.
MOD_RES 619 619 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 631 631 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 61 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042846.
VAR_SEQ 53 98 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042847.
VAR_SEQ 59 233 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057269.
VARIANT 383 383 A -> V (in DKCB6; dbSNP:rs786200999).
{ECO:0000269|PubMed:25893599}.
/FTId=VAR_073782.
VARIANT 421 421 K -> R (in PFBMFT4; dbSNP:rs777090017).
{ECO:0000269|PubMed:25848748}.
/FTId=VAR_073783.
MUTAGEN 28 28 D->A: Loss of function but does not
abolish ability to bind RNA. Induces a
decrease in degradation of mRNAs
containing AREs.
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 28 28 D->C: Loss of function in the presence of
Mg(2+) but not in the presence of Mn(2+),
Zn(2+), Co(2+) or Cd(2+).
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 30 30 E->A: Loss of function but does not
abolish ability to bind RNA. Induces a
decrease in degradation of mRNAs
containing AREs.
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 30 30 E->C: Loss of function in the presence of
Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+).
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 31 31 F->A: Reduced affinity for poly(A). Loss
of activity.
{ECO:0000269|PubMed:16281054}.
MUTAGEN 34 34 I->A: Reduced affinity for poly(A).
Strongly reduced activity.
{ECO:0000269|PubMed:16281054}.
MUTAGEN 113 113 I->A: Loss of dimerization. Loss of
activity. {ECO:0000269|PubMed:16281054}.
MUTAGEN 115 115 F->A: Reduced affinity for poly(A).
Little effect on activity.
MUTAGEN 123 123 F->A: Loss of dimerization. Loss of
activity. {ECO:0000269|PubMed:16281054}.
MUTAGEN 292 292 D->A: Loss of function but does not
abolish ability to bind RNA.
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:15358788}.
MUTAGEN 292 292 D->C: Loss of function in the presence of
Mg(2+) but not in the presence of Mn(2+),
Zn(2+), Co(2+) or Cd(2+).
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:15358788}.
MUTAGEN 326 326 K->A: Reduced affinity for poly(A).
Little effect on activity.
MUTAGEN 377 377 H->A: Loss of activity.
{ECO:0000269|PubMed:16281054}.
MUTAGEN 382 382 D->A: Loss of function but does not
abolish ability to bind RNA. Induces a
decrease in degradation of mRNAs
containing AREs.
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 382 382 D->C: Loss of function in the presence of
Mg(2+) but not in the presence of Mn(2+),
Zn(2+), Co(2+) or Cd(2+).
{ECO:0000269|PubMed:11742007,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15358788}.
MUTAGEN 557 557 S->A: Strong reduction of phosphorylation
by MAPKAPK2.
HELIX 5 21 {ECO:0000244|PDB:2A1R}.
STRAND 23 32 {ECO:0000244|PDB:2A1R}.
STRAND 36 38 {ECO:0000244|PDB:2A1R}.
HELIX 50 60 {ECO:0000244|PDB:2A1R}.
TURN 61 63 {ECO:0000244|PDB:2A1R}.
STRAND 66 77 {ECO:0000244|PDB:2A1R}.
TURN 78 81 {ECO:0000244|PDB:2A1R}.
STRAND 82 92 {ECO:0000244|PDB:2A1R}.
STRAND 97 101 {ECO:0000244|PDB:2A1R}.
STRAND 105 109 {ECO:0000244|PDB:2A1R}.
HELIX 110 118 {ECO:0000244|PDB:2A1R}.
HELIX 123 127 {ECO:0000244|PDB:2A1R}.
HELIX 136 141 {ECO:0000244|PDB:2A1R}.
HELIX 175 177 {ECO:0000244|PDB:2A1S}.
HELIX 178 192 {ECO:0000244|PDB:2A1S}.
HELIX 207 217 {ECO:0000244|PDB:2A1S}.
TURN 222 224 {ECO:0000244|PDB:2A1S}.
STRAND 228 231 {ECO:0000244|PDB:2A1S}.
STRAND 237 240 {ECO:0000244|PDB:2A1S}.
STRAND 245 248 {ECO:0000244|PDB:2A1S}.
TURN 249 252 {ECO:0000244|PDB:2A1S}.
HELIX 260 265 {ECO:0000244|PDB:2A1R}.
HELIX 271 280 {ECO:0000244|PDB:2A1R}.
STRAND 283 288 {ECO:0000244|PDB:2A1R}.
HELIX 290 300 {ECO:0000244|PDB:2A1R}.
HELIX 308 318 {ECO:0000244|PDB:2A1R}.
STRAND 320 324 {ECO:0000244|PDB:2A1R}.
HELIX 325 329 {ECO:0000244|PDB:2A1R}.
TURN 332 337 {ECO:0000244|PDB:2A1R}.
HELIX 343 349 {ECO:0000244|PDB:2A1R}.
STRAND 360 362 {ECO:0000244|PDB:2A1R}.
HELIX 379 397 {ECO:0000244|PDB:2A1R}.
HELIX 398 400 {ECO:0000244|PDB:2A1R}.
STRAND 401 403 {ECO:0000244|PDB:2A1R}.
TURN 413 415 {ECO:0000244|PDB:2A1S}.
HELIX 416 418 {ECO:0000244|PDB:2A1R}.
STRAND 419 429 {ECO:0000244|PDB:2A1S}.
STRAND 445 451 {ECO:0000244|PDB:3CTR}.
HELIX 458 464 {ECO:0000244|PDB:3CTR}.
TURN 465 467 {ECO:0000244|PDB:3CTR}.
STRAND 468 477 {ECO:0000244|PDB:3CTR}.
STRAND 480 488 {ECO:0000244|PDB:3CTR}.
HELIX 490 498 {ECO:0000244|PDB:3CTR}.
HELIX 509 513 {ECO:0000244|PDB:3CTR}.
SEQUENCE 639 AA; 73451 MW; 6994BE39384DF7AC CRC64;
MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP EERYQKLKKH
SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS SPDVKFVCQS SSIDFLASQG
FDFNKVFRNG IPYLNQEEER QLREQYDEKR SQANGAGALS YVSPNTSKCP VTIPEDQKKF
IDQVVEKIED LLQSEENKNL DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV
ISKVDEEERK RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL KETPFNPPKV
ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF LSPPKIHVSA RSKLIEPFFN
KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV TFPKEWKTSD LYQLFSAFGN IQISWIDDTS
AFVSLSQPEQ VKIAVNTSKY AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN
PQCIPYTLQN HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP
LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW


Related products :

Catalog number Product name Quantity
EIAAB29922 DAN,Deadenylating nuclease,Deadenylation nuclease,Homo sapiens,Human,PARN,Poly(A)-specific ribonuclease PARN,Polyadenylate-specific ribonuclease
EIAAB29921 Bos taurus,Bovine,DAN,Deadenylating nuclease,Deadenylation nuclease,PARN,Poly(A)-specific ribonuclease PARN,Polyadenylate-specific ribonuclease
PARP10 PARN Gene poly(A)-specific ribonuclease (deadenylation nuclease)
201-20-4039 PARN{poly(A)-specific ribonuclease (deadenylation nuclease)}rabbit.pAb 0.2ml
CSB-EL017456HU Human poly(A)-specific ribonuclease (deadenylation nuclease) (PARN) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL017456BO Bovine poly(A)-specific ribonuclease (deadenylation nuclease) (PARN) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL017456MO Mouse poly(A)-specific ribonuclease (deadenylation nuclease) (PARN) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB29920 Mouse,Mus musculus,Parn,Poly(A)-specific ribonuclease PARN,Polyadenylate-specific ribonuclease
CSB-PA017456GA01HU Rabbit anti-human poly(A)-specific ribonuclease (deadenylation nuclease) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA017456GA01HU Rabbit anti-human poly(A)-specific ribonuclease (deadenylation nuclease) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-EL017456MO Mouse Poly(A)-specific ribonuclease PARN (PARN) ELISA kit 96T
CSB-EL017456HU Human Poly(A)-specific ribonuclease PARN (PARN) ELISA kit 96T
CSB-EL017456BO Bovine Poly(A)-specific ribonuclease PARN (PARN) ELISA kit 96T
PARN_MOUSE ELISA Kit FOR Poly(A)-specific ribonuclease PARN; organism: Mouse; gene name: Parn 96T
DL-PARN-Hu Human Poly A Specific Ribonuclease (PARN) ELISA Kit 96T
E92176Hu ELISA Kit for Poly A Specific Ribonuclease (PARN) 96T/Kit
E0168r Human ELISA Kit FOR Poly(A)-specific ribonuclease PARN 96T
SAM50_MOUSE Human ELISA Kit FOR Poly(A)-specific ribonuclease PARN 96T
QY-E03739 Human Poly A Specific Ribonuclease(PARN)ELISA Kit 96T
EPHB1_CHICK Human ELISA Kit FOR Poly(A)-specific ribonuclease PARN 96T
201-12-4584 Human Poly A Specific Ribonuclease(PARN)ELISA Kit 96T
UB-E03739 Human Poly A Specific Ribonuclease(PARN)ELISA Kit 96T
CSB-YP017456HU Recombinant human Poly(A)-specific ribonuclease PARN 500ug
abx108620 Polyclonal Rabbit Poly(A)-specific ribonuclease PARN Antibody (HRP) 100 μg
PNLIPRP1 PNLDC1 Gene poly(A)-specific ribonuclease (PARN)-like domain containing 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur