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Cleavage and polyadenylation specificity factor subunit 7 (Cleavage and polyadenylation specificity factor 59 kDa subunit) (CFIm59) (CPSF 59 kDa subunit) (Pre-mRNA cleavage factor Im 59 kDa subunit)

 CPSF7_HUMAN             Reviewed;         471 AA.
Q8N684; B3KU04; C9K0Q4; Q7Z3H9; Q9H025; Q9H9V1;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 148.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 7;
AltName: Full=Cleavage and polyadenylation specificity factor 59 kDa subunit;
Short=CFIm59;
Short=CPSF 59 kDa subunit;
AltName: Full=Pre-mRNA cleavage factor Im 59 kDa subunit;
Name=CPSF7;
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 1).
TISSUE=Cervix carcinoma;
Rueegsegger U., Blank D., Dettwiler S., Keller W.;
"Cloning of a second SR protein related subunit of human pre-mRNA
cleavage factor I.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORM 2).
TISSUE=Bone marrow, and Embryonic brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Uterus;
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]
FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, AND
RNA-BINDING.
PubMed=8626397; DOI=10.1074/jbc.271.11.6107;
Rueegsegger U., Beyer K., Keller W.;
"Purification and characterization of human cleavage factor Im
involved in the 3' end processing of messenger RNA precursors.";
J. Biol. Chem. 271:6107-6113(1996).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-413, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, 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).
[12]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=20695905; DOI=10.1111/j.1365-2443.2010.01436.x;
Kim S., Yamamoto J., Chen Y., Aida M., Wada T., Handa H.,
Yamaguchi Y.;
"Evidence that cleavage factor Im is a heterotetrameric protein
complex controlling alternative polyadenylation.";
Genes Cells 15:1003-1013(2010).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, 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).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-354, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 50-182 IN COMPLEX WITH
NUDT21/CPSF5, AND SUBUNIT.
Structural genomics consortium (SGC);
"Crystal structure of the complex between the 25 kDA subunit and the
59 kDA subunit (RRM domain) of human cleavage factor Im.";
Submitted (JUL-2010) to the PDB data bank.
-!- FUNCTION: Component of the cleavage factor Im complex (CFIm) that
plays a key role in pre-mRNA 3'-processing. Binds to cleavage and
polyadenylation RNA substrates. {ECO:0000269|PubMed:8626397}.
-!- SUBUNIT: Component of the cleavage factor Im (CFIm) complex,
composed of, at least, NUDT21/CPSF5 and CPSF6 or CPSF7. Within the
cleavage factor Im complex, the NUDT21/CPSF5 homodimer is at the
core of a heterotetramer, and is clasped by two additional
subunits (CPSF6 or CPSF7). Interacts with NUDT21/CPSF5.
{ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:8626397,
ECO:0000269|Ref.17}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-746909, EBI-717810;
Q9H6L4:ARMC7; NbExp=3; IntAct=EBI-746909, EBI-742909;
P54253:ATXN1; NbExp=2; IntAct=EBI-746909, EBI-930964;
P49760:CLK2; NbExp=3; IntAct=EBI-746909, EBI-750020;
Q7L775:EPM2AIP1; NbExp=3; IntAct=EBI-746909, EBI-6255981;
P49773:HINT1; NbExp=4; IntAct=EBI-11523759, EBI-1054330;
O43639:NCK2; NbExp=4; IntAct=EBI-746909, EBI-713635;
O43809:NUDT21; NbExp=5; IntAct=EBI-746909, EBI-355720;
Q06455-4:RUNX1T1; NbExp=3; IntAct=EBI-746909, EBI-10224192;
Q15437:SEC23B; NbExp=3; IntAct=EBI-746909, EBI-742673;
P84022:SMAD3; NbExp=3; IntAct=EBI-11523759, EBI-347161;
Q9BV90:SNRNP25; NbExp=3; IntAct=EBI-746909, EBI-9675976;
P26368:U2AF2; NbExp=2; IntAct=EBI-746909, EBI-742339;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20695905}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N684-1; Sequence=Displayed;
Name=2;
IsoId=Q8N684-2; Sequence=VSP_017194;
Name=3;
IsoId=Q8N684-3; Sequence=VSP_038975;
-!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH18135.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14118.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD97884.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ275970; CAC81661.1; -; mRNA.
EMBL; AK022591; BAB14118.1; ALT_INIT; mRNA.
EMBL; AK096343; BAG53266.1; -; mRNA.
EMBL; AL512759; CAC21678.1; -; mRNA.
EMBL; BX537888; CAD97884.1; ALT_INIT; mRNA.
EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC018135; AAH18135.1; ALT_INIT; mRNA.
CCDS; CCDS44619.1; -. [Q8N684-1]
CCDS; CCDS44620.1; -. [Q8N684-2]
CCDS; CCDS8006.2; -. [Q8N684-3]
RefSeq; NP_001129512.1; NM_001136040.2. [Q8N684-1]
RefSeq; NP_001136037.1; NM_001142565.1. [Q8N684-2]
RefSeq; NP_079087.3; NM_024811.3. [Q8N684-3]
RefSeq; XP_005274356.1; XM_005274299.4. [Q8N684-1]
RefSeq; XP_011543560.1; XM_011545258.2. [Q8N684-1]
RefSeq; XP_011543561.1; XM_011545259.2. [Q8N684-2]
UniGene; Hs.718984; -.
PDB; 3N9U; X-ray; 1.92 A; C/I=50-182.
PDBsum; 3N9U; -.
ProteinModelPortal; Q8N684; -.
SMR; Q8N684; -.
BioGrid; 122957; 79.
CORUM; Q8N684; -.
IntAct; Q8N684; 53.
MINT; MINT-1469392; -.
STRING; 9606.ENSP00000345412; -.
iPTMnet; Q8N684; -.
PhosphoSitePlus; Q8N684; -.
SwissPalm; Q8N684; -.
BioMuta; CPSF7; -.
DMDM; 74759932; -.
EPD; Q8N684; -.
MaxQB; Q8N684; -.
PaxDb; Q8N684; -.
PeptideAtlas; Q8N684; -.
PRIDE; Q8N684; -.
DNASU; 79869; -.
Ensembl; ENST00000340437; ENSP00000345412; ENSG00000149532. [Q8N684-3]
Ensembl; ENST00000394888; ENSP00000378352; ENSG00000149532. [Q8N684-1]
Ensembl; ENST00000439958; ENSP00000397203; ENSG00000149532. [Q8N684-2]
Ensembl; ENST00000448745; ENSP00000407394; ENSG00000149532. [Q8N684-2]
GeneID; 79869; -.
KEGG; hsa:79869; -.
UCSC; uc001nrp.4; human. [Q8N684-1]
CTD; 79869; -.
DisGeNET; 79869; -.
EuPathDB; HostDB:ENSG00000149532.15; -.
GeneCards; CPSF7; -.
HGNC; HGNC:30098; CPSF7.
HPA; HPA041094; -.
neXtProt; NX_Q8N684; -.
OpenTargets; ENSG00000149532; -.
PharmGKB; PA165543380; -.
eggNOG; KOG4849; Eukaryota.
eggNOG; ENOG4111NBM; LUCA.
GeneTree; ENSGT00730000110905; -.
HOGENOM; HOG000111137; -.
HOVERGEN; HBG056699; -.
InParanoid; Q8N684; -.
KO; K14398; -.
OMA; EDRHDDY; -.
OrthoDB; EOG091G0CVC; -.
PhylomeDB; Q8N684; -.
TreeFam; TF316430; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
ChiTaRS; CPSF7; human.
EvolutionaryTrace; Q8N684; -.
GeneWiki; FLJ12529; -.
GenomeRNAi; 79869; -.
PMAP-CutDB; Q8N684; -.
PRO; PR:Q8N684; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149532; -.
ExpressionAtlas; Q8N684; baseline and differential.
Genevisible; Q8N684; HS.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005849; C:mRNA cleavage factor complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
CDD; cd12644; RRM_CFIm59; 1.
InterPro; IPR034772; CPSF6/7.
InterPro; IPR034770; CPSF7.
InterPro; IPR034773; CPSF7_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR23204; PTHR23204; 1.
PANTHER; PTHR23204:SF2; PTHR23204:SF2; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Ubl conjugation.
CHAIN 1 471 Cleavage and polyadenylation specificity
factor subunit 7.
/FTId=PRO_0000081527.
DOMAIN 82 162 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 51 54 Poly-Pro.
COMPBIAS 218 329 Pro-rich.
COMPBIAS 418 469 Arg-rich.
MOD_RES 203 203 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BTV2}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
CROSSLNK 354 354 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MGRPESAGGGSRGPFEGGGRARRAGGIFLTLSILRT
RDLPSGAM (in isoform 3). {ECO:0000305}.
/FTId=VSP_038975.
VAR_SEQ 176 184 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017194.
CONFLICT 335 335 A -> V (in Ref. 3; CAD97884).
{ECO:0000305}.
CONFLICT 353 353 S -> F (in Ref. 3; CAD97884).
{ECO:0000305}.
CONFLICT 387 387 E -> D (in Ref. 2; BAB14118).
{ECO:0000305}.
STRAND 83 87 {ECO:0000244|PDB:3N9U}.
HELIX 95 104 {ECO:0000244|PDB:3N9U}.
STRAND 110 117 {ECO:0000244|PDB:3N9U}.
TURN 119 121 {ECO:0000244|PDB:3N9U}.
STRAND 124 133 {ECO:0000244|PDB:3N9U}.
HELIX 135 144 {ECO:0000244|PDB:3N9U}.
STRAND 156 159 {ECO:0000244|PDB:3N9U}.
HELIX 162 176 {ECO:0000244|PDB:3N9U}.
SEQUENCE 471 AA; 52050 MW; 69529E441D742CF9 CRC64;
MSEGVDLIDI YADEEFNQDP EFNNTDQIDL YDDVLTATSQ PSDDRSSSTE PPPPVRQEPS
PKPNNKTPAI LYTYSGLRNR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA
NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRECVRV
PRGGIPPRAH SRDSSDSADG RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP
PIPPPPPLSS SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
ATVGPPPDTY MKASAPYNHH GSRDSGPPPS TVSEAEFEDI MKRNRAISSS AISKAVSGAS
AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL HGIEAKSYSV GASGSSSRKR
HRSRERSPSR SRESSRRHRD LLHNEDRHDD YFQERNREHE RHRDRERDRH H


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EIAAB09115 Cleavage and polyadenylation specificity factor 30 kDa subunit,Cleavage and polyadenylation specificity factor subunit 4,CPSF 30 kDa subunit,CPSF30,CPSF4,Homo sapiens,Human,NAR,NEB1,Neb-1,No arches ho
EIAAB09116 Cleavage and polyadenylation specificity factor 30 kDa subunit,Cleavage and polyadenylation specificity factor subunit 4,Clipper homolog,Clipper_CPSF 30K,CPSF 30 kDa subunit,Cpsf30,Cpsf4,Mouse,Mus mus
EIAAB09107 Cleavage and polyadenylation specificity factor 100 kDa subunit,Cleavage and polyadenylation specificity factor subunit 2,CPSF 100 kDa subunit,CPSF100,CPSF2,Homo sapiens,Human,KIAA1367
EIAAB09109 Cleavage and polyadenylation specificity factor 100 kDa subunit,Cleavage and polyadenylation specificity factor subunit 2,CPSF 100 kDa subunit,Cpsf100,Cpsf2,Mcpsf,Mouse,Mus musculus
EIAAB09106 Cleavage and polyadenylation specificity factor 160 kDa subunit,Cleavage and polyadenylation specificity factor subunit 1,CPSF 160 kDa subunit,CPSF1,CPSF160,Homo sapiens,Human
18-003-44209 Cleavage and polyadenylation specificity factor subunit 4 - Cleavage and polyadenylation specificity factor 30 kDa subunit; CPSF 30 kDa subunit; NS1 effector domain-binding protein 1; Neb-1; No arches 0.05 mg Aff Pur
20-372-60192 cleavage and polyadenylation specific factor 4. 30kDa (CPSF4). mRNA - Mouse monoclonal anti-human CPSF4 antibody; Cleavage and polyadenylation specificity factor 30 kDa subunit; CPSF 30 kDa subunit; N 0.1 mg
EIAAB09114 Bos taurus,Bovine,Cleavage and polyadenylation specificity factor 30 kDa subunit,Cleavage and polyadenylation specificity factor subunit 4,CPSF 30 kDa subunit,CPSF30,CPSF4
EIAAB09108 Bos taurus,Bovine,Cleavage and polyadenylation specificity factor 100 kDa subunit,Cleavage and polyadenylation specificity factor subunit 2,CPSF 100 kDa subunit,CPSF100,CPSF2
EIAAB09104 Cleavage and polyadenylation specificity factor 160 kDa subunit,Cleavage and polyadenylation specificity factor subunit 1,CPSF 160 kDa subunit,Cpsf1,Cpsf160,Mouse,Mus musculus
EIAAB09105 Bos taurus,Bovine,Cleavage and polyadenylation specificity factor 160 kDa subunit,Cleavage and polyadenylation specificity factor subunit 1,CPSF 160 kDa subunit,CPSF1,CPSF160
EIAAB09120 CFIm25,CFIM25,Cleavage and polyadenylation specificity factor 25 kDa subunit,Cleavage and polyadenylation specificity factor subunit 5,CPSF 25 kDa subunit,CPSF25,CPSF5,Homo sapiens,Human,Nucleoside di
EIAAB09113 Cleavage and polyadenylation specificity factor 30 kDa subunit,Cleavage and polyadenylation specificity factor subunit 4,CPSF 30 kDa subunit,Cpsf4,Rat,Rattus norvegicus
20-372-60265 nudix (nucleoside diphosphate linked moiety X)-type motif 21 (NUDT21). mRNA - Mouse monoclonal anti-human NUDT21 antibody; Cleavage and polyadenylation specificity factor 25 kDa subunit; CPSF 25 kDa s 0.1 mg
CPSF4_RAT Rat ELISA Kit FOR Cleavage and polyadenylation specificity factor subunit 4 96T
E10076h Bovine ELISA Kit FOR Cleavage and polyadenylation specificity factor subunit 5 96T
CPSF2_MOUSE Mouse ELISA Kit FOR Cleavage and polyadenylation specificity factor subunit 2 96T


 

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