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182 kDa tankyrase-1-binding protein

 TB182_HUMAN             Reviewed;        1729 AA.
Q9C0C2; A7E2F8; Q6PJ35; Q6ZV74;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
27-SEP-2017, entry version 148.
RecName: Full=182 kDa tankyrase-1-binding protein;
Name=TNKS1BP1; Synonyms=KIAA1741, TAB182;
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), AND VARIANT SER-322.
TISSUE=Placenta, and Testis;
PubMed=11854288; DOI=10.1074/jbc.M112266200;
Seimiya H., Smith S.;
"The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains
multiple binding sites for telomeric repeat binding factor 1 (TRF1)
and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182).";
J. Biol. Chem. 277:14116-14126(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
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).
[5]
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).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1729 (ISOFORM 1).
TISSUE=Spleen;
PubMed=12693554; DOI=10.1093/dnares/10.1.49;
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
Ohara O.;
"Characterization of long cDNA clones from human adult spleen. II. The
complete sequences of 81 cDNA clones.";
DNA Res. 10:49-57(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-833; SER-836;
SER-1383; SER-1385 AND SER-1666, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-695; SER-836;
SER-1103; SER-1138; SER-1620; SER-1621 AND SER-1666, 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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836; SER-1248 AND
SER-1331, AND 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-691; SER-836
AND SER-1103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-239; SER-287;
SER-429; SER-435; SER-494; SER-498; SER-601; SER-672; SER-712;
SER-744; SER-762; SER-872; SER-877; SER-893; SER-920; SER-936;
THR-979; SER-983; SER-987; SER-1008; SER-1029; SER-1103; SER-1133;
SER-1138; SER-1178; SER-1297; SER-1328; SER-1331; SER-1439; SER-1533;
SER-1545; SER-1558; THR-1563; SER-1620; SER-1621; SER-1652 AND
SER-1666, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-494; SER-691;
SER-836; SER-1620; SER-1621 AND SER-1666, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-221; SER-429;
SER-435; SER-437; SER-601; SER-672; SER-691; SER-762; SER-836;
SER-872; SER-882; SER-893; SER-987; SER-1008; SER-1024; SER-1103;
SER-1133; SER-1138; SER-1248; SER-1253; THR-1282; SER-1297; SER-1383;
SER-1385; SER-1533; SER-1620; SER-1621; SER-1652; SER-1666 AND
SER-1715, 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).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-601; SER-672;
SER-691; SER-836; SER-851; SER-872; SER-893; SER-899; SER-1054;
SER-1138; SER-1385; SER-1533; SER-1545; SER-1620; SER-1621; SER-1631
AND SER-1666, 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).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-178; SER-228;
SER-429; SER-435; SER-437; SER-494; SER-601; SER-672; SER-691;
SER-836; SER-872; SER-882; SER-893; SER-899; SER-920; SER-936;
SER-987; SER-1013; SER-1024; SER-1029; SER-1054; SER-1073; SER-1103;
SER-1138; SER-1158; THR-1282; SER-1297; SER-1383; SER-1385; SER-1533;
SER-1620; SER-1621; SER-1652; SER-1666 AND SER-1715, 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-221; SER-228;
SER-301; SER-429; SER-494; SER-498; SER-601; SER-672; SER-691;
SER-724; SER-762; SER-806; SER-836; SER-893; TYR-897; SER-976;
SER-1004; SER-1008; SER-1024; SER-1073; SER-1091; SER-1103; SER-1138;
SER-1158; THR-1282; SER-1297; SER-1435; SER-1439; SER-1450; SER-1452;
SER-1473; SER-1476; SER-1503; SER-1506; THR-1518; SER-1533; SER-1545;
SER-1620 AND SER-1621, 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).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1644, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- SUBUNIT: Binds to the ANK repeat domain of TNKS1 and TNKS2.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton.
Chromosome. Note=Colocalizes with chromosomes during mitosis, and
in the cytoplasm with cortical actin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9C0C2-1; Sequence=Displayed;
Name=2;
IsoId=Q9C0C2-2; Sequence=VSP_026000, VSP_026001, VSP_026002;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in testis, ovary, lung, skeletal
muscle, heart, prostate and pancreas, and at very low levels in
brain and peripheral blood leukocytes.
-!- PTM: ADP-ribosylated by TNKS1 (in vitro).
-!- SEQUENCE CAUTION:
Sequence=BAB21832.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB84939.1; Type=Frameshift; Positions=1070, 1098, 1466; Evidence={ECO:0000305};
Sequence=BAB84939.1; Type=Frameshift; Positions=1071, 1097, 1467; Evidence={ECO:0000305};
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EMBL; AF441771; AAM15531.1; -; mRNA.
EMBL; AB051528; BAB21832.2; ALT_INIT; mRNA.
EMBL; AK124903; BAC85989.1; -; mRNA.
EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW73731.1; -; Genomic_DNA.
EMBL; BC023622; AAH23622.1; -; mRNA.
EMBL; BC150333; AAI50334.1; -; mRNA.
EMBL; AK074113; BAB84939.1; ALT_FRAME; mRNA.
CCDS; CCDS7951.1; -. [Q9C0C2-1]
RefSeq; NP_203754.2; NM_033396.2. [Q9C0C2-1]
RefSeq; XP_006718788.1; XM_006718725.3. [Q9C0C2-1]
UniGene; Hs.530730; -.
ProteinModelPortal; Q9C0C2; -.
SMR; Q9C0C2; -.
BioGrid; 124540; 49.
ELM; Q9C0C2; -.
IntAct; Q9C0C2; 27.
MINT; MINT-4538987; -.
STRING; 9606.ENSP00000350990; -.
iPTMnet; Q9C0C2; -.
PhosphoSitePlus; Q9C0C2; -.
BioMuta; TNKS1BP1; -.
DMDM; 317373547; -.
EPD; Q9C0C2; -.
MaxQB; Q9C0C2; -.
PaxDb; Q9C0C2; -.
PeptideAtlas; Q9C0C2; -.
PRIDE; Q9C0C2; -.
Ensembl; ENST00000358252; ENSP00000350990; ENSG00000149115. [Q9C0C2-1]
Ensembl; ENST00000532437; ENSP00000437271; ENSG00000149115. [Q9C0C2-1]
GeneID; 85456; -.
KEGG; hsa:85456; -.
UCSC; uc001njr.4; human. [Q9C0C2-1]
CTD; 85456; -.
EuPathDB; HostDB:ENSG00000149115.13; -.
GeneCards; TNKS1BP1; -.
HGNC; HGNC:19081; TNKS1BP1.
HPA; HPA037929; -.
HPA; HPA037930; -.
MIM; 607104; gene.
neXtProt; NX_Q9C0C2; -.
OpenTargets; ENSG00000149115; -.
PharmGKB; PA38789; -.
eggNOG; ENOG410IK8U; Eukaryota.
eggNOG; ENOG410ZTHW; LUCA.
GeneTree; ENSGT00730000111391; -.
HOGENOM; HOG000001569; -.
HOVERGEN; HBG080593; -.
InParanoid; Q9C0C2; -.
OMA; FEWTFPT; -.
OrthoDB; EOG091G01HQ; -.
PhylomeDB; Q9C0C2; -.
TreeFam; TF336029; -.
Reactome; R-HSA-429947; Deadenylation of mRNA.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
ChiTaRS; TNKS1BP1; human.
GeneWiki; TNKS1BP1; -.
GenomeRNAi; 85456; -.
PRO; PR:Q9C0C2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149115; -.
CleanEx; HS_TNKS1BP1; -.
ExpressionAtlas; Q9C0C2; baseline and differential.
Genevisible; Q9C0C2; HS.
GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071532; F:ankyrin repeat binding; IMP:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
GO; GO:0044877; F:macromolecular complex binding; IPI:BHF-UCL.
GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IMP:BHF-UCL.
GO; GO:0007004; P:telomere maintenance via telomerase; NAS:UniProtKB.
InterPro; IPR032764; Tankyrase-bd_C.
Pfam; PF15327; Tankyrase_bdg_C; 1.
SMART; SM01319; Tankyrase_bdg_C; 1.
1: Evidence at protein level;
ADP-ribosylation; Alternative splicing; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 1729 182 kDa tankyrase-1-binding protein.
/FTId=PRO_0000072437.
REGION 210 1572 Acidic.
REGION 1450 1542 Tankyrase-binding.
MOTIF 1629 1635 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1723 1729 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 2 103 Arg/Glu/Lys/Pro-rich (charged).
COMPBIAS 127 767 Pro-rich.
COMPBIAS 1010 1340 Gly-rich.
COMPBIAS 1572 1729 Arg/Glu/Lys-rich (charged).
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 131 131 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 239 239 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000250|UniProtKB:P58871}.
MOD_RES 601 601 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 712 712 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 833 833 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 836 836 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 851 851 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 872 872 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 877 877 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 897 897 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 899 899 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 976 976 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 979 979 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1004 1004 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1008 1008 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1013 1013 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1024 1024 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1054 1054 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1073 1073 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1103 1103 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1138 1138 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1178 1178 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1248 1248 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1282 1282 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1331 1331 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648}.
MOD_RES 1383 1383 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1385 1385 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1435 1435 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1439 1439 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 1450 1450 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1473 1473 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1476 1476 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1503 1503 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1506 1506 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1518 1518 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1533 1533 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1545 1545 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1558 1558 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1563 1563 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1620 1620 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1621 1621 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1631 1631 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1644 1644 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1652 1652 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1666 1666 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1715 1715 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 549 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_026000.
VAR_SEQ 1275 1327 GVGQADWTPDLGLRNMAPGAVCSPGESKELGVGQMDWGNNL
GLRDLEVTCDPD -> LGRHIYALCITLRTPPTPSLPWISS
LVVEGFVPSSPPSLSLSASSSSLPWVFF (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_026001.
VAR_SEQ 1328 1729 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_026002.
VARIANT 322 322 T -> S (in dbSNP:rs4939134).
{ECO:0000269|PubMed:11854288}.
/FTId=VAR_028141.
VARIANT 714 714 S -> N (in dbSNP:rs34203865).
/FTId=VAR_032615.
CONFLICT 84 84 L -> P (in Ref. 1; AAM15531).
{ECO:0000305}.
CONFLICT 388 388 P -> S (in Ref. 1; AAM15531).
{ECO:0000305}.
CONFLICT 554 554 Q -> H (in Ref. 7; BAB84939).
{ECO:0000305}.
CONFLICT 604 604 P -> S (in Ref. 1; AAM15531).
{ECO:0000305}.
CONFLICT 1450 1450 S -> F (in Ref. 1; AAM15531).
{ECO:0000305}.
SEQUENCE 1729 AA; 181796 MW; 561FA5C27C923036 CRC64;
MKVSTLRESS AMASPLPREM EEELVPTGSE PGDTRAKPPV KPKPRALPAK PALPAKPSLL
VPVGPRPPRG PLAELPSARK MNMLAGPQPY GGSKRPLPFA PRPAVEASTG GEATQETGKE
EAGKEEPPPL TPPARCAAPG GVRKAPAPFR PASERFAATT VEEILAKMEQ PRKEVLASPD
RLWGSRLTFN HDGSSRYGPR TYGTTTAPRD EDGSTLFRGW SQEGPVKSPA ECREEHSKTP
EERSLPSDLA FNGDLAKAAS SELPADISKP WIPSSPAPSS ENGGPASPGL PAEASGSGPG
SPHLHPPDKS SPCHSQLLEA QTPEASQASP CPAVTPSAPS AALPDEGSRH TPSPGLPAEG
APEAPRPSSP PPEVLEPHSL DQPPATSPRP LIEVGELLDL TRTFPSGGEE EAKGDAHLRP
TSLVQRRFSE GVLQSPSQDQ EKLGGSLAAL PQGQGSQLAL DRPFGAESNW SLSQSFEWTF
PTRPSGLGVW RLDSPPPSPI TEASEAAEAA EAGNLAVSSR EEGVSQQGQG AGSAPSGSGS
SWVQGDDPSM SLTQKGDGES QPQFPAVPLE PLPTTEGTPG LPLQQAEERY ESQEPLAGQE
SPLPLATREA ALPILEPVLG QEQPAAPDQP CVLFADAPEP GQALPVEEEA VTLARAETTQ
ARTEAQDLCR ASPEPPGPES SSRWLDDLLA SPPPSGGGAR RGAGAELKDT QSPSTCSEGL
LGWSQKDLQS EFGITGDPQP SSFSPSSWCQ GASQDYGLGG ASPRGDPGLG ERDWTSKYGQ
GAGEGSTREW ASRCGIGQEE MEASSSQDQS KVSAPGVLTA QDRVVGKPAQ LGTQRSQEAD
VQDWEFRKRD SQGTYSSRDA ELQDQEFGKR DSLGTYSSRD VSLGDWEFGK RDSLGAYASQ
DANEQGQDLG KRDHHGRYSS QDADEQDWEF QKRDVSLGTY GSRAAEPQEQ EFGKSAWIRD
YSSGGSSRTL DAQDRSFGTR PLSSGFSPEE AQQQDEEFEK KIPSVEDSLG EGSRDAGRPG
ERGSGGLFSP STAHVPDGAL GQRDQSSWQN SDASQEVGGH QERQQAGAQG PGSADLEDGE
MGKRGWVGEF SLSVGPQREA AFSPGQQDWS RDFCIEASER SYQFGIIGND RVSGAGFSPS
SKMEGGHFVP PGKTTAGSVD WTDQLGLRNL EVSSCVGSGG SSEARESAVG QMGWSGGLSL
RDMNLTGCLE SGGSEEPGGI GVGEKDWTSD VNVKSKDLAE VGEGGGHSQA RESGVGQTDW
SGVEAGEFLK SRERGVGQAD WTPDLGLRNM APGAVCSPGE SKELGVGQMD WGNNLGLRDL
EVTCDPDSGG SQGLRGCGVG QMDWTQDLAP QNVELFGAPS EAREHGVGGV SQCPEPGLRH
NGSLSPGLEA RDPLEARELG VGETSGPETQ GEDYSSSSLE PHPADPGMET GEALSFGASP
GRCPARPPPS GSQGLLEEML AASSSKAVAR RESAASGLGG LLEEEGAGAG AAQEEVLEPG
RDSPPSWRPQ PDGEASQTED VDGTWGSSAA RWSDQGPAQT SRRPSQGPPA RSPSQDFSFI
EDTEILDSAM YRSRANLGRK RGHRAPVIRP GGTLGLSEAA DSDAHLFQDS TEPRASRVPS
SDEEVVEEPQ SRRTRMSLGT KGLKVNLFPG LSPSALKAKL RPRNRSAEEG ELAESKSSQK
ESAVQRSKSC KVPGLGKPLT LPPKPEKSSG SEGSSPNWLQ ALKLKKKKV


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