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Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3)

 PDS5B_HUMAN             Reviewed;        1447 AA.
Q9NTI5; Q5R3S3; Q5W0K8; Q6NSC3; Q8IXT6; Q9H5N8; Q9Y2I5; Q9Y451;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=Sister chromatid cohesion protein PDS5 homolog B;
AltName: Full=Androgen-induced proliferation inhibitor;
AltName: Full=Androgen-induced prostate proliferative shutoff-associated protein AS3;
Name=PDS5B;
Synonyms=APRIN, AS3 {ECO:0000312|EMBL:AAD22134.2},
KIAA0979 {ECO:0000312|EMBL:BAA76823.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
PubMed=9459187; DOI=10.1016/S0960-0760(97)00122-2;
Geck P., Szelei J., Jimenez J., Lin T.-M., Sonnenschein C., Soto A.M.;
"Expression of novel genes linked to the androgen-induced,
proliferative shutoff in prostate cancer cells.";
J. Steroid Biochem. Mol. Biol. 63:211-218(1997).
[2] {ECO:0000305, ECO:0000312|EMBL:AAD22134.2}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Prostate {ECO:0000312|EMBL:AAD22134.2};
PubMed=10215036; DOI=10.1016/S0960-0760(98)00165-4;
Geck P., Szelei J., Jimenez J., Sonnenschein C., Soto A.M.;
"Early gene expression during androgen-induced inhibition of
proliferation of prostate cancer cells: a new suppressor candidate on
chromosome 13, in the BRCA2-Rb1 locus.";
J. Steroid Biochem. Mol. Biol. 68:41-50(1999).
[3] {ECO:0000305, ECO:0000312|EMBL:BAA76823.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:BAA76823.2};
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[4]
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).
[5] {ECO:0000305, ECO:0000312|EMBL:BAB15584.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Colon {ECO:0000312|EMBL:BAB15584.1};
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).
[6] {ECO:0000312|EMBL:CAB69911.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Rhodes S., Huckle E.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000312|EMBL:CAB69911.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[8] {ECO:0000305, ECO:0000312|EMBL:AAH39256.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Prostate {ECO:0000312|EMBL:AAH70274.1}, and
Testis {ECO:0000312|EMBL:AAH39256.1};
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).
[9] {ECO:0000305}
FUNCTION.
PubMed=10963680; DOI=10.1073/pnas.97.18.10185;
Geck P., Maffini M.V., Szelei J., Sonnenschein C., Soto A.M.;
"Androgen-induced proliferative quiescence in prostate cancer cells:
the role of AS3 as its mediator.";
Proc. Natl. Acad. Sci. U.S.A. 97:10185-10190(2000).
[10] {ECO:0000305}
FUNCTION, AND INTERACTION WITH COHESIN COMPLEX.
PubMed=15855230; DOI=10.1242/jcs.02355;
Losada A., Yokochi T., Hirano T.;
"Functional contribution of Pds5 to cohesin-mediated cohesion in human
cells and Xenopus egg extracts.";
J. Cell Sci. 118:2133-2141(2005).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358 AND THR-1370, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1367, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182; SER-1283 AND
SER-1358, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1334, 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).
[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]
FUNCTION, AND INTERACTION WITH WAPL AND RAD21.
PubMed=19696148; DOI=10.1101/gad.1844309;
Shintomi K., Hirano T.;
"Releasing cohesin from chromosome arms in early mitosis: opposing
actions of Wapl-Pds5 and Sgo1.";
Genes Dev. 23:2224-2236(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1162; SER-1166;
SER-1176; SER-1182; SER-1191; SER-1257; SER-1283; SER-1358 AND
THR-1370, 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]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1136, 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).
[21]
INTERACTION WITH WAPL AND CDCA5.
PubMed=21111234; DOI=10.1016/j.cell.2010.10.031;
Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A.,
Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K.,
Peters J.M.;
"Sororin mediates sister chromatid cohesion by antagonizing wapl.";
Cell 143:737-749(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1182; SER-1283
AND SER-1358, 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).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1182;
SER-1283; SER-1358; THR-1381 AND SER-1383, 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140; SER-1166;
SER-1176; SER-1182; THR-1255; SER-1257; SER-1259; SER-1283; SER-1319;
SER-1358 AND THR-1370, 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166, 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).
-!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which
may stabilize cohesin complex association with chromatin. May
couple sister chromatid cohesion during mitosis to DNA
replication. Cohesion ensures that chromosome partitioning is
accurate in both meiotic and mitotic cells and plays an important
role in DNA repair. Plays a role in androgen-induced proliferative
arrest in prostate cells. {ECO:0000269|PubMed:10963680,
ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19696148}.
-!- SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21;
the interaction is direct. Interacts with WAPL (via FGF motifs) or
CDCA5 (via the FGF motif); the interaction is direct, cohesin-
dependent and competitive (Probable).
{ECO:0000305|PubMed:15855230, ECO:0000305|PubMed:19696148,
ECO:0000305|PubMed:21111234}.
-!- INTERACTION:
P51587:BRCA2; NbExp=26; IntAct=EBI-1175604, EBI-79792;
O60216:RAD21; NbExp=4; IntAct=EBI-1175604, EBI-80739;
Q9UQE7:SMC3; NbExp=7; IntAct=EBI-1175604, EBI-80718;
Q8WVM7:STAG1; NbExp=3; IntAct=EBI-1175604, EBI-1175097;
Q8N3U4:STAG2; NbExp=3; IntAct=EBI-1175604, EBI-1057252;
Q7Z5K2:WAPL; NbExp=9; IntAct=EBI-1175604, EBI-1022242;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:10231032};
IsoId=Q9NTI5-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:10215036};
IsoId=Q9NTI5-2; Sequence=VSP_052402;
Name=3 {ECO:0000269|PubMed:15489334};
IsoId=Q9NTI5-3; Sequence=VSP_052399, VSP_052400;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000269|PubMed:15489334};
IsoId=Q9NTI5-4; Sequence=VSP_052397, VSP_052398;
Note=No experimental confirmation available. {ECO:0000305};
Name=5 {ECO:0000269|PubMed:14702039};
IsoId=Q9NTI5-5; Sequence=VSP_052396, VSP_052401;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9459187}.
-!- INDUCTION: By the synthetic androgen R1881 in prostate carcinoma
cells undergoing proliferative arrest. Maximum levels occur 18-20
hours after androgen exposure. {ECO:0000269|PubMed:9459187}.
-!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA76823.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U95825; AAD22134.2; -; mRNA.
EMBL; AB023196; BAA76823.2; ALT_INIT; mRNA.
EMBL; AK026889; BAB15584.1; -; mRNA.
EMBL; AL137201; CAB69911.1; -; mRNA.
EMBL; AL138820; CAH73160.2; -; Genomic_DNA.
EMBL; Z75889; CAH73160.2; JOINED; Genomic_DNA.
EMBL; Z75889; CAI10806.2; -; Genomic_DNA.
EMBL; AL138820; CAI10806.2; JOINED; Genomic_DNA.
EMBL; BC039256; AAH39256.1; -; mRNA.
EMBL; BC070274; AAH70274.1; -; mRNA.
CCDS; CCDS41878.1; -. [Q9NTI5-1]
RefSeq; NP_055847.1; NM_015032.3. [Q9NTI5-1]
RefSeq; XP_016875939.1; XM_017020450.1. [Q9NTI5-1]
UniGene; Hs.744901; -.
PDB; 5HDT; X-ray; 2.71 A; A/B=21-1120.
PDBsum; 5HDT; -.
ProteinModelPortal; Q9NTI5; -.
SMR; Q9NTI5; -.
BioGrid; 116685; 61.
CORUM; Q9NTI5; -.
DIP; DIP-35420N; -.
IntAct; Q9NTI5; 24.
MINT; MINT-3073997; -.
STRING; 9606.ENSP00000313851; -.
iPTMnet; Q9NTI5; -.
PhosphoSitePlus; Q9NTI5; -.
BioMuta; PDS5B; -.
DMDM; 74725312; -.
EPD; Q9NTI5; -.
MaxQB; Q9NTI5; -.
PaxDb; Q9NTI5; -.
PeptideAtlas; Q9NTI5; -.
PRIDE; Q9NTI5; -.
DNASU; 23047; -.
Ensembl; ENST00000315596; ENSP00000313851; ENSG00000083642. [Q9NTI5-1]
Ensembl; ENST00000450460; ENSP00000401619; ENSG00000083642. [Q9NTI5-2]
GeneID; 23047; -.
KEGG; hsa:23047; -.
UCSC; uc010abf.4; human. [Q9NTI5-1]
CTD; 23047; -.
DisGeNET; 23047; -.
EuPathDB; HostDB:ENSG00000083642.18; -.
GeneCards; PDS5B; -.
HGNC; HGNC:20418; PDS5B.
HPA; HPA039513; -.
HPA; HPA040015; -.
MIM; 605333; gene.
neXtProt; NX_Q9NTI5; -.
OpenTargets; ENSG00000083642; -.
PharmGKB; PA162399098; -.
eggNOG; KOG1525; Eukaryota.
eggNOG; ENOG410XQW7; LUCA.
GeneTree; ENSGT00390000012488; -.
HOVERGEN; HBG108241; -.
InParanoid; Q9NTI5; -.
KO; K11267; -.
OMA; YVFSAHF; -.
OrthoDB; EOG091G00ZG; -.
PhylomeDB; Q9NTI5; -.
TreeFam; TF106415; -.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
ChiTaRS; PDS5B; human.
GeneWiki; PDS5B; -.
GenomeRNAi; 23047; -.
PRO; PR:Q9NTI5; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000083642; -.
CleanEx; HS_PDS5B; -.
ExpressionAtlas; Q9NTI5; baseline and differential.
Genevisible; Q9NTI5; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; TAS:Reactome.
GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
SUPFAM; SSF48371; SSF48371; 5.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Complete proteome; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1447 Sister chromatid cohesion protein PDS5
homolog B.
/FTId=PRO_0000287424.
REPEAT 383 419 HEAT. {ECO:0000255}.
DNA_BIND 1249 1261 A.T hook 1. {ECO:0000255}.
DNA_BIND 1287 1299 A.T hook 2. {ECO:0000255}.
DNA_BIND 1372 1384 A.T hook 3. {ECO:0000255}.
MOD_RES 1136 1136 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1140 1140 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1162 1162 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1176 1176 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1182 1182 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1191 1191 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1255 1255 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1319 1319 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1334 1334 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1358 1358 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1366 1366 Phosphoserine.
{ECO:0000250|UniProtKB:Q4VA53}.
MOD_RES 1367 1367 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1369 1369 Phosphoserine.
{ECO:0000250|UniProtKB:Q4VA53}.
MOD_RES 1370 1370 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1381 1381 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1383 1383 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1417 1417 Phosphoserine.
{ECO:0000250|UniProtKB:Q4VA53}.
VAR_SEQ 1 1230 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_052396.
VAR_SEQ 105 122 DIFMFITRQLKGLEDTKS -> ASTDLNNSKIDRYFDLSF
(in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052397.
VAR_SEQ 123 1447 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052398.
VAR_SEQ 491 529 ALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKV
-> YVSNIKFCSFHPLQYIGFYGKETTNTCILKCNLCSVNI
V (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052399.
VAR_SEQ 530 1447 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052400.
VAR_SEQ 1356 1447 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_052401.
VAR_SEQ 1392 1447 Missing (in isoform 2).
{ECO:0000303|PubMed:10215036}.
/FTId=VSP_052402.
CONFLICT 256 256 F -> S (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 326 326 H -> N (in Ref. 8; AAH39256).
{ECO:0000305}.
CONFLICT 394 394 R -> G (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 535 535 N -> S (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 742 742 T -> A (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1115 1115 E -> G (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1156 1156 S -> G (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1197 1197 K -> R (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1225 1225 Q -> R (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1242 1242 K -> R (in Ref. 2; AAD22134).
{ECO:0000305}.
CONFLICT 1359 1359 P -> S (in Ref. 2; AAD22134).
{ECO:0000305}.
STRAND 24 26 {ECO:0000244|PDB:5HDT}.
HELIX 28 44 {ECO:0000244|PDB:5HDT}.
HELIX 50 63 {ECO:0000244|PDB:5HDT}.
HELIX 66 69 {ECO:0000244|PDB:5HDT}.
HELIX 74 91 {ECO:0000244|PDB:5HDT}.
HELIX 100 113 {ECO:0000244|PDB:5HDT}.
HELIX 114 118 {ECO:0000244|PDB:5HDT}.
HELIX 125 138 {ECO:0000244|PDB:5HDT}.
HELIX 140 146 {ECO:0000244|PDB:5HDT}.
HELIX 150 164 {ECO:0000244|PDB:5HDT}.
HELIX 171 186 {ECO:0000244|PDB:5HDT}.
STRAND 187 189 {ECO:0000244|PDB:5HDT}.
HELIX 193 200 {ECO:0000244|PDB:5HDT}.
HELIX 201 203 {ECO:0000244|PDB:5HDT}.
HELIX 205 210 {ECO:0000244|PDB:5HDT}.
HELIX 212 224 {ECO:0000244|PDB:5HDT}.
HELIX 226 240 {ECO:0000244|PDB:5HDT}.
HELIX 252 254 {ECO:0000244|PDB:5HDT}.
HELIX 255 265 {ECO:0000244|PDB:5HDT}.
HELIX 267 270 {ECO:0000244|PDB:5HDT}.
TURN 271 273 {ECO:0000244|PDB:5HDT}.
HELIX 274 280 {ECO:0000244|PDB:5HDT}.
HELIX 286 301 {ECO:0000244|PDB:5HDT}.
HELIX 307 310 {ECO:0000244|PDB:5HDT}.
HELIX 312 319 {ECO:0000244|PDB:5HDT}.
HELIX 320 323 {ECO:0000244|PDB:5HDT}.
HELIX 327 343 {ECO:0000244|PDB:5HDT}.
HELIX 345 350 {ECO:0000244|PDB:5HDT}.
HELIX 352 358 {ECO:0000244|PDB:5HDT}.
HELIX 364 380 {ECO:0000244|PDB:5HDT}.
HELIX 382 384 {ECO:0000244|PDB:5HDT}.
HELIX 387 396 {ECO:0000244|PDB:5HDT}.
HELIX 402 419 {ECO:0000244|PDB:5HDT}.
HELIX 427 432 {ECO:0000244|PDB:5HDT}.
TURN 433 435 {ECO:0000244|PDB:5HDT}.
HELIX 436 442 {ECO:0000244|PDB:5HDT}.
HELIX 443 445 {ECO:0000244|PDB:5HDT}.
HELIX 449 461 {ECO:0000244|PDB:5HDT}.
HELIX 470 481 {ECO:0000244|PDB:5HDT}.
HELIX 486 514 {ECO:0000244|PDB:5HDT}.
HELIX 519 533 {ECO:0000244|PDB:5HDT}.
HELIX 539 555 {ECO:0000244|PDB:5HDT}.
HELIX 557 567 {ECO:0000244|PDB:5HDT}.
HELIX 573 585 {ECO:0000244|PDB:5HDT}.
HELIX 596 608 {ECO:0000244|PDB:5HDT}.
HELIX 615 629 {ECO:0000244|PDB:5HDT}.
HELIX 634 638 {ECO:0000244|PDB:5HDT}.
HELIX 642 659 {ECO:0000244|PDB:5HDT}.
HELIX 662 664 {ECO:0000244|PDB:5HDT}.
HELIX 667 677 {ECO:0000244|PDB:5HDT}.
HELIX 682 695 {ECO:0000244|PDB:5HDT}.
HELIX 699 702 {ECO:0000244|PDB:5HDT}.
HELIX 704 720 {ECO:0000244|PDB:5HDT}.
HELIX 723 736 {ECO:0000244|PDB:5HDT}.
HELIX 740 754 {ECO:0000244|PDB:5HDT}.
HELIX 761 763 {ECO:0000244|PDB:5HDT}.
HELIX 764 776 {ECO:0000244|PDB:5HDT}.
TURN 778 781 {ECO:0000244|PDB:5HDT}.
HELIX 782 791 {ECO:0000244|PDB:5HDT}.
HELIX 794 797 {ECO:0000244|PDB:5HDT}.
HELIX 815 817 {ECO:0000244|PDB:5HDT}.
HELIX 820 839 {ECO:0000244|PDB:5HDT}.
HELIX 846 859 {ECO:0000244|PDB:5HDT}.
TURN 860 862 {ECO:0000244|PDB:5HDT}.
HELIX 872 890 {ECO:0000244|PDB:5HDT}.
HELIX 893 896 {ECO:0000244|PDB:5HDT}.
HELIX 901 908 {ECO:0000244|PDB:5HDT}.
HELIX 909 912 {ECO:0000244|PDB:5HDT}.
HELIX 916 931 {ECO:0000244|PDB:5HDT}.
HELIX 937 939 {ECO:0000244|PDB:5HDT}.
HELIX 941 948 {ECO:0000244|PDB:5HDT}.
HELIX 952 975 {ECO:0000244|PDB:5HDT}.
HELIX 980 984 {ECO:0000244|PDB:5HDT}.
HELIX 988 990 {ECO:0000244|PDB:5HDT}.
HELIX 991 1000 {ECO:0000244|PDB:5HDT}.
HELIX 1011 1028 {ECO:0000244|PDB:5HDT}.
HELIX 1036 1047 {ECO:0000244|PDB:5HDT}.
STRAND 1053 1055 {ECO:0000244|PDB:5HDT}.
HELIX 1059 1079 {ECO:0000244|PDB:5HDT}.
STRAND 1081 1085 {ECO:0000244|PDB:5HDT}.
TURN 1095 1097 {ECO:0000244|PDB:5HDT}.
SEQUENCE 1447 AA; 164667 MW; 145C30308EA3EFD5 CRC64;
MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH
DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYA
LQSAAGKDAA KQIAWIKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG
KAQDFMKKFT QVLEDDEKIR KQLEVLVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK
GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ
FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK
NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
CLVKNINVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC
LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDAK MNEKLYTVCD VAMNIIMSKS
TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTTNV LGAVNKPLSS
AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK
RDDSDLVRSE LEKPRGRKKT PVTEQEEKLG MDDLTKLVQE QKPKGSQRSR KRGHTASESD
EQQWPEEKRL KEDILENEDE QNSPPKKGKR GRPPKPLGGG TPKEEPTMKT SKKGSKKKSG
PPAPEEEEEE ERQSGNTEQK SKSKQHRVSR RAQQRAESPE SSAIESTQST PQKGRGRPSK
TPSPSQPKKN VRVGRSKQAA TKENDSSEEV DVFQGSSPVD DIPQEETEEE EVSTVNVRRR
SAKRERR


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