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DNA damage-binding protein 1 (DDB p127 subunit) (Damage-specific DNA-binding protein 1) (UV-damaged DNA-binding factor)

 DDB1_MOUSE              Reviewed;        1140 AA.
Q3U1J4; Q3U4D0; Q3U8G3; Q3UJC4; Q99LV3; Q9QYK0; Q9WV39;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
27-SEP-2017, entry version 112.
RecName: Full=DNA damage-binding protein 1;
AltName: Full=DDB p127 subunit;
AltName: Full=Damage-specific DNA-binding protein 1;
AltName: Full=UV-damaged DNA-binding factor;
Name=Ddb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Fetal brain;
PubMed=10574459; DOI=10.1093/dnares/6.5.319;
Seki N., Hayashi A., Hattori A., Kozuma S., Sasaki M., Suzuki Y.,
Sugano S., Muramatsu M., Saito T.;
"cDNA cloning, tissue expression, and chromosomal assignment of a
mouse gene, encoding a 127 kDa UV-damaged DNA binding protein which is
defective in XPE cells.";
DNA Res. 6:319-322(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
Zhang L., Sabatinos S.A., Richardson C.D.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Bone marrow, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH DDB2, AND PHOSPHORYLATION.
PubMed=12107171; DOI=10.1074/jbc.M204416200;
Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.;
"Interaction between UV-damaged DNA binding activity proteins and the
c-Abl tyrosine kinase.";
J. Biol. Chem. 277:34870-34878(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-
damaged DNA-binding protein complex (the UV-DDB complex). The UV-
DDB complex may recognize UV-induced DNA damage and recruit
proteins of the nucleotide excision repair pathway (the NER
pathway) to initiate DNA repair. The UV-DDB complex preferentially
binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts
(6-4 PP), apurinic sites and short mismatches. Also appears to
function as a component of numerous distinct DCX (DDB1-CUL4-X-box)
E3 ubiquitin-protein ligase complexes which mediate the
ubiquitination and subsequent proteasomal degradation of target
proteins. The functional specificity of the DCX E3 ubiquitin-
protein ligase complex is determined by the variable substrate
recognition component recruited by DDB1. DCX(DDB2) (also known as
DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate
histone H2A, histone H3 and histone H4 at sites of UV-induced DNA
damage. The ubiquitination of histones may facilitate their
removal from the nucleosome and promote subsequent DNA repair.
DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by
XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent
polyubiquitination of CDT1 and MDM2-dependent ubiquitination of
TP53 in response to radiation-induced DNA damage and during DNA
replication. DCX(ERCC8) (the CSA complex) plays a role in
transcription-coupled repair (TCR). May also play a role in
ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2
(By similarity). {ECO:0000250, ECO:0000269|PubMed:12107171}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
DDB2; the heterodimer dimerizes to give rise to a heterotetramer
when bound to damaged DNA. The UV-DDB complex interacts with
monoubiquitinated histone H2A and binds to XPC via the DDB2
subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-
protein ligase complexes which consist of a core of DDB1, CUL4A or
CUL4B and RBX1. DDB1 may recruit specific substrate targeting
subunits to the DCX complex. These substrate targeting subunits
are generally known as DCAF (DDB1- and CUL4-associated factor) or
CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with
AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4, DCAF5, DCAF6, DCAF7,
DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15, DCAF16, DCAF17,
DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, KATNB1, NLE1, NUP43,
PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, DCAF1,
WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42, WDR53, WDR59, WDR61,
WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the
COP9 signalosome, and this inhibits the E3 ubiquitin-protein
ligase activity of the complex. Interacts with NF2, TSC1 and TSC2.
Interacts with AGO1 and AGO2. Associates with the E3 ligase
complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP
complex). Interacts directly with DYRK2 (By similarity). Interacts
with TRPC4AP (By similarity). {ECO:0000250|UniProtKB:Q16531}.
-!- INTERACTION:
Q923J1:Trpm7; NbExp=2; IntAct=EBI-2552275, EBI-8010314;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Primarily cytoplasmic. Translocates to the
nucleus following UV irradiation and subsequently accumulates at
sites of DNA damage (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pregnant,
lactating and involuting mammary gland.
{ECO:0000269|PubMed:10574459}.
-!- DEVELOPMENTAL STAGE: Ubiquitously expressed at E8.5, E9.5, E12.5,
and E19.5. {ECO:0000269|PubMed:10574459}.
-!- DOMAIN: The core of the protein consists of three WD40 beta-
propeller domains. {ECO:0000250}.
-!- PTM: Phosphorylated by ABL1. {ECO:0000269|PubMed:12107171}.
-!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
dependent proteolysis (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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EMBL; AB026432; BAA84699.1; -; mRNA.
EMBL; AF159853; AAD42230.1; -; mRNA.
EMBL; AK146522; BAE27231.1; -; mRNA.
EMBL; AK152228; BAE31055.1; -; mRNA.
EMBL; AK154303; BAE32502.1; -; mRNA.
EMBL; AK155020; BAE32993.1; -; mRNA.
EMBL; AK155920; BAE33503.1; -; mRNA.
EMBL; AK157491; BAE34102.1; -; mRNA.
EMBL; BC002210; AAH02210.1; -; mRNA.
EMBL; BC009661; AAH09661.1; -; mRNA.
CCDS; CCDS37915.1; -.
PIR; JC7152; JC7152.
RefSeq; NP_056550.1; NM_015735.1.
UniGene; Mm.289915; -.
UniGene; Mm.466856; -.
ProteinModelPortal; Q3U1J4; -.
SMR; Q3U1J4; -.
BioGrid; 199074; 59.
DIP; DIP-56812N; -.
IntAct; Q3U1J4; 63.
MINT; MINT-4131128; -.
STRING; 10090.ENSMUSP00000025649; -.
iPTMnet; Q3U1J4; -.
PhosphoSitePlus; Q3U1J4; -.
SwissPalm; Q3U1J4; -.
EPD; Q3U1J4; -.
MaxQB; Q3U1J4; -.
PaxDb; Q3U1J4; -.
PeptideAtlas; Q3U1J4; -.
PRIDE; Q3U1J4; -.
Ensembl; ENSMUST00000025649; ENSMUSP00000025649; ENSMUSG00000024740.
GeneID; 13194; -.
KEGG; mmu:13194; -.
UCSC; uc008gqm.1; mouse.
CTD; 1642; -.
MGI; MGI:1202384; Ddb1.
eggNOG; KOG1897; Eukaryota.
eggNOG; ENOG410XPF6; LUCA.
GeneTree; ENSGT00530000063396; -.
HOVERGEN; HBG005460; -.
InParanoid; Q3U1J4; -.
KO; K10610; -.
OMA; GIGIQEH; -.
OrthoDB; EOG091G017I; -.
PhylomeDB; Q3U1J4; -.
TreeFam; TF105840; -.
Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-MMU-5696400; Dual Incision in GG-NER.
Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-MMU-6782135; Dual incision in TC-NER.
Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-MMU-8951664; Neddylation.
UniPathway; UPA00143; -.
ChiTaRS; Ddb1; mouse.
PRO; PR:Q3U1J4; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024740; -.
CleanEx; MM_DDB1; -.
Genevisible; Q3U1J4; MM.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0097602; F:cullin family protein binding; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
GO; GO:0051702; P:interaction with symbiont; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
GO; GO:1902188; P:positive regulation of viral release from host cell; ISO:MGI.
GO; GO:0010498; P:proteasomal protein catabolic process; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
InterPro; IPR031297; DDB1.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
PANTHER; PTHR10644:SF11; PTHR10644:SF11; 1.
Pfam; PF03178; CPSF_A; 1.
SUPFAM; SSF50998; SSF50998; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; DNA damage; DNA repair;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q16531}.
CHAIN 2 1140 DNA damage-binding protein 1.
/FTId=PRO_0000281036.
REGION 2 768 Interaction with CDT1. {ECO:0000250}.
REGION 13 356 WD repeat beta-propeller A.
{ECO:0000250}.
REGION 391 708 WD repeat beta-propeller B; Interaction
with CUL4A. {ECO:0000250}.
REGION 709 1043 WD repeat beta-propeller C.
{ECO:0000250}.
REGION 771 1140 Interaction with CDT1 and CUL4A.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q16531}.
MOD_RES 1067 1067 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16531}.
MOD_RES 1125 1125 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESW0}.
CROSSLNK 1121 1121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q16531}.
CONFLICT 40 40 E -> K (in Ref. 2; AAD42230).
{ECO:0000305}.
CONFLICT 297 297 L -> P (in Ref. 2; AAD42230).
{ECO:0000305}.
CONFLICT 600 600 H -> R (in Ref. 2; AAD42230).
{ECO:0000305}.
CONFLICT 601 601 Y -> C (in Ref. 3; BAE32502).
{ECO:0000305}.
CONFLICT 689 689 D -> N (in Ref. 3; BAE27231).
{ECO:0000305}.
CONFLICT 715 715 V -> D (in Ref. 3; BAE32502).
{ECO:0000305}.
CONFLICT 795 795 D -> G (in Ref. 3; BAE32502).
{ECO:0000305}.
CONFLICT 845 845 Q -> L (in Ref. 3; BAE32502).
{ECO:0000305}.
CONFLICT 979 979 K -> R (in Ref. 3; BAE33503).
{ECO:0000305}.
SEQUENCE 1140 AA; 126853 MW; 9799298D52E60AE4 CRC64;
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI
IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPGRE
TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
QEPKALVSEW KEPQGKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC
LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
PRKICYQEVS QCFGVLSSRI EVQDSSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGEA
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH


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Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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

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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
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IBAN lautet DE8839050000107569353
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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
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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