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CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)

 CLAP1_HUMAN             Reviewed;        1538 AA.
Q7Z460; A2RU21; B7ZLX3; F5GWS0; O75118; Q2KHQ9; Q5H9P0; Q8N5B8;
Q9BQT5;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=CLIP-associating protein 1;
AltName: Full=Cytoplasmic linker-associated protein 1;
AltName: Full=Multiple asters homolog 1;
AltName: Full=Protein Orbit homolog 1;
Short=hOrbit1;
Name=CLASP1; Synonyms=KIAA0622, MAST1;
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).
Maiato H., Sunkel C.E., Earnshaw W.C.;
"Full length cDNA of a human homologue of Drosophila melanogaster
multiple asters (MAST) gene.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2).
TISSUE=Eye;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-266, FUNCTION, SUBCELLULAR LOCATION,
ALTERNATIVE SPLICING, AND INTERACTION WITH CLIP2; MICROTUBULES AND
RSN.
TISSUE=Brain;
PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
Galjart N.;
"Clasps are CLIP-115 and -170 associating proteins involved in the
regional regulation of microtubule dynamics in motile fibroblasts.";
Cell 104:923-935(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3).
TISSUE=Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-1538.
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12837247; DOI=10.1016/S0092-8674(03)00465-3;
Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E.,
Earnshaw W.C.;
"Human CLASP1 is an outer kinetochore component that regulates spindle
microtubule dynamics.";
Cell 113:891-904(2003).
[8]
INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=16145243; DOI=10.1247/csf.30.7;
Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N.,
Matsukage A.;
"Microtubule bundle formation and cell death induced by the human
CLASP/Orbit N-terminal fragment.";
Cell Struct. Funct. 30:7-13(2005).
[9]
FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, AND
SUBCELLULAR LOCATION.
PubMed=15631994; DOI=10.1083/jcb.200405094;
Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S.,
Akhmanova A.;
"CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end
dynamics at the cell cortex.";
J. Cell Biol. 168:141-153(2005).
[10]
INTERACTION WITH ERC1 AND PHLDB2, AND SUBCELLULAR LOCATION.
PubMed=16824950; DOI=10.1016/j.devcel.2006.05.012;
Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S.,
Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F.,
Akhmanova A.;
"CLASPs attach microtubule plus ends to the cell cortex through a
complex with LL5beta.";
Dev. Cell 11:21-32(2006).
[11]
FUNCTION.
PubMed=16866869; DOI=10.1111/j.1365-2443.2006.00990.x;
Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A.,
Tsukita S., Vorobjev I.;
"Mammalian CLASPs are required for mitotic spindle organization and
kinetochore alignment.";
Genes Cells 11:845-857(2006).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16914514; DOI=10.1091/mbc.E06-07-0579;
Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
"Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
regulating spindle and kinetochore function.";
Mol. Biol. Cell 17:4526-4542(2006).
[13]
FUNCTION, INTERACTION WITH GCC2, AND SUBCELLULAR LOCATION.
PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
"Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules
at the trans-Golgi network.";
Dev. Cell 12:917-930(2007).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-649;
THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099,
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-688;
SER-797 AND SER-1091, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646 AND SER-1223, 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).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646 AND
SER-684, 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-545; SER-558;
SER-559; SER-568; SER-600; SER-636; SER-646; SER-647; SER-649;
SER-695; SER-705; SER-787; SER-797; SER-823; SER-1091 AND SER-1196,
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).
[23]
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: Microtubule plus-end tracking protein that promotes the
stabilization of dynamic microtubules. Involved in the nucleation
of noncentrosomal microtubules originating from the trans-Golgi
network (TGN). Required for the polarization of the cytoplasmic
microtubule arrays in migrating cells towards the leading edge of
the cell. May act at the cell cortex to enhance the frequency of
rescue of depolymerizing microtubules by attaching their plus-ends
to cortical platforms composed of ERC1 and PHLDB2. This cortical
microtubule stabilizing activity is regulated at least in part by
phosphatidylinositol 3-kinase signaling. Also performs a similar
stabilizing function at the kinetochore which is essential for the
bipolar alignment of chromosomes on the mitotic spindle.
{ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:12837247,
ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16866869,
ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864}.
-!- SUBUNIT: Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules,
PHLDB2 and RSN. The interaction with ERC1 may be mediated by
PHLDB2. Interacts with GCC2; recruits CLASP1 to Golgi membranes.
Interacts with MACF1 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9JK25:Clip1 (xeno); NbExp=2; IntAct=EBI-913476, EBI-908338;
O55156:Clip2 (xeno); NbExp=3; IntAct=EBI-913476, EBI-349416;
Q96AA8:JAKMIP2; NbExp=3; IntAct=EBI-10257534, EBI-752007;
O60333:KIF1B; NbExp=3; IntAct=EBI-913476, EBI-465633;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-913476, EBI-413317;
P61981:YWHAG; NbExp=2; IntAct=EBI-913476, EBI-359832;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
spindle. Golgi apparatus, trans-Golgi network {ECO:0000305}.
Note=Localizes to microtubule plus ends. Localizes to centrosomes,
kinetochores and the mitotic spindle from prometaphase.
Subsequently localizes to the spindle midzone from anaphase and to
the midbody from telophase. In migrating cells localizes to the
plus ends of microtubules within the cell body and to the entire
microtubule lattice within the lamella. Localizes to the cell
cortex and this requires ERC1 and PHLDB2.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q7Z460-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z460-2; Sequence=VSP_022386, VSP_022387, VSP_022389;
Name=3;
IsoId=Q7Z460-3; Sequence=VSP_022386, VSP_022387, VSP_022388,
VSP_022389;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q7Z460-4; Sequence=VSP_054412, VSP_054413, VSP_022386,
VSP_054414, VSP_022389;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q7Z460-5; Sequence=VSP_057272, VSP_022386, VSP_022387,
VSP_022389;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH32563.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAX88872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF347693; AAQ15051.1; -; mRNA.
EMBL; AC012447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC013399; AAX88872.1; ALT_SEQ; Genomic_DNA.
EMBL; AC018737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032563; AAH32563.1; ALT_INIT; mRNA.
EMBL; BC112940; AAI12941.1; -; mRNA.
EMBL; BC132723; AAI32724.1; -; mRNA.
EMBL; BC144107; AAI44108.1; -; mRNA.
EMBL; AJ288057; CAC35156.1; -; mRNA.
EMBL; CR933722; CAI46251.1; -; mRNA.
EMBL; AB014522; BAA31597.1; -; mRNA.
PIR; T00387; T00387.
RefSeq; NP_001135745.1; NM_001142273.1. [Q7Z460-5]
RefSeq; NP_001135746.1; NM_001142274.1. [Q7Z460-2]
RefSeq; NP_001193980.1; NM_001207051.1. [Q7Z460-4]
RefSeq; NP_056097.1; NM_015282.2. [Q7Z460-1]
RefSeq; XP_011509150.1; XM_011510848.1. [Q7Z460-3]
UniGene; Hs.469840; -.
UniGene; Hs.708183; -.
PDB; 4K92; X-ray; 2.00 A; A/B=284-552.
PDBsum; 4K92; -.
ProteinModelPortal; Q7Z460; -.
SMR; Q7Z460; -.
BioGrid; 116919; 35.
IntAct; Q7Z460; 40.
MINT; MINT-1683081; -.
STRING; 9606.ENSP00000263710; -.
iPTMnet; Q7Z460; -.
PhosphoSitePlus; Q7Z460; -.
SwissPalm; Q7Z460; -.
BioMuta; CLASP1; -.
DMDM; 74723323; -.
EPD; Q7Z460; -.
MaxQB; Q7Z460; -.
PaxDb; Q7Z460; -.
PeptideAtlas; Q7Z460; -.
PRIDE; Q7Z460; -.
Ensembl; ENST00000263710; ENSP00000263710; ENSG00000074054. [Q7Z460-1]
Ensembl; ENST00000397587; ENSP00000380717; ENSG00000074054. [Q7Z460-5]
Ensembl; ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
Ensembl; ENST00000541377; ENSP00000441625; ENSG00000074054. [Q7Z460-4]
GeneID; 23332; -.
KEGG; hsa:23332; -.
UCSC; uc061nlf.1; human. [Q7Z460-1]
CTD; 23332; -.
DisGeNET; 23332; -.
EuPathDB; HostDB:ENSG00000074054.17; -.
GeneCards; CLASP1; -.
HGNC; HGNC:17088; CLASP1.
HPA; HPA065219; -.
MIM; 605852; gene.
neXtProt; NX_Q7Z460; -.
OpenTargets; ENSG00000074054; -.
PharmGKB; PA38436; -.
eggNOG; KOG2956; Eukaryota.
eggNOG; ENOG410ZMY0; LUCA.
GeneTree; ENSGT00390000001762; -.
HOGENOM; HOG000236347; -.
HOVERGEN; HBG079692; -.
InParanoid; Q7Z460; -.
KO; K16578; -.
OMA; NPQYVWD; -.
OrthoDB; EOG091G0GTV; -.
PhylomeDB; Q7Z460; -.
TreeFam; TF101155; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-428890; Role of Abl in Robo-Slit signaling.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; CLASP1; human.
GeneWiki; CLASP1; -.
GenomeRNAi; 23332; -.
PMAP-CutDB; Q7Z460; -.
PRO; PR:Q7Z460; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000074054; -.
CleanEx; HS_CLASP1; -.
CleanEx; HS_MAST1; -.
ExpressionAtlas; Q7Z460; baseline and differential.
Genevisible; Q7Z460; HS.
GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0031592; C:centrosomal corona; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
GO; GO:0043515; F:kinetochore binding; IMP:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IDA:MGI.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
GO; GO:0051294; P:establishment of spindle orientation; IDA:MGI.
GO; GO:0007163; P:establishment or maintenance of cell polarity; NAS:UniProtKB.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0006903; P:vesicle targeting; IMP:UniProtKB.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR028399; CLASP_1.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR034085; TOG.
PANTHER; PTHR21567:SF49; PTHR21567:SF49; 1.
Pfam; PF12348; CLASP_N; 2.
SMART; SM01349; TOG; 4.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS50077; HEAT_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Golgi apparatus; Kinetochore; Microtubule; Mitosis;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1538 CLIP-associating protein 1.
/FTId=PRO_0000089847.
REPEAT 87 124 HEAT 1.
REPEAT 163 200 HEAT 2.
REPEAT 405 440 HEAT 3.
REPEAT 441 477 HEAT 4.
REPEAT 974 1011 HEAT 5.
REPEAT 1342 1379 HEAT 6.
REPEAT 1460 1497 HEAT 7.
REGION 662 785 Interaction with microtubules, MAPRE1 and
MAPRE3. {ECO:0000269|PubMed:15631994}.
REGION 1254 1538 Interaction with CLIP2. {ECO:0000250}.
REGION 1254 1538 Interaction with PHLDB2 and RSN.
{ECO:0000269|PubMed:16824950}.
REGION 1256 1538 Localization to kinetochores.
COILED 1299 1330 {ECO:0000255}.
COMPBIAS 530 765 Ser-rich.
COMPBIAS 1526 1532 Poly-Ser.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TV8}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 646 646 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 656 656 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 711 711 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 797 797 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1095 1095 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80TV8}.
MOD_RES 1099 1099 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1113 1113 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TV8}.
MOD_RES 1196 1196 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 637 637 L -> LESRHMREDMEYIGLDS (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054412.
VAR_SEQ 637 637 L -> LDGTTTKAE (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057272.
VAR_SEQ 673 682 RSRSANPAGA -> P (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054413.
VAR_SEQ 737 772 Missing (in isoform 2, isoform 3 and
isoform 4, isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_022386.
VAR_SEQ 808 808 L -> LLLGDSRSK (in isoform 2, isoform 3
and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_022387.
VAR_SEQ 808 808 L -> LLLGDSRS (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054414.
VAR_SEQ 911 911 K -> KIADSEAECEDKEGNLFPSEVSCT (in isoform
3). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_022388.
VAR_SEQ 1123 1161 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_022389.
VARIANT 233 233 I -> T (in dbSNP:rs17761055).
/FTId=VAR_053818.
CONFLICT 251 251 R -> G (in Ref. 5; CAI46251).
{ECO:0000305}.
CONFLICT 556 556 S -> F (in Ref. 5; CAI46251).
{ECO:0000305}.
HELIX 297 306 {ECO:0000244|PDB:4K92}.
HELIX 317 331 {ECO:0000244|PDB:4K92}.
HELIX 338 353 {ECO:0000244|PDB:4K92}.
HELIX 356 358 {ECO:0000244|PDB:4K92}.
HELIX 362 367 {ECO:0000244|PDB:4K92}.
HELIX 370 377 {ECO:0000244|PDB:4K92}.
HELIX 382 399 {ECO:0000244|PDB:4K92}.
HELIX 400 403 {ECO:0000244|PDB:4K92}.
HELIX 404 415 {ECO:0000244|PDB:4K92}.
TURN 416 419 {ECO:0000244|PDB:4K92}.
HELIX 423 439 {ECO:0000244|PDB:4K92}.
HELIX 445 451 {ECO:0000244|PDB:4K92}.
HELIX 452 454 {ECO:0000244|PDB:4K92}.
HELIX 458 474 {ECO:0000244|PDB:4K92}.
HELIX 477 479 {ECO:0000244|PDB:4K92}.
TURN 480 482 {ECO:0000244|PDB:4K92}.
HELIX 484 495 {ECO:0000244|PDB:4K92}.
HELIX 500 516 {ECO:0000244|PDB:4K92}.
HELIX 518 527 {ECO:0000244|PDB:4K92}.
HELIX 530 537 {ECO:0000244|PDB:4K92}.
SEQUENCE 1538 AA; 169451 MW; 6E03BD948C227F8D CRC64;
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN
FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS
DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI
PRSQGCSRET SPNRIGLARS SRIPRPSMSQ GCSRDTSRES SRDTSPARGF PPLDRFGLGQ
PGRIPGSVNA MRVLSTSTDL EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY
GSRNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI
FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ
KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK YIESLARQMD PTDFVNSSET
RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM LLGALPKTFQ DGATKLLHNH
LKNSSNTSVG SPSNTIGRTP SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP
PFSQPNSIPT APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL
NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT QPPRAFPGPR
ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH SDLVADLLKE LSNHNERVEE
RKGALLELLK ITREDSLGVW EEHFKTILLL LLETLGDKDH SIRALALRVL REILRNQPAR
FKNYAELTIM KTLEAHKDSH KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL
AAIKMQTKVV ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK
PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS


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