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Abnormal spindle-like microcephaly-associated protein (Abnormal spindle protein homolog) (Asp homolog)

 ASPM_HUMAN              Reviewed;        3477 AA.
Q8IZT6; Q4G1H1; Q5VYL3; Q86UX4; Q8IUL2; Q8IZJ7; Q8IZJ8; Q8IZJ9;
Q8N4D1; Q9NVS1; Q9NVT6;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
12-SEP-2018, entry version 158.
RecName: Full=Abnormal spindle-like microcephaly-associated protein;
AltName: Full=Abnormal spindle protein homolog;
Short=Asp homolog;
Name=ASPM; Synonyms=MCPH5;
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), FUNCTION, INVOLVEMENT IN
MCPH5, AND VARIANT HIS-2494.
TISSUE=Colon adenocarcinoma, and Fetal brain;
PubMed=12355089; DOI=10.1038/ng995;
Bond J., Roberts E., Mochida G.H., Hampshire D.J., Scott S.,
Askham J.M., Springell K., Mahadevan M., Crow Y.J., Markham A.F.,
Walsh C.A., Woods C.G.;
"ASPM is a major determinant of cerebral cortical size.";
Nat. Genet. 32:316-320(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-2494.
PubMed=14704186;
Zhang J.;
"Evolution of the human ASPM gene, a major determinant of brain
size.";
Genetics 165:2063-2070(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE
SPLICING, AND SUBCELLULAR LOCATION.
PubMed=15972725; DOI=10.1093/hmg/ddi220;
Kouprina N., Pavlicek A., Collins N.K., Nakano M., Noskov V.N.,
Ohzeki J.I., Mochida G.H., Risinger J.I., Goldsmith P., Gunsior M.,
Solomon G., Gersch W., Kim J.H., Barrett J.C., Walsh C.A., Jurka J.,
Masumoto H., Larionov V.;
"The microcephaly ASPM gene is expressed in proliferating tissues and
encodes for a mitotic spindle protein.";
Hum. Mol. Genet. 14:2155-2165(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-147 AND 709-3477 (ISOFORM
2), AND VARIANT PHE-1090.
TISSUE=Kidney, and Lymph;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2740-3477 (ISOFORM 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).
[8]
INVOLVEMENT IN MCPH5, AND VARIANTS GLY-2562; ILE-2647 AND ARG-3132.
PubMed=14574646; DOI=10.1086/379085;
Bond J., Scott S., Hampshire D.J., Springell K., Corry P.,
Abramowicz M.J., Mochida G.H., Hennekam R.C.M., Maher E.R.,
Fryns J.-P., Alswaid A., Jafri H., Rashid Y., Mubaidin A., Walsh C.A.,
Roberts E., Woods C.G.;
"Protein-truncating mutations in ASPM cause variable reduction in
brain size.";
Am. J. Hum. Genet. 73:1170-1177(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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-392, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-283; SER-425
AND SER-1103, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-392, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-283 AND
SER-392, 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).
[14]
INVOLVEMENT IN MCPH5.
PubMed=22989186; DOI=10.1111/j.1399-0004.2012.01949.x;
Papari E., Bastami M., Farhadi A., Abedini S.S., Hosseini M.,
Bahman I., Mohseni M., Garshasbi M., Moheb L.A., Behjati F.,
Kahrizi K., Ropers H.H., Najmabadi H.;
"Investigation of primary microcephaly in Bushehr province of Iran:
novel STIL and ASPM mutations.";
Clin. Genet. 83:488-490(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-425; SER-605
AND SER-1103, 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).
[16]
FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, AND SUBCELLULAR
LOCATION.
PubMed=28436967; DOI=10.1038/ncb3511;
Jiang K., Rezabkova L., Hua S., Liu Q., Capitani G.,
Maarten Altelaar A.F., Heck A.J.R., Kammerer R.A., Steinmetz M.O.,
Akhmanova A.;
"Microtubule minus-end regulation at spindle poles by an ASPM-katanin
complex.";
Nat. Cell Biol. 19:480-492(2017).
[17]
VARIANTS HIS-2494; ASP-2526; ILE-2647 AND PRO-3180.
PubMed=16673149; DOI=10.1007/s10048-006-0042-4;
Gul A., Hassan M.J., Mahmood S., Chen W., Rahmani S., Naseer M.I.,
Dellefave L., Muhammad N., Rafiq M.A., Ansar M., Chishti M.S., Ali G.,
Siddique T., Ahmad W.;
"Genetic studies of autosomal recessive primary microcephaly in 33
Pakistani families: Novel sequence variants in ASPM gene.";
Neurogenetics 7:105-110(2006).
[18]
VARIANT ILE-2647.
PubMed=18204051; DOI=10.1093/hmg/ddn021;
Wang J.-K., Li Y., Su B.;
"A common SNP of MCPH1 is associated with cranial volume variation in
Chinese population.";
Hum. Mol. Genet. 17:1329-1335(2008).
[19]
VARIANT PRO-3180.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Involved in mitotic spindle regulation and coordination
of mitotic processes. The function in regulating microtubule
dynamics at spindle poles including spindle orientation, astral
microtubule density and poleward microtubule flux seems to depend
on the association with the katanin complex formed by KATNA1 and
KATNB1. Enhances the microtubule lattice severing activity of
KATNA1 by recruiting the katanin complex to microtubules. Can
block microtubule minus-end growth and reversely this function can
be enhanced by the katanin complex (PubMed:28436967). May have a
preferential role in regulating neurogenesis.
{ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:15972725,
ECO:0000269|PubMed:28436967}.
-!- SUBUNIT: Interacts with KATNA1 and KATNB1; katanin complex
formation KATNA1:KATNB1 is required for the association.
{ECO:0000269|PubMed:28436967}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:15972725}. Nucleus
{ECO:0000250}. Note=The nuclear-cytoplasmic distribution could be
regulated by the availability of calmodulin (By similarity).
Localizes to spindle poles during mitosis (PubMed:19690332).
Associates with microtubule minus ends (By similarity).
{ECO:0000250|UniProtKB:Q8CJ27}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IZT6-1; Sequence=Displayed;
Name=2;
IsoId=Q8IZT6-2; Sequence=VSP_010680;
Note=No experimental confirmation available.;
-!- DISEASE: Microcephaly 5, primary, autosomal recessive (MCPH5)
[MIM:608716]: A disease defined as a head circumference more than
3 standard deviations below the age-related mean. Brain weight is
markedly reduced and the cerebral cortex is disproportionately
small. Despite this marked reduction in size, the gyral pattern is
relatively well preserved, with no major abnormality in cortical
architecture. Affected individuals are mentally retarded. Primary
microcephaly is further defined by the absence of other syndromic
features or significant neurological deficits due to degenerative
brain disorder. {ECO:0000269|PubMed:12355089,
ECO:0000269|PubMed:14574646, ECO:0000269|PubMed:22989186}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH34607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA91676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ASPMID44463ch1q31.html";
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EMBL; AF509326; AAN40011.1; -; mRNA.
EMBL; AY099890; AAM44119.1; -; mRNA.
EMBL; AY099891; AAM44120.1; -; mRNA.
EMBL; AY099892; AAM44121.1; -; mRNA.
EMBL; AY099893; AAM44122.1; -; mRNA.
EMBL; AY101201; AAM48745.1; -; mRNA.
EMBL; AY367065; AAR12641.1; -; mRNA.
EMBL; AY971956; AAY46814.1; -; mRNA.
EMBL; AL353809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91274.1; -; Genomic_DNA.
EMBL; BC015396; AAH15396.1; -; mRNA.
EMBL; BC034607; AAH34607.1; ALT_INIT; mRNA.
EMBL; AK001411; BAA91676.1; ALT_INIT; mRNA.
CCDS; CCDS1389.1; -. [Q8IZT6-1]
CCDS; CCDS55672.1; -. [Q8IZT6-2]
RefSeq; NP_001193775.1; NM_001206846.1. [Q8IZT6-2]
RefSeq; NP_060606.3; NM_018136.4. [Q8IZT6-1]
UniGene; Hs.121028; -.
ProteinModelPortal; Q8IZT6; -.
SMR; Q8IZT6; -.
BioGrid; 129236; 75.
IntAct; Q8IZT6; 54.
STRING; 9606.ENSP00000356379; -.
CarbonylDB; Q8IZT6; -.
iPTMnet; Q8IZT6; -.
PhosphoSitePlus; Q8IZT6; -.
BioMuta; ASPM; -.
DMDM; 215273935; -.
EPD; Q8IZT6; -.
MaxQB; Q8IZT6; -.
PaxDb; Q8IZT6; -.
PeptideAtlas; Q8IZT6; -.
PRIDE; Q8IZT6; -.
ProteomicsDB; 71424; -.
ProteomicsDB; 71425; -. [Q8IZT6-2]
Ensembl; ENST00000294732; ENSP00000294732; ENSG00000066279. [Q8IZT6-2]
Ensembl; ENST00000367409; ENSP00000356379; ENSG00000066279. [Q8IZT6-1]
GeneID; 259266; -.
KEGG; hsa:259266; -.
UCSC; uc001gtu.4; human. [Q8IZT6-1]
CTD; 259266; -.
DisGeNET; 259266; -.
EuPathDB; HostDB:ENSG00000066279.16; -.
GeneCards; ASPM; -.
GeneReviews; ASPM; -.
HGNC; HGNC:19048; ASPM.
HPA; CAB017816; -.
MalaCards; ASPM; -.
MIM; 605481; gene.
MIM; 608716; phenotype.
neXtProt; NX_Q8IZT6; -.
OpenTargets; ENSG00000066279; -.
Orphanet; 2512; Autosomal recessive primary microcephaly.
PharmGKB; PA38782; -.
eggNOG; KOG0165; Eukaryota.
eggNOG; ENOG410XSAR; LUCA.
GeneTree; ENSGT00560000077332; -.
HOGENOM; HOG000034105; -.
HOVERGEN; HBG050595; -.
InParanoid; Q8IZT6; -.
KO; K16743; -.
OMA; LQSYFRM; -.
OrthoDB; EOG091G0332; -.
PhylomeDB; Q8IZT6; -.
TreeFam; TF351180; -.
SIGNOR; Q8IZT6; -.
ChiTaRS; ASPM; human.
GeneWiki; ASPM_(gene); -.
GenomeRNAi; 259266; -.
PRO; PR:Q8IZT6; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000066279; Expressed in 122 organ(s), highest expression level in liver.
ExpressionAtlas; Q8IZT6; baseline and differential.
Genevisible; Q8IZT6; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
GO; GO:0036449; C:microtubule minus-end; IDA:HGNC.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0097431; C:mitotic spindle pole; IDA:HGNC.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0021873; P:forebrain neuroblast division; IEA:Ensembl.
GO; GO:0051661; P:maintenance of centrosome location; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0045769; P:negative regulation of asymmetric cell division; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0051445; P:regulation of meiotic cell cycle; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0090306; P:spindle assembly involved in meiosis; IEA:Ensembl.
GO; GO:0051653; P:spindle localization; IMP:HGNC.
GO; GO:0007051; P:spindle organization; IMP:HGNC.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR031549; ASH.
InterPro; IPR029955; ASPM.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR44613; PTHR44613; 3.
Pfam; PF15780; ASH; 1.
Pfam; PF00307; CH; 1.
Pfam; PF00612; IQ; 40.
SMART; SM00033; CH; 2.
SMART; SM00015; IQ; 63.
SUPFAM; SSF47576; SSF47576; 3.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF52540; SSF52540; 18.
PROSITE; PS50021; CH; 2.
PROSITE; PS50096; IQ; 39.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Mental retardation; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Primary microcephaly;
Reference proteome; Repeat.
CHAIN 1 3477 Abnormal spindle-like microcephaly-
associated protein.
/FTId=PRO_0000191332.
DOMAIN 920 1056 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 1110 1261 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 1347 1378 IQ 1. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1393 1422 IQ 2. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1582 1613 IQ 3. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1632 1661 IQ 4. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1655 1684 IQ 5. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1728 1757 IQ 6. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1751 1782 IQ 7. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1801 1830 IQ 8. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1824 1853 IQ 9. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1874 1903 IQ 10. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1897 1928 IQ 11. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1947 1978 IQ 12. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1970 2001 IQ 13. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2020 2049 IQ 14. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2043 2074 IQ 15. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2093 2124 IQ 16. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2116 2147 IQ 17. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2166 2197 IQ 18. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2189 2218 IQ 19. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2239 2270 IQ 20. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2262 2293 IQ 21. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2311 2342 IQ 22. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2334 2365 IQ 23. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2384 2415 IQ 24. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2407 2438 IQ 25. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2457 2488 IQ 26. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2530 2561 IQ 27. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2624 2653 IQ 28. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2665 2696 IQ 29. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2688 2719 IQ 30. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2738 2767 IQ 31. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2859 2890 IQ 32. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2909 2938 IQ 33. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2932 2963 IQ 34. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 2954 2985 IQ 35. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 3029 3060 IQ 36. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 3079 3110 IQ 37. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 3181 3210 IQ 38. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 3204 3235 IQ 39. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
REGION 308 409 Sufficient for interaction with
KATNA1:KATNB1.
{ECO:0000250|UniProtKB:Q8CJ27}.
COILED 1057 1078 {ECO:0000255}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1103 1103 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1356 2940 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15972725}.
/FTId=VSP_010680.
VARIANT 313 313 I -> V (in dbSNP:rs12025066).
/FTId=VAR_047263.
VARIANT 430 430 R -> G (in dbSNP:rs6428388).
/FTId=VAR_024369.
VARIANT 869 869 T -> S (in dbSNP:rs7551108).
/FTId=VAR_046758.
VARIANT 1090 1090 S -> F (in dbSNP:rs16841081).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046759.
VARIANT 2494 2494 Y -> H (in dbSNP:rs964201).
{ECO:0000269|PubMed:12355089,
ECO:0000269|PubMed:14704186,
ECO:0000269|PubMed:16673149}.
/FTId=VAR_046760.
VARIANT 2526 2526 N -> D (in dbSNP:rs587783267).
{ECO:0000269|PubMed:16673149}.
/FTId=VAR_071930.
VARIANT 2562 2562 S -> G (in dbSNP:rs41310927).
{ECO:0000269|PubMed:14574646}.
/FTId=VAR_019084.
VARIANT 2620 2620 Q -> H (in dbSNP:rs12138336).
/FTId=VAR_046761.
VARIANT 2647 2647 L -> I (in dbSNP:rs3762271).
{ECO:0000269|PubMed:14574646,
ECO:0000269|PubMed:16673149,
ECO:0000269|PubMed:18204051}.
/FTId=VAR_019085.
VARIANT 3132 3132 L -> R (in dbSNP:rs36004306).
{ECO:0000269|PubMed:14574646}.
/FTId=VAR_019086.
VARIANT 3180 3180 Q -> P (in dbSNP:rs193251130).
{ECO:0000269|PubMed:16673149,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_071931.
VARIANT 3258 3258 H -> R (in dbSNP:rs7528827).
/FTId=VAR_046762.
CONFLICT 2355 2355 Q -> R (in Ref. 1; AAN40011 and 2;
AAR12641). {ECO:0000305}.
CONFLICT 2977 2977 I -> V (in Ref. 7; BAA91676).
{ECO:0000305}.
CONFLICT 3049 3049 F -> S (in Ref. 7; BAA91676).
{ECO:0000305}.
SEQUENCE 3477 AA; 409800 MW; EB6EDAD3FF186108 CRC64;
MANRRVGRGC WEVSPTERRP PAGLRGPAAE EEASSPPVLS LSHFCRSPFL CFGDVLLGAS
RTLSLALDNP NEEVAEVKIS HFPAADLGFS VSQRCFVLQP KEKIVISVNW TPLKEGRVRE
IMTFLVNDVL KHQAILLGNA EEQKKKKRSL WDTIKKKKIS ASTSHNRRVS NIQNVNKTFS
VSQKVDRVRS PLQACENLAM NEGGPPTENN SLILEENKIP ISPISPAFNE CHGATCLPLS
VRRSTTYSSL HASENRELLN VHSANVSKVS FNEKAVTETS FNSVNVNGQR GENSKLSLTP
NCSSTLNITQ SQIHFLSPDS FVNNSHGANN ELELVTCLSS DMFMKDNSQP VHLESTIAHE
IYQKILSPDS FIKDNYGLNQ DLESESVNPI LSPNQFLKDN MAYMCTSQQT CKVPLSNENS
QVPQSPEDWR KSEVSPRIPE CQGSKSPKAI FEELVEMKSN YYSFIKQNNP KFSAVQDISS
HSHNKQPKRR PILSATVTKR KATCTRENQT EINKPKAKRC LNSAVGEHEK VINNQKEKED
FHSYLPIIDP ILSKSKSYKN EVTPSSTTAS VARKRKSDGS MEDANVRVAI TEHTEVREIK
RIHFSPSEPK TSAVKKTKNV TTPISKRISN REKLNLKKKT DLSIFRTPIS KTNKRTKPII
AVAQSSLTFI KPLKTDIPRH PMPFAAKNMF YDERWKEKQE QGFTWWLNFI LTPDDFTVKT
NISEVNAATL LLGIENQHKI SVPRAPTKEE MSLRAYTARC RLNRLRRAAC RLFTSEKMVK
AIKKLEIEIE ARRLIVRKDR HLWKDVGERQ KVLNWLLSYN PLWLRIGLET TYGELISLED
NSDVTGLAMF ILNRLLWNPD IAAEYRHPTV PHLYRDGHEE ALSKFTLKKL LLLVCFLDYA
KISRLIDHDP CLFCKDAEFK ASKEILLAFS RDFLSGEGDL SRHLGLLGLP VNHVQTPFDE
FDFAVTNLAV DLQCGVRLVR TMELLTQNWD LSKKLRIPAI SRLQKMHNVD IVLQVLKSRG
IELSDEHGNT ILSKDIVDRH REKTLRLLWK IAFAFQVDIS LNLDQLKEEI AFLKHTKSIK
KTISLLSCHS DDLINKKKGK RDSGSFEQYS ENIKLLMDWV NAVCAFYNKK VENFTVSFSD
GRVLCYLIHH YHPCYVPFDA ICQRTTQTVE CTQTGSVVLN SSSESDDSSL DMSLKAFDHE
NTSELYKELL ENEKKNFHLV RSAVRDLGGI PAMINHSDMS NTIPDEKVVI TYLSFLCARL
LDLRKEIRAA RLIQTTWRKY KLKTDLKRHQ EREKAARIIQ LAVINFLAKQ RLRKRVNAAL
VIQKYWRRVL AQRKLLMLKK EKLEKVQNKA ASLIQGYWRR YSTRQRFLKL KYYSIILQSR
IRMIIAVTSY KRYLWATVTI QRHWRAYLRR KQDQQRYEML KSSTLIIQSM FRKWKQRKMQ
SQVKATVILQ RAFREWHLRK QAKEENSAII IQSWYRMHKE LRKYIYIRSC VVIIQKRFRC
FQAQKLYKRR KESILTIQKY YKAYLKGKIE RTNYLQKRAA AIQLQAAFRR LKAHNLCRQI
RAACVIQSYW RMRQDRVRFL NLKKTIIKFQ AHVRKHQQRQ KYKKMKKAAV IIQTHFRAYI
FAMKVLASYQ KTRSAVIVLQ SAYRGMQARK MYIHILTSVI KIQSYYRAYV SKKEFLSLKN
ATIKLQSTVK MKQTRKQYLH LRAAALFIQQ CYRSKKIAAQ KREEYMQMRE SCIKLQAFVR
GYLVRKQMRL QRKAVISLQS YFRMRKARQY YLKMYKAIIV IQNYYHAYKA QVNQRKNFLQ
VKKAATCLQA AYRGYKVRQL IKQQSIAALK IQSAFRGYNK RVKYQSVLQS IIKIQRWYRA
YKTLHDTRTH FLKTKAAVIS LQSAYRGWKV RKQIRREHQA ALKIQSAFRM AKAQKQFRLF
KTAALVIQQN FRAWTAGRKQ CMEYIELRHA VLVLQSMWKG KTLRRQLQRQ HKCAIIIQSY
YRMHVQQKKW KIMKKAALLI QKYYRAYSIG REQNHLYLKT KAAVVTLQSA YRGMKVRKRI
KDCNKAAVTI QSKYRAYKTK KKYATYRASA IIIQRWYRGI KITNHQHKEY LNLKKTAIKI
QSVYRGIRVR RHIQHMHRAA TFIKAMFKMH QSRISYHTMR KAAIVIQVRC RAYYQGKMQR
EKYLTILKAV KVLQASFRGV RVRRTLRKMQ TAATLIQSNY RRYRQQTYFN KLKKITKTVQ
QRYWAMKERN IQFQRYNKLR HSVIYIQAIF RGKKARRHLK MMHIAATLIQ RRFRTLMMRR
RFLSLKKTAI LIQRKYRAHL CTKHHLQFLQ VQNAVIKIQS SYRRWMIRKR MREMHRAATF
IQSTFRMHRL HMRYQALKQA SVVIQQQYQA NRAAKLQRQH YLRQRHSAVI LQAAFRGMKT
RRHLKSMHSS ATLIQSRFRS LLVRRRFISL KKATIFVQRK YRATICAKHK LYQFLHLRKA
AITIQSSYRR LMVKKKLQEM QRAAVLIQAT FRMYRTYITF QTWKHASILI QQHYRTYRAA
KLQRENYIRQ WHSAVVIQAA YKGMKARQLL REKHKASIVI QSTYRMYRQY CFYQKLQWAT
KIIQEKYRAN KKKQKVFQHN ELKKETCVQA GFQDMNIKKQ IQEQHQAAII IQKHCKAFKI
RKHYLHLRAT VVSIQRRYRK LTAVRTQAVI CIQSYYRGFK VRKDIQNMHR AATLIQSFYR
MHRAKVDYET KKTAIVVIQN YYRLYVRVKT ERKNFLAVQK SVRTIQAAFR GMKVRQKLKN
VSEEKMAAIV NQSALCCYRS KTQYEAVQSE GVMIQEWYKA SGLACSQEAE YHSQSRAAVT
IQKAFCRMVT RKLETQKCAA LRIQFFLQMA VYRRRFVQQK RAAITLQHYF RTWQTRKQFL
LYRKAAVVLQ NHYRAFLSAK HQRQVYLQIR SSVIIIQARS KGFIQKRKFQ EIKNSTIKIQ
AMWRRYRAKK YLCKVKAACK IQAWYRCWRA HKEYLAILKA VKIIQGCFYT KLERTRFLNV
RASAIIIQRK WRAILPAKIA HEHFLMIKRH RAACLIQAHY RGYKGRQVFL RQKSAALIIQ
KYIRAREAGK HERIKYIEFK KSTVILQALV RGWLVRKRFL EQRAKIRLLH FTAAAYYHLN
AVRIQRAYKL YLAVKNANKQ VNSVICIQRW FRARLQEKRF IQKYHSIKKI EHEGQECLSQ
RNRAASVIQK AVRHFLLRKK QEKFTSGIIK IQALWRGYSW RKKNDCTKIK AIRLSLQVVN
REIREENKLY KRTALALHYL LTYKHLSAIL EALKHLEVVT RLSPLCCENM AQSGAISKIF
VLIRSCNRSI PCMEVIRYAV QVLLNVSKYE KTTSAVYDVE NCIDILLELL QIYREKPGNK
VADKGGSIFT KTCCLLAILL KTTNRASDVR SRSKVVDRIY SLYKLTAHKH KMNTERILYK
QKKNSSISIP FIPETPVRTR IVSRLKPDWV LRRDNMEEIT NPLQAIQMVM DTLGIPY


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