Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

GATOR complex protein DEPDC5 (DEP domain-containing protein 5)

 DEPD5_HUMAN             Reviewed;        1603 AA.
O75140; A6H8V6; A8MPX9; B4DH93; B9EGN9; Q5K3V5; Q5THY9; Q5THZ0;
Q5THZ1; Q5THZ3; Q68DR1; Q6MZX3; Q6PEZ1; Q9UGV8; Q9UH13;
03-APR-2002, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
25-OCT-2017, entry version 148.
RecName: Full=GATOR complex protein DEPDC5 {ECO:0000305};
AltName: Full=DEP domain-containing protein 5 {ECO:0000312|HGNC:HGNC:18423};
Name=DEPDC5 {ECO:0000312|HGNC:HGNC:18423};
Synonyms=KIAA0645 {ECO:0000312|EMBL:BAA31620.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 9).
TISSUE=Cerebellum;
PubMed=15770670; DOI=10.1002/gcc.20181;
Seng T.J., Ichimura K., Liu L., Tingby O., Pearson D.M., Collins V.P.;
"Complex chromosome 22 rearrangements in astrocytic tumors identified
using microsatellite and chromosome 22 tile path array analysis.";
Genes Chromosomes Cancer 43:181-193(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[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] (ISOFORMS 1; 2 AND 10).
TISSUE=Placenta, and Testis;
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 571-1603 (ISOFORM 6), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-1603 (ISOFORM 9).
TISSUE=Fetal brain;
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).
[8]
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).
[9]
FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND SUBUNIT.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[10]
FUNCTION.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, 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).
[12]
SUBCELLULAR LOCATION.
PubMed=28199306; DOI=10.1038/nature21423;
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M.,
Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M.,
Abu-Remaileh M., Frankel W.N., Sabatini D.M.;
"KICSTOR recruits GATOR1 to the lysosome and is necessary for
nutrients to regulate mTORC1.";
Nature 543:438-442(2017).
[13]
INVOLVEMENT IN FFEVF1, AND VARIANTS FFEVF1 ASP-214; PRO-542; PRO-1081;
PHE-1154 AND GLN-1268.
PubMed=26505888; DOI=10.1002/ana.24547;
Epilepsy Electroclinical Study Group;
Ricos M.G., Hodgson B.L., Pippucci T., Saidin A., Ong Y.S.,
Heron S.E., Licchetta L., Bisulli F., Bayly M.A., Hughes J.,
Baldassari S., Palombo F., Santucci M., Meletti S., Berkovic S.F.,
Rubboli G., Thomas P.Q., Scheffer I.E., Tinuper P., Geoghegan J.,
Schreiber A.W., Dibbens L.M.;
"Mutations in the mammalian target of rapamycin pathway regulators
NPRL2 and NPRL3 cause focal epilepsy.";
Ann. Neurol. 79:120-131(2016).
[14]
INVOLVEMENT IN FFEVF1, AND VARIANT FFEVF1 ARG-1065.
PubMed=27173016; DOI=10.1111/epi.13391;
Weckhuysen S., Marsan E., Lambrecq V., Marchal C., Morin-Brureau M.,
An-Gourfinkel I., Baulac M., Fohlen M., Kallay Zetchi C., Seeck M.,
de la Grange P., Dermaut B., Meurs A., Thomas P., Chassoux F.,
Leguern E., Picard F., Baulac S.;
"Involvement of GATOR complex genes in familial focal epilepsies and
focal cortical dysplasia.";
Epilepsia 57:994-1003(2016).
[15]
VARIANTS FFEVF1 VAL-452; ARG-1073 AND LEU-1104, AND INVOLVEMENT IN
FFEVF1.
PubMed=23542697; DOI=10.1038/ng.2599;
Dibbens L.M., de Vries B., Donatello S., Heron S.E., Hodgson B.L.,
Chintawar S., Crompton D.E., Hughes J.N., Bellows S.T., Klein K.M.,
Callenbach P.M., Corbett M.A., Gardner A.E., Kivity S., Iona X.,
Regan B.M., Weller C.M., Crimmins D., O'Brien T.J., Guerrero-Lopez R.,
Mulley J.C., Dubeau F., Licchetta L., Bisulli F., Cossette P.,
Thomas P.Q., Gecz J., Serratosa J., Brouwer O.F., Andermann F.,
Andermann E., van den Maagdenberg A.M., Pandolfo M., Berkovic S.F.,
Scheffer I.E.;
"Mutations in DEPDC5 cause familial focal epilepsy with variable
foci.";
Nat. Genet. 45:546-551(2013).
[16]
VARIANT FFEVF1 GLN-485, AND TISSUE SPECIFICITY.
PubMed=23542701; DOI=10.1038/ng.2601;
Ishida S., Picard F., Rudolf G., Noe E., Achaz G., Thomas P.,
Genton P., Mundwiller E., Wolff M., Marescaux C., Miles R., Baulac M.,
Hirsch E., Leguern E., Baulac S.;
"Mutations of DEPDC5 cause autosomal dominant focal epilepsies.";
Nat. Genet. 45:552-555(2013).
[17]
VARIANTS FFEVF1 ILE-90 AND LEU-272.
PubMed=24591017; DOI=10.1002/ana.24127;
Lal D., Reinthaler E.M., Schubert J., Muhle H., Riesch E., Kluger G.,
Jabbari K., Kawalia A., Baumel C., Holthausen H., Hahn A., Feucht M.,
Neophytou B., Haberlandt E., Becker F., Altmuller J., Thiele H.,
Lemke J.R., Lerche H., Nurnberg P., Sander T., Weber Y., Zimprich F.,
Neubauer B.A.;
"DEPDC5 mutations in genetic focal epilepsies of childhood.";
Ann. Neurol. 75:788-792(2014).
[18]
VARIANT FFEVF1 MET-864.
PubMed=24283814; DOI=10.1111/cge.12311;
Martin C., Meloche C., Rioux M.F., Nguyen D.K., Carmant L.,
Andermann E., Gravel M., Cossette P.;
"A recurrent mutation in DEPDC5 predisposes to focal epilepsies in the
French-Canadian population.";
Clin. Genet. 86:570-574(2014).
[19]
VARIANTS FFEVF1 ILE-90; LEU-272; VAL-452; GLN-485; MET-864; ARG-1073
AND GLY-1162, CHARACTERIZATION VARIANTS FFEVF1 ILE-90; LEU-272;
VAL-452; GLN-485; MET-864; ARG-1073 AND GLY-1162, AND IDENTIFICATION
IN GATOR COMPLEX.
PubMed=25366275; DOI=10.1002/humu.22723;
van Kranenburg M., Hoogeveen-Westerveld M., Nellist M.;
"Preliminary functional assessment and classification of DEPDC5
variants associated with focal epilepsy.";
Hum. Mutat. 36:200-209(2015).
-!- FUNCTION: As a component of the GATOR1 complex functions as an
inhibitor of the amino acid-sensing branch of the TORC1 pathway.
The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and
RRAGB within RRAGC-containing heterodimers, thereby deactivating
RRAGs, releasing mTORC1 from lysosomal surface and inhibiting
mTORC1 signaling. The GATOR1 complex is negatively regulated by
GATOR2 the other GATOR subcomplex in this amino acid-sensing
branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25457612}.
-!- SUBUNIT: Within the GATOR complex, component of the GATOR1
subcomplex, made of DEPDC5, NPRL2 and NPRL3. GATOR1 mediates the
strong interaction of the GATOR complex with RRAGA/RRAGC and
RRAGB/RRAGC heterodimers. {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25366275}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P61460}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P61460}. Lysosome membrane
{ECO:0000269|PubMed:28199306}. Note=Localization to lysosomes is
amino acid-independent. {ECO:0000269|PubMed:28199306}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=10;
IsoId=O75140-10; Sequence=Displayed;
Name=2;
IsoId=O75140-2; Sequence=VSP_014933, VSP_014934;
Note=No experimental confirmation available.;
Name=4;
IsoId=O75140-4; Sequence=VSP_014938;
Note=No experimental confirmation available.;
Name=5;
IsoId=O75140-5; Sequence=VSP_014941;
Note=No experimental confirmation available.;
Name=6;
IsoId=O75140-6; Sequence=VSP_014936, VSP_014939, VSP_014940;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=8;
IsoId=O75140-8; Sequence=VSP_014936, VSP_014938;
Note=No experimental confirmation available.;
Name=9;
IsoId=O75140-9; Sequence=VSP_014937;
Name=1;
IsoId=O75140-1; Sequence=VSP_014937, VSP_014938;
-!- TISSUE SPECIFICITY: Expressed in developing and adult brain.
{ECO:0000269|PubMed:23542701}.
-!- DISEASE: Epilepsy, familial focal, with variable foci 1 (FFEVF1)
[MIM:604364]: An autosomal dominant form of epilepsy characterized
by focal seizures arising from different cortical regions in
different family members. Many patients have an aura and show
automatisms during the seizures, whereas others may have nocturnal
seizures. There is often secondary generalization. Some patients
show abnormal interictal EEG, and some patients may have
intellectual disability or autism spectrum disorders. Seizure
onset usually occurs in the first or second decades, although
later onset has been reported, and there is phenotypic variability
within families. Penetrance of the disorder is incomplete.
{ECO:0000269|PubMed:23542697, ECO:0000269|PubMed:23542701,
ECO:0000269|PubMed:24283814, ECO:0000269|PubMed:24591017,
ECO:0000269|PubMed:25366275, ECO:0000269|PubMed:26505888,
ECO:0000269|PubMed:27173016}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Inactivating mutations and truncating deletions in
the genes encoding GATOR1 proteins, including DEPDC5, are detected
in glioblastoma and ovarian tumors and are associated with loss of
heterozygosity events. Inactivation of GATOR1 proteins promotes
constitutive localization of mTORC1 to the lysosomal membrane and
blocks mTORC1 inactivation following amino acid withdrawal
(PubMed:23723238). {ECO:0000269|PubMed:23723238}.
-!- SIMILARITY: Belongs to the IML1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31620.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAG27890.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
Sequence=CAH18159.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ698950; CAG27889.1; -; mRNA.
EMBL; AJ698951; CAG27890.1; ALT_SEQ; mRNA.
EMBL; AJ704764; CAG28924.1; -; mRNA.
EMBL; AB014545; BAA31620.2; ALT_INIT; mRNA.
EMBL; AK294987; BAG58054.1; -; mRNA.
EMBL; AC005004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL022331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z83856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z82190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW59996.1; -; Genomic_DNA.
EMBL; BC057797; AAH57797.1; -; mRNA.
EMBL; BC136612; AAI36613.1; -; mRNA.
EMBL; BC146766; AAI46767.1; -; mRNA.
EMBL; BX640828; CAE45904.1; -; mRNA.
EMBL; CR749304; CAH18159.1; ALT_INIT; mRNA.
CCDS; CCDS43006.1; -. [O75140-1]
CCDS; CCDS43007.1; -. [O75140-2]
CCDS; CCDS46692.1; -. [O75140-9]
CCDS; CCDS56229.1; -. [O75140-8]
CCDS; CCDS74849.1; -. [O75140-10]
PIR; T00376; T00376.
RefSeq; NP_001007189.1; NM_001007188.2. [O75140-2]
RefSeq; NP_001129501.1; NM_001136029.2. [O75140-9]
RefSeq; NP_001229825.1; NM_001242896.1. [O75140-10]
RefSeq; NP_001229826.1; NM_001242897.1. [O75140-8]
RefSeq; NP_055477.1; NM_014662.4. [O75140-1]
RefSeq; XP_005261919.1; XM_005261862.1. [O75140-10]
RefSeq; XP_011528859.1; XM_011530557.2. [O75140-9]
RefSeq; XP_011528860.1; XM_011530558.2. [O75140-4]
RefSeq; XP_011528861.1; XM_011530559.2. [O75140-1]
RefSeq; XP_011528865.1; XM_011530563.2. [O75140-8]
RefSeq; XP_016884598.1; XM_017029109.1. [O75140-9]
RefSeq; XP_016884599.1; XM_017029110.1. [O75140-4]
RefSeq; XP_016884600.1; XM_017029111.1. [O75140-1]
UniGene; Hs.435022; -.
ProteinModelPortal; O75140; -.
BioGrid; 115034; 14.
CORUM; O75140; -.
DIP; DIP-62050N; -.
IntAct; O75140; 7.
STRING; 9606.ENSP00000371546; -.
iPTMnet; O75140; -.
PhosphoSitePlus; O75140; -.
BioMuta; DEPDC5; -.
PaxDb; O75140; -.
PeptideAtlas; O75140; -.
PRIDE; O75140; -.
Ensembl; ENST00000382111; ENSP00000371545; ENSG00000100150. [O75140-5]
Ensembl; ENST00000382112; ENSP00000371546; ENSG00000100150. [O75140-9]
Ensembl; ENST00000400242; ENSP00000383101; ENSG00000100150. [O75140-2]
Ensembl; ENST00000400246; ENSP00000383105; ENSG00000100150. [O75140-10]
Ensembl; ENST00000400248; ENSP00000383107; ENSG00000100150. [O75140-1]
Ensembl; ENST00000400249; ENSP00000383108; ENSG00000100150. [O75140-1]
Ensembl; ENST00000535622; ENSP00000440210; ENSG00000100150. [O75140-8]
GeneID; 9681; -.
KEGG; hsa:9681; -.
UCSC; uc003alr.3; human. [O75140-10]
CTD; 9681; -.
DisGeNET; 9681; -.
EuPathDB; HostDB:ENSG00000100150.16; -.
GeneCards; DEPDC5; -.
HGNC; HGNC:18423; DEPDC5.
HPA; HPA054969; -.
HPA; HPA055619; -.
MalaCards; DEPDC5; -.
MIM; 604364; phenotype.
MIM; 614191; gene.
neXtProt; NX_O75140; -.
OpenTargets; ENSG00000100150; -.
Orphanet; 101046; Autosomal dominant epilepsy with auditory features.
Orphanet; 98784; Autosomal dominant nocturnal frontal lobe epilepsy.
Orphanet; 98820; Familial focal epilepsy with variable foci.
Orphanet; 1945; Rolandic epilepsy.
PharmGKB; PA134864958; -.
eggNOG; KOG3572; Eukaryota.
eggNOG; ENOG410XQVG; LUCA.
GeneTree; ENSGT00390000016559; -.
HOGENOM; HOG000290718; -.
HOVERGEN; HBG051337; -.
InParanoid; O75140; -.
KO; K20404; -.
OMA; IMFNKVV; -.
OrthoDB; EOG091G0205; -.
ChiTaRS; DEPDC5; human.
GeneWiki; DEPDC5; -.
GenomeRNAi; 9681; -.
PRO; PR:O75140; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100150; -.
CleanEx; HS_DEPDC5; -.
ExpressionAtlas; O75140; baseline and differential.
Genevisible; O75140; HS.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:1990130; C:GATOR1 complex; IDA:SGD.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:SGD.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000591; DEP_dom.
InterPro; IPR027244; IML1.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR13179; PTHR13179; 1.
Pfam; PF00610; DEP; 1.
Pfam; PF12257; IML1; 1.
SMART; SM00049; DEP; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50186; DEP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Epilepsy; GTPase activation; Lysosome; Membrane; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 1603 GATOR complex protein DEPDC5.
/FTId=PRO_0000079865.
DOMAIN 1187 1262 DEP. {ECO:0000255|PROSITE-
ProRule:PRU00066}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 556 559 DVLE -> EHLG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014933.
VAR_SEQ 560 1603 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014934.
VAR_SEQ 624 701 Missing (in isoform 6 and isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_014936.
VAR_SEQ 724 733 ILTLSAPPVV -> M (in isoform 1 and isoform
9). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15770670,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9734811}.
/FTId=VSP_014937.
VAR_SEQ 1089 1110 Missing (in isoform 1, isoform 4 and
isoform 8). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15770670,
ECO:0000303|PubMed:9734811}.
/FTId=VSP_014938.
VAR_SEQ 1230 1338 IMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVA
MQQPATTWHTAGVDDFASFQRKWFEVAFVAEELVHSEIPAF
LLPWLPSRPASYASRHSSFSRSFGGRS -> VMQWPCSSPP
PPGTQQEWTTSPASSASGLRWPLWQKSSCTLRFLPFSCPGC
LTGQPPMQVGTAPLAEVLEDGARRQHF (in isoform
6). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_014939.
VAR_SEQ 1339 1603 Missing (in isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_014940.
VAR_SEQ 1460 1603 FEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKP
QYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCE
ERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCIN
RDNRLVTFWTSCLEKMHASAP -> LGLYKINILPLLLTSL
LRTSLSISTLQEQCFCSCPTPSASSQGSSGGGGTPPAPPTR
TCSARSGSATTGPTTPCSPKHGAPAPQGMKSLLIGC (in
isoform 5). {ECO:0000305}.
/FTId=VSP_014941.
VARIANT 90 90 V -> I (in FFEVF1; does not inhibit
DEPDC5 signaling; does not change kinase
activity of mTORC1; does not change
association with the GATOR complex;
inhibits slightly RRAGA/RRAGC and RRAGB/
RRAGC heterodimer formation;
dbSNP:rs768456731).
{ECO:0000269|PubMed:24591017,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_072363.
VARIANT 214 214 H -> D (in FFEVF1; unknown pathological
significance).
{ECO:0000269|PubMed:26505888}.
/FTId=VAR_077128.
VARIANT 272 272 V -> L (in FFEVF1; does not inhibit
DEPDC5 signaling; does not change kinase
activity of mTORC1; does not change
association with the GATOR complex; does
not change RRAGA/RRAGC and RRAGB/RRAGC
heterodimer formation;
dbSNP:rs187334123).
{ECO:0000269|PubMed:24591017,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_072364.
VARIANT 452 452 A -> V (in FFEVF1; inhibits slightly
DEPDC5 signaling; stimulates slightly
kinase activity of mTORC1; does not
change association with the GATOR
complex; does not change RRAGA/RRAGC and
RRAGB/RRAGC heterodimer formation;
dbSNP:rs202226316).
{ECO:0000269|PubMed:23542697,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_069263.
VARIANT 485 485 R -> Q (in FFEVF1; does not inhibit
DEPDC5 signaling; stimulates slightly
kinase activity of mTORC1; does not
change association with the GATOR
complex; does not change RRAGA/RRAGC and
RRAGB/RRAGC heterodimer formation).
{ECO:0000269|PubMed:23542701,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_069264.
VARIANT 491 491 S -> T (in dbSNP:rs8138516).
/FTId=VAR_024338.
VARIANT 542 542 Q -> P (in FFEVF1; unknown pathological
significance).
{ECO:0000269|PubMed:26505888}.
/FTId=VAR_077129.
VARIANT 641 641 A -> V (in dbSNP:rs16989528).
/FTId=VAR_053953.
VARIANT 712 712 S -> F (in dbSNP:rs16989535).
/FTId=VAR_053954.
VARIANT 864 864 T -> M (in FFEVF1; inhibits slightly
DEPDC5 signaling; does not change kinase
activity of mTORC1; does not change
association with the GATOR complex; does
not change RRAGA/RRAGC and RRAGB/RRAGC
heterodimer formation;
dbSNP:rs564667614).
{ECO:0000269|PubMed:24283814,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_072365.
VARIANT 1065 1065 K -> R (in FFEVF1; unknown pathological
significance; dbSNP:rs757609394).
{ECO:0000269|PubMed:27173016}.
/FTId=VAR_077130.
VARIANT 1073 1073 S -> R (in FFEVF1; inhibits slightly
DEPDC5 signaling; does not change kinase
activity of mTORC1; does not change
association with the GATOR complex; does
not change RRAGA/RRAGC and RRAGB/RRAGC
heterodimer formation;
dbSNP:rs754608531).
{ECO:0000269|PubMed:23542697,
ECO:0000269|PubMed:25366275}.
/FTId=VAR_069265.
VARIANT 1081 1081 T -> P (in FFEVF1; unknown pathological
significance; dbSNP:rs142540948).
{ECO:0000269|PubMed:26505888}.
/FTId=VAR_077131.
VARIANT 1104 1104 S -> L (in FFEVF1; dbSNP:rs79027628).
{ECO:0000269|PubMed:23542697}.
/FTId=VAR_069266.
VARIANT 1154 1154 S -> F (in FFEVF1; unknown pathological
significance; dbSNP:rs578244490).
{ECO:0000269|PubMed:26505888}.
/FTId=VAR_077132.
VARIANT 1162 1162 S -> G (in FFEVF1; does not inhibit
DEPDC5 signaling; does not change kinase
activity of mTORC1; does not change
association with the GATOR complex; does
not change RRAGA/RRAGC and RRAGB/RRAGC
heterodimer formation).
{ECO:0000269|PubMed:25366275}.
/FTId=VAR_072366.
VARIANT 1268 1268 R -> Q (in FFEVF1; unknown pathological
significance).
{ECO:0000269|PubMed:26505888}.
/FTId=VAR_077133.
CONFLICT 1365 1365 D -> G (in Ref. 7; CAH18159).
{ECO:0000305}.
CONFLICT 1430 1430 L -> P (in Ref. 7; CAH18159).
{ECO:0000305}.
CONFLICT 1561 1561 S -> G (in Ref. 7; CAH18159).
{ECO:0000305}.
SEQUENCE 1603 AA; 181264 MW; 19664228B566A080 CRC64;
MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE
DLQKETISVD QTVTQVFRLR PYQDVYVNVV DPKDVTLDLV ELTFKDQYIG RGDMWRLKKS
LVSTCAYITQ KVEFAGIRAQ AGELWVKNEK VMCGYISEDT RVVFRSTSAM VYIFIQMSCE
MWDFDIYGDL YFEKAVNGFL ADLFTKWKEK NCSHEVTVVL FSRTFYDAKS VDEFPEINRA
SIRQDHKGRF YEDFYKVVVQ NERREEWTSL LVTIKKLFIQ YPVLVRLEQA EGFPQGDNST
SAQGNYLEAI NLSFNVFDKH YINRNFDRTG QMSVVITPGV GVFEVDRLLM ILTKQRMIDN
GIGVDLVCMG EQPLHAVPLF KLHNRSAPRD SRLGDDYNIP HWINHSFYTS KSQLFCNSFT
PRIKLAGKKP ASEKAKNGRD TSLGSPKESE NALPIQVDYD AYDAQVFRLP GPSRAQCLTT
CRSVRERESH SRKSASSCDV SSSPSLPSRT LPTEEVRSQA SDDSSLGKSA NILMIPHPHL
HQYEVSSSLG YTSTRDVLEN MMEPPQRDSS APGRFHVGSA ESMLHVRPGG YTPQRALINP
FAPSRMPMKL TSNRRRWMHT FPVGPSGEAI QIHHQTRQNM AELQGSGQRD PTHSSAELLE
LAYHEAAGRH SNSRQPGDGM SFLNFSGTEE LSVGLLSNSG AGMNPRTQNK DSLEDSVSTS
PDPILTLSAP PVVPGFCCTV GVDWKSLTTP ACLPLTTDYF PDRQGLQNDY TEGCYDLLPE
ADIDRRDEDG VQMTAQQVFE EFICQRLMQG YQIIVQPKTQ KPNPAVPPPL SSSPLYSRGL
VSRNRPEEED QYWLSMGRTF HKVTLKDKMI TVTRYLPKYP YESAQIHYTY SLCPSHSDSE
FVSCWVEFSH ERLEEYKWNY LDQYICSAGS EDFSLIESLK FWRTRFLLLP ACVTATKRIT
EGEAHCDIYG DRPRADEDEW QLLDGFVRFV EGLNRIRRRH RSDRMMRKGT AMKGLQMTGP
ISTHSLESTA PPVGKKGTSA LSALLEMEAS QKCLGEQQAA VHGGKSSAQS AESSSVAMTP
TYMDSPRKDG AFFMEFVRSP RTASSAFYPQ VSVDQTATPM LDGTSLGICT GQSMDRGNSQ
TFGNSQNIGE QGYSSTNSSD SSSQQLVASS LTSSSTLTEI LEAMKHPSTG VQLLSEQKGL
SPYCFISAEV VHWLVNHVEG IQTQAMAIDI MQKMLEEQLI THASGEAWRT FIYGFYFYKI
VTDKEPDRVA MQQPATTWHT AGVDDFASFQ RKWFEVAFVA EELVHSEIPA FLLPWLPSRP
ASYASRHSSF SRSFGGRSQA AALLAATVPE QRTVTLDVDV NNRTDRLEWC SCYYHGNFSL
NAAFEIKLHW MAVTAAVLFE MVQGWHRKAT SCGFLLVPVL EGPFALPSYL YGDPLRAQLF
IPLNISCLLK EGSEHLFDSF EPETYWDRMH LFQEAIAHRF GFVQDKYSAS AFNFPAENKP
QYIHVTGTVF LQLPYSKRKF SGQQRRRRNS TSSTNQNMFC EERVGYNWAY NTMLTKTWRS
SATGDEKFAD RLLKDFTDFC INRDNRLVTF WTSCLEKMHA SAP


Related products :

Catalog number Product name Quantity
CSB-EL006728MO Mouse DEP domain-containing protein 5(DEPDC5) ELISA kit 96T
CSB-EL006728HU Human DEP domain-containing protein 5(DEPDC5) ELISA kit 96T
EIAAB10939 DEP domain-containing protein 5,Depdc5,Kiaa0645,Mouse,Mus musculus
CSB-EL006728MO Mouse DEP domain-containing protein 5(DEPDC5) ELISA kit SpeciesMouse 96T
CSB-EL006728HU Human DEP domain-containing protein 5(DEPDC5) ELISA kit SpeciesHuman 96T
DEPD5_MOUSE ELISA Kit FOR DEP domain-containing protein 5; organism: Mouse; gene name: Depdc5 96T
EIAAB10938 DEP domain-containing protein 5,DEPDC5,Homo sapiens,Human,KIAA0645
DEPD5_HUMAN ELISA Kit FOR DEP domain-containing protein 5; organism: Human; gene name: DEPDC5 96T
EIAAB41650 Homo sapiens,Human,T-complex testis-specific protein 3,T-complex-associated testis-expressed protein 3,TCTE3,Tcte-3,Tctex1 domain-containing protein 3,TCTEX1D3
EIAAB44855 E3 ubiquitin-protein ligase subunit KPC2,Kip1 ubiquitination-promoting complex protein 2,Kpc2,Rat,Rattus norvegicus,UBA domain-containing protein 1,Ubac1,Ubadc1,Ubiquitin-associated domain-containing
EIAAB44853 E3 ubiquitin-protein ligase subunit KPC2,Kip1 ubiquitination-promoting complex protein 2,Kpc2,Mouse,Mus musculus,UBA domain-containing protein 1,Ubac1,Ubadc1,Ubiquitin-associated domain-containing pro
31-354 TGFBR2 is a member of the Ser_Thr protein kinase family and the TGFB receptor subfamily. The protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with ano 0.1 mg
DERA DEPDC5 Gene DEP domain containing 5
DEPDC5 DEPDC1B Gene DEP domain containing 1B
EIAAB12853 Elongator complex protein 1,ELP1,ELP1,Homo sapiens,Human,IKAP,IkappaB kinase complex-associated protein,IKBKAP,IKK complex-associated protein,p150
EIAAB12854 Elongator complex protein 1,ELP1,ELP1,IKAP,IkappaB kinase complex-associated protein,IKBKAP,IKK complex-associated protein,Oryctolagus cuniculus,Rabbit
EIAAB12856 Elongator complex protein 1,ELP1,Elp1,Ikap,IkappaB kinase complex-associated protein,Ikbkap,IKK complex-associated protein,Rat,Rattus norvegicus
EIAAB12855 Elongator complex protein 1,ELP1,Elp1,Ikap,IkappaB kinase complex-associated protein,Ikbkap,IKK complex-associated protein,Mouse,Mus musculus
EIAAB37261 Mouse,Mus musculus,SAM domain, SH3 domain and nuclear localization signals protein 1,SAM domain-containing protein SAMSN-1,Samsn1,SH3 protein expressed in lymphocytes 2,SH3-lymphocyte protein 2,SLy2
25-203 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
28-082 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
EIAAB12528 CAP-binding protein complex-interacting protein 1,DJ-1-binding protein,DJBP,DJBP,EFCAB6,EF-hand calcium-binding domain-containing protein 6,Homo sapiens,Human,KIAA1672
EIAAB44856 E3 ubiquitin-protein ligase subunit KPC2,GBDR1,Glialblastoma cell differentiation-related protein 1,Homo sapiens,Human,Kip1 ubiquitination-promoting complex protein 2,KPC2,UBA domain-containing protei
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

france@gentaur.com | Gentaur

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
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
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
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur