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Tuberin (Tuberous sclerosis 2 protein)

 TSC2_HUMAN              Reviewed;        1807 AA.
P49815; A7E2E2; B4DIL8; B4DIQ7; B4DRN2; B7Z2B8; C9J378; O75275;
Q4LE71; Q8TAZ1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
25-OCT-2017, entry version 196.
RecName: Full=Tuberin;
AltName: Full=Tuberous sclerosis 2 protein;
Name=TSC2; Synonyms=TSC4;
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), AND VARIANT ARG-802.
TISSUE=Brain;
PubMed=8269512; DOI=10.1016/0092-8674(93)90618-Z;
The European chromosome 16 tuberous sclerosis consortium;
Nellist M., Janssen B., Brook-Carter P.T., Hesseling-Janssen A.L.W.,
Maheshwar M.M., Verhoef S., van den Ouweland A.M.W., Lindhout D.,
Eussen B., Cordeiro I., Santos H., Halley D.J.J., Sampson J.R.,
Ward C.J., Peral B., Thomas S., Hughes J., Harris P.C.,
Roelfsema J.H., Saris J.J., Spruit L., Peters D.J.M., Dauwerse J.G.,
Breuning M.H.;
"Identification and characterization of the tuberous sclerosis gene on
chromosome 16.";
Cell 75:1305-1315(1993).
[2]
SEQUENCE REVISION.
Sampson J.R.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1; 2 AND 3).
PubMed=7558029; DOI=10.1006/geno.1995.1079;
Xu L., Sterner C., Maheshwar M.M., Wilson P.J., Nellist M.,
Short M.P., Haines J.L., Sampson J.R., Ramesh V.;
"Alternative splicing of the tuberous sclerosis 2 (TSC2) gene in human
and mouse tissues.";
Genomics 27:475-480(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-94; PHE-320;
PHE-619 AND ARG-802.
PubMed=8789450; DOI=10.1093/hmg/5.1.131;
Maheshwar M.M., Sandford R., Nellist M., Cheadle J.P., Sgotto B.,
Vaudin M., Sampson J.R.;
"Comparative analysis and genomic structure of the tuberous sclerosis
2 (TSC2) gene in human and pufferfish.";
Hum. Mol. Genet. 5:131-137(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
TISSUE=Brain;
PubMed=24722188; DOI=10.1038/ncomms4650;
Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L.,
Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S.,
Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.,
Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S.,
Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M.,
Iakoucheva L.M.;
"Protein interaction network of alternatively spliced isoforms from
brain links genetic risk factors for autism.";
Nat. Commun. 5:3650-3650(2014).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6; 7 AND 8).
TISSUE=Amygdala, and Hippocampus;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Aortic endothelium;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-199.
TISSUE=Placenta;
PubMed=9831664; DOI=10.1016/S0378-1119(98)00485-5;
Imai K., Sarker A.H., Akiyama K., Ikeda S., Yao M., Tsutsui K.,
Shohmori T., Seki S.;
"Genomic structure and sequence of a human homologue (NTHL1/NTH1) of
Escherichia coli endonuclease III with those of the adjacent parts of
TSC2 and SLC9A3R2 genes.";
Gene 222:287-295(1998).
[12]
INTERACTION WITH RABEP1.
PubMed=9045618; DOI=10.1074/jbc.272.10.6097;
Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S.;
"The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5
GTPase activating protein (GAP) in modulating endocytosis.";
J. Biol. Chem. 272:6097-6100(1997).
[13]
INTERACTION WITH TSC1.
PubMed=9580671; DOI=10.1093/hmg/7.6.1053;
van Slegtenhorst M.A., Nellist M., Nagelkerken B., Cheadle J.P.,
Snell R.G., van den Ouweland A.M.W., Reuser A., Sampson J.R.,
Halley D.J.J., van der Sluijs P.;
"Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
products.";
Hum. Mol. Genet. 7:1053-1057(1998).
[14]
INTERACTION WITH TSC1.
PubMed=10585443; DOI=10.1074/jbc.274.50.35647;
Nellist M., van Slegtenhorst M.A., Goedbloed M.,
van den Ouweland A.M.W., Halley D.J.J., van der Sluijs P.;
"Characterization of the cytosolic tuberin-hamartin complex. Tuberin
is a cytosolic chaperone for hamartin.";
J. Biol. Chem. 274:35647-35652(1999).
[15]
INVOLVEMENT IN LAM.
PubMed=11829138; DOI=10.1007/s10038-002-8651-8;
Sato T., Seyama K., Fujii H., Maruyama H., Setoguchi Y., Iwakami S.,
Fukuchi Y., Hino O.;
"Mutation analysis of the TSC1 and TSC2 genes in Japanese patients
with pulmonary lymphangioleiomyomatosis.";
J. Hum. Genet. 47:20-28(2002).
[16]
PHOSPHORYLATION AT SER-939 AND THR-1462.
PubMed=12150915; DOI=10.1016/S1097-2765(02)00568-3;
Manning B.D., Tee A.R., Logsdon M.N., Blenis J., Cantley L.C.;
"Identification of the tuberous sclerosis complex-2 tumor suppressor
gene product tuberin as a target of the phosphoinositide 3-kinase/akt
pathway.";
Mol. Cell 10:151-162(2002).
[17]
FUNCTION, AND CHARACTERIZATION OF VARIANTS TSC2 MET-599 AND SER-1651.
PubMed=12271141; DOI=10.1073/pnas.202476899;
Tee A.R., Fingar D.C., Manning B.D., Kwiatkowski D.J., Cantley L.C.,
Blenis J.;
"Tuberous sclerosis complex-1 and -2 gene products function together
to inhibit mammalian target of rapamycin (mTOR)-mediated downstream
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 99:13571-13576(2002).
[18]
PHOSPHORYLATION AT THR-1330 AND SER-1448, AND MUTAGENESIS OF THR-1330
AND SER-1448.
PubMed=14651849; DOI=10.1016/S0092-8674(03)00929-2;
Inoki K., Zhu T., Guan K.L.;
"TSC2 mediates cellular energy response to control cell growth and
survival.";
Cell 115:577-590(2003).
[19]
FUNCTION, MUTAGENESIS OF 1637-LYS--ARG-1639; ARG-1745 AND
1749-ARG--ARG-1751, AND CHARACTERIZATION OF VARIANTS TSC2 LYS-1643;
SER-1651; LYS-1681 AND PRO-1743.
PubMed=15340059; DOI=10.1128/MCB.24.18.7965-7975.2004;
Li Y., Inoki K., Guan K.-L.;
"Biochemical and functional characterizations of small GTPase Rheb and
TSC2 GAP activity.";
Mol. Cell. Biol. 24:7965-7975(2004).
[20]
PHOSPHORYLATION AT SER-1798.
PubMed=15342917; DOI=10.1073/pnas.0405659101;
Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J.;
"Tumor-promoting phorbol esters and activated Ras inactivate the
tuberous sclerosis tumor suppressor complex via p90 ribosomal S6
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 101:13489-13494(2004).
[21]
PHOSPHORYLATION AT SER-1387; SER-1418 AND SER-1420, IDENTIFICATION BY
MASS SPECTROMETRY, INTERACTION WITH HSPA1; HSPA8 AND TSC1, AND
CHARACTERIZATION OF VARIANTS TSC2 TRP-611 AND GLN-611.
PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175;
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,
Luider T.M.;
"Phosphorylation and binding partner analysis of the TSC1-TSC2
complex.";
Biochem. Biophys. Res. Commun. 333:818-826(2005).
[22]
FUNCTION IN PROTEIN TRANSPORT.
PubMed=16707451; DOI=10.1158/0008-5472.CAN-05-4510;
Jiang X., Yeung R.S.;
"Regulation of microtubule-dependent protein transport by the
TSC2/mammalian target of rapamycin pathway.";
Cancer Res. 66:5258-5269(2006).
[23]
INTERACTION WITH HERC1 AND TSC1.
PubMed=16464865; DOI=10.1074/jbc.C500451200;
Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R.,
Rosa J.L., Guan K.-L.;
"TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and
the HERC1 ubiquitin ligase.";
J. Biol. Chem. 281:8313-8316(2006).
[24]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL38.
PubMed=18407068; DOI=10.1016/j.chom.2008.03.002;
Moorman N.J., Cristea I.M., Terhune S.S., Rout M.P., Chait B.T.,
Shenk T.;
"Human cytomegalovirus protein UL38 inhibits host cell stress
responses by antagonizing the tuberous sclerosis protein complex.";
Cell Host Microbe 3:253-262(2008).
[25]
UBIQUITINATION BY MYCBP2, PHOSPHORYLATION AT SER-540; SER-664;
SER-939; THR-1462 AND SER-1798, AND CHARACTERIZATION OF VARIANT
GLN-611.
PubMed=18308511; DOI=10.1016/j.cellsig.2008.01.020;
Han S., Witt R.M., Santos T.M., Polizzano C., Sabatini B.L.,
Ramesh V.;
"Pam (Protein associated with Myc) functions as an E3 ubiquitin ligase
and regulates TSC/mTOR signaling.";
Cell. Signal. 20:1084-1091(2008).
[26]
UBIQUITINATION, AND INTERACTION WITH FBXW5.
PubMed=18381890; DOI=10.1101/gad.1624008;
Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J.,
Xiong Y.;
"WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by
DDB1-CUL4-ROC1 ligase.";
Genes Dev. 22:866-871(2008).
[27]
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).
[28]
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-927; SER-981; SER-1132;
SER-1155; SER-1337; SER-1338; SER-1387; SER-1411; SER-1420 AND
SER-1452, 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).
[30]
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).
[31]
PHOSPHORYLATION BY DAPK1, AND INTERACTION WITH DAPK1.
PubMed=18974095; DOI=10.1074/jbc.M805165200;
Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
Hupp T.;
"Peptide combinatorial libraries identify TSC2 as a death-associated
protein kinase (DAPK) death domain-binding protein and reveal a
stimulatory role for DAPK in mTORC1 signaling.";
J. Biol. Chem. 284:334-344(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155; THR-1462 AND
SER-1798, 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1346 AND SER-1798, 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).
[34]
INTERACTION WITH NAA10.
PubMed=20145209; DOI=10.1126/scisignal.2000590;
Kuo H.P., Lee D.F., Chen C.T., Liu M., Chou C.K., Lee H.J., Du Y.,
Xie X., Wei Y., Xia W., Weihua Z., Yang J.Y., Yen C.J., Huang T.H.,
Tan M., Xing G., Zhao Y., Lin C.H., Tsai S.F., Fidler I.J., Hung M.C.;
"ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR
signaling pathway.";
Sci. Signal. 3:RA9-RA9(2010).
[35]
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).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1132, 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).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-981; SER-1346; SER-1364;
SER-1411; SER-1420; SER-1452 AND SER-1799, 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).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1411, 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).
[39]
INTERACTION WITH RRAGA.
PubMed=25936802; DOI=10.1016/j.molcel.2015.03.033;
Deng L., Jiang C., Chen L., Jin J., Wei J., Zhao L., Chen M., Pan W.,
Xu Y., Chu H., Wang X., Ge X., Li D., Liao L., Liu M., Li L., Wang P.;
"The ubiquitination of RagA GTPase by RNF152 negatively regulates
mTORC1 activation.";
Mol. Cell 58:804-818(2015).
[40]
FUNCTION, INTERACTION WITH TSC1, INVOLVEMENT IN FCORD2, VARIANT FCORD2
ILE-1547, AND CHARACTERIZATION OF VARIANT FCORD2 ILE-1547.
PubMed=28215400; DOI=10.1016/j.ajhg.2017.01.030;
Lim J.S., Gopalappa R., Kim S.H., Ramakrishna S., Lee M., Kim W.I.,
Kim J., Park S.M., Lee J., Oh J.H., Kim H.D., Park C.H., Lee J.S.,
Kim S., Kim D.S., Han J.M., Kang H.C., Kim H.H., Lee J.H.;
"Somatic mutations in TSC1 and TSC2 cause focal cortical dysplasia.";
Am. J. Hum. Genet. 100:454-472(2017).
[41]
VARIANTS TSC2 ILE-449; TRP-611; LEU-1227; TRP-1240; PHE-1509 DEL AND
GLU-1712.
PubMed=8824881; DOI=10.1093/hmg/5.2.249;
Wilson P.J., Ramesh V., Kristiansen A., Bove C., Jozwiak S.,
Kwiatkowski D.J., Short M.P., Haines J.L.;
"Novel mutations detected in the TSC2 gene from both sporadic and
familial TSC patients.";
Hum. Mol. Genet. 5:249-256(1996).
[42]
VARIANTS TSC2 PHE-1509 DEL; MET-1594; LYS-1643; SER-1651; LEU-1675 AND
LYS-1681.
PubMed=9302281; DOI=10.1093/hmg/6.11.1991;
Maheshwar M.M., Cheadle J.P., Jones A.C., Myring J., Fryer A.E.,
Harris P.C., Sampson J.R.;
"The GAP-related domain of tuberin, the product of the TSC2 gene, is a
target for missense mutations in tuberous sclerosis.";
Hum. Mol. Genet. 6:1991-1996(1997).
[43]
VARIANTS TSC2.
PubMed=9463313; DOI=10.1086/301705;
Au K.-S., Rodriguez J.A., Finch J.L., Volcik K.A., Roach E.S.,
Delgado M.R., Rodriguez E. Jr., Northrup H.;
"Germ-line mutational analysis of the TSC2 gene in 90 tuberous-
sclerosis patients.";
Am. J. Hum. Genet. 62:286-294(1998).
[44]
VARIANTS TSC2.
PubMed=9829910;
DOI=10.1002/(SICI)1098-1004(1998)12:6<408::AID-HUMU7>3.0.CO;2-P;
Beauchamp R.L., Banwell A., McNamara P., Jacobsen M., Higgins E.,
Northrup H., Short M.P., Sims K., Ozelius L., Ramesh V.;
"Exon scanning of the entire TSC2 gene for germline mutations in 40
unrelated patients with tuberous sclerosis.";
Hum. Mutat. 12:408-416(1998).
[45]
VARIANTS TSC2.
PubMed=10732801; DOI=10.1007/s100480050039;
Gilbert J.R., Guy V., Kumar A., Wolpert C., Kandt R., Aylesworth A.,
Roses A.D., Pericak-Vance M.A.;
"Mutation and polymorphism analysis in the tuberous sclerosis 2 (TSC2)
gene.";
Neurogenetics 1:267-272(1998).
[46]
VARIANTS TSC2, AND VARIANTS.
PubMed=10205261; DOI=10.1086/302381;
Jones A.C., Shyamsundar M.M., Thomas M.W., Maynard J.,
Idziaszczyk S.A., Tomkins S., Sampson J.R., Cheadle J.P.;
"Comprehensive mutation analysis of TSC1 and TSC2- and phenotypic
correlations in 150 families with tuberous sclerosis.";
Am. J. Hum. Genet. 64:1305-1315(1999).
[47]
VARIANT TSC2 ARG-717.
PubMed=10069705;
DOI=10.1002/(SICI)1096-8628(19990219)82:5<368::AID-AJMG2>3.0.CO;2-I;
Zhang H., Yamamoto T., Nanba E., Kitamura Y., Terada T., Akaboshi S.,
Yuasa I., Ohtani K., Nakamoto S., Takeshita K., Ohno K.;
"Novel TSC2 mutation in a patient with pulmonary tuberous sclerosis:
lack of loss of heterozygosity in a lung cyst.";
Am. J. Med. Genet. 82:368-370(1999).
[48]
VARIANTS TSC2, AND VARIANTS.
PubMed=10735580; DOI=10.1046/j.1469-1809.1999.6350383.x;
Choy Y.S., Dabora S.L., Hall F., Ramesh V., Niida Y., Franz D.,
Kasprzyk-Obara J., Reeve M.P., Kwiatkowski D.J.;
"Superiority of denaturing high performance liquid chromatography over
single-stranded conformation and conformation-sensitive gel
electrophoresis for mutation detection in TSC2.";
Ann. Hum. Genet. 63:383-391(1999).
[49]
VARIANTS TSC2, AND VARIANTS.
TISSUE=Blood, and Lymphoblast;
PubMed=10533067;
DOI=10.1002/(SICI)1098-1004(199911)14:5<412::AID-HUMU7>3.0.CO;2-K;
Niida Y., Lawrence-Smith N., Banwell A., Hammer E., Lewis J.,
Beauchamp R.L., Sims K., Ramesh V., Ozelius L.;
"Analysis of both TSC1 and TSC2 for germline mutations in 126
unrelated patients with tuberous sclerosis.";
Hum. Mutat. 14:412-422(1999).
[50]
VARIANTS TSC2 ARG-137; GLN-611; ASN-647; ARG-717; GLU-769; MET-963 AND
LEU-1675, VARIANT PHE-320, AND POSSIBLE ASSOCIATION WITH TSC.
PubMed=10570911; DOI=10.1007/s100380050185;
Zhang H., Nanba E., Yamamoto T., Ninomiya H., Ohno K., Mizuguchi M.,
Takeshita K.;
"Mutational analysis of TSC1 and TSC2 genes in Japanese patients with
tuberous sclerosis complex.";
J. Hum. Genet. 44:391-396(1999).
[51]
VARIANTS TSC2 TRP-611; TRP-905; PRO-1744 AND 1746-HIS--ARG-1751 DEL,
AND VARIANT PHE-320.
TISSUE=Peripheral blood leukocyte;
PubMed=10607950;
DOI=10.1002/(SICI)1096-8628(20000117)90:2<123::AID-AJMG7>3.3.CO;2-C;
Yamashita Y., Ono J., Okada S., Wataya-Kaneda M., Yoshikawa K.,
Nishizawa M., Hirayama Y., Kobayashi E., Seyama K., Hino O.;
"Analysis of all exons of TSC1 and TSC2 genes for germline mutations
in Japanese patients with tuberous sclerosis: report of 10
mutations.";
Am. J. Med. Genet. 90:123-126(2000).
[52]
VARIANT LAM GLN-611.
PubMed=10823953; DOI=10.1073/pnas.97.11.6085;
Carsillo T., Astrinidis A., Henske E.P.;
"Mutations in the tuberous sclerosis complex gene TSC2 are a cause of
sporadic pulmonary lymphangioleiomyomatosis.";
Proc. Natl. Acad. Sci. U.S.A. 97:6085-6090(2000).
[53]
VARIANTS TSC2 SER-1651; PHE-1653; LEU-1675 AND 1746-HIS--ARG-1751 DEL,
AND VARIANTS THR-607; VAL-862; SER-1429 AND ARG-1450.
PubMed=15024740; DOI=10.1002/humu.9225;
Feng J.-H., Yamamoto T., Nanba E., Ninomiya H., Oka A., Ohno K.;
"Novel TSC2 mutations and decreased expression of tuberin in cultured
tumor cells with an insertion mutation.";
Hum. Mutat. 23:397-397(2004).
[54]
VARIANTS TSC2 GLN-611; TRP-611 AND PRO-1027, AND VARIANTS GLN-367;
ARG-1341; ASN-1636 AND LEU-1673.
PubMed=15595939; DOI=10.1111/j.1600-0404.2004.00366.x;
Ali M., Girimaji S.C., Markandaya M., Shukla A.K., Sacchidanand S.,
Kumar A.;
"Mutation and polymorphism analysis of TSC1 and TSC2 genes in Indian
patients with tuberous sclerosis complex.";
Acta Neurol. Scand. 111:54-63(2005).
-!- FUNCTION: In complex with TSC1, this tumor suppressor inhibits the
nutrient-mediated or growth factor-stimulated phosphorylation of
S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Acts
as a GTPase-activating protein (GAP) for the small GTPase RHEB, a
direct activator of the protein kinase activity of mTORC1. May
also play a role in microtubule-mediated protein transport. Also
stimulates the intrinsic GTPase activity of the Ras-related
proteins RAP1A and RAB5. {ECO:0000269|PubMed:12271141,
ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:16707451,
ECO:0000269|PubMed:28215400}.
-!- SUBUNIT: Interacts with TSC1 and HERC1; the interaction with TSC1
stabilizes TSC2 and prevents the interaction with HERC1
(PubMed:9580671, PubMed:10585443, PubMed:15963462,
PubMed:16464865). May also interact with the adapter molecule
RABEP1 (PubMed:9045618). The final complex contains TSC2 and
RABEP1 linked to RAB5 (Probable). Interacts with HSPA1 and HSPA8
(PubMed:15963462). Interacts with DAPK1 (PubMed:18974095).
Interacts with FBXW5 (PubMed:18381890). Interacts with NAA10 (via
C-terminal domain) (PubMed:20145209). Interacts with RRAGA
(polyubiquitinated) (PubMed:25936802). Interacts with human
cytomegalovirus protein UL38; this interaction inhibits cellular
stress response mediated by mTORC1 (PubMed:18407068).
{ECO:0000269|PubMed:10585443, ECO:0000269|PubMed:15963462,
ECO:0000269|PubMed:16464865, ECO:0000269|PubMed:18381890,
ECO:0000269|PubMed:18407068, ECO:0000269|PubMed:18974095,
ECO:0000269|PubMed:20145209, ECO:0000269|PubMed:25936802,
ECO:0000269|PubMed:28215400, ECO:0000269|PubMed:9045618,
ECO:0000269|PubMed:9580671, ECO:0000305}.
-!- INTERACTION:
P62136:PPP1CA; NbExp=2; IntAct=EBI-396587, EBI-357253;
O00141:SGK1; NbExp=4; IntAct=EBI-396587, EBI-1042854;
Q96EB6:SIRT1; NbExp=2; IntAct=EBI-396587, EBI-1802965;
Q92574:TSC1; NbExp=10; IntAct=EBI-396587, EBI-1047085;
P31946:YWHAB; NbExp=4; IntAct=EBI-396587, EBI-359815;
P63104:YWHAZ; NbExp=7; IntAct=EBI-396587, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein. Note=At steady state found in association with membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=P49815-1; Sequence=Displayed;
Name=2;
IsoId=P49815-2; Sequence=VSP_004470;
Note=No experimental confirmation available.;
Name=3;
IsoId=P49815-3; Sequence=VSP_004471;
Note=No experimental confirmation available.;
Name=4;
IsoId=P49815-4; Sequence=VSP_004472;
Name=5;
IsoId=P49815-5; Sequence=VSP_004471, VSP_004472;
Name=6;
IsoId=P49815-6; Sequence=VSP_038355, VSP_004470, VSP_004472;
Name=7;
IsoId=P49815-7; Sequence=VSP_054163, VSP_004470, VSP_004472;
Note=No experimental confirmation available.;
Name=8; Synonyms=H, I;
IsoId=P49815-8; Sequence=VSP_055896, VSP_055897;
Note=May be due to an intron retention.;
-!- TISSUE SPECIFICITY: Liver, brain, heart, lymphocytes, fibroblasts,
biliary epithelium, pancreas, skeletal muscle, kidney, lung and
placenta.
-!- PTM: Phosphorylation at Ser-1387, Ser-1418 or Ser-1420 does not
affect interaction with TSC1. Phosphorylation at Ser-939 and Thr-
1462 by PKB/AKT1 is induced by growth factor stimulation.
Phosphorylation by AMPK activates it and leads to negatively
regulates the mTORC1 complex. Phosphorylated at Ser-1798 by
RPS6KA1; phosphorylation inhibits TSC2 ability to suppress mTORC1
signaling. Phosphorylated by DAPK1. {ECO:0000269|PubMed:12150915,
ECO:0000269|PubMed:15342917, ECO:0000269|PubMed:15963462,
ECO:0000269|PubMed:18308511}.
-!- PTM: Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase
complex, leading to its subsequent degradation. Ubiquitinated by
MYCBP2 independently of its phosphorylation status leading to
subsequent degradation; association with TSC1 protects from
ubiquitination. {ECO:0000269|PubMed:18308511,
ECO:0000269|PubMed:18381890}.
-!- DISEASE: Tuberous sclerosis 2 (TSC2) [MIM:613254]: An autosomal
dominant multi-system disorder that affects especially the brain,
kidneys, heart, and skin. It is characterized by hamartomas
(benign overgrowths predominantly of a cell or tissue type that
occurs normally in the organ) and hamartias (developmental
abnormalities of tissue combination). Clinical manifestations
include epilepsy, learning difficulties, behavioral problems, and
skin lesions. Seizures can be intractable and premature death can
occur from a variety of disease-associated causes.
{ECO:0000269|PubMed:10069705, ECO:0000269|PubMed:10205261,
ECO:0000269|PubMed:10533067, ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:10607950, ECO:0000269|PubMed:10732801,
ECO:0000269|PubMed:10735580, ECO:0000269|PubMed:12271141,
ECO:0000269|PubMed:15024740, ECO:0000269|PubMed:15340059,
ECO:0000269|PubMed:15595939, ECO:0000269|PubMed:15963462,
ECO:0000269|PubMed:8824881, ECO:0000269|PubMed:9302281,
ECO:0000269|PubMed:9463313, ECO:0000269|PubMed:9829910}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Lymphangioleiomyomatosis (LAM) [MIM:606690]: Progressive
and often fatal lung disease characterized by a diffuse
proliferation of abnormal smooth muscle cells in the lungs. It
affects almost exclusively young women and can occur as an
isolated disorder or in association with tuberous sclerosis
complex. {ECO:0000269|PubMed:10823953,
ECO:0000269|PubMed:11829138}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Focal cortical dysplasia 2 (FCORD2) [MIM:607341]: A form
of focal cortical dysplasia, a malformation of cortical
development that results in medically refractory epilepsy in the
pediatric population and in adults. FCORD2 is a severe form, with
onset usually in childhood, characterized by disrupted cortical
lamination and specific cytological abnormalities. It is
classified in 2 subtypes: type IIA characterized by dysmorphic
neurons and lack of balloon cells; type IIB with dysmorphic
neurons and balloon cells. {ECO:0000269|PubMed:28215400}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SEQUENCE CAUTION:
Sequence=BAE06082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TSC2ID184.html";
-!- WEB RESOURCE: Name=Tuberous sclerosis database Tuberous sclerosis
2 (TSC2); Note=Leiden Open Variation Database (LOVD);
URL="http://www.LOVD.nl/TSC2";
-----------------------------------------------------------------------
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EMBL; X75621; CAA53287.1; -; mRNA.
EMBL; L48546; AAB41564.1; -; Genomic_DNA.
EMBL; L48517; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48518; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48519; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48521; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48522; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48523; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48524; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48525; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48526; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48527; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48528; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48529; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48530; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48531; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48532; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48533; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48534; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48535; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48536; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48537; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48538; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48539; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48540; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48541; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48542; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48543; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48544; AAB41564.1; JOINED; Genomic_DNA.
EMBL; L48545; AAB41564.1; JOINED; Genomic_DNA.
EMBL; KJ535038; AHW56677.1; -; mRNA.
EMBL; KJ535051; AHW56690.1; -; mRNA.
EMBL; AK294548; BAH11804.1; -; mRNA.
EMBL; AK295672; BAG58530.1; -; mRNA.
EMBL; AK295728; BAG58569.1; -; mRNA.
EMBL; AK299343; BAG61344.1; -; mRNA.
EMBL; AB210000; BAE06082.1; ALT_INIT; mRNA.
EMBL; AC005600; AAC34210.1; -; Genomic_DNA.
EMBL; AC093513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85556.1; -; Genomic_DNA.
EMBL; BC150300; AAI50301.1; -; mRNA.
EMBL; BC025364; AAH25364.1; -; mRNA.
EMBL; BC046929; AAH46929.1; -; mRNA.
EMBL; AB014460; BAA32694.1; -; Genomic_DNA.
CCDS; CCDS10458.1; -. [P49815-1]
CCDS; CCDS45384.1; -. [P49815-4]
CCDS; CCDS58408.1; -. [P49815-5]
CCDS; CCDS81933.1; -. [P49815-6]
CCDS; CCDS81934.1; -. [P49815-7]
PIR; A49420; A49420.
RefSeq; NP_000539.2; NM_000548.4. [P49815-1]
RefSeq; NP_001070651.1; NM_001077183.2. [P49815-5]
RefSeq; NP_001107854.1; NM_001114382.2. [P49815-4]
RefSeq; NP_001305756.1; NM_001318827.1. [P49815-6]
RefSeq; NP_001305758.1; NM_001318829.1. [P49815-7]
RefSeq; NP_001305760.1; NM_001318831.1.
RefSeq; NP_001305761.1; NM_001318832.1.
RefSeq; XP_005255586.2; XM_005255529.4. [P49815-2]
RefSeq; XP_016879105.1; XM_017023616.1. [P49815-3]
UniGene; Hs.90303; -.
ProteinModelPortal; P49815; -.
BioGrid; 113100; 75.
CORUM; P49815; -.
IntAct; P49815; 20.
MINT; MINT-250244; -.
STRING; 9606.ENSP00000219476; -.
iPTMnet; P49815; -.
PhosphoSitePlus; P49815; -.
SwissPalm; P49815; -.
BioMuta; TSC2; -.
DMDM; 269849475; -.
EPD; P49815; -.
MaxQB; P49815; -.
PaxDb; P49815; -.
PeptideAtlas; P49815; -.
PRIDE; P49815; -.
Ensembl; ENST00000219476; ENSP00000219476; ENSG00000103197. [P49815-1]
Ensembl; ENST00000350773; ENSP00000344383; ENSG00000103197. [P49815-4]
Ensembl; ENST00000382538; ENSP00000371978; ENSG00000103197. [P49815-7]
Ensembl; ENST00000401874; ENSP00000384468; ENSG00000103197. [P49815-5]
Ensembl; ENST00000439673; ENSP00000399232; ENSG00000103197. [P49815-6]
GeneID; 7249; -.
KEGG; hsa:7249; -.
UCSC; uc002con.4; human. [P49815-1]
CTD; 7249; -.
DisGeNET; 7249; -.
EuPathDB; HostDB:ENSG00000103197.16; -.
GeneCards; TSC2; -.
GeneReviews; TSC2; -.
HGNC; HGNC:12363; TSC2.
HPA; CAB002225; -.
HPA; HPA030409; -.
HPA; HPA049679; -.
MalaCards; TSC2; -.
MIM; 191092; gene.
MIM; 606690; phenotype.
MIM; 607341; phenotype.
MIM; 613254; phenotype.
neXtProt; NX_P49815; -.
OpenTargets; ENSG00000103197; -.
Orphanet; 88924; Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis.
Orphanet; 538; Lymphangioleiomyomatosis.
Orphanet; 805; Tuberous sclerosis.
PharmGKB; PA37035; -.
eggNOG; KOG3687; Eukaryota.
eggNOG; ENOG410XPFJ; LUCA.
GeneTree; ENSGT00760000119182; -.
HOGENOM; HOG000045987; -.
HOVERGEN; HBG018005; -.
InParanoid; P49815; -.
KO; K07207; -.
OMA; VTWDILL; -.
OrthoDB; EOG091G00O2; -.
PhylomeDB; P49815; -.
TreeFam; TF324484; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165181; Inhibition of TSC complex formation by PKB.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-8854214; TBC/RABGAPs.
SignaLink; P49815; -.
SIGNOR; P49815; -.
GeneWiki; TSC2; -.
GenomeRNAi; 7249; -.
PRO; PR:P49815; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103197; -.
CleanEx; HS_TSC2; -.
ExpressionAtlas; P49815; baseline and differential.
Genevisible; P49815; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0033596; C:TSC1-TSC2 complex; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
GO; GO:0043276; P:anoikis; IGI:ParkinsonsUK-UCL.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0006897; P:endocytosis; TAS:ProtInc.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:1901525; P:negative regulation of mitophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; IGI:ParkinsonsUK-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IGI:ParkinsonsUK-UCL.
GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0008104; P:protein localization; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0030100; P:regulation of endocytosis; ISS:UniProtKB.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR035974; Rap/Ran-GAP_sf.
InterPro; IPR000331; Rap_GAP_dom.
InterPro; IPR003913; Tuberin.
InterPro; IPR018515; Tuberin-type_domain.
InterPro; IPR027107; Tuberin/Ral-act_asu.
InterPro; IPR024584; Tuberin_N.
PANTHER; PTHR10063; PTHR10063; 1.
Pfam; PF11864; DUF3384; 1.
Pfam; PF02145; Rap_GAP; 1.
Pfam; PF03542; Tuberin; 1.
PRINTS; PR01431; TUBERIN.
SUPFAM; SSF111347; SSF111347; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50085; RAPGAP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Epilepsy; GTPase activation; Host-virus interaction; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Tumor suppressor;
Ubl conjugation.
CHAIN 1 1807 Tuberin.
/FTId=PRO_0000065654.
DOMAIN 1531 1758 Rap-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00165}.
REGION 1 400 Required for interaction with TSC1.
MOD_RES 540 540 Phosphoserine.
{ECO:0000269|PubMed:18308511}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000269|PubMed:18308511}.
MOD_RES 927 927 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 939 939 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:12150915,
ECO:0000269|PubMed:18308511}.
MOD_RES 981 981 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1132 1132 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1330 1330 Phosphothreonine; by AMPK.
{ECO:0000269|PubMed:14651849}.
MOD_RES 1337 1337 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1346 1346 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1364 1364 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1387 1387 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:15963462}.
MOD_RES 1411 1411 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1418 1418 Phosphoserine.
{ECO:0000269|PubMed:15963462}.
MOD_RES 1420 1420 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15963462}.
MOD_RES 1448 1448 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:14651849}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1462 1462 Phosphothreonine; by PKB/AKT1.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:12150915,
ECO:0000269|PubMed:18308511}.
MOD_RES 1764 1764 Phosphoserine.
{ECO:0000250|UniProtKB:Q61037}.
MOD_RES 1798 1798 Phosphoserine; by RPS6KA1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15342917,
ECO:0000269|PubMed:18308511}.
MOD_RES 1799 1799 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 49 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054163.
VAR_SEQ 76 112 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038355.
VAR_SEQ 113 239 GERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHI
TYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEY
IARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAES
LPLF -> VRPRATLGWVTSGCPLTVLSLLGRVWTPASVSC
WAQGLGADGLWSWMACGVSWCHEVCVTVGTASSPVNRWSLH
LPLMGCSGDHMRQFSQSAEIVPGSWCGATVLFCPCTLSGPL
PCSLHSICAGLG (in isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:24722188}.
/FTId=VSP_055896.
VAR_SEQ 240 1807 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:24722188}.
/FTId=VSP_055897.
VAR_SEQ 946 989 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.7}.
/FTId=VSP_004471.
VAR_SEQ 946 988 Missing (in isoform 2, isoform 6 and
isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_004470.
VAR_SEQ 1272 1294 Missing (in isoform 4, isoform 5, isoform
6 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7}.
/FTId=VSP_004472.
VARIANT 94 94 P -> T (in dbSNP:rs1051616).
{ECO:0000269|PubMed:8789450}.
/FTId=VAR_008019.
VARIANT 137 137 H -> R (in TSC2; unknown pathological
significance; dbSNP:rs45517107).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009415.
VARIANT 160 160 L -> V (in dbSNP:rs45517109).
/FTId=VAR_009416.
VARIANT 227 227 C -> Y (in TSC2; dbSNP:rs45517122).
/FTId=VAR_008020.
VARIANT 258 258 K -> N (in TSC2; dbSNP:rs137854875).
/FTId=VAR_009417.
VARIANT 261 261 R -> P (in TSC2; dbSNP:rs45502703).
/FTId=VAR_009418.
VARIANT 261 261 R -> W (in dbSNP:rs45517130).
/FTId=VAR_009419.
VARIANT 286 286 M -> T (in dbSNP:rs45517136).
/FTId=VAR_009420.
VARIANT 286 286 M -> V (in dbSNP:rs1800748).
/FTId=VAR_009421.
VARIANT 292 292 L -> P (in TSC2; dbSNP:rs45517138).
/FTId=VAR_005646.
VARIANT 294 294 G -> E (in TSC2; dbSNP:rs45487497).
/FTId=VAR_009422.
VARIANT 304 304 W -> WGMALW (in TSC2).
/FTId=VAR_009423.
VARIANT 309 309 L -> Q (in dbSNP:rs137853986).
/FTId=VAR_009424.
VARIANT 320 320 L -> F (could be associated with TSC2;
dbSNP:rs1131825).
{ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:10607950,
ECO:0000269|PubMed:8789450}.
/FTId=VAR_009425.
VARIANT 331 331 N -> K (in TSC2; dbSNP:rs45517153).
/FTId=VAR_008021.
VARIANT 361 361 L -> P (in TSC2; dbSNP:rs45517147).
/FTId=VAR_009426.
VARIANT 365 365 Missing (in TSC2).
/FTId=VAR_009427.
VARIANT 367 367 R -> Q (in dbSNP:rs1800725).
{ECO:0000269|PubMed:15595939}.
/FTId=VAR_009428.
VARIANT 378 378 P -> L (in dbSNP:rs45517154).
/FTId=VAR_009429.
VARIANT 407 407 Y -> D (in TSC2; dbSNP:rs45517156).
/FTId=VAR_005647.
VARIANT 440 440 G -> S (in dbSNP:rs45484298).
/FTId=VAR_009430.
VARIANT 449 449 M -> I (in TSC2; dbSNP:rs45443091).
{ECO:0000269|PubMed:8824881}.
/FTId=VAR_005648.
VARIANT 463 463 I -> V (in dbSNP:rs45517171).
/FTId=VAR_009431.
VARIANT 486 486 N -> I (in TSC2; dbSNP:rs45486599).
/FTId=VAR_008022.
VARIANT 490 490 I -> V (in dbSNP:rs45517175).
/FTId=VAR_008023.
VARIANT 525 525 N -> S (in TSC2; dbSNP:rs45457694).
/FTId=VAR_009432.
VARIANT 536 536 A -> V (in dbSNP:rs45517187).
/FTId=VAR_008024.
VARIANT 583 583 A -> T (in dbSNP:rs1800729).
/FTId=VAR_009433.
VARIANT 593 593 H -> R (in dbSNP:rs45517198).
/FTId=VAR_009434.
VARIANT 599 599 K -> M (in TSC2; impairs repression of
EIF4EBP1 phosphorylation;
dbSNP:rs45517202).
{ECO:0000269|PubMed:12271141}.
/FTId=VAR_009435.
VARIANT 607 607 A -> T (in dbSNP:rs45517203).
{ECO:0000269|PubMed:15024740}.
/FTId=VAR_005649.
VARIANT 611 611 R -> Q (in TSC2 and LAM; impairs
phosphorylation at S-1387, S-1418 and S-
1420; enhances ubiquitination by MYCBP2;
dbSNP:rs28934872).
{ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:10823953,
ECO:0000269|PubMed:15595939,
ECO:0000269|PubMed:15963462,
ECO:0000269|PubMed:18308511}.
/FTId=VAR_005650.
VARIANT 611 611 R -> W (in TSC2; impairs phosphorylation
at S-1387, S-1418 and S-1420;
dbSNP:rs45469298).
{ECO:0000269|PubMed:10607950,
ECO:0000269|PubMed:15595939,
ECO:0000269|PubMed:15963462,
ECO:0000269|PubMed:8824881}.
/FTId=VAR_005651.
VARIANT 614 614 A -> D (in TSC2; dbSNP:rs45454398).
/FTId=VAR_009436.
VARIANT 615 615 F -> S (in dbSNP:rs45481105).
/FTId=VAR_008025.
VARIANT 619 619 L -> F (in dbSNP:rs1131826).
{ECO:0000269|PubMed:8789450}.
/FTId=VAR_060584.
VARIANT 647 647 D -> N (in TSC2; unknown pathological
significance; dbSNP:rs45509392).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009437.
VARIANT 694 694 Missing (in TSC2).
/FTId=VAR_009438.
VARIANT 696 696 C -> Y (in TSC2; dbSNP:rs45486196).
/FTId=VAR_009439.
VARIANT 717 717 L -> R (in TSC2; dbSNP:rs45517214).
{ECO:0000269|PubMed:10069705,
ECO:0000269|PubMed:10570911}.
/FTId=VAR_009440.
VARIANT 769 769 V -> E (in TSC2; unknown pathological
significance; dbSNP:rs45499191).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009441.
VARIANT 802 802 S -> R (in dbSNP:rs1051621).
{ECO:0000269|PubMed:8269512,
ECO:0000269|PubMed:8789450}.
/FTId=VAR_060585.
VARIANT 816 816 P -> L (in TSC2; dbSNP:rs45517236).
/FTId=VAR_008026.
VARIANT 826 826 L -> M (in TSC2; dbSNP:rs45517238).
/FTId=VAR_005652.
VARIANT 862 862 A -> V (in dbSNP:rs45517249).
{ECO:0000269|PubMed:15024740}.
/FTId=VAR_018600.
VARIANT 895 895 M -> V (in TSC2; dbSNP:rs45470695).
/FTId=VAR_009442.
VARIANT 905 905 R -> Q (in TSC2; dbSNP:rs45517259).
/FTId=VAR_005653.
VARIANT 905 905 R -> W (in TSC2; dbSNP:rs45517258).
{ECO:0000269|PubMed:10607950}.
/FTId=VAR_005654.
VARIANT 963 963 V -> M (in TSC2; unknown pathological
significance; dbSNP:rs45517275).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009443.
VARIANT 1027 1027 L -> P (in TSC2; dbSNP:rs45438192).
{ECO:0000269|PubMed:15595939}.
/FTId=VAR_022919.
VARIANT 1084 1084 D -> E (in TSC2; dbSNP:rs45517286).
/FTId=VAR_005655.
VARIANT 1141 1141 A -> V (in dbSNP:rs34870424).
/FTId=VAR_057014.
VARIANT 1144 1144 V -> M (in TSC2; dbSNP:rs45517294).
/FTId=VAR_008027.
VARIANT 1200 1200 R -> W (in TSC2; dbSNP:rs45438205).
/FTId=VAR_005656.
VARIANT 1227 1227 P -> L (in TSC2).
{ECO:0000269|PubMed:8824881}.
/FTId=VAR_005657.
VARIANT 1240 1240 R -> W (in TSC2).
{ECO:0000269|PubMed:8824881}.
/FTId=VAR_005658.
VARIANT 1282 1282 S -> G (in dbSNP:rs45446700).
/FTId=VAR_009444.
VARIANT 1295 1295 D -> V (in TSC2).
/FTId=VAR_005659.
VARIANT 1315 1315 P -> S (in TSC2; dbSNP:rs397514916).
/FTId=VAR_008028.
VARIANT 1329 1329 R -> H (in TSC2; dbSNP:rs45517323).
/FTId=VAR_008029.
VARIANT 1341 1341 S -> R (in dbSNP:rs45462593).
{ECO:0000269|PubMed:15595939}.
/FTId=VAR_022920.
VARIANT 1429 1429 A -> S (in dbSNP:rs45474795).
{ECO:0000269|PubMed:15024740}.
/FTId=VAR_018601.
VARIANT 1450 1450 P -> R (in dbSNP:rs45517338).
{ECO:0000269|PubMed:15024740}.
/FTId=VAR_018602.
VARIANT 1497 1497 P -> R (in TSC2; dbSNP:rs45497997).
/FTId=VAR_009445.
VARIANT 1498 1498 S -> N (in TSC2; dbSNP:rs137854879).
/FTId=VAR_009446.
VARIANT 1509 1509 Missing (in TSC2; unknown pathological
significance).
{ECO:0000269|PubMed:8824881,
ECO:0000269|PubMed:9302281}.
/FTId=VAR_005660.
VARIANT 1547 1547 V -> I (in FCORD2; somatic mutation;
decreased function in negative regulation
of TOR signaling; does not affect
interaction with TSC1;
dbSNP:rs745895675).
{ECO:0000269|PubMed:28215400}.
/FTId=VAR_078847.
VARIANT 1549 1549 Y -> C (in TSC2; dbSNP:rs45517355).
/FTId=VAR_005661.
VARIANT 1594 1594 L -> M (in TSC2; unknown pathological
significance; dbSNP:rs45511204).
{ECO:0000269|PubMed:9302281}.
/FTId=VAR_009447.
VARIANT 1614 1614 Missing (in TSC2).
/FTId=VAR_005662.
VARIANT 1620 1620 H -> Y (in TSC2; dbSNP:rs45446901).
/FTId=VAR_009448.
VARIANT 1636 1636 D -> N (in dbSNP:rs45482398).
{ECO:0000269|PubMed:15595939}.
/FTId=VAR_022921.
VARIANT 1643 1643 N -> I (in TSC2; dbSNP:rs45517380).
/FTId=VAR_005663.
VARIANT 1643 1643 N -> K (in TSC2; Abolishes GAP activity;
dbSNP:rs45517381).
{ECO:0000269|PubMed:15340059,
ECO:0000269|PubMed:9302281}.
/FTId=VAR_009449.
VARIANT 1650 1650 Y -> C (in TSC2; dbSNP:rs45501091).
/FTId=VAR_005664.
VARIANT 1651 1651 N -> S (in TSC2; greatly reduces the
ability to enhance the RHEB GTPase
activity; dbSNP:rs45517382).
{ECO:0000269|PubMed:12271141,
ECO:0000269|PubMed:15024740,
ECO:0000269|PubMed:15340059,
ECO:0000269|PubMed:9302281}.
/FTId=VAR_009450.
VARIANT 1653 1653 S -> F (in TSC2; dbSNP:rs45517383).
{ECO:0000269|PubMed:15024740}.
/FTId=VAR_018603.
VARIANT 1673 1673 V -> L (in dbSNP:rs45490993).
{ECO:0000269|PubMed:15595939}.
/FTId=VAR_022922.
VARIANT 1675 1675 P -> L (in TSC2; dbSNP:rs45483392).
{ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:15024740,
ECO:0000269|PubMed:9302281}.
/FTId=VAR_009451.
VARIANT 1681 1681 N -> K (in TSC2; Abolishes GAP activity;
dbSNP:rs45476793).
{ECO:0000269|PubMed:15340059,
ECO:0000269|PubMed:9302281}.
/FTId=VAR_009452.
VARIANT 1690 1690 D -> Y (in TSC2; dbSNP:rs137854882).
/FTId=VAR_005665.
VARIANT 1704 1704 S -> T (in TSC2; dbSNP:rs45474691).
/FTId=VAR_009453.
VARIANT 1709 1709 P -> L (in TSC2; dbSNP:rs45517393).
/FTId=VAR_008030.
VARIANT 1712 1712 A -> E (in TSC2).
{ECO:0000269|PubMed:8824881}.
/FTId=VAR_005666.
VARIANT 1743 1743 R -> P (in TSC2; Abolishes GAP activity;
dbSNP:rs45507199).
{ECO:0000269|PubMed:15340059}.
/FTId=VAR_009454.
VARIANT 1743 1743 R -> Q (in TSC2; dbSNP:rs45507199).
/FTId=VAR_008031.
VARIANT 1744 1744 L -> P (in TSC2; dbSNP:rs45517413).
{ECO:0000269|PubMed:10607950}.
/FTId=VAR_009455.
VARIANT 1746 1751 Missing (in TSC2).
{ECO:0000269|PubMed:10607950,
ECO:0000269|PubMed:15024740}.
/FTId=VAR_009456.
VARIANT 1750 1750 L -> F (in TSC2; dbSNP:rs45459299).
/FTId=VAR_005667.
VARIANT 1773 1773 H -> P (in TSC2; dbSNP:rs45517418).
/FTId=VAR_008032.
VARIANT 1774 1774 S -> T (in dbSNP:rs9209).
/FTId=VAR_057015.
VARIANT 1783 1783 E -> Q (in TSC2).
/FTId=VAR_008033.
VARIANT 1787 1787 G -> S (in dbSNP:rs45517419).
/FTId=VAR_009457.
VARIANT 1791 1791 G -> S (in dbSNP:rs45517421).
/FTId=VAR_009458.
MUTAGEN 939 939 S->A: Inhibits insulin-stimulated
phosphorylation and activation of S6K1;
when associated with A-1462.
MUTAGEN 1330 1330 T->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
1448. {ECO:0000269|PubMed:14651849}.
MUTAGEN 1448 1448 S->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
1330. {ECO:0000269|PubMed:14651849}.
MUTAGEN 1462 1462 T->A: Inhibits insulin-stimulated
phosphorylation and activation of S6K1;
when associated with A-939.
MUTAGEN 1637 1639 KKR->QQQ: Abolishes GAP activity.
{ECO:0000269|PubMed:15340059}.
MUTAGEN 1745 1745 R->Q: Abolishes GAP activity.
{ECO:0000269|PubMed:15340059}.
MUTAGEN 1749 1751 RLR->QLQ: No effect.
{ECO:0000269|PubMed:15340059}.
CONFLICT 187 187 N -> S (in Ref. 7; BAG61344).
{ECO:0000305}.
CONFLICT 210 210 A -> V (in Ref. 10; AAI50301).
{ECO:0000305}.
CONFLICT 335 335 S -> P (in Ref. 7; BAG61344).
{ECO:0000305}.
CONFLICT 392 392 E -> V (in Ref. 7; BAG58569).
{ECO:0000305}.
CONFLICT 422 422 S -> P (in Ref. 7; BAG58569).
{ECO:0000305}.
CONFLICT 660 660 S -> N (in Ref. 7; BAG61344).
{ECO:0000305}.
CONFLICT 704 704 K -> E (in Ref. 10; AAI50301).
{ECO:0000305}.
CONFLICT 706 706 L -> P (in Ref. 7; BAG58569).
{ECO:0000305}.
CONFLICT 1015 1015 L -> M (in Ref. 10; AAI50301).
{ECO:0000305}.
CONFLICT 1239 1239 E -> V (in Ref. 7; BAG61344).
{ECO:0000305}.
CONFLICT 1398 1398 L -> V (in Ref. 7; BAG61344).
{ECO:0000305}.
CONFLICT 1672 1672 I -> M (in Ref. 10; AAI50301).
{ECO:0000305}.
CONFLICT 1807 1807 V -> A (in Ref. 7; BAG61344).
{ECO:0000305}.
SEQUENCE 1807 AA; 200608 MW; 7B915C46970D7D31 CRC64;
MAKPTSKDSG LKEKFKILLG LGTPRPNPRS AEGKQTEFII TAEILRELSM ECGLNNRIRM
IGQICEVAKT KKFEEHAVEA LWKAVADLLQ PERPLEARHA VLALLKAIVQ GQGERLGVLR
ALFFKVIKDY PSNEDLHERL EVFKALTDNG RHITYLEEEL ADFVLQWMDV GLSSEFLLVL
VNLVKFNSCY LDEYIARMVQ MICLLCVRTA SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI
VTLCRTINVK ELCEPCWKLM RNLLGTHLGH SAIYNMCHLM EDRAYMEDAP LLRGAVFFVG
MALWGAHRLY SLRNSPTSVL PSFYQAMACP NEVVSYEIVL SITRLIKKYR KELQVVAWDI
LLNIIERLLQ QLQTLDSPEL RTIVHDLLTT VEELCDQNEF HGSQERYFEL VERCADQRPE
SSLLNLISYR AQSIHPAKDG WIQNLQALME RFFRSESRGA VRIKVLDVLS FVLLINRQFY
EEELINSVVI SQLSHIPEDK DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS
PPPELEERDV AAYSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYEML VSHIQLHYKH
SYTLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCVCDYME PERGSEKKTS
GPLSPPTGPP GPAPAGPAVR LGSVPYSLLF RVLLQCLKQE SDWKVLKLVL GRLPESLRYK
VLIFTSPCSV DQLCSALCSM LSGPKTLERL RGAPEGFSRT DLHLAVVPVL TALISYHNYL
DKTKQREMVY CLEQGLIHRC ASQCVVALSI CSVEMPDIII KALPVLVVKL THISATASMA
VPLLEFLSTL ARLPHLYRNF AAEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC
RLPFRKDFVP FITKGLRSNV LLSFDDTPEK DSFRARSTSL NERPKSLRIA RPPKQGLNNS
PPVKEFKESS AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSVAQ ADDSLKNLHL
ELTETCLDMM ARYVFSNFTA VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL
LGLDSGELQS GPESSSSPGV HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG
ALDVPASQFL GSATSPGPRT APAAKPEKAS AGTRVPVQEK TNLAAYVPLL TQGWAEILVR
RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHRDTALY KSLSVPAAST
AKPPPLPRSN TVASFSSLYQ SSCQGQLHRS VSWADSAVVM EEGSPGEVPV LVEPPGLEDV
EAALGMDRRT DAYSRSSSVS SQEEKSLHAE ELVGRGIPIE RVVSSEGGRP SVDLSFQPSQ
PLSKSSSSPE LQTLQDILGD PGDKADVGRL SPEVKARSQS GTLDGESAAW SASGEDSRGQ
PEGPLPSSSP RSPSGLRPRG YTISDSAPSR RGKRVERDAL KSRATASNAE KVPGINPSFV
FLQLYHSPFF GDESNKPILL PNESQSFERS VQLLDQIPSY DTHKIAVLYV GEGQSNSELA
ILSNEHGSYR YTEFLTGLGR LIELKDCQPD KVYLGGLDVC GEDGQFTYCW HDDIMQAVFH
IATLMPTKDV DKHRCDKKRH LGNDFVSIVY NDSGEDFKLG TIKGQFNFVH VIVTPLDYEC
NLVSLQCRKD MEGLVDTSVA KIVSDRNLPF VARQMALHAN MASQVHHSRS NPTDIYPSKW
IARLRHIKRL RQRICEEAAY SNPSLPLVHP PSHSKAPAQT PAEPTPGYEV GQRKRLISSV
EDFTEFV


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EIAAB44186 Mouse,Mus musculus,Tsc2,Tuberin,Tuberous sclerosis 2 protein homolog
EIAAB44187 Homo sapiens,Human,TSC2,TSC4,Tuberin,Tuberous sclerosis 2 protein
3507P TSC2 _ Tuberous sclerosis complex 2 _ Tuberin (C-Terminus) Peptide 0.05 mg
3509P TSC2 _ Tuberous sclerosis complex 2 _ Tuberin (N-Terminus) Peptide 0.05 mg
18-661-15239 Hamartin - Tuberous sclerosis 1 protein Polyclonal 0.1 mg
18-661-15238 Hamartin - Tuberous sclerosis 1 protein Polyclonal 0.1 mg
EIAAB44183 Hamartin,Rat,Rattus norvegicus,Tsc1,Tuberous sclerosis 1 protein homolog
EIAAB44184 Hamartin,Kiaa0243,Mouse,Mus musculus,Tsc1,Tuberous sclerosis 1 protein homolog
EIAAB44182 Hamartin,Homo sapiens,Human,KIAA0243,TSC,TSC1,Tuberous sclerosis 1 protein
201-20-6100 TSC2{tuberous sclerosis 2}rabbit.pAb 0.2ml
ABP-PAB-11185 Tuberous sclerosis 1 (Tsc1) polyclonal antibody 100 ug
ABP-PAB-11184 Tuberous sclerosis 1 (TSC1) polyclonal antibody 100 ug
YSRTAHP1001 Tuberous Sclerosis Complex 1 (TSC1), Rabbit anti_; WB 0.1 mg.
P3392Rb Rabbit anti_ tuberous sclerosis 1 polyclonal Anti 40ug/0.2ml
YSRTAHP1001T Tuberous Sclerosis Complex 1 (TSC1), Rabbit anti_; WB 50 ug.
18-783-78300 RABBIT ANTI TSC1 - TUBEROUS SCLEROSIS COMPLEX 1; Polyclonal 0.1 mg
3503P TSC1 _ Tuberous sclerosis complex 1 _ Hamartin (C-Terminus) Peptide 0.05 mg
GWB-EF85D5 Tuberous Sclerosis 1 (TSC1) Rabbit anti-Human Polyclonal Antibody
3505P TSC1 _ Tuberous sclerosis complex 1 _ Hamartin (Intermediate Domain) Peptide 0.05 mg
GWB-43C119 Tuberous Sclerosis 2 (TSC2) Rabbit anti-Human Polyclonal (pSer664) Antibody
GWB-A8F6C5 Tuberous Sclerosis 1 (TSC1) Rabbit anti-Human Polyclonal (C-Terminus) Antibody
GWB-D08949 Tuberous Sclerosis 2 (TSC2) Rabbit anti-Human Polyclonal (C-Terminus) Antibody


 

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