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Hamartin (Tuberous sclerosis 1 protein)

 TSC1_HUMAN              Reviewed;        1164 AA.
Q92574; B7Z897; Q5VVN5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 2.
25-OCT-2017, entry version 174.
RecName: Full=Hamartin;
AltName: Full=Tuberous sclerosis 1 protein;
Name=TSC1; Synonyms=KIAA0243, TSC;
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-587.
PubMed=9242607; DOI=10.1126/science.277.5327.805;
van Slegtenhorst M.A., de Hoogt R., Hermans C., Nellist M.,
Janssen B., Verhoef S., Lindhout D., van den Ouweland A.M.W.,
Halley D.J.J., Young J., Burley M., Jeremiah S., Woodward K.,
Nahmias J., Fox M., Ekong R., Osborne J., Wolfe J., Povey S.,
Snell R.G., Cheadle J.P., Jones A.C., Tachataki M., Ravine D.,
Sampson J.R., Reeve M.P., Richardson P., Wilmer F., Munro C.,
Hawkins T.L., Sepp T., Ali J.B.M., Ward S., Green A.J., Yates J.R.W.,
Kwiatkowska J., Henske E.P., Short M.P., Haines J.H., Jozwiak S.,
Kwiatkowski D.J.;
"Identification of the tuberous sclerosis gene TSC1 on chromosome
9q34.";
Science 277:805-808(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-1164 (ISOFORM 1/2).
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 568-586.
Fang L., Wang N., Murong S.X., Wu Z.Y., Lin M.T.;
"A silent mutation 1947 T-->C in exon 15 of TSC1 in Chinese.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH TSC2.
PubMed=9809973;
Plank T.L., Yeung R.S., Henske E.P.;
"Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
interacts with tuberin and appears to be localized to cytoplasmic
vesicles.";
Cancer Res. 58:4766-4770(1998).
[8]
INTERACTION WITH TSC2.
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).
[9]
INTERACTION WITH TSC2.
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).
[10]
INVOLVEMENT IN LAM, AND VARIANT TSC1 165-CYS--SER-1164 DEL.
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).
[11]
FUNCTION.
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).
[12]
FUNCTION.
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).
[13]
PHOSPHORYLATION AT SER-505, IDENTIFICATION BY MASS SPECTROMETRY, AND
INTERACTION WITH DOCK7 AND TSC2.
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).
[14]
INTERACTION WITH TSC2.
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).
[15]
INTERACTION WITH TBC1D7.
PubMed=17658474; DOI=10.1016/j.bbrc.2007.07.011;
Nakashima A., Yoshino K., Miyamoto T., Eguchi S., Oshiro N.,
Kikkawa U., Yonezawa K.;
"Identification of TBC7 having TBC domain as a novel binding protein
to TSC1-TSC2 complex.";
Biochem. Biophys. Res. Commun. 361:218-223(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-511 AND
SER-598, 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).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, 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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-505 AND
SER-521, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1100, 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).
[25]
FUNCTION, INTERACTION WITH TSC2, INVOLVEMENT IN FCORD2, VARIANTS
FCORD2 TRP-22 AND CYS-204, AND CHARACTERIZATION OF VARIANTS FCORD2
TRP-22 AND CYS-204.
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).
[26]
VARIANT TSC1 GLU-726, AND VARIANTS THR-322; TYR-732 AND SER-1035.
TISSUE=Peripheral blood;
PubMed=9328481; DOI=10.1093/hmg/6.12.2155;
Jones A.C., Daniells C.E., Snell R.G., Tachataki M., Idziaszczyk S.A.,
Krawczak M., Sampson J.R., Cheadle J.P.;
"Molecular genetic and phenotypic analysis reveals differences between
TSC1 and TSC2 associated familial and sporadic tuberous sclerosis.";
Hum. Mol. Genet. 6:2155-2161(1997).
[27]
VARIANTS THR-322; ARG-587; TYR-732; SER-1035 AND SER-1108.
TISSUE=Blood;
PubMed=9924605; DOI=10.1046/j.1469-1809.1998.6240277.x;
Kwiatkowska J., Jozwiak S., Hall F., Henske E.P., Haines J.L.,
McNamara P., Braiser J., Wigowska-Sowinska J., Kasprzyk-Obara J.,
Short M.P., Kwiatkowski D.J.;
"Comprehensive mutational analysis of the TSC1 gene: observations on
frequency of mutation, associated features, and nonpenetrance.";
Ann. Hum. Genet. 62:277-285(1998).
[28]
VARIANT TSC1 PRO-72.
PubMed=10533069;
DOI=10.1002/(SICI)1098-1004(199911)14:5<428::AID-HUMU9>3.0.CO;2-5;
Benit P., Kara-Mostefa A., Hadj-Rabia S., Munnich A., Bonnefont J.-P.;
"Protein truncation test for screening hamartin gene mutations and
report of new disease-causing mutations.";
Hum. Mutat. 14:428-432(1999).
[29]
VARIANTS THR-322; TYR-732 AND GLN-809.
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).
[30]
VARIANTS TSC1 ILE-417; GLU-654 AND SER-899, AND VARIANT THR-322.
TISSUE=Blood;
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).
[31]
VARIANTS TSC1, AND VARIANTS.
TISSUE=Peripheral blood;
PubMed=10227394;
Van Slegtenhorst M.A., Verhoef S., Tempelaars A., Bakker L., Wang Q.,
Wessels M., Bakker R., Nellist M., Lindhout D., Halley D.J.J.,
van den Ouweland A.M.W.;
"Mutational spectrum of the TSC1 gene in a cohort of 225 tuberous
sclerosis complex patients: no evidence for genotype-phenotype
correlation.";
J. Med. Genet. 36:285-289(1999).
[32]
VARIANTS THR-322; ILE-417; ASP-577 AND ARG-829.
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).
[33]
VARIANT TSC1 GLN-500.
PubMed=10874311;
DOI=10.1002/1098-1004(200007)16:1<88::AID-HUMU15>3.3.CO;2-A;
Hass J., Mayer K., Rott H.-D.;
"Tuberous sclerosis type 1: three novel mutations detected in exon 15
by a combination of HDA and TGGE.";
Hum. Mutat. 16:88-88(2000).
[34]
VARIANT TYR-732.
PubMed=12112044; DOI=10.1002/ana.10251;
Becker A.J., Urbach H., Scheffler B., Baden T., Normann S., Lahl R.,
Pannek H.W., Tuxhorn I., Elger C.E., Schramm J., Wiestler O.D.,
Bluemcke I.;
"Focal cortical dysplasia of Taylor's balloon cell type: mutational
analysis of the TSC1 gene indicates a pathogenic relationship to
tuberous sclerosis.";
Ann. Neurol. 52:29-37(2002).
[35]
VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND ILE-417, AND
CHARACTERIZATION OF VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND
ILE-417.
PubMed=18397877; DOI=10.1093/hmg/ddn098;
Pymar L.S., Platt F.M., Askham J.M., Morrison E.E., Knowles M.A.;
"Bladder tumour-derived somatic TSC1 missense mutations cause loss of
function via distinct mechanisms.";
Hum. Mol. Genet. 17:2006-2017(2008).
[36]
VARIANTS TSC1 PRO-117; VAL-128 DEL; PRO-180; HIS-191; 198-ASN-PHE-199
DELINS ILE; ARG-224; LYS-246; ARG-305 AND TRP-305, VARIANTS GLN-509;
SER-1035 AND HIS-1097, CHARACTERIZATION OF VARIANTS TSC1 PRO-117;
VAL-128 DEL; PRO-180; HIS-191; 198-ASN-PHE-199 DELINS ILE; ARG-224;
LYS-246; ARG-305 AND TRP-305, AND CHARACTERIZATION OF VARIANTS
GLN-509; SER-1035 AND HIS-1097.
PubMed=18830229; DOI=10.1038/ejhg.2008.170;
Nellist M., van den Heuvel D., Schluep D., Exalto C., Goedbloed M.,
Maat-Kievit A., van Essen T., van Spaendonck-Zwarts K., Jansen F.,
Helderman P., Bartalini G., Vierimaa O., Penttinen M.,
van den Ende J., van den Ouweland A., Halley D.;
"Missense mutations to the TSC1 gene cause tuberous sclerosis
complex.";
Eur. J. Hum. Genet. 17:319-328(2009).
[37]
VARIANTS TSC1 ARG-61; ILE-126; ASP-132; ILE-133; GLN-336; SER-362;
ILE-411; SER-448; PRO-523; VAL-567; HIS-693; ARG-698; HIS-701;
SER-762; GLY-811; THR-883; VAL-978; SER-1043 DEL AND TYR-1146,
VARIANTS SER-158 AND PRO-204, CHARACTERIZATION OF VARIANTS TSC1
ARG-61; PRO-117; ILE-126; ASP-132; ILE-133; GLN-336; SER-362; ILE-411;
SER-448; PRO-523; VAL-567; HIS-693; ARG-698; HIS-701; SER-762;
GLY-811; THR-883; VAL-978; SER-1043 DEL AND TYR-1146, AND
CHARACTERIZATION OF VARIANTS SER-158 AND PRO-204.
PubMed=22161988; DOI=10.1002/humu.22007;
Hoogeveen-Westerveld M., Ekong R., Povey S., Karbassi I., Batish S.D.,
den Dunnen J.T., van Eeghen A., Thiele E., Mayer K., Dies K., Wen L.,
Thompson C., Sparagana S.P., Davies P., Aalfs C., van den Ouweland A.,
Halley D., Nellist M.;
"Functional assessment of TSC1 missense variants identified in
individuals with tuberous sclerosis complex.";
Hum. Mutat. 33:476-479(2012).
-!- FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or
growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by
negatively regulating mTORC1 signaling. Seems not to be required
for TSC2 GAP activity towards RHEB. Implicated as a tumor
suppressor. Involved in microtubule-mediated protein transport,
but this seems to be due to unregulated mTOR signaling.
{ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:15340059,
ECO:0000269|PubMed:28215400}.
-!- SUBUNIT: Interacts with TSC2, leading to stabilize TSC2. In the
absence of TSC2, TSC1 self-aggregates (PubMed:10585443,
PubMed:15963462, PubMed:16464865, PubMed:9580671, PubMed:9809973,
PubMed:28215400). Interacts with DOCK7 (PubMed:15963462).
Interacts with FBXW5 (PubMed:18381890). Interacts with TBC1D7
(PubMed:17658474). {ECO:0000269|PubMed:10585443,
ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:16464865,
ECO:0000269|PubMed:17658474, ECO:0000269|PubMed:18381890,
ECO:0000269|PubMed:28215400, ECO:0000269|PubMed:9580671,
ECO:0000269|PubMed:9809973}.
-!- INTERACTION:
Q00994:BEX3; NbExp=5; IntAct=EBI-1047085, EBI-741753;
O14920:IKBKB; NbExp=3; IntAct=EBI-1047085, EBI-81266;
Q16539:MAPK14; NbExp=2; IntAct=EBI-1047085, EBI-73946;
P49815:TSC2; NbExp=10; IntAct=EBI-1047085, EBI-396587;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9809973}.
Membrane {ECO:0000269|PubMed:9809973}; Peripheral membrane protein
{ECO:0000269|PubMed:9809973}. Note=At steady state found in
association with membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92574-1; Sequence=Displayed;
Name=2;
IsoId=Q92574-2; Sequence=VSP_042890;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, followed
by heart, brain, placenta, pancreas, lung, liver and kidney. Also
expressed in embryonic kidney cells.
-!- DOMAIN: The C-terminal putative coiled-coil domain is necessary
for interaction with TSC2.
-!- PTM: Phosphorylation at Ser-505 does not affect interaction with
TSC2. {ECO:0000269|PubMed:15963462}.
-!- DISEASE: Tuberous sclerosis 1 (TSC1) [MIM:191100]: 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:10227394, ECO:0000269|PubMed:10533069,
ECO:0000269|PubMed:10570911, ECO:0000269|PubMed:10874311,
ECO:0000269|PubMed:11829138, ECO:0000269|PubMed:18830229,
ECO:0000269|PubMed:22161988, ECO:0000269|PubMed:9328481}. 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: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.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TSC1ID183.html";
-!- WEB RESOURCE: Name=Tuberous sclerosis database Tuberous sclerosis
1 (TSC1); Note=Leiden Open Variation Database (LOVD);
URL="http://www.LOVD.nl/TSC1";
-----------------------------------------------------------------------
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EMBL; AF013168; AAC51674.1; -; mRNA.
EMBL; AK303030; BAH13883.1; -; mRNA.
EMBL; AL445645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW88021.1; -; Genomic_DNA.
EMBL; AC002096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D87683; BAA13436.1; -; mRNA.
EMBL; AF234185; AAF61948.1; -; Genomic_DNA.
CCDS; CCDS55350.1; -. [Q92574-2]
CCDS; CCDS6956.1; -. [Q92574-1]
PIR; T03814; T03814.
RefSeq; NP_000359.1; NM_000368.4. [Q92574-1]
RefSeq; NP_001155898.1; NM_001162426.1.
RefSeq; NP_001155899.1; NM_001162427.1. [Q92574-2]
RefSeq; XP_005272268.1; XM_005272211.1. [Q92574-1]
RefSeq; XP_006717334.1; XM_006717271.1. [Q92574-1]
RefSeq; XP_011517281.1; XM_011518979.2. [Q92574-1]
RefSeq; XP_016870585.1; XM_017015096.1. [Q92574-1]
RefSeq; XP_016870586.1; XM_017015097.1. [Q92574-1]
UniGene; Hs.370854; -.
PDB; 4Z6Y; X-ray; 2.81 A; C/D/F/H=938-993.
PDB; 5EJC; X-ray; 3.10 A; C/D/E/F=939-992.
PDBsum; 4Z6Y; -.
PDBsum; 5EJC; -.
ProteinModelPortal; Q92574; -.
SMR; Q92574; -.
BioGrid; 113099; 51.
CORUM; Q92574; -.
IntAct; Q92574; 42.
MINT; MINT-1534928; -.
STRING; 9606.ENSP00000298552; -.
iPTMnet; Q92574; -.
PhosphoSitePlus; Q92574; -.
BioMuta; TSC1; -.
DMDM; 9297077; -.
EPD; Q92574; -.
PaxDb; Q92574; -.
PeptideAtlas; Q92574; -.
PRIDE; Q92574; -.
DNASU; 7248; -.
Ensembl; ENST00000298552; ENSP00000298552; ENSG00000165699. [Q92574-1]
Ensembl; ENST00000440111; ENSP00000394524; ENSG00000165699. [Q92574-1]
Ensembl; ENST00000545250; ENSP00000444017; ENSG00000165699. [Q92574-2]
GeneID; 7248; -.
KEGG; hsa:7248; -.
UCSC; uc064wss.1; human. [Q92574-1]
CTD; 7248; -.
DisGeNET; 7248; -.
EuPathDB; HostDB:ENSG00000165699.13; -.
GeneCards; TSC1; -.
GeneReviews; TSC1; -.
HGNC; HGNC:12362; TSC1.
HPA; CAB011568; -.
HPA; CAB012481; -.
HPA; HPA074132; -.
MalaCards; TSC1; -.
MIM; 191100; phenotype.
MIM; 605284; gene.
MIM; 606690; phenotype.
MIM; 607341; phenotype.
neXtProt; NX_Q92574; -.
OpenTargets; ENSG00000165699; -.
Orphanet; 269008; Isolated focal cortical dysplasia type IIb.
Orphanet; 538; Lymphangioleiomyomatosis.
Orphanet; 805; Tuberous sclerosis.
PharmGKB; PA37034; -.
eggNOG; ENOG410IG36; Eukaryota.
eggNOG; ENOG411020J; LUCA.
GeneTree; ENSGT00390000014148; -.
HOGENOM; HOG000232119; -.
HOVERGEN; HBG012559; -.
InParanoid; Q92574; -.
KO; K07206; -.
OMA; PYDHLFE; -.
OrthoDB; EOG091G01O5; -.
PhylomeDB; Q92574; -.
TreeFam; TF325466; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165181; Inhibition of TSC complex formation by PKB.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-8854214; TBC/RABGAPs.
SignaLink; Q92574; -.
SIGNOR; Q92574; -.
ChiTaRS; TSC1; human.
GeneWiki; TSC1; -.
GenomeRNAi; 7248; -.
PRO; PR:Q92574; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165699; -.
CleanEx; HS_TSC1; -.
ExpressionAtlas; Q92574; baseline and differential.
Genevisible; Q92574; HS.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005811; C:lipid droplet; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0033596; C:TSC1-TSC2 complex; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; ISS:ParkinsonsUK-UCL.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0030030; P:cell projection organization; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; ISS:ParkinsonsUK-UCL.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0046323; P:glucose import; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043379; P:memory T cell differentiation; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0016242; P:negative regulation of macroautophagy; ISS:ParkinsonsUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0051492; P:regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
GO; GO:0006407; P:rRNA export from nucleus; IMP:UniProtKB.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR007483; Hamartin.
PANTHER; PTHR15154; PTHR15154; 1.
Pfam; PF04388; Hamartin; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Disease mutation; Epilepsy; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Tumor suppressor.
CHAIN 1 1164 Hamartin.
/FTId=PRO_0000065651.
COILED 721 997 {ECO:0000255}.
COMPBIAS 1034 1037 Poly-Gly.
COMPBIAS 1038 1043 Poly-Ser.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15963462}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1100 1100 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 70 120 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042890.
VARIANT 22 22 R -> W (in FCORD2; somatic mutation;
decreased interaction with TSC2;
decreased function in negative regulation
of TOR signaling; dbSNP:rs749030456).
{ECO:0000269|PubMed:28215400}.
/FTId=VAR_078844.
VARIANT 51 51 E -> D (in TSC1; unknown pathological
significance; dbSNP:rs118203342).
/FTId=VAR_009397.
VARIANT 61 61 L -> R (in TSC1; unknown pathological
significance; reduced expression; altered
subcellular localization; reduced
inhibition of TORC1 signaling;
dbSNP:rs118203345).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070636.
VARIANT 68 68 H -> R (in a bladder tumor; somatic
mutation; reduced stability; does not
affect interaction with TSC2;
dbSNP:rs118203347).
{ECO:0000269|PubMed:18397877}.
/FTId=VAR_054386.
VARIANT 72 72 L -> P (in TSC1; dbSNP:rs118203354).
{ECO:0000269|PubMed:10533069}.
/FTId=VAR_054387.
VARIANT 117 117 L -> P (in TSC1; reduced expression;
altered subcellular localization; reduced
interaction with TSC2; reduced inhibition
of TORC1 signaling; dbSNP:rs118203368).
{ECO:0000269|PubMed:18830229,
ECO:0000269|PubMed:22161988}.
/FTId=VAR_070637.
VARIANT 126 126 V -> I (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514843).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070638.
VARIANT 128 128 Missing (in TSC1; reduced expression;
reduced inhibition of TORC1 signaling).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070639.
VARIANT 132 132 G -> D (in TSC1; unknown pathological
significance; reduced expression; altered
subcellular localization; reduced
inhibition of TORC1 signaling;
dbSNP:rs397514784).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070640.
VARIANT 133 133 V -> I (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203381).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070641.
VARIANT 158 158 F -> C (in a bladder tumor; somatic
mutation; reduced stability; does not
affect interaction with TSC2;
dbSNP:rs118203385).
{ECO:0000269|PubMed:18397877}.
/FTId=VAR_054388.
VARIANT 158 158 F -> S (found in a patient suspected of
having tuberous sclerosis; unknown
pathological significance; reduced
expression; altered subcellular
localization; reduced inhibition of TORC1
signaling; dbSNP:rs118203385).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070642.
VARIANT 165 1164 Missing (in TSC1).
{ECO:0000269|PubMed:11829138}.
/FTId=VAR_078845.
VARIANT 180 180 L -> P (in TSC1; reduced expression;
reduced inhibition of TORC1 signaling;
dbSNP:rs118203396).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070643.
VARIANT 190 190 R -> S.
/FTId=VAR_009398.
VARIANT 191 191 L -> H (in TSC1; reduced expression;
reduced inhibition of TORC1 signaling;
dbSNP:rs118203403).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_009399.
VARIANT 198 199 NF -> I (in TSC1; reduced expression;
altered subcellular localization; reduced
interaction with TSC2; reduced inhibition
of TORC1 signaling).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_009400.
VARIANT 204 204 R -> C (in FCORD2; somatic mutation;
decreased interaction with TSC2;
decreased function in negative regulation
of TOR signaling).
{ECO:0000269|PubMed:28215400}.
/FTId=VAR_078846.
VARIANT 204 204 R -> P (found in a patient suspected of
having tuberous sclerosis; reduced
expression; altered subcellular
localization; reduced inhibition of TORC1
signaling; dbSNP:rs397514834).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070644.
VARIANT 206 206 H -> D (in a bladder tumor; somatic
mutation; reduced stability; does not
affect interaction with TSC2).
{ECO:0000269|PubMed:18397877}.
/FTId=VAR_054389.
VARIANT 216 216 F -> L (in a bladder tumor; diffuse
punctate cytoplasmic distribution in
aminoacid-starved conditions; does not
affect interaction with TSC2).
{ECO:0000269|PubMed:18397877}.
/FTId=VAR_054390.
VARIANT 224 224 M -> R (in TSC1; reduced expression;
reduced inhibition of TORC1 signaling;
dbSNP:rs118203426).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_009401.
VARIANT 246 246 R -> K (in TSC1; unknown pathological
significance; no effect on expression; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203436).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070645.
VARIANT 305 305 G -> R (in TSC1; unknown pathological
significance; no effect on expression; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203468).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070646.
VARIANT 305 305 G -> W (in TSC1; unknown pathological
significance; no effect on expression; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203468).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070647.
VARIANT 322 322 M -> T (in dbSNP:rs1073123).
{ECO:0000269|PubMed:10533067,
ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:10607950,
ECO:0000269|PubMed:9328481,
ECO:0000269|PubMed:9924605}.
/FTId=VAR_009402.
VARIANT 336 336 R -> Q (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514808).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070648.
VARIANT 362 362 P -> S (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514864).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070649.
VARIANT 411 411 L -> I (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514840).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070650.
VARIANT 417 417 T -> I (in TSC1; unknown pathological
significance; does not affect interaction
with TSC2; dbSNP:rs77464996).
{ECO:0000269|PubMed:10570911,
ECO:0000269|PubMed:10607950,
ECO:0000269|PubMed:18397877}.
/FTId=VAR_009403.
VARIANT 448 448 P -> S (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203518).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070651.
VARIANT 500 500 R -> Q (in TSC1; dbSNP:rs118203538).
{ECO:0000269|PubMed:10874311}.
/FTId=VAR_054391.
VARIANT 509 509 R -> Q (rare polymorphism; no effect on
expression; no effect on inhibition of
TORC1 signaling; dbSNP:rs118203543).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070652.
VARIANT 523 523 A -> P (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203548).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070653.
VARIANT 567 567 A -> V (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514880).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070654.
VARIANT 577 577 E -> D (in dbSNP:rs118203571).
{ECO:0000269|PubMed:10607950}.
/FTId=VAR_009404.
VARIANT 586 589 CKIP -> S (in TSC1).
/FTId=VAR_009405.
VARIANT 587 587 K -> R (in dbSNP:rs118203576).
{ECO:0000269|PubMed:9242607,
ECO:0000269|PubMed:9924605}.
/FTId=VAR_009406.
VARIANT 654 654 Q -> E (in TSC1; dbSNP:rs75820036).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009407.
VARIANT 693 693 D -> H (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514800).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070655.
VARIANT 698 698 L -> R (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514802).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070656.
VARIANT 701 701 Q -> H (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203639).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070657.
VARIANT 726 726 A -> E (in TSC1; dbSNP:rs118203655).
{ECO:0000269|PubMed:9328481}.
/FTId=VAR_009408.
VARIANT 732 732 H -> Y (rare polymorphism; might be
associated with susceptibility to focal
cortical dysplasia of the Taylor balloon
cell type; dbSNP:rs118203657).
{ECO:0000269|PubMed:10533067,
ECO:0000269|PubMed:12112044,
ECO:0000269|PubMed:9328481,
ECO:0000269|PubMed:9924605}.
/FTId=VAR_009409.
VARIANT 762 762 N -> S (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203670).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070658.
VARIANT 809 809 E -> Q (in dbSNP:rs118203692).
{ECO:0000269|PubMed:10533067}.
/FTId=VAR_009410.
VARIANT 811 811 R -> G (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514814).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070659.
VARIANT 829 829 S -> R (in dbSNP:rs118203699).
{ECO:0000269|PubMed:10607950}.
/FTId=VAR_009411.
VARIANT 883 883 A -> T (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs118203721).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070660.
VARIANT 899 899 T -> S (in TSC1; dbSNP:rs76801599).
{ECO:0000269|PubMed:10570911}.
/FTId=VAR_009412.
VARIANT 978 978 L -> V (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514859).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070661.
VARIANT 1035 1035 G -> S (rare polymorphism; no effect on
expression; no effect on inhibition of
TORC1 signaling; dbSNP:rs118203742).
{ECO:0000269|PubMed:18830229,
ECO:0000269|PubMed:9328481,
ECO:0000269|PubMed:9924605}.
/FTId=VAR_009413.
VARIANT 1043 1043 Missing (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070662.
VARIANT 1097 1097 R -> H (rare polymorphism; no effect on
expression; no effect on inhibition of
TORC1 signaling; dbSNP:rs118203750).
{ECO:0000269|PubMed:18830229}.
/FTId=VAR_070663.
VARIANT 1108 1108 G -> S (in dbSNP:rs118203753).
{ECO:0000269|PubMed:9924605}.
/FTId=VAR_009414.
VARIANT 1146 1146 D -> Y (in TSC1; unknown pathological
significance; no effect on expression; no
effect on subcellular localization; no
effect on inhibition of TORC1 signaling;
dbSNP:rs397514806).
{ECO:0000269|PubMed:22161988}.
/FTId=VAR_070664.
HELIX 941 971 {ECO:0000244|PDB:4Z6Y}.
HELIX 975 991 {ECO:0000244|PDB:4Z6Y}.
SEQUENCE 1164 AA; 129767 MW; EF15509385C7AACC CRC64;
MAQQANVGEL LAMLDSPMLG VRDDVTAVFK ENLNSDRGPM LVNTLVDYYL ETSSQPALHI
LTTLQEPHDK HLLDRINEYV GKAATRLSIL SLLGHVIRLQ PSWKHKLSQA PLLPSLLKCL
KMDTDVVVLT TGVLVLITML PMIPQSGKQH LLDFFDIFGR LSSWCLKKPG HVAEVYLVHL
HASVYALFHR LYGMYPCNFV SFLRSHYSMK ENLETFEEVV KPMMEHVRIH PELVTGSKDH
ELDPRRWKRL ETHDVVIECA KISLDPTEAS YEDGYSVSHQ ISARFPHRSA DVTTSPYADT
QNSYGCATST PYSTSRLMLL NMPGQLPQTL SSPSTRLITE PPQATLWSPS MVCGMTTPPT
SPGNVPPDLS HPYSKVFGTT AGGKGTPLGT PATSPPPAPL CHSDDYVHIS LPQATVTPPR
KEERMDSARP CLHRQHHLLN DRGSEEPPGS KGSVTLSDLP GFLGDLASEE DSIEKDKEEA
AISRELSEIT TAEAEPVVPR GGFDSPFYRD SLPGSQRKTH SAASSSQGAS VNPEPLHSSL
DKLGPDTPKQ AFTPIDLPCG SADESPAGDR ECQTSLETSI FTPSPCKIPP PTRVGFGSGQ
PPPYDHLFEV ALPKTAHHFV IRKTEELLKK AKGNTEEDGV PSTSPMEVLD RLIQQGADAH
SKELNKLPLP SKSVDWTHFG GSPPSDEIRT LRDQLLLLHN QLLYERFKRQ QHALRNRRLL
RKVIKAAALE EHNAAMKDQL KLQEKDIQMW KVSLQKEQAR YNQLQEQRDT MVTKLHSQIR
QLQHDREEFY NQSQELQTKL EDCRNMIAEL RIELKKANNK VCHTELLLSQ VSQKLSNSES
VQQQMEFLNR QLLVLGEVNE LYLEQLQNKH SDTTKEVEMM KAAYRKELEK NRSHVLQQTQ
RLDTSQKRIL ELESHLAKKD HLLLEQKKYL EDVKLQARGQ LQAAESRYEA QKRITQVFEL
EILDLYGRLE KDGLLKKLEE EKAEAAEAAE ERLDCCNDGC SDSMVGHNEE ASGHNGETKT
PRPSSARGSS GSRGGGGSSS SSSELSTPEK PPHQRAGPFS SRWETTMGEA SASIPTTVGS
LPSSKSFLGM KARELFRNKS ESQCDEDGMT SSLSESLKTE LGKDLGVEAK IPLNLDGPHP
SPPTPDSVGQ LHIMDYNETH HEHS


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