TSC1_MOUSE
ID TSC1_MOUSE Reviewed; 1161 AA.
AC Q9EP53; A2AHW1; Q3UHF2; Q7TS92; Q80U55; Q924U7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Hamartin;
DE AltName: Full=Tuberous sclerosis 1 protein homolog;
GN Name=Tsc1; Synonyms=Kiaa0243;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=11130985; DOI=10.1007/s003350010203;
RA Cheadle J.P., Dobbie L., Idziaszczyk S., Hodges A.K., Smith A.J.H.,
RA Sampson J.R., Young J.M.;
RT "Genomic organization and comparative analysis of the mouse tuberous
RT sclerosis 1 (Tsc1) locus.";
RL Mamm. Genome 11:1135-1138(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=129/Sv;
RX PubMed=11438694; DOI=10.1073/pnas.151033798;
RA Kobayashi T., Minowa O., Sugitani Y., Takai S., Mitani H., Kobayashi E.,
RA Noda T., Hino O.;
RT "A germ-line Tsc1 mutation causes tumor development and embryonic lethality
RT that are similar, but not identical to, those caused by Tsc2 mutation in
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8762-8767(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-1161 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [8]
RP FUNCTION.
RX PubMed=16707451; DOI=10.1158/0008-5472.can-05-4510;
RA Jiang X., Yeung R.S.;
RT "Regulation of microtubule-dependent protein transport by the
RT TSC2/mammalian target of rapamycin pathway.";
RL Cancer Res. 66:5258-5269(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, INTERACTION WITH HSP90AA1, AND DISRUPTION PHENOTYPE.
RX PubMed=29127155; DOI=10.15252/embj.201796700;
RA Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L.,
RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H.,
RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.;
RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding
RT of kinase and non-kinase clients.";
RL EMBO J. 36:3650-3665(2017).
CC -!- FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or
CC growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by
CC negatively regulating mTORC1 signaling (By similarity). Implicated as a
CC tumor suppressor. Involved in microtubule-mediated protein transport,
CC but this seems to be due to unregulated mTOR signaling
CC (PubMed:16707451). Acts as a co-chaperone for HSP90AA1 facilitating
CC HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and
CC glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding
CC to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155).
CC Competes with the activating co-chaperone AHSA1 for binding to
CC HSP90AA1, thereby providing a reciprocal regulatory mechanism for
CC chaperoning of client proteins (By similarity). Recruits TSC2 to
CC HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2
CC and ubiquitin ligase HERC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q92574, ECO:0000269|PubMed:16707451,
CC ECO:0000269|PubMed:29127155}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2 (By similarity). Forms a complex composed of
CC chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client
CC protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain
CC co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a complex
CC containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to
CC the complex (By similarity). Interacts (via C-terminus) with the closed
CC form of HSP90AA1 (via the middle domain and TPR repeat-binding motif)
CC (PubMed:29127155). Interacts with TSC2; the interaction stabilizes TSC2
CC and prevents TSC2 self-aggregation (By similarity). Interacts with
CC DOCK7 (By similarity). Interacts with FBXW5 (By similarity). Interacts
CC with TBC1D7 (By similarity). Interacts with WDR45B (By similarity).
CC Interacts with RPAP3 and URI1 (By similarity).
CC {ECO:0000250|UniProtKB:Q92574, ECO:0000269|PubMed:29127155}.
CC -!- INTERACTION:
CC Q9EP53; D3YZU1: Shank1; NbExp=2; IntAct=EBI-1202690, EBI-2314988;
CC Q9EP53; Q61037: Tsc2; NbExp=6; IntAct=EBI-1202690, EBI-7924402;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92574}.
CC Membrane {ECO:0000250|UniProtKB:Q92574}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q92574}. Note=At steady state found in
CC association with membranes. {ECO:0000250|UniProtKB:Q92574}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9EP53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EP53-2; Sequence=VSP_037747;
CC Name=3;
CC IsoId=Q9EP53-3; Sequence=VSP_037747, VSP_037748;
CC Name=4;
CC IsoId=Q9EP53-4; Sequence=VSP_037747, VSP_037749;
CC -!- DOMAIN: The putative coiled-coil domain is necessary for interaction
CC with TSC2. {ECO:0000250|UniProtKB:Q92574}.
CC -!- PTM: Phosphorylation at Ser-502 does not affect interaction with TSC2.
CC {ECO:0000250|UniProtKB:Q92574}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in glia causes an increase
CC in HSP90AA1 ATPase activity and a down-regulation of ULK1, ERBB2, ESR1
CC and NR3C1 protein levels in the brain. {ECO:0000269|PubMed:29127155}.
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DR EMBL; AJ271911; CAC20676.1; -; Genomic_DNA.
DR EMBL; AJ271912; CAC20677.1; -; mRNA.
DR EMBL; AK147428; BAE27905.1; -; mRNA.
DR EMBL; AB047561; BAB60810.1; -; mRNA.
DR EMBL; AL731851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08392.1; -; Genomic_DNA.
DR EMBL; BC052399; AAH52399.1; -; mRNA.
DR EMBL; AK122229; BAC65511.1; -; mRNA.
DR CCDS; CCDS15844.1; -. [Q9EP53-2]
DR CCDS; CCDS71013.1; -. [Q9EP53-3]
DR CCDS; CCDS79762.1; -. [Q9EP53-1]
DR RefSeq; NP_001276504.1; NM_001289575.1. [Q9EP53-1]
DR RefSeq; NP_001276505.1; NM_001289576.1. [Q9EP53-3]
DR RefSeq; NP_075025.2; NM_022887.4. [Q9EP53-2]
DR RefSeq; XP_011237446.1; XM_011239144.1. [Q9EP53-2]
DR AlphaFoldDB; Q9EP53; -.
DR SMR; Q9EP53; -.
DR BioGRID; 211115; 132.
DR IntAct; Q9EP53; 122.
DR MINT; Q9EP53; -.
DR STRING; 10090.ENSMUSP00000109500; -.
DR iPTMnet; Q9EP53; -.
DR PhosphoSitePlus; Q9EP53; -.
DR EPD; Q9EP53; -.
DR jPOST; Q9EP53; -.
DR MaxQB; Q9EP53; -.
DR PaxDb; Q9EP53; -.
DR PeptideAtlas; Q9EP53; -.
DR PRIDE; Q9EP53; -.
DR ProteomicsDB; 300032; -. [Q9EP53-1]
DR ProteomicsDB; 300033; -. [Q9EP53-2]
DR ProteomicsDB; 300034; -. [Q9EP53-3]
DR ProteomicsDB; 300035; -. [Q9EP53-4]
DR Antibodypedia; 3164; 1882 antibodies from 46 providers.
DR DNASU; 64930; -.
DR Ensembl; ENSMUST00000028155; ENSMUSP00000028155; ENSMUSG00000026812. [Q9EP53-2]
DR Ensembl; ENSMUST00000113867; ENSMUSP00000109498; ENSMUSG00000026812. [Q9EP53-3]
DR Ensembl; ENSMUST00000113869; ENSMUSP00000109500; ENSMUSG00000026812. [Q9EP53-1]
DR Ensembl; ENSMUST00000113870; ENSMUSP00000109501; ENSMUSG00000026812. [Q9EP53-2]
DR GeneID; 64930; -.
DR KEGG; mmu:64930; -.
DR UCSC; uc008iyw.2; mouse. [Q9EP53-1]
DR UCSC; uc008iyx.2; mouse. [Q9EP53-3]
DR UCSC; uc008iyz.2; mouse. [Q9EP53-2]
DR CTD; 7248; -.
DR MGI; MGI:1929183; Tsc1.
DR VEuPathDB; HostDB:ENSMUSG00000026812; -.
DR eggNOG; ENOG502QQPT; Eukaryota.
DR GeneTree; ENSGT00390000014148; -.
DR HOGENOM; CLU_011546_0_0_1; -.
DR InParanoid; Q9EP53; -.
DR OMA; NRMASYS; -.
DR OrthoDB; 131264at2759; -.
DR PhylomeDB; Q9EP53; -.
DR TreeFam; TF325466; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 64930; 20 hits in 82 CRISPR screens.
DR ChiTaRS; Tsc1; mouse.
DR PRO; PR:Q9EP53; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EP53; protein.
DR Bgee; ENSMUSG00000026812; Expressed in ventromedial nucleus of hypothalamus and 263 other tissues.
DR ExpressionAtlas; Q9EP53; baseline and differential.
DR Genevisible; Q9EP53; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0033596; C:TSC1-TSC2 complex; ISO:MGI.
DR GO; GO:0042030; F:ATPase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IMP:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; ISS:ParkinsonsUK-UCL.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0046323; P:glucose import; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0043379; P:memory T cell differentiation; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0045859; P:regulation of protein kinase activity; IGI:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0006407; P:rRNA export from nucleus; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007483; Hamartin.
DR PANTHER; PTHR15154; PTHR15154; 1.
DR Pfam; PF04388; Hamartin; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Coiled coil; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..1161
FT /note="Hamartin"
FT /id="PRO_0000379922"
FT REGION 296..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..784
FT /note="Mediates interaction with WDR45B"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT REGION 1003..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 721..849
FT /evidence="ECO:0000255"
FT COILED 879..917
FT /evidence="ECO:0000255"
FT COILED 967..991
FT /evidence="ECO:0000255"
FT COMPBIAS 419..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92574"
FT VAR_SEQ 381
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11438694,
FT ECO:0000303|PubMed:12693553, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037747"
FT VAR_SEQ 678..682
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037748"
FT VAR_SEQ 1056..1067
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037749"
SQ SEQUENCE 1161 AA; 128746 MW; F80ACF8492007801 CRC64;
MAQLANIGEL LSMLDSSTLG VRDDVTAIFK ESLNSERGPM LVNTLVDYYL ETNSQPVLHI
LTTLQEPHDK HLLDKINEYV GKAATRLSIL SLLGHVVRLQ PSWKHKLSQA PLLPSLLKCL
KMDTDVVVLT TGVLVLITML PMIPQSGKQH LLDFFDIFGR LSSWCLKKPG HVTEVYLVHL
HASVYALFHR LYGMYPCNFV SFLRSHYSMK ENVETFEEVV KPMMEHVRIH PELVTGSKDH
ELDPRRWKTL ETHDVVIECA KISLDPTEAS YEDGYSVSHQ LSACFPYRSA DVTTSPYVDT
QNSYGGSTST PSSSSRLMLF SPPGQLPQSL SSPSTRLLPE PLQASLWSPS AVCGMTTPPT
SPGNVPADLS HPYSKAFGTT AGGKGTPSGT PATSPPPAPP CPQDDCVHGS AAQASATAPR
KEERADSSRP YLHRQSNDRG LEDPPGSKGS VTLRNLPDFL GDLASEEDSI EKDKEEAAIS
KELSEITTAE ADPVVPRGGF DSPFYRDSLS GSQRKTHSAA SGTQGSSVNP EPLHSSLDKH
GPDTPKQAFT PIDPPSGSAD VSPAGDRDRQ TSLETSILTP SPCKIPPQRG VSFGSGQLPP
YDHLFEVALP KTACHFVSKK TEELLKKVKG NPEEDCVPST SPMEVLDRLI EQGAGAHSKE
LSRLSLPSKS VDWTHFGGSP PSDELRTLRD QLLLLHNQLL YERFKRQQHA LRNRRLLRKV
IRAAALEEHN AAMKDQLKLQ EKDIQMWKVS LQKEQARYSQ LQEQRDTMVT QLHSQIRQLQ
HDREEFYNQS QELQTKLEDC RNMIAELRVE LKKANNKVCH TELLLSQVSQ KLSNSESVQQ
QMEFLNRQLL VLGEVNELYL EQLQSKHPDT TKEVEMMKTA YRKELEKNRS HLLQQNQRLD
ASQRRVLELE SLLAKKDHLL LEQKKYLEDV KSQASGQLLA AESRYEAQRK ITRVLELEIL
DLYGRLEKDG RLRKLEEDRA EAAEAAEERL DCCSDGCTDS LVGHNEEASG HNGETRTSRP
GGTRASCGGR VTGGSSSSSS ELSTPEKPPS QRFSSRWEPA LGEPSSSIPT TVGSLPSSKS
FLGMKARELF RNKSESQCDE DSVTMSSSSL SETLKTELGK DSGTENKTSL SLDAPHPSSP
NSDNVGQLHI MDYNETHPEH S
