Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9EP53 (TSC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hamartin
Alternative name(s):
Tuberous sclerosis 1 protein homolog
Gene names
Name:Tsc1
Synonyms:Kiaa0243
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling By similarity. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling By similarity.

Subunit structure

Interacts with TSC2, leading to stabilize TSC2. In the absence of TSC2, TSC1 self-aggregates. Interacts with DOCK7 By similarity. Interacts with FBXW5 and TBC1D7 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Note: At steady state found in association with membranes By similarity.

Domain

The putative coiled-coil domain is necessary for interaction with TSC2 By similarity.

Post-translational modification

Phosphorylation at Ser-502 does not affect interaction with TSC2.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rho GTPase activity

Inferred from electronic annotation. Source: Compara

cardiac muscle cell differentiation

Inferred from mutant phenotype Ref.2. Source: MGI

cell projection organization

Inferred from mutant phenotype PubMed 16286931. Source: MGI

cell-matrix adhesion

Inferred from electronic annotation. Source: Compara

cerebral cortex development

Inferred from mutant phenotype PubMed 17522300. Source: MGI

hippocampus development

Inferred from mutant phenotype PubMed 17522300. Source: MGI

kidney development

Inferred from mutant phenotype PubMed 15888477. Source: MGI

myelination

Inferred from mutant phenotype PubMed 17522300. Source: MGI

negative regulation of TOR signaling cascade

Inferred from electronic annotation. Source: Compara

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.2. Source: MGI

negative regulation of cell size

Inferred from mutant phenotype PubMed 15664737PubMed 16286931PubMed 17522300. Source: MGI

negative regulation of translation

Inferred from electronic annotation. Source: Compara

neural tube closure

Inferred from mutant phenotype Ref.2. Source: MGI

positive regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Compara

potassium ion transport

Inferred from mutant phenotype PubMed 16393152. Source: MGI

protein heterooligomerization

Inferred from electronic annotation. Source: Compara

protein stabilization

Inferred from electronic annotation. Source: Compara

rRNA export from nucleus

Inferred from electronic annotation. Source: Compara

regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Compara

regulation of protein kinase activity

Inferred from genetic interaction PubMed 15185396. Source: MGI

regulation of stress fiber assembly

Inferred from electronic annotation. Source: Compara

response to insulin stimulus

Inferred from electronic annotation. Source: Compara

synapse organization

Inferred from mutant phenotype PubMed 16286931. Source: MGI

   Cellular_componentTSC1-TSC2 complex

Inferred from electronic annotation. Source: Compara

actin filament

Inferred from electronic annotation. Source: Compara

cell cortex

Inferred from electronic annotation. Source: Compara

cytoplasm

Inferred from direct assay PubMed 11741832PubMed 16286931. Source: MGI

growth cone

Inferred from electronic annotation. Source: Compara

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Compara

lamellipodium

Inferred from electronic annotation. Source: Compara

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTPase regulator activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9EP53-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9EP53-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-381: Missing.
Isoform 3 (identifier: Q9EP53-3)

The sequence of this isoform differs from the canonical sequence as follows:
     381-381: Missing.
     678-682: Missing.
Isoform 4 (identifier: Q9EP53-4)

The sequence of this isoform differs from the canonical sequence as follows:
     381-381: Missing.
     1056-1067: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11611161Hamartin
PRO_0000379922

Regions

Coiled coil721 – 849129 Potential
Coiled coil879 – 91739 Potential
Coiled coil967 – 99125 Potential
Compositional bias312 – 3154Poly-Ser
Compositional bias692 – 6954Poly-Leu
Compositional bias1035 – 10406Poly-Ser
Compositional bias1106 – 11116Poly-Ser

Amino acid modifications

Modified residue3941Phosphoserine Ref.8
Modified residue5021Phosphoserine By similarity
Modified residue5081Phosphoserine By similarity
Modified residue5951Phosphoserine By similarity

Natural variations

Alternative sequence3811Missing in isoform 2, isoform 3 and isoform 4.
VSP_037747
Alternative sequence678 – 6825Missing in isoform 3.
VSP_037748
Alternative sequence1056 – 106712Missing in isoform 4.
VSP_037749

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F80ACF8492007801

FASTA1,161128,746
        10         20         30         40         50         60 
MAQLANIGEL LSMLDSSTLG VRDDVTAIFK ESLNSERGPM LVNTLVDYYL ETNSQPVLHI 

        70         80         90        100        110        120 
LTTLQEPHDK HLLDKINEYV GKAATRLSIL SLLGHVVRLQ PSWKHKLSQA PLLPSLLKCL 

       130        140        150        160        170        180 
KMDTDVVVLT TGVLVLITML PMIPQSGKQH LLDFFDIFGR LSSWCLKKPG HVTEVYLVHL 

       190        200        210        220        230        240 
HASVYALFHR LYGMYPCNFV SFLRSHYSMK ENVETFEEVV KPMMEHVRIH PELVTGSKDH 

       250        260        270        280        290        300 
ELDPRRWKTL ETHDVVIECA KISLDPTEAS YEDGYSVSHQ LSACFPYRSA DVTTSPYVDT 

       310        320        330        340        350        360 
QNSYGGSTST PSSSSRLMLF SPPGQLPQSL SSPSTRLLPE PLQASLWSPS AVCGMTTPPT 

       370        380        390        400        410        420 
SPGNVPADLS HPYSKAFGTT AGGKGTPSGT PATSPPPAPP CPQDDCVHGS AAQASATAPR 

       430        440        450        460        470        480 
KEERADSSRP YLHRQSNDRG LEDPPGSKGS VTLRNLPDFL GDLASEEDSI EKDKEEAAIS 

       490        500        510        520        530        540 
KELSEITTAE ADPVVPRGGF DSPFYRDSLS GSQRKTHSAA SGTQGSSVNP EPLHSSLDKH 

       550        560        570        580        590        600 
GPDTPKQAFT PIDPPSGSAD VSPAGDRDRQ TSLETSILTP SPCKIPPQRG VSFGSGQLPP 

       610        620        630        640        650        660 
YDHLFEVALP KTACHFVSKK TEELLKKVKG NPEEDCVPST SPMEVLDRLI EQGAGAHSKE 

       670        680        690        700        710        720 
LSRLSLPSKS VDWTHFGGSP PSDELRTLRD QLLLLHNQLL YERFKRQQHA LRNRRLLRKV 

       730        740        750        760        770        780 
IRAAALEEHN AAMKDQLKLQ EKDIQMWKVS LQKEQARYSQ LQEQRDTMVT QLHSQIRQLQ 

       790        800        810        820        830        840 
HDREEFYNQS QELQTKLEDC RNMIAELRVE LKKANNKVCH TELLLSQVSQ KLSNSESVQQ 

       850        860        870        880        890        900 
QMEFLNRQLL VLGEVNELYL EQLQSKHPDT TKEVEMMKTA YRKELEKNRS HLLQQNQRLD 

       910        920        930        940        950        960 
ASQRRVLELE SLLAKKDHLL LEQKKYLEDV KSQASGQLLA AESRYEAQRK ITRVLELEIL 

       970        980        990       1000       1010       1020 
DLYGRLEKDG RLRKLEEDRA EAAEAAEERL DCCSDGCTDS LVGHNEEASG HNGETRTSRP 

      1030       1040       1050       1060       1070       1080 
GGTRASCGGR VTGGSSSSSS ELSTPEKPPS QRFSSRWEPA LGEPSSSIPT TVGSLPSSKS 

      1090       1100       1110       1120       1130       1140 
FLGMKARELF RNKSESQCDE DSVTMSSSSL SETLKTELGK DSGTENKTSL SLDAPHPSSP 

      1150       1160 
NSDNVGQLHI MDYNETHPEH S

« Hide

Isoform 2 [UniParc].

Checksum: 3D47312F1393101A
Show »

FASTA1,160128,675
Isoform 3 [UniParc].

Checksum: ED4C4AE278DFECED
Show »

FASTA1,155128,249
Isoform 4 [UniParc].

Checksum: 3E6EB98C8A3DC42E
Show »

FASTA1,148127,377

References

« Hide 'large scale' references
[1]"Genomic organization and comparative analysis of the mouse tuberous sclerosis 1 (Tsc1) locus."
Cheadle J.P., Dobbie L., Idziaszczyk S., Hodges A.K., Smith A.J.H., Sampson J.R., Young J.M.
Mamm. Genome 11:1135-1138(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"A germ-line Tsc1 mutation causes tumor development and embryonic lethality that are similar, but not identical to, those caused by Tsc2 mutation in mice."
Kobayashi T., Minowa O., Sugitani Y., Takai S., Mitani H., Kobayashi E., Noda T., Hino O.
Proc. Natl. Acad. Sci. U.S.A. 98:8762-8767(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: 129/Sv.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Strain: C57BL/6.
Tissue: Brain.
[7]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-1161 (ISOFORM 3).
Tissue: Brain.
[8]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ271911 Genomic DNA. Translation: CAC20676.1.
AJ271912 mRNA. Translation: CAC20677.1.
AK147428 mRNA. Translation: BAE27905.1.
AB047561 mRNA. Translation: BAB60810.1.
AL731851 Genomic DNA. Translation: CAM22294.1.
AL731851 Genomic DNA. Translation: CAM22295.1.
AL731851 Genomic DNA. Translation: CAM22296.2.
CH466542 Genomic DNA. Translation: EDL08392.1.
BC052399 mRNA. Translation: AAH52399.1.
AK122229 mRNA. Translation: BAC65511.1.
IPIIPI00109178.
IPI00754969.
IPI00756571.
IPI00943454.
RefSeqNP_075025.2. NM_022887.3.
UniGeneMm.224354.

3D structure databases

ProteinModelPortalQ9EP53.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9EP53. 1 interaction.
STRING10090.ENSMUSP00000109500.

PTM databases

PhosphoSiteQ9EP53.

Proteomic databases

PaxDbQ9EP53.
PRIDEQ9EP53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028155; ENSMUSP00000028155; ENSMUSG00000026812.
ENSMUST00000113867; ENSMUSP00000109498; ENSMUSG00000026812.
ENSMUST00000113869; ENSMUSP00000109500; ENSMUSG00000026812.
ENSMUST00000113870; ENSMUSP00000109501; ENSMUSG00000026812.
GeneID64930.
KEGGmmu:64930.
UCSCuc008iyv.1. mouse.
uc008iyw.1. mouse.
uc008iyx.1. mouse.

Organism-specific databases

CTD7248.
MGIMGI:1929183. Tsc1.
RougeSearch...

Phylogenomic databases

eggNOGNOG68098.
GeneTreeENSGT00390000014148.
HOGENOMHOG000232119.
InParanoidQ9EP53.
KOK07206.
OMAEHNAAMK.
OrthoDBEOG4S4PFD.

Gene expression databases

ArrayExpressQ9EP53.
BgeeQ9EP53.
GenevestigatorQ9EP53.

Family and domain databases

InterProIPR007483. Hamartin.
[Graphical view]
PANTHERPTHR15154. PTHR15154. 1 hit.
PfamPF04388. Hamartin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320227.
SOURCESearch...

Entry information

Entry nameTSC1_MOUSE
AccessionPrimary (citable) accession number: Q9EP53
Secondary accession number(s): A2AHW1 expand/collapse secondary AC list , Q3UHF2, Q7TS92, Q80U55, Q924U7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents