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Protein

Hamartin

Gene

Tsc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • chaperone binding Source: MGI
  • GTPase regulator activity Source: GO_Central
  • protein N-terminus binding Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: MGI
  • adaptive immune response Source: MGI
  • adult locomotory behavior Source: ParkinsonsUK-UCL
  • cardiac muscle cell differentiation Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell projection organization Source: MGI
  • cellular response to oxygen-glucose deprivation Source: ParkinsonsUK-UCL
  • cerebral cortex development Source: MGI
  • glucose import Source: MGI
  • hippocampus development Source: MGI
  • kidney development Source: MGI
  • memory T cell differentiation Source: MGI
  • myelination Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cell size Source: MGI
  • negative regulation of insulin receptor signaling pathway Source: GO_Central
  • negative regulation of macroautophagy Source: ParkinsonsUK-UCL
  • negative regulation of TOR signaling Source: ParkinsonsUK-UCL
  • negative regulation of translation Source: MGI
  • nervous system development Source: MGI
  • neural tube closure Source: MGI
  • positive regulation of focal adhesion assembly Source: MGI
  • potassium ion transport Source: MGI
  • protein heterooligomerization Source: Ensembl
  • protein stabilization Source: MGI
  • regulation of actin cytoskeleton organization Source: GO_Central
  • regulation of cell cycle Source: GO_Central
  • regulation of cell-matrix adhesion Source: MGI
  • regulation of GTPase activity Source: GO_Central
  • regulation of neuron death Source: ParkinsonsUK-UCL
  • regulation of phosphoprotein phosphatase activity Source: MGI
  • regulation of protein kinase activity Source: MGI
  • regulation of stress fiber assembly Source: MGI
  • regulation of translation Source: MGI
  • response to insulin Source: MGI
  • rRNA export from nucleus Source: MGI
  • synapse organization Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165181. Inhibition of TSC complex formation by PKB.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Hamartin
Alternative name(s):
Tuberous sclerosis 1 protein homolog
Gene namesi
Name:Tsc1
Synonyms:Kiaa0243
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1929183. Tsc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11611161HamartinPRO_0000379922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei502 – 5021PhosphoserineCombined sources
Modified residuei508 – 5081PhosphoserineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei592 – 5921PhosphoserineCombined sources
Modified residuei595 – 5951PhosphoserineBy similarity
Modified residuei1094 – 10941PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EP53.
MaxQBiQ9EP53.
PaxDbiQ9EP53.
PeptideAtlasiQ9EP53.
PRIDEiQ9EP53.

PTM databases

iPTMnetiQ9EP53.
PhosphoSiteiQ9EP53.

Expressioni

Gene expression databases

BgeeiQ9EP53.
ExpressionAtlasiQ9EP53. baseline and differential.
GenevisibleiQ9EP53. MM.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Tsc2Q610375EBI-1202690,EBI-7924402

GO - Molecular functioni

  • chaperone binding Source: MGI
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi211115. 26 interactions.
IntActiQ9EP53. 23 interactions.
STRINGi10090.ENSMUSP00000028155.

Structurei

3D structure databases

ProteinModelPortaliQ9EP53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili721 – 849129Sequence analysisAdd
BLAST
Coiled coili879 – 91739Sequence analysisAdd
BLAST
Coiled coili967 – 99125Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi312 – 3154Poly-Ser
Compositional biasi692 – 6954Poly-Leu
Compositional biasi1035 – 10406Poly-Ser
Compositional biasi1106 – 11116Poly-Ser

Domaini

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG36. Eukaryota.
ENOG411020J. LUCA.
GeneTreeiENSGT00390000014148.
HOGENOMiHOG000232119.
InParanoidiQ9EP53.
KOiK07206.
OMAiPKQAFTP.
OrthoDBiEOG7NKKJH.
TreeFamiTF325466.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view]
PANTHERiPTHR15154. PTHR15154. 1 hit.
PfamiPF04388. Hamartin. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EP53-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAQLANIGEL LSMLDSSTLG VRDDVTAIFK ESLNSERGPM LVNTLVDYYL
60 70 80 90 100
ETNSQPVLHI LTTLQEPHDK HLLDKINEYV GKAATRLSIL SLLGHVVRLQ
110 120 130 140 150
PSWKHKLSQA PLLPSLLKCL KMDTDVVVLT TGVLVLITML PMIPQSGKQH
160 170 180 190 200
LLDFFDIFGR LSSWCLKKPG HVTEVYLVHL HASVYALFHR LYGMYPCNFV
210 220 230 240 250
SFLRSHYSMK ENVETFEEVV KPMMEHVRIH PELVTGSKDH ELDPRRWKTL
260 270 280 290 300
ETHDVVIECA KISLDPTEAS YEDGYSVSHQ LSACFPYRSA DVTTSPYVDT
310 320 330 340 350
QNSYGGSTST PSSSSRLMLF SPPGQLPQSL SSPSTRLLPE PLQASLWSPS
360 370 380 390 400
AVCGMTTPPT SPGNVPADLS HPYSKAFGTT AGGKGTPSGT PATSPPPAPP
410 420 430 440 450
CPQDDCVHGS AAQASATAPR KEERADSSRP YLHRQSNDRG LEDPPGSKGS
460 470 480 490 500
VTLRNLPDFL GDLASEEDSI EKDKEEAAIS KELSEITTAE ADPVVPRGGF
510 520 530 540 550
DSPFYRDSLS GSQRKTHSAA SGTQGSSVNP EPLHSSLDKH GPDTPKQAFT
560 570 580 590 600
PIDPPSGSAD VSPAGDRDRQ TSLETSILTP SPCKIPPQRG VSFGSGQLPP
610 620 630 640 650
YDHLFEVALP KTACHFVSKK TEELLKKVKG NPEEDCVPST SPMEVLDRLI
660 670 680 690 700
EQGAGAHSKE LSRLSLPSKS VDWTHFGGSP PSDELRTLRD QLLLLHNQLL
710 720 730 740 750
YERFKRQQHA LRNRRLLRKV IRAAALEEHN AAMKDQLKLQ EKDIQMWKVS
760 770 780 790 800
LQKEQARYSQ LQEQRDTMVT QLHSQIRQLQ HDREEFYNQS QELQTKLEDC
810 820 830 840 850
RNMIAELRVE LKKANNKVCH TELLLSQVSQ KLSNSESVQQ QMEFLNRQLL
860 870 880 890 900
VLGEVNELYL EQLQSKHPDT TKEVEMMKTA YRKELEKNRS HLLQQNQRLD
910 920 930 940 950
ASQRRVLELE SLLAKKDHLL LEQKKYLEDV KSQASGQLLA AESRYEAQRK
960 970 980 990 1000
ITRVLELEIL DLYGRLEKDG RLRKLEEDRA EAAEAAEERL DCCSDGCTDS
1010 1020 1030 1040 1050
LVGHNEEASG HNGETRTSRP GGTRASCGGR VTGGSSSSSS ELSTPEKPPS
1060 1070 1080 1090 1100
QRFSSRWEPA LGEPSSSIPT TVGSLPSSKS FLGMKARELF RNKSESQCDE
1110 1120 1130 1140 1150
DSVTMSSSSL SETLKTELGK DSGTENKTSL SLDAPHPSSP NSDNVGQLHI
1160
MDYNETHPEH S
Length:1,161
Mass (Da):128,746
Last modified:March 1, 2001 - v1
Checksum:iF80ACF8492007801
GO
Isoform 2 (identifier: Q9EP53-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,160
Mass (Da):128,675
Checksum:i3D47312F1393101A
GO
Isoform 3 (identifier: Q9EP53-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     381-381: Missing.
     678-682: Missing.

Show »
Length:1,155
Mass (Da):128,249
Checksum:iED4C4AE278DFECED
GO
Isoform 4 (identifier: Q9EP53-4) [UniParc]FASTAAdd to basket

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

Show »
Length:1,148
Mass (Da):127,377
Checksum:i3E6EB98C8A3DC42E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei381 – 3811Missing in isoform 2, isoform 3 and isoform 4. 4 PublicationsVSP_037747
Alternative sequencei678 – 6825Missing in isoform 3. 2 PublicationsVSP_037748
Alternative sequencei1056 – 106712Missing in isoform 4. 1 PublicationVSP_037749Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15844.1. [Q9EP53-2]
CCDS71013.1. [Q9EP53-3]
CCDS79762.1. [Q9EP53-1]
RefSeqiNP_001276504.1. NM_001289575.1. [Q9EP53-1]
NP_001276505.1. NM_001289576.1. [Q9EP53-3]
NP_075025.2. NM_022887.4. [Q9EP53-2]
XP_011237446.1. XM_011239144.1. [Q9EP53-2]
UniGeneiMm.224354.

Genome annotation databases

EnsembliENSMUST00000028155; ENSMUSP00000028155; ENSMUSG00000026812. [Q9EP53-2]
ENSMUST00000113867; ENSMUSP00000109498; ENSMUSG00000026812. [Q9EP53-3]
ENSMUST00000113869; ENSMUSP00000109500; ENSMUSG00000026812. [Q9EP53-1]
ENSMUST00000113870; ENSMUSP00000109501; ENSMUSG00000026812. [Q9EP53-2]
GeneIDi64930.
KEGGimmu:64930.
UCSCiuc008iyw.2. mouse. [Q9EP53-1]
uc008iyx.2. mouse. [Q9EP53-3]
uc008iyz.2. mouse. [Q9EP53-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15844.1. [Q9EP53-2]
CCDS71013.1. [Q9EP53-3]
CCDS79762.1. [Q9EP53-1]
RefSeqiNP_001276504.1. NM_001289575.1. [Q9EP53-1]
NP_001276505.1. NM_001289576.1. [Q9EP53-3]
NP_075025.2. NM_022887.4. [Q9EP53-2]
XP_011237446.1. XM_011239144.1. [Q9EP53-2]
UniGeneiMm.224354.

3D structure databases

ProteinModelPortaliQ9EP53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211115. 26 interactions.
IntActiQ9EP53. 23 interactions.
STRINGi10090.ENSMUSP00000028155.

PTM databases

iPTMnetiQ9EP53.
PhosphoSiteiQ9EP53.

Proteomic databases

EPDiQ9EP53.
MaxQBiQ9EP53.
PaxDbiQ9EP53.
PeptideAtlasiQ9EP53.
PRIDEiQ9EP53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028155; ENSMUSP00000028155; ENSMUSG00000026812. [Q9EP53-2]
ENSMUST00000113867; ENSMUSP00000109498; ENSMUSG00000026812. [Q9EP53-3]
ENSMUST00000113869; ENSMUSP00000109500; ENSMUSG00000026812. [Q9EP53-1]
ENSMUST00000113870; ENSMUSP00000109501; ENSMUSG00000026812. [Q9EP53-2]
GeneIDi64930.
KEGGimmu:64930.
UCSCiuc008iyw.2. mouse. [Q9EP53-1]
uc008iyx.2. mouse. [Q9EP53-3]
uc008iyz.2. mouse. [Q9EP53-2]

Organism-specific databases

CTDi7248.
MGIiMGI:1929183. Tsc1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IG36. Eukaryota.
ENOG411020J. LUCA.
GeneTreeiENSGT00390000014148.
HOGENOMiHOG000232119.
InParanoidiQ9EP53.
KOiK07206.
OMAiPKQAFTP.
OrthoDBiEOG7NKKJH.
TreeFamiTF325466.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165181. Inhibition of TSC complex formation by PKB.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiTsc1. mouse.
PROiQ9EP53.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EP53.
ExpressionAtlasiQ9EP53. baseline and differential.
GenevisibleiQ9EP53. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view]
PANTHERiPTHR15154. PTHR15154. 1 hit.
PfamiPF04388. Hamartin. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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/6J.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiTSC1_MOUSE
AccessioniPrimary (citable) accession number: Q9EP53
Secondary accession number(s): A2AHW1
, Q3UHF2, Q7TS92, Q80U55, Q924U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.