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Q9Z136 (TSC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Hamartin
Alternative name(s):
Tuberous sclerosis 1 protein homolog
Gene names
Name:Tsc1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1163 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 DOCK7 By similarity. Interacts with TSC2, leading to stabilize TSC2. In the absence of TSC2, TSC1 self-aggregates. Interacts with FBXW5 and TBC1D7 By similarity. Ref.2

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Note: At steady state found in association with membranes By similarity. Ref.2

Tissue specificity

Highly expressed in brain, spleen and kidney, followed by liver and heart.

Domain

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

Post-translational modification

Phosphorylation at Ser-505 does not affect interaction with TSC2.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell projection organization

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from electronic annotation. Source: Ensembl

negative regulation of TOR signaling

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell size

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of translation

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

positive regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from direct assay PubMed 17379185. Source: RGD

protein stabilization

Inferred from electronic annotation. Source: Ensembl

rRNA export from nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of Ras GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 15611338. Source: RGD

regulation of cell cycle

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of focal adhesion assembly

Inferred from mutant phenotype PubMed 15611338. Source: RGD

regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of stress fiber assembly

Inferred from mutant phenotype PubMed 15611338. Source: RGD

response to insulin

Inferred from electronic annotation. Source: Ensembl

synapse organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentTSC1-TSC2 complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

actin filament

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred from direct assay PubMed 12147258. Source: RGD

cytosol

Inferred from direct assay PubMed 12147258. Source: RGD

growth cone

Inferred from direct assay PubMed 12226091. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 12147258. Source: RGD

lamellipodium

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 17379185. Source: RGD

   Molecular_functionGTPase activating protein binding

Inferred from physical interaction PubMed 17379185. Source: RGD

GTPase regulator activity

Inferred from mutant phenotype PubMed 15611338. Source: RGD

protein N-terminus binding

Inferred from physical interaction PubMed 17379185. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11631163Hamartin
PRO_0000065652

Regions

Coiled coil721 – 919199 Potential
Coiled coil970 – 99425 Potential
Compositional bias1038 – 10436Poly-Ser

Amino acid modifications

Modified residue5051Phosphoserine By similarity
Modified residue5111Phosphoserine By similarity
Modified residue5981Phosphoserine By similarity

Experimental info

Mutagenesis2871H → Q in chemically induced renal carcinogenesis. Ref.1
Mutagenesis6741V → L in chemically induced renal carcinogenesis. Ref.1
Mutagenesis10271R → W in chemically induced renal carcinogenesis. Ref.1
Mutagenesis11061M → V in chemically induced renal carcinogenesis. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z136 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: CB5AE6A12AE3B0A1

FASTA1,163129,022
        10         20         30         40         50         60 
MAQLANIGEL LSMLDSSTLG VRDDVTTIFK ESLNSERGPM LVNTLVDYYL ETNSQPVLHI 

        70         80         90        100        110        120 
LTTLQEPHDK HLLDKMNEYV 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 YEDGDAVSHQ LSACFPHRSA DVTTSSYVDT 

       310        320        330        340        350        360 
QNSYGGATST PSSTSRLMLF STPGQLPQSL SSLSTRPLPE PLQASLWSPS AVCGMTTPPT 

       370        380        390        400        410        420 
SPGNVPADLS HPYSKAFGTT TGGKGTPSGT PATSPPPAPP CPQDDCAHGP ASQASATPPR 

       430        440        450        460        470        480 
KEERADSSRP YLPRQQDVPS DRGLEDLPGS KGSVTLRNLP DFLGDLASEE DSIEKDKEEA 

       490        500        510        520        530        540 
AISKELSEIT TAEADPVAPR GGFDSPFYRD SLSGSQRKTH SAASGTQGFS VNPEPLHSSL 

       550        560        570        580        590        600 
DKHGPDTPKQ AFTPIDPPSG SADASPAGDR DRQTSLETSI LTPSPCKIPP QRGVSFGSGQ 

       610        620        630        640        650        660 
LPPYDHLFEV ALPKTACHFV SKKTEELLKK AKGNPEEDCV PSTSPMEVLD RLLEQGAGAH 

       670        680        690        700        710        720 
SKELSRLSLP SKSVDWTHFG GSPPSDEIRT LRDQLLLLHN QLLYERFKRQ QHALRNRRLL 

       730        740        750        760        770        780 
RKVIRAAALE EHNAAMKDQL KLQEKDIQMW KVSLQKEQAR YSQLQQQRDT MVTQLHSQIR 

       790        800        810        820        830        840 
QLQHDREEFY NQSQELQTKL EDCRSMIAEL RVELKKANSK VCHTELLLSQ VSQKLSNSES 

       850        860        870        880        890        900 
VQQQMEFLNR QLLVLGEVNE LYLEQLQSKH PDTTKEVEMM KTAYRKELEK NRSHLLQQNQ 

       910        920        930        940        950        960 
RLDASQRRVL ELESLLAKKD HLLLEQKKYL EDVKSQASGQ LLAAESRYEA QRKITRVLEL 

       970        980        990       1000       1010       1020 
EILDLYGRLE KDGRLQKLEE DRAEAAEAAE ERLDCCTDGC SDSLLGHNEE AAGHNGETRT 

      1030       1040       1050       1060       1070       1080 
SRPGGTRASC GGRVTGGSSS SSSELSTPEK PPNQRFSSRW EPTMGEPSSS IPTTVGSLPS 

      1090       1100       1110       1120       1130       1140 
SKSFLGMKTR ELFRNKSESQ CDEDGMTMSS FSETLKTELG KDSAGMENKT PPSLDAPHPS 

      1150       1160 
SPSSDSMGQL HIMDYNETHH EHS 

« Hide

References

[1]"Isolation and characterization of a rat homologue of the human tuberous sclerosis 1 gene (Tsc1) and analysis of its mutations in rat renal carcinomas."
Satake N., Kobayashi T., Kobayashi E., Izumi K., Hino O.
Cancer Res. 59:849-855(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF HIS-287; VAL-674; ARG-1027 AND MET-1106.
Strain: Long Evans.
Tissue: Kidney.
[2]"Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles."
Plank T.L., Yeung R.S., Henske E.P.
Cancer Res. 58:4766-4770(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TSC2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011821 mRNA. Translation: BAA75254.1.
RefSeqNP_068626.1. NM_021854.1.
XP_006233905.1. XM_006233843.1.
XP_006233906.1. XM_006233844.1.
XP_006233907.1. XM_006233845.1.
XP_006233908.1. XM_006233846.1.
XP_006233909.1. XM_006233847.1.
XP_006233910.1. XM_006233848.1.
UniGeneRn.205837.
Rn.230448.

3D structure databases

ProteinModelPortalQ9Z136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248838. 6 interactions.
IntActQ9Z136. 1 interaction.
STRING10116.ENSRNOP00000016904.

PTM databases

PhosphoSiteQ9Z136.

Proteomic databases

PaxDbQ9Z136.
PRIDEQ9Z136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016904; ENSRNOP00000016904; ENSRNOG00000011470.
GeneID60445.
KEGGrno:60445.
UCSCRGD:620124. rat.

Organism-specific databases

CTD7248.
RGD620124. Tsc1.

Phylogenomic databases

eggNOGNOG68098.
GeneTreeENSGT00390000014148.
HOGENOMHOG000232119.
HOVERGENHBG012559.
InParanoidQ9Z136.
KOK07206.
OMANAAMKDQ.
OrthoDBEOG7NKKJH.
PhylomeDBQ9Z136.
TreeFamTF325466.

Gene expression databases

GenevestigatorQ9Z136.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view]
PANTHERPTHR15154. PTHR15154. 1 hit.
PfamPF04388. Hamartin. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio612184.
PROQ9Z136.

Entry information

Entry nameTSC1_RAT
AccessionPrimary (citable) accession number: Q9Z136
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program