SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Z136

- TSC1_RAT

UniProt

Q9Z136 - TSC1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Hamartin
Gene
Tsc1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

GO - Molecular functioni

  1. GTPase activating protein binding Source: RGD
  2. GTPase regulator activity Source: RGD
  3. protein N-terminus binding Source: RGD
Complete GO annotation...

GO - Biological processi

  1. activation of Rho GTPase activity Source: Ensembl
  2. cardiac muscle cell differentiation Source: Ensembl
  3. cell projection organization Source: Ensembl
  4. cell-matrix adhesion Source: Ensembl
  5. cerebral cortex development Source: Ensembl
  6. hippocampus development Source: Ensembl
  7. kidney development Source: Ensembl
  8. myelination Source: Ensembl
  9. negative regulation of TOR signaling Source: RefGenome
  10. negative regulation of cell proliferation Source: Ensembl
  11. negative regulation of cell size Source: Ensembl
  12. negative regulation of insulin receptor signaling pathway Source: RefGenome
  13. negative regulation of translation Source: Ensembl
  14. neural tube closure Source: Ensembl
  15. positive regulation of focal adhesion assembly Source: Ensembl
  16. potassium ion transport Source: Ensembl
  17. protein heterooligomerization Source: RGD
  18. protein stabilization Source: Ensembl
  19. rRNA export from nucleus Source: Ensembl
  20. regulation of Ras GTPase activity Source: RefGenome
  21. regulation of actin cytoskeleton organization Source: RGD
  22. regulation of cell cycle Source: RefGenome
  23. regulation of focal adhesion assembly Source: RGD
  24. regulation of phosphoprotein phosphatase activity Source: Ensembl
  25. regulation of protein kinase activity Source: Ensembl
  26. regulation of stress fiber assembly Source: RGD
  27. response to insulin Source: Ensembl
  28. synapse organization Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Hamartin
Alternative name(s):
Tuberous sclerosis 1 protein homolog
Gene namesi
Name:Tsc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi620124. Tsc1.

Subcellular locationi

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity
Note: At steady state found in association with membranes By similarity.1 Publication

GO - Cellular componenti

  1. TSC1-TSC2 complex Source: RefGenome
  2. actin filament Source: Ensembl
  3. cell cortex Source: Ensembl
  4. cytoskeleton Source: RGD
  5. cytosol Source: RGD
  6. growth cone Source: RGD
  7. intracellular membrane-bounded organelle Source: RGD
  8. lamellipodium Source: Ensembl
  9. membrane Source: UniProtKB-SubCell
  10. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi287 – 2871H → Q in chemically induced renal carcinogenesis. 1 Publication
Mutagenesisi674 – 6741V → L in chemically induced renal carcinogenesis. 1 Publication
Mutagenesisi1027 – 10271R → W in chemically induced renal carcinogenesis. 1 Publication
Mutagenesisi1106 – 11061M → V in chemically induced renal carcinogenesis. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11631163Hamartin
PRO_0000065652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei505 – 5051Phosphoserine By similarity
Modified residuei511 – 5111Phosphoserine By similarity
Modified residuei598 – 5981Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z136.
PRIDEiQ9Z136.

PTM databases

PhosphoSiteiQ9Z136.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9Z136.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi248838. 6 interactions.
IntActiQ9Z136. 1 interaction.
STRINGi10116.ENSRNOP00000016904.

Structurei

3D structure databases

ProteinModelPortaliQ9Z136.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili721 – 919199 Reviewed prediction
Add
BLAST
Coiled coili970 – 99425 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1038 – 10436Poly-Ser

Domaini

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG68098.
GeneTreeiENSGT00390000014148.
HOGENOMiHOG000232119.
HOVERGENiHBG012559.
InParanoidiQ9Z136.
KOiK07206.
OMAiNAAMKDQ.
OrthoDBiEOG7NKKJH.
PhylomeDBiQ9Z136.
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.

Sequencei

Sequence statusi: Complete.

Q9Z136-1 [UniParc]FASTAAdd to Basket

« Hide

MAQLANIGEL LSMLDSSTLG VRDDVTTIFK ESLNSERGPM LVNTLVDYYL     50
ETNSQPVLHI LTTLQEPHDK HLLDKMNEYV GKAATRLSIL SLLGHVVRLQ 100
PSWKHKLSQA PLLPSLLKCL KMDTDVVVLT TGVLVLITML PMIPQSGKQH 150
LLDFFDIFGR LSSWCLKKPG HVTEVYLVHL HASVYALFHR LYGMYPCNFV 200
SFLRSHYSMK ENVETFEEVV KPMMEHVRIH PELVTGSKDH ELDPRRWKTL 250
ETHDVVIECA KISLDPTEAS YEDGDAVSHQ LSACFPHRSA DVTTSSYVDT 300
QNSYGGATST PSSTSRLMLF STPGQLPQSL SSLSTRPLPE PLQASLWSPS 350
AVCGMTTPPT SPGNVPADLS HPYSKAFGTT TGGKGTPSGT PATSPPPAPP 400
CPQDDCAHGP ASQASATPPR KEERADSSRP YLPRQQDVPS DRGLEDLPGS 450
KGSVTLRNLP DFLGDLASEE DSIEKDKEEA AISKELSEIT TAEADPVAPR 500
GGFDSPFYRD SLSGSQRKTH SAASGTQGFS VNPEPLHSSL DKHGPDTPKQ 550
AFTPIDPPSG SADASPAGDR DRQTSLETSI LTPSPCKIPP QRGVSFGSGQ 600
LPPYDHLFEV ALPKTACHFV SKKTEELLKK AKGNPEEDCV PSTSPMEVLD 650
RLLEQGAGAH SKELSRLSLP SKSVDWTHFG GSPPSDEIRT LRDQLLLLHN 700
QLLYERFKRQ QHALRNRRLL RKVIRAAALE EHNAAMKDQL KLQEKDIQMW 750
KVSLQKEQAR YSQLQQQRDT MVTQLHSQIR QLQHDREEFY NQSQELQTKL 800
EDCRSMIAEL RVELKKANSK VCHTELLLSQ VSQKLSNSES VQQQMEFLNR 850
QLLVLGEVNE LYLEQLQSKH PDTTKEVEMM KTAYRKELEK NRSHLLQQNQ 900
RLDASQRRVL ELESLLAKKD HLLLEQKKYL EDVKSQASGQ LLAAESRYEA 950
QRKITRVLEL EILDLYGRLE KDGRLQKLEE DRAEAAEAAE ERLDCCTDGC 1000
SDSLLGHNEE AAGHNGETRT SRPGGTRASC GGRVTGGSSS SSSELSTPEK 1050
PPNQRFSSRW EPTMGEPSSS IPTTVGSLPS SKSFLGMKTR ELFRNKSESQ 1100
CDEDGMTMSS FSETLKTELG KDSAGMENKT PPSLDAPHPS SPSSDSMGQL 1150
HIMDYNETHH EHS 1163
Length:1,163
Mass (Da):129,022
Last modified:May 1, 1999 - v1
Checksum:iCB5AE6A12AE3B0A1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011821 mRNA. Translation: BAA75254.1.
RefSeqiNP_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.
UniGeneiRn.205837.
Rn.230448.

Genome annotation databases

EnsembliENSRNOT00000016904; ENSRNOP00000016904; ENSRNOG00000011470.
GeneIDi60445.
KEGGirno:60445.
UCSCiRGD:620124. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011821 mRNA. Translation: BAA75254.1 .
RefSeqi NP_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.
UniGenei Rn.205837.
Rn.230448.

3D structure databases

ProteinModelPortali Q9Z136.
ModBasei Search...

Protein-protein interaction databases

BioGridi 248838. 6 interactions.
IntActi Q9Z136. 1 interaction.
STRINGi 10116.ENSRNOP00000016904.

PTM databases

PhosphoSitei Q9Z136.

Proteomic databases

PaxDbi Q9Z136.
PRIDEi Q9Z136.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016904 ; ENSRNOP00000016904 ; ENSRNOG00000011470 .
GeneIDi 60445.
KEGGi rno:60445.
UCSCi RGD:620124. rat.

Organism-specific databases

CTDi 7248.
RGDi 620124. Tsc1.

Phylogenomic databases

eggNOGi NOG68098.
GeneTreei ENSGT00390000014148.
HOGENOMi HOG000232119.
HOVERGENi HBG012559.
InParanoidi Q9Z136.
KOi K07206.
OMAi NAAMKDQ.
OrthoDBi EOG7NKKJH.
PhylomeDBi Q9Z136.
TreeFami TF325466.

Miscellaneous databases

NextBioi 612184.
PROi Q9Z136.

Gene expression databases

Genevestigatori Q9Z136.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view ]
PANTHERi PTHR15154. PTHR15154. 1 hit.
Pfami PF04388. Hamartin. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTSC1_RAT
AccessioniPrimary (citable) accession number: Q9Z136
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

Similar proteinsi