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Q9Z136

- TSC1_RAT

UniProt

Q9Z136 - TSC1_RAT

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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).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

GO - Biological processi

  1. activation of Rho GTPase activity Source: Ensembl
  2. cardiac muscle cell differentiation Source: Ensembl
  3. cell-matrix adhesion Source: Ensembl
  4. cell projection organization 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 cell proliferation Source: Ensembl
  10. negative regulation of cell size Source: Ensembl
  11. negative regulation of insulin receptor signaling pathway Source: RefGenome
  12. negative regulation of TOR signaling 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. regulation of actin cytoskeleton organization Source: RGD
  20. regulation of cell cycle Source: RefGenome
  21. regulation of focal adhesion assembly Source: RGD
  22. regulation of phosphoprotein phosphatase activity Source: Ensembl
  23. regulation of protein kinase activity Source: Ensembl
  24. regulation of Ras GTPase activity Source: RefGenome
  25. regulation of stress fiber assembly Source: RGD
  26. response to insulin Source: Ensembl
  27. rRNA export from nucleus Source: Ensembl
  28. synapse organization Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_232838. Regulation of Rheb GTPase activity by AMPK.
REACT_255904. Inhibition of TSC complex formation by PKB.

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

GO - Cellular componenti

  1. actin filament Source: Ensembl
  2. cell cortex Source: Ensembl
  3. cytoskeleton Source: RGD
  4. cytosol Source: RGD
  5. growth cone Source: RGD
  6. intracellular membrane-bounded organelle Source: RGD
  7. lamellipodium Source: Ensembl
  8. membrane Source: UniProtKB-KW
  9. protein complex Source: RGD
  10. TSC1-TSC2 complex Source: RefGenome
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 – 11631163HamartinPRO_0000065652Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9Z136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili721 – 919199Sequence AnalysisAdd
BLAST
Coiled coili970 – 99425Sequence AnalysisAdd
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

        10         20         30         40         50
MAQLANIGEL LSMLDSSTLG VRDDVTTIFK ESLNSERGPM LVNTLVDYYL
60 70 80 90 100
ETNSQPVLHI LTTLQEPHDK HLLDKMNEYV 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 YEDGDAVSHQ LSACFPHRSA DVTTSSYVDT
310 320 330 340 350
QNSYGGATST PSSTSRLMLF STPGQLPQSL SSLSTRPLPE PLQASLWSPS
360 370 380 390 400
AVCGMTTPPT SPGNVPADLS HPYSKAFGTT TGGKGTPSGT PATSPPPAPP
410 420 430 440 450
CPQDDCAHGP ASQASATPPR KEERADSSRP YLPRQQDVPS DRGLEDLPGS
460 470 480 490 500
KGSVTLRNLP DFLGDLASEE DSIEKDKEEA AISKELSEIT TAEADPVAPR
510 520 530 540 550
GGFDSPFYRD SLSGSQRKTH SAASGTQGFS VNPEPLHSSL DKHGPDTPKQ
560 570 580 590 600
AFTPIDPPSG SADASPAGDR DRQTSLETSI LTPSPCKIPP QRGVSFGSGQ
610 620 630 640 650
LPPYDHLFEV ALPKTACHFV SKKTEELLKK AKGNPEEDCV PSTSPMEVLD
660 670 680 690 700
RLLEQGAGAH SKELSRLSLP SKSVDWTHFG GSPPSDEIRT LRDQLLLLHN
710 720 730 740 750
QLLYERFKRQ QHALRNRRLL RKVIRAAALE EHNAAMKDQL KLQEKDIQMW
760 770 780 790 800
KVSLQKEQAR YSQLQQQRDT MVTQLHSQIR QLQHDREEFY NQSQELQTKL
810 820 830 840 850
EDCRSMIAEL RVELKKANSK VCHTELLLSQ VSQKLSNSES VQQQMEFLNR
860 870 880 890 900
QLLVLGEVNE LYLEQLQSKH PDTTKEVEMM KTAYRKELEK NRSHLLQQNQ
910 920 930 940 950
RLDASQRRVL ELESLLAKKD HLLLEQKKYL EDVKSQASGQ LLAAESRYEA
960 970 980 990 1000
QRKITRVLEL EILDLYGRLE KDGRLQKLEE DRAEAAEAAE ERLDCCTDGC
1010 1020 1030 1040 1050
SDSLLGHNEE AAGHNGETRT SRPGGTRASC GGRVTGGSSS SSSELSTPEK
1060 1070 1080 1090 1100
PPNQRFSSRW EPTMGEPSSS IPTTVGSLPS SKSFLGMKTR ELFRNKSESQ
1110 1120 1130 1140 1150
CDEDGMTMSS FSETLKTELG KDSAGMENKT PPSLDAPHPS SPSSDSMGQL
1160
HIMDYNETHH EHS
Length:1,163
Mass (Da):129,022
Last modified:May 1, 1999 - v1
Checksum:iCB5AE6A12AE3B0A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011821 mRNA. Translation: BAA75254.1.
RefSeqiNP_068626.1. NM_021854.1.
XP_006233905.1. XM_006233843.2.
XP_006233906.1. XM_006233844.2.
XP_006233907.1. XM_006233845.2.
XP_006233908.1. XM_006233846.2.
XP_006233909.1. XM_006233847.2.
UniGeneiRn.205837.
Rn.230448.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011821 mRNA. Translation: BAA75254.1 .
RefSeqi NP_068626.1. NM_021854.1.
XP_006233905.1. XM_006233843.2.
XP_006233906.1. XM_006233844.2.
XP_006233907.1. XM_006233845.2.
XP_006233908.1. XM_006233846.2.
XP_006233909.1. XM_006233847.2.
UniGenei Rn.205837.
Rn.230448.

3D structure databases

ProteinModelPortali Q9Z136.
ModBasei Search...
MobiDBi 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.

Enzyme and pathway databases

Reactomei REACT_232838. Regulation of Rheb GTPase activity by AMPK.
REACT_255904. Inhibition of TSC complex formation by PKB.

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: November 26, 2014
This is version 98 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