Sequence information
Variant position: 117 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1164 The length of the canonical sequence.
Location on the sequence:
IRLQPSWKHKLSQAPLLPSL
L KCLKMDTDVVVLTTGVLVLI
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human IRLQPSWKHKLSQAPLLPSLL KCLKMDTDVVVLTTGVLVLI
Mouse VRLQPSWKHKLSQAPLLPSLL KCLKMDTDVVVLTTGVLVLI
Rat VRLQPSWKHKLSQAPLLPSLL KCLKMDTDVVVLTTGVLVLI
Fission yeast RQAVGEWWDQIF-FPFLNSPT QLKPVFSDLKSILFYILIFH
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
1 – 1164
Hamartin
Alternative sequence
70 – 120
Missing. In isoform 2.
Literature citations
Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
Woodford M.R.; Sager R.A.; Marris E.; Dunn D.M.; Blanden A.R.; Murphy R.L.; Rensing N.; Shapiro O.; Panaretou B.; Prodromou C.; Loh S.N.; Gutmann D.H.; Bourboulia D.; Bratslavsky G.; Wong M.; Mollapour M.;
EMBO J. 36:3650-3665(2017)
Cited for: FUNCTION; IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; STIP1; CDC37; PPP5C; PTGES3; TSC2; AKT; CDK4; RAF1 AND NR3C1; INTERACTION WITH HSP90AA1 AND TSC2; VARIANT PRO-117;
Missense mutations to the TSC1 gene cause tuberous sclerosis complex.
Nellist M.; van den Heuvel D.; Schluep D.; Exalto C.; Goedbloed M.; Maat-Kievit A.; van Essen T.; van Spaendonck-Zwarts K.; Jansen F.; Helderman P.; Bartalini G.; Vierimaa O.; Penttinen M.; van den Ende J.; van den Ouweland A.; Halley D.;
Eur. J. Hum. Genet. 17:319-328(2009)
Cited for: VARIANTS TSC1 PRO-117; VAL-128 DEL; PRO-180; HIS-191; 198-ASN-PHE-199 DELINS ILE; ARG-224; LYS-246; ARG-305 AND TRP-305; VARIANTS GLN-509; SER-1035 AND HIS-1097; CHARACTERIZATION OF VARIANTS TSC1 PRO-117; VAL-128 DEL; PRO-180; HIS-191; 198-ASN-PHE-199 DELINS ILE; ARG-224; LYS-246; ARG-305 AND TRP-305; CHARACTERIZATION OF VARIANTS GLN-509; SER-1035 AND HIS-1097;
Functional assessment of TSC1 missense variants identified in individuals with tuberous sclerosis complex.
Hoogeveen-Westerveld M.; Ekong R.; Povey S.; Karbassi I.; Batish S.D.; den Dunnen J.T.; van Eeghen A.; Thiele E.; Mayer K.; Dies K.; Wen L.; Thompson C.; Sparagana S.P.; Davies P.; Aalfs C.; van den Ouweland A.; Halley D.; Nellist M.;
Hum. Mutat. 33:476-479(2012)
Cited for: VARIANTS TSC1 ARG-61; ILE-126; ASP-132; ILE-133; GLN-336; SER-362; ILE-411; PRO-523; HIS-693; ARG-698; HIS-701; SER-762; GLY-811; THR-883; VAL-978; SER-1043 DEL AND TYR-1146; VARIANTS SER-158; PRO-204; SER-448 AND VAL-567; CHARACTERIZATION OF VARIANTS TSC1 ARG-61; PRO-117; ILE-126; ASP-132; ILE-133; GLN-336; SER-362; ILE-411; PRO-523; HIS-693; ARG-698; HIS-701; SER-762; GLY-811; THR-883; VAL-978; SER-1043 DEL AND TYR-1146; CHARACTERIZATION OF VARIANTS SER-158; PRO-204; SER-448 AND VAL-567;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.