Sequence information
Variant position: 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 205 The length of the canonical sequence.
Location on the sequence:
TLTVEAPMPKLATQSNEITI
P VTFESRAQLGGPEAAKSDET
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 TLTVEAPMPKLATQSNEITIP VTFESRAQLGGPEAAKSDET
TLTVEAPMPKPATQSAEITIP VTFEARAQIGGPEAGKSEQS
Mouse TLTVEAPLPKAVTQSAEITIP VTFEARAQIGGPEAGKSEQS
Rat TLTVEAPLPKAVTQSAEITIP VTFEARAQIGGPE---SEQS
Pig TLSVEAPLPKPATQSAEITIP VTFEARAQLGGTEAGKSEKP
Bovine TLTVEAPLPKSATQSAEITIP VTFQARAQLGGPEAGKSEQP
Chicken MLTVEAPLPKPAIQSSEITIP VTVEAK----------KEEP
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 – 205
Heat shock protein beta-1
Domain
76 – 184
sHSP
Region
70 – 205
Interaction with TGFB1I1
Modified residue
174 – 174
Phosphothreonine
Modified residue
176 – 176
Phosphoserine
Modified residue
199 – 199
Phosphoserine
Literature citations
Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy.
Evgrafov O.V.; Mersiyanova I.; Irobi J.; Van Den Bosch L.; Dierick I.; Leung C.L.; Schagina O.; Verpoorten N.; Van Impe K.; Fedotov V.; Dadali E.; Auer-Grumbach M.; Windpassinger C.; Wagner K.; Mitrovic Z.; Hilton-Jones D.; Talbot K.; Martin J.-J.; Vasserman N.; Tverskaya S.; Polyakov A.; Liem R.K.H.; Gettemans J.; Robberecht W.; De Jonghe P.; Timmerman V.;
Nat. Genet. 36:602-606(2004)
Cited for: VARIANTS CMT2F PHE-135 AND TRP-136; VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182;
Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy.
Almeida-Souza L.; Goethals S.; de Winter V.; Dierick I.; Gallardo R.; Van Durme J.; Irobi J.; Gettemans J.; Rousseau F.; Schymkowitz J.; Timmerman V.; Janssens S.;
J. Biol. Chem. 285:12778-12786(2010)
Cited for: VARIANT TYR-156; CHARACTERIZATION OF VARIANT TYR-156; CHARACTERIZATION OF VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182; CHARACTERIZATION OF VARIANT CMT2F TRP-136; FUNCTION; SUBUNIT;
Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated phosphorylation of neurofilaments.
Holmgren A.; Bouhy D.; De Winter V.; Asselbergh B.; Timmermans J.P.; Irobi J.; Timmerman V.;
Acta Neuropathol. 126:93-108(2013)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS HMN2B TRP-127 AND LEU-182; CHARACTERIZATION OF VARIANT CMT2F PHE-135;
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.