Variant position: 39 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:
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 FRDWYP-HSRLFDQAFGLPRL PEEWSQWLGGSSWPGYVRPLP
Mouse FRDWYPAHSRLFDQAFGVPRL PDEWSQWFSAAGWPGYVRPL
Rat FRDWYPAHSRLFDQAFGVPRF PDEWSQWFSSAGWPGYVRPL
Pig FRDWYPAHSRLFDQAFGLPRL PEEWSQWLSHSGWPGYVRPL
Bovine FRDWYPAHSRLFDQAFGLPRL PEEWSQWLSHSGWPGYVRAL
Chicken FRDWYH-GSRLFDQSFGMPHI PEDWYKWPSGSAWPGYFRLL
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
1 – 205 Heat shock protein beta-1
26 – 26 Phosphoserine
Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2.
Houlden H.; Laura M.; Wavrant-De Vrieze F.; Blake J.; Wood N.; Reilly M.M.;
Cited for: VARIANTS HMN2B LEU-39; ARG-84; MET-99; PHE-135 AND GLY-140;
HSPB1 and HSPB8 in inherited neuropathies: study of an Italian cohort of dHMN and CMT2 patients.
Capponi S.; Geroldi A.; Fossa P.; Grandis M.; Ciotti P.; Gulli R.; Schenone A.; Mandich P.; Bellone E.;
J. Peripher. Nerv. Syst. 16:287-294(2011)
Cited for: VARIANTS HMN2B ARG-34; LYS-41; LEU-136 AND ILE-180; VARIANTS CMT2F LEU-39; LEU-136 AND TRP-188;
Characterization of mutants of human small heat shock protein HspB1 carrying replacements in the n-terminal domain and associated with hereditary motor neuron diseases.
Muranova L.K.; Weeks S.D.; Strelkov S.V.; Gusev N.B.;
PLoS ONE 10:E0126248-E0126248(2015)
Cited for: CHARACTERIZATION OF VARIANTS HMN2B ARG-34; LEU-39 AND LYS-41;
Axonal Neuropathies due to Mutations in Small Heat Shock Proteins: Clinical, Genetic, and Functional Insights into Novel Mutations.
Echaniz-Laguna A.; Geuens T.; Petiot P.; Pereon Y.; Adriaenssens E.; Haidar M.; Capponi S.; Maisonobe T.; Fournier E.; Dubourg O.; Degos B.; Salachas F.; Lenglet T.; Eymard B.; Delmont E.; Pouget J.; Juntas Morales R.; Goizet C.; Latour P.; Timmerman V.; Stojkovic T.;
Hum. Mutat. 38:556-568(2017)
Cited for: VARIANTS HMN2B SER-7; LEU-39; ASP-53; TRP-127; ARG-128; ILE-151; 175-GLN--LYS-205 DEL; ILE-180 AND LEU-187; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS HMN2B SER-7; ASP-53; ARG-128 AND LEU-187;
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.