Variant position: 99 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 RQLSSGVSEIRHTADRWRVS LDVNHFAPDELTVKTKDGVVE
Mouse RQLSSGVSEIRQTADRWRVS LDVNHFAPEELTVKTKEGVVE
Rat RQLSSGVSEIRQTADRWRVS LDVNHFAPEELTVKTKEGVVE
Pig RQLSSGVSEIQQTADRWRVS LDVNHFAPEELTVKTKDGVVE
Bovine RQLSSGVSEIQQTADRWRVS LDVNHFAPEELTVKTKDGVVE
Chicken -ELSSGISEIRQSADSWKVT LDVNHFAPEELVVKTKDNIVE
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
76 – 184 sHSP
70 – 205 Interaction with TGFB1I1
82 – 82 Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5
83 – 83 Phosphoserine
86 – 86 Phosphoserine
98 – 98 Phosphoserine
82 – 82 S -> D. Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78.
94 – 100
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;
Structure and properties of G84R and L99M mutants of human small heat shock protein HspB1 correlating with motor neuropathy.
Nefedova V.V.; Sudnitsyna M.V.; Strelkov S.V.; Gusev N.B.;
Arch. Biochem. Biophys. 538:16-24(2013)
Cited for: CHARACTERIZATION OF VARIANTS HMN2B ARG-84 AND MET-99; INTERACTION WITH HSPB6;
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.