Home  |  Contact

UniProtKB/Swiss-Prot P04792: Variant p.Ser156Tyr

Heat shock protein beta-1
Gene: HSPB1
Chromosomal location: 7q11.2-q22
Variant information

Variant position:  156
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Serine (S) to Tyrosine (Y) at position 156 (S156Y, p.Ser156Tyr).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from small size and polar (S) to large size and aromatic (Y)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  Rare polymorphism; no effect on oligomerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding.
Any additional useful information about the variant.



Sequence information

Variant position:  156
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:   RCFTRKYTLPPGVDPTQVSS  S LSPEGTLTVEAPMPKLATQS
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                         RCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQS

                              RRLTPKYTLPPGVDPTLVSSSLSPEGTLTVEAPMPKPATQS

Mouse                         RCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQS

Rat                           RCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQS

Pig                           RCFTRKYTLPPGVDPTQVSSSLSPEGTLSVEAPLPKPATQS

Bovine                        RCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKSATQS

Chicken                       RCFTRKYTLPPGVEATAVRSSLSPDGMLTVEAPLPKPAIQS

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.

TypePositionsDescription
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
Beta strand 154 – 157


Literature citations

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;

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.