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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BR39: Variant p.Ser165Phe

Junctophilin-2
Gene: JPH2
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Variant information Variant position: help 165 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Serine (S) to Phenylalanine (F) at position 165 (S165F, p.Ser165Phe). 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: help Change from small size and polar (S) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 165 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 696 The length of the canonical sequence.
Location on the sequence: help QSVPYGMAVVVRSPLRTSLS S LRSEHSNGTVAPDSPASPAS 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         QSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPDSPASPAS

Mouse                         QSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPD---SPAA

Rat                           QSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPD---SPAA

Rabbit                        QSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPDSPASPAA
Sequence annotation in neighborhood: help 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 – 696 Junctophilin-2
Chain 1 – 572 Junctophilin-2 N-terminal fragment
Topological domain 1 – 674 Cytoplasmic
Region 164 – 193 Disordered
Compositional bias 164 – 179 Polar residues
Modified residue 162 – 162 Phosphoserine
Modified residue 165 – 165 Phosphoserine
Alternative sequence 130 – 696 Missing. In isoform 2.



Literature citations
S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle.
Woo J.S.; Hwang J.H.; Ko J.K.; Weisleder N.; Kim do H.; Ma J.; Lee E.H.;
Biochem. J. 427:125-134(2010)
Cited for: PHOSPHORYLATION AT SER-165; INTERACTION WITH TRPC3; FUNCTION; CHARACTERIZATION OF VARIANT PHE-165; Mutations in JPH2-encoded junctophilin-2 associated with hypertrophic cardiomyopathy in humans.
Landstrom A.P.; Weisleder N.; Batalden K.B.; Bos J.M.; Tester D.J.; Ommen S.R.; Wehrens X.H.; Claycomb W.C.; Ko J.K.; Hwang M.; Pan Z.; Ma J.; Ackerman M.J.;
J. Mol. Cell. Cardiol. 42:1026-1035(2007)
Cited for: VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165; CHARACTERIZATION OF VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165;
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.