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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9C000: Variant p.Met77Thr

NACHT, LRR and PYD domains-containing protein 1
Gene: NLRP1
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Variant information Variant position: help 77 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 Methionine (M) to Threonine (T) at position 77 (M77T, p.Met77Thr). 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 medium size and hydrophobic (M) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 MSPC; destabilization of the N-terminal fragment. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1473 The length of the canonical sequence.
Location on the sequence: help LVAQYGEQRAWDLALHTWEQ M GLRSLCAQAQEGAGHSPSFP 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                         LVAQYGEQRAWDLALHTWEQMGLRSLCAQAQEGAGHSPSFP

Zebrafish                     LNELIDH-------LNLFKVLG----------------DFS
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 – 1473 NACHT, LRR and PYD domains-containing protein 1
Chain 1 – 1212 NACHT, LRR and PYD domains-containing protein 1, N-terminus
Domain 1 – 92 Pyrin
Modified residue 93 – 93 Phosphoserine; by MAPK11 and MAPK14
Mutagenesis 76 – 76 Q -> A. No effect on cleavage by HRV-14 Protease 3C.
Mutagenesis 85 – 85 Q -> A. No effect on cleavage by HRV-14 Protease 3C.
Mutagenesis 87 – 87 Q -> A. No effect on cleavage by HRV-14 Protease 3C.
Helix 63 – 77



Literature citations
Whole exome sequencing identifies a mutation for a novel form of corneal intraepithelial dyskeratosis.
Soler V.J.; Tran-Viet K.N.; Galiacy S.D.; Limviphuvadh V.; Klemm T.P.; St Germain E.; Fournie P.R.; Guillaud C.; Maurer-Stroh S.; Hawthorne F.; Suarez C.; Kantelip B.; Afshari N.A.; Creveaux I.; Luo X.; Meng W.; Calvas P.; Cassagne M.; Arne J.L.; Rozen S.G.; Malecaze F.; Young T.L.;
J. Med. Genet. 50:246-254(2013)
Cited for: VARIANT MSPC THR-77; TISSUE SPECIFICITY; Enteroviral 3C protease activates the human NLRP1 inflammasome in airway epithelia.
Robinson K.S.; Teo D.E.T.; Tan K.S.; Toh G.A.; Ong H.H.; Lim C.K.; Lay K.; Au B.V.; Lew T.S.; Chu J.J.H.; Chow V.T.K.; Wang Y.; Zhong F.L.; Reversade B.;
Science 0:0-0(2020)
Cited for: CHARACTERIZATION OF VARIANT MSPC THR-77; FUNCTION; ACTIVITY REGULATION; PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION); UBIQUITINATION; MUTAGENESIS OF GLN-76; GLN-85; GLN-87; GLN-110; GLN-130; GLN-139; GLN-158; GLN-171; GLN-191; GLN-199; GLN-205 AND PHE-1212;
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.