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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P40763: Variant p.Thr716Met

Signal transducer and activator of transcription 3
Gene: STAT3
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Variant information Variant position: help 716 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 Threonine (T) to Methionine (M) at position 716 (T716M, p.Thr716Met). 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 polar (T) to medium size and hydrophobic (M) 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 ADMIO1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 716 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 770 The length of the canonical sequence.
Location on the sequence: help EADPGSAAPYLKTKFICVTP T TCSNTIDLPMSPRTLDSLMQ 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                         EA-DPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQ

Mouse                         EA-DPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLM

Rat                           EA-DPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLM

Pig                           EA-DPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLM

Bovine                        EA-DPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLM

Chicken                       EATDSGSAAPYLKTKFICVTPTSFSNTIDLPMSPRTLDSLM
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 2 – 770 Signal transducer and activator of transcription 3
Modified residue 705 – 705 Phosphotyrosine; by FER and PTK6
Modified residue 707 – 707 N6-acetyllysine
Modified residue 714 – 714 Phosphothreonine
Modified residue 727 – 727 Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE
Alternative sequence 701 – 701 Missing. In isoform Del-701.
Alternative sequence 716 – 722 TTCSNTI -> FIDAVWK. In isoform 3.
Mutagenesis 705 – 705 Y -> F. Inhibits leptin-mediated transactivation of CCND1 promoter. Abolished phosphorylation by isoform M2 of PKM (PKM2).



Literature citations
Activating germline mutations in STAT3 cause early-onset multi-organ autoimmune disease.
Flanagan S.E.; Haapaniemi E.; Russell M.A.; Caswell R.; Lango Allen H.; De Franco E.; McDonald T.J.; Rajala H.; Ramelius A.; Barton J.; Heiskanen K.; Heiskanen-Kosma T.; Kajosaari M.; Murphy N.P.; Milenkovic T.; Seppaenen M.; Lernmark A.; Mustjoki S.; Otonkoski T.; Kere J.; Morgan N.G.; Ellard S.; Hattersley A.T.;
Nat. Genet. 46:812-814(2014)
Cited for: VARIANTS ADMIO1 ARG-392; LYS-646; ASN-658 AND MET-716; INVOLVEMENT IN ADMIO1;
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.