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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01137: Variant p.His222Asp

Transforming growth factor beta-1 proprotein
Gene: TGFB1
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Variant information Variant position: help 222 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 Histidine (H) to Aspartate (D) at position 222 (H222D, p.His222Asp). 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 (H) to medium size and acidic (D) 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 CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 222 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 390 The length of the canonical sequence.
Location on the sequence: help GVVRQWLSRGGEIEGFRLSA H CSCDSRDNTLQVDINGFTTG 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                         GVVRQWLSRGGEIEGFRLSAHCSCD---SRDNTLQVDINGFTTG

                              GVVRQWLSHGGEVEGFRLSAHCSCD---SKDNTLQVDINGF

Mouse                         GVVRQWLNQGDGIQGFRFSAHCSCD---SKDNKLHVEINGI

Rat                           GVVRQWLNQGDGIQGFRFSAHCSCD---SKDNVLHVEINGI

Pig                           GVVRQWLTRREAIEGFRLSAHCSCD---SKDNTLHVEINGF

Bovine                        GVVRQWLTRREEIEGFRLSAHCSCD---SKDNTLQVDINGF

Sheep                         GVVRQWLTHREEIEGFRLSAHCSCD---SKDNTLQVDINGF

Horse                         GVVRQWLSQGGAMEGFRLSAHCSCD---SKDNTLRVGINGF

Chicken                       DAVHQWLSGSELLGVFKLSVHCPCEMGPGHADEMRISIEGF

Xenopus laevis                KTVNEWLKRAEENEQFGLQPACKCPTPQAKD----IDIEGF
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 30 – 278 Latency-associated peptide
Region 75 – 271 Arm domain
Disulfide bond 223 – 223 Interchain (with C-225)
Disulfide bond 225 – 225 Interchain (with C-223)
Mutagenesis 237 – 237 N -> A. Does not affect integrin-binding or activation of TGF-beta-1.
Beta strand 213 – 228



Literature citations
Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein.
Janssens K.; ten Dijke P.; Ralston S.H.; Bergmann C.; Van Hul W.;
J. Biol. Chem. 278:7718-7724(2003)
Cited for: CHARACTERIZATION OF VARIANTS CAEND HIS-81; CYS-218; ASP-222 AND ARG-225;
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.