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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01137: Variant p.Cys225Arg

Transforming growth factor beta-1 proprotein
Gene: TGFB1
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Variant information Variant position: help 225 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 Cysteine (C) to Arginine (R) at position 225 (C225R, p.Cys225Arg). 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 (C) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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; 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 225 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 RQWLSRGGEIEGFRLSAHCS C DSRDNTLQVDINGFTTGRRG 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                         RQWLSRGGEIEGFRLSAHCSCD---SRDNTLQVDINGFTTGRRG

                              RQWLSHGGEVEGFRLSAHCSCD---SKDNTLQVDINGFSSS

Mouse                         RQWLNQGDGIQGFRFSAHCSCD---SKDNKLHVEINGISPK

Rat                           RQWLNQGDGIQGFRFSAHCSCD---SKDNVLHVEINGISPK

Pig                           RQWLTRREAIEGFRLSAHCSCD---SKDNTLHVEINGFNSG

Bovine                        RQWLTRREEIEGFRLSAHCSCD---SKDNTLQVDINGFSSG

Sheep                         RQWLTHREEIEGFRLSAHCSCD---SKDNTLQVDINGFSSG

Horse                         RQWLSQGGAMEGFRLSAHCSCD---SKDNTLRVGINGFSSS

Chicken                       HQWLSGSELLGVFKLSVHCPCEMGPGHADEMRISIEGFEQQ

Xenopus laevis                NEWLKRAEENEQFGLQPACKCPTPQAKD----IDIEGFPAL
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
Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease.
Kinoshita A.; Saito T.; Tomita H.; Makita Y.; Yoshida K.; Ghadami M.; Yamada K.; Kondo S.; Ikegawa S.; Nishimura G.; Fukushima Y.; Nakagomi T.; Saito H.; Sugimoto T.; Kamegaya M.; Hisa K.; Murray J.C.; Taniguchi N.; Niikawa N.; Yoshiura K.;
Nat. Genet. 26:19-20(2000)
Cited for: VARIANTS CAEND CYS-218; HIS-218 AND ARG-225; Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease.
Janssens K.; Gershoni-Baruch R.; Guanabens N.; Migone N.; Ralston S.; Bonduelle M.; Lissens W.; Van Maldergem L.; Vanhoenacker F.; Verbruggen L.; Van Hul W.;
Nat. Genet. 26:273-275(2000)
Cited for: VARIANTS CAEND HIS-81; CYS-218 AND ARG-225; 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.