Variant position: 225 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 390 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human RQWLSRGGEIEGFRLSAHCS CDSRDNTLQVDINGFTTGRRG
Mouse RQWLNQGDGIQGFRFSAHCS CDSKDNKLHVEINGISPKRRG
Rat RQWLNQGDGIQGFRFSAHCS CDSKDNVLHVEINGISPKRRG
Pig RQWLTRREAIEGFRLSAHCS CDSKDNTLHVEINGFNSGRRG
Bovine RQWLTRREEIEGFRLSAHCS CDSKDNTLQVDINGFSSGRRG
Sheep RQWLTHREEIEGFRLSAHCS CDSKDNTLQVDINGFSSGRRG
Dog RQWLSHGGEVEGFRLSAHCS CDSKDNTLQVDINGFSSSRRG
Horse RQWLSQGGAMEGFRLSAHCS CDSKDNTLRVGINGFSSSRRG
Xenopus laevis NEWLKRAEENEQFGLQPACK CPTPQAK-DIDIEGF-PALRG
Sequence annotation in neighborhood: 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.
Type Positions Description
30 – 278 Latency-associated peptide
75 – 271 Arm domain
223 – 223 Interchain (with C-225)
225 – 225 Interchain (with C-223)
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 CE 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 CE 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 CE HIS-81; CYS-218; ASP-222 AND ARG-225;
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