Variant position: 106 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 167 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 IPITYPTTAPEIAVPELDGK TAKMYRGGKICLTDHFKPLWA
Mouse IPITYPTTAPEIAVPELDGK TAKMYRGGKICLTDHFKPLWA
Rat IPITYPTTAPEIAVPELDGK TAKMYRGGKICLTDHFKPLWA
Bovine IPITYPTTAPEIAVPELDGK TAKMYRGGKICLTDHFKPLWA
Zebrafish IPVTYPATAPEVAIPELDGK TAKMYRGGKICLTDHFKPLWA
Caenorhabditis elegans IPITYPVTAPEIALPELDGK TAKMYRGGKICLSEHFKPLWA
Drosophila IPVTYPTTAPEIALPELDGK TAKMYRGGKICLTDHFKPLWA
Slime mold MPVTYPETAPEIAIPELDGK TEKMYRGGKICLTIHFKPLWS
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
1 – 167 Ubiquitin-fold modifier-conjugating enzyme 1
116 – 116 Glycyl thioester intermediate
116 – 116 C -> S. Instead of the formation of an intermediate complex with a thiol ester bond between UFC1 (E2-like enzyme) and UFM1 (substrate), a stable complex with an O-ester bond is formed.
Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development.
Nahorski M.S.; Maddirevula S.; Ishimura R.; Alsahli S.; Brady A.F.; Begemann A.; Mizushima T.; Guzman-Vega F.J.; Obata M.; Ichimura Y.; Alsaif H.S.; Anazi S.; Ibrahim N.; Abdulwahab F.; Hashem M.; Monies D.; Abouelhoda M.; Meyer B.F.; Alfadhel M.; Eyaid W.; Zweier M.; Steindl K.; Rauch A.; Arold S.T.; Woods C.G.; Komatsu M.; Alkuraya F.S.;
Cited for: FUNCTION; INTERACTION WITH UFM1; INTERACTION WITH UBA5; MUTAGENESIS OF CYS-116; ACTIVE SITE; INVOLVEMENT IN NEDSG; VARIANTS NEDSG GLN-23 AND ILE-106; CHARACTERIZATION OF VARIANTS NEDSG GLN-23 AND ILE-106;
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.