Variant position: 81 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 85 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 QTAGNVFLKHGSELRIIPRD RVGSC-----
Mouse QTAGNVFLKHGSELRIIPRD RVGSC
Rat QTAGNVFLKHGSELRLIPRD RVGSC
Bovine QTAGNVFLKHGSELRIIPRD RVGHC
Chicken QTAGNVFLKHGSDLRIIPRD RVGSS
Xenopus laevis QTAGNVFLKHGSELRLIPRD RVGSC
Xenopus tropicalis QTAGNVFLKHGSELRLIPRD RVGSC
Zebrafish QTAGNVFLKHGSELRIIPRD RVGGG
Caenorhabditis elegans QPAGNIFLKHGSELRLIPRD RVGH-
Drosophila QTAGNVFLKHGSELRLIPRD RVGHQ
Slime mold QTSGNIFLKNGSDLRLIPRD RVGGL
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 – 83 Ubiquitin-fold modifier 1
69 – 69 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)
83 – 83 Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
79 – 79 R -> A. Slightly reduced interaction with UFM1.
83 – 83 G -> A. Confers resistance to cleavage.
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 UFC1; INVOLVEMENT IN HLD14; VARIANT HLD14 CYS-81; CHARACTERIZATION OF VARIANT HLD14 CYS-81;
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