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UniProtKB/Swiss-Prot P61960: Variant p.Arg81Cys

Ubiquitin-fold modifier 1
Gene: UFM1
Variant information

Variant position:  81
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Arginine (R) to Cysteine (C) at position 81 (R81C, p.Arg81Cys).
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:  Change from large size and basic (R) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In HLD14; decreased ability to form thioester bonds with UBA5 and UFC1; decreased protein ufmylation; does not affect the cellular response to endoplasmic reticulum stress.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

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:   QTAGNVFLKHGSELRIIPRD  R VGSC
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                         QTAGNVFLKHGSELRIIPRDRVGSC-----

Mouse                         QTAGNVFLKHGSELRIIPRDRVGSC

Rat                           QTAGNVFLKHGSELRLIPRDRVGSC

Bovine                        QTAGNVFLKHGSELRIIPRDRVGHC

Chicken                       QTAGNVFLKHGSDLRIIPRDRVGSS

Xenopus laevis                QTAGNVFLKHGSELRLIPRDRVGSC

Xenopus tropicalis            QTAGNVFLKHGSELRLIPRDRVGSC

Zebrafish                     QTAGNVFLKHGSELRIIPRDRVGGG

Caenorhabditis elegans        QPAGNIFLKHGSELRLIPRDRVGH-

Drosophila                    QTAGNVFLKHGSELRLIPRDRVGHQ

Slime mold                    QTSGNIFLKNGSDLRLIPRDRVGGL

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.

Chain 1 – 83 Ubiquitin-fold modifier 1
Cross 69 – 69 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)
Cross 83 – 83 Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
Mutagenesis 79 – 79 R -> A. Slightly reduced interaction with UFM1.
Mutagenesis 83 – 83 G -> A. Confers resistance to cleavage.

Literature citations

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.;
Brain 141:1934-1945(2018)

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.