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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9NUQ7: Variant p.Cys302Ser

Ufm1-specific protease 2
Gene: UFSP2
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Variant information Variant position: help 302 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 Serine (S) at position 302 (C302S, p.Cys302Ser). 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 small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 SEMDDR; catalytically inactive; loss of protease activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 302 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 469 The length of the canonical sequence.
Location on the sequence: help QGIYGYHHYMQDRIDDNGWG C AYRSLQTICSWFKHQGYTER 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                         QGIYGYHHYMQDRIDDNGWGCAYRSLQTICSWFKHQGYTER

Mouse                         QGTYAYHHYMQDRIDDNGWGCAYRSLQTICSWFRHQGYTER

Rat                           QGTYAYHHYMQNRVDDNGWGCAYRSLQTVCSWFRHQGYTER

Chicken                       HGTYSYHHYMQDRTDDSGWGCAYRSLQTICSWFKQQGYVDA

Xenopus laevis                QGLYSYHHYMQDRMDDNGWGCAYRSLQTICSWFKYQGYTDK

Zebrafish                     QGVYSYHHYMQDRVDDDGWGCAYRSLQTICSWFQQQGYVET

Drosophila                    NGNYHYYHYLQQQVQDKGWGCAYRSLQTICSWFVLQGYTNA
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 1 – 469 Ufm1-specific protease 2
Active site 302 – 302
Mutagenesis 302 – 302 C -> A. Catalytically inactive; loss of protease activity.



Literature citations
Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and breast cancer development.
Yoo H.M.; Kang S.H.; Kim J.Y.; Lee J.E.; Seong M.W.; Lee S.W.; Ka S.H.; Sou Y.S.; Komatsu M.; Tanaka K.; Lee S.T.; Noh D.Y.; Baek S.H.; Jeon Y.J.; Chung C.H.;
Mol. Cell 56:261-274(2014)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT SEMDDR SER-302; INTERACTION WITH TRIP4;
MRE11 UFMylation promotes ATM activation.
Wang Z.; Gong Y.; Peng B.; Shi R.; Fan D.; Zhao H.; Zhu M.; Zhang H.; Lou Z.; Zhou J.; Zhu W.G.; Cong Y.S.; Xu X.;
Nucleic Acids Res. 47:4124-4135(2019)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT SEMDDR SER-302;
Variant of the catalytic cysteine of UFSP2 leads to spondyloepimetaphyseal dysplasia type Di Rocco.
Mattern L.; Begemann M.; Delbrueck H.; Holschbach P.; Schroeder S.; Schacht S.M.; Kurth I.; Elbracht M.;
Bone Rep. 18:101683-101683(2023)
Cited for: VARIANT SEMDDR SER-302;
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.