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UniProtKB/Swiss-Prot P57740: Variant p.Met101Ile

Nuclear pore complex protein Nup107
Gene: NUP107
Variant information

Variant position:  101
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Methionine (M) to Isoleucine (I) at position 101 (M101I, p.Met101Ile).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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

Involvement in disease:  Galloway-Mowat syndrome 7 (GAMOS7) [MIM:618348]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS7 inheritance is autosomal recessive. {ECO:0000269|PubMed:28117080, ECO:0000269|PubMed:28280135, ECO:0000269|PubMed:30179222}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In GAMOS7; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased protein amount detected by Western blot in patient cells; affects exon 4 splicing resulting in decreased levels of wild-type mature transcript; impairs assembly of nuclear pore complex.
Any additional useful information about the variant.

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



Sequence information

Variant position:  101
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  925
The length of the canonical sequence.

Location on the sequence:   GTGGKSPRLTQSSGFFGNLS  M VTNLDDSNWAAAFSSQRSGL
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                         GTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGL

Mouse                         GTEGRSPRHTQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGL

Rat                           GTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGF

Drosophila                    -------ILEKSNAEQNELSLMEDTGD--------------

Fission yeast                 -------VLGHKKNGSSSIQELIEMDE--------------

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.

TypePositionsDescription
Chain 1 – 925 Nuclear pore complex protein Nup107
Modified residue 86 – 86 Phosphoserine
Alternative sequence 1 – 151 Missing. In isoform 3.


Literature citations

Homozygous mutation in NUP107 leads to microcephaly with steroid-resistant nephrotic condition similar to Galloway-Mowat syndrome.
Rosti R.O.; Sotak B.N.; Bielas S.L.; Bhat G.; Silhavy J.L.; Aslanger A.D.; Altunoglu U.; Bilge I.; Tasdemir M.; Yzaguirrem A.D.; Musaev D.; Infante S.; Thuong W.; Marin-Valencia I.; Nelson S.F.; Kayserili H.; Gleeson J.G.;
J. Med. Genet. 54:399-403(2017)
Cited for: INVOLVEMENT IN GAMOS7; VARIANT GAMOS7 ILE-101; CHARACTERIZATION OF VARIANT GAMOS7 ILE-101;

Genomic and clinical profiling of a national nephrotic syndrome cohort advocates a precision medicine approach to disease management.
Bierzynska A.; McCarthy H.J.; Soderquest K.; Sen E.S.; Colby E.; Ding W.Y.; Nabhan M.M.; Kerecuk L.; Hegde S.; Hughes D.; Marks S.; Feather S.; Jones C.; Webb N.J.; Ognjanovic M.; Christian M.; Gilbert R.D.; Sinha M.D.; Lord G.M.; Simpson M.; Koziell A.B.; Welsh G.I.; Saleem M.A.;
Kidney Int. 91:937-947(2017)
Cited for: INVOLVEMENT IN GAMOS7; VARIANTS GAMOS7 ILE-101 AND TYR-442;

Mutations in multiple components of the nuclear pore complex cause nephrotic syndrome.
Braun D.A.; Lovric S.; Schapiro D.; Schneider R.; Marquez J.; Asif M.; Hussain M.S.; Daga A.; Widmeier E.; Rao J.; Ashraf S.; Tan W.; Lusk C.P.; Kolb A.; Jobst-Schwan T.; Schmidt J.M.; Hoogstraten C.A.; Eddy K.; Kitzler T.M.; Shril S.; Moawia A.; Schrage K.; Khayyat A.I.A.; Lawson J.A.; Gee H.Y.; Warejko J.K.; Hermle T.; Majmundar A.J.; Hugo H.; Budde B.; Motameny S.; Altmueller J.; Noegel A.A.; Fathy H.M.; Gale D.P.; Waseem S.S.; Khan A.; Kerecuk L.; Hashmi S.; Mohebbi N.; Ettenger R.; Serdaroglu E.; Alhasan K.A.; Hashem M.; Goncalves S.; Ariceta G.; Ubetagoyena M.; Antonin W.; Baig S.M.; Alkuraya F.S.; Shen Q.; Xu H.; Antignac C.; Lifton R.P.; Mane S.; Nuernberg P.; Khokha M.K.; Hildebrandt F.;
J. Clin. Invest. 128:4313-4328(2018)
Cited for: FUNCTION; INTERACTION WITH NUP133; INVOLVEMENT IN GAMOS7; INVOLVEMENT IN NPHS11; VARIANT GAMOS7 ILE-101; VARIANTS NPHS11 GLU-710 DEL AND CYS-889; CHARACTERIZATION OF VARIANT GAMOS7 ILE-101; CHARACTERIZATION OF VARIANT NPHS11 CYS-889;

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.