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UniProtKB/Swiss-Prot Q15043: Variant p.Phe98Val

Metal cation symporter ZIP14
Gene: SLC39A14
Variant information

Variant position:  98
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 Phenylalanine (F) to Valine (V) at position 98 (F98V, p.Phe98Val).
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 aromatic (F) to medium size and hydrophobic (V)
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

Variant description:  In HMNDYT2; no effect on protein abundance; no effect on subcellular localization at the plasma membrane and within the cytoplasm; decreased manganese ion transmembrane transporter activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  98
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  492
The length of the canonical sequence.

Location on the sequence:   VTQHVQGHRNLSTCFSSGDL  F TAHNFSEQSRIGSSELQEFC
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                         VTQHVQGHRNLSTCFSSGDLFTAHNFSEQSRIGSSELQEFC

Mouse                         VSQPKEGPRNLSTCFSSGDLFAAHNLSERSQIGASEFQEFC

Bovine                        ISQPVQGPRNLSTCFSSGELFAAHNLSHQSQIGEREFQEFC

Xenopus tropicalis            -------QRNMSQCLSSSTLFAAHNLTSGSVVDAEGFQSFC

Zebrafish                     DSKTQPTRTNASKCLA-ADTLAVYGMSEQSRIDERGLQQIC

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 31 – 492 Metal cation symporter ZIP14
Topological domain 31 – 157 Extracellular
Glycosylation 87 – 87 N-linked (GlcNAc...) asparagine
Glycosylation 102 – 102 N-linked (GlcNAc...) asparagine
Mutagenesis 87 – 87 N -> A. Decreased N-glycosylation.
Mutagenesis 102 – 102 N -> A. Decreased N-glycosylation.


Literature citations

Mutations in SLC39A14 disrupt manganese homeostasis and cause childhood-onset parkinsonism-dystonia.
Tuschl K.; Meyer E.; Valdivia L.E.; Zhao N.; Dadswell C.; Abdul-Sada A.; Hung C.Y.; Simpson M.A.; Chong W.K.; Jacques T.S.; Woltjer R.L.; Eaton S.; Gregory A.; Sanford L.; Kara E.; Houlden H.; Cuno S.M.; Prokisch H.; Valletta L.; Tiranti V.; Younis R.; Maher E.R.; Spencer J.; Straatman-Iwanowska A.; Gissen P.; Selim L.A.; Pintos-Morell G.; Coroleu-Lletget W.; Mohammad S.S.; Yoganathan S.; Dale R.C.; Thomas M.; Rihel J.; Bodamer O.A.; Enns C.A.; Hayflick S.J.; Clayton P.T.; Mills P.B.; Kurian M.A.; Wilson S.W.;
Nat. Commun. 7:11601-11601(2016)
Cited for: FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY (ISOFORM 2); INVOLVEMENT IN HMNDYT2; MOTIF; VARIANTS HMNDYT2 VAL-98; ARG-383 AND LYS-469; CHARACTERIZATION OF VARIANTS HMNDYT2 VAL-98; ARG-383 AND LYS-469;

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.