Variant position: 4 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1256 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 MLF KLLQRQTYTCLSHRYGLYVCF
Mouse MLL KLLQRQTYTCLSHRYGLYVCF
Zebrafish SLL KLLQRQTYTCLSHRYGLYLCF
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 – 928 N-acetylglucosamine-1-phosphotransferase subunit alpha
Mislocalization of phosphotransferase as a cause of mucolipidosis III alphabeta.
van Meel E.; Qian Y.; Kornfeld S.A.;
Proc. Natl. Acad. Sci. U.S.A. 111:3532-3537(2014)
Cited for: CHARACTERIZATION OF VARIANTS MLIIIA GLN-4 AND TYR-15;
Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition.
Qian Y.; van Meel E.; Flanagan-Steet H.; Yox A.; Steet R.; Kornfeld S.;
J. Biol. Chem. 290:3045-3056(2015)
Cited for: CHARACTERIZATION OF VARIANTS MLII LEU-81; ASP-182; PRO-205; LEU-334; LEU-348; LEU-374; ASN-732; ARG-928; VAL-955; CYS-986; PRO-1001; VAL-1054 AND MET-1236; CHARACTERIZATION OF VARIANTS MLIIIA GLN-4; TYR-15; VAL-190; GLN-334; PHE-399; THR-403; ALA-407; TYR-442; GLY-461; SER-468; TYR-505; PRO-587; PRO-926; TYR-956; GLY-1018 AND SER-1153; CHARACTERIZATION OF VARIANTS ARG-523; THR-592 AND TRP-785;
Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-Hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene.
Kudo M.; Brem M.S.; Canfield W.M.;
Am. J. Hum. Genet. 78:451-463(2006)
Cited for: VARIANT MLIIIA GLN-4;
Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III.
Zarghooni M.; Dittakavi S.S.;
Am. J. Med. Genet. A 149A:2753-2761(2009)
Cited for: VARIANTS MLII ASP-182; PRO-205; ASN-732; ARG-928; VAL-955 AND VAL-1054; VARIANT MLIIIA GLN-4; CHARACTERIZATION OF VARIANT MLIIIA GLN-4;
Phenotype and genotype in mucolipidoses II and III alpha/beta: a study of 61 probands.
Cathey S.S.; Leroy J.G.; Wood T.; Eaves K.; Simensen R.J.; Kudo M.; Stevenson R.E.; Friez M.J.;
J. Med. Genet. 47:38-48(2010)
Cited for: VARIANTS MLIIIA GLN-4; TYR-15; VAL-190; GLN-334; PHE-399; SER-468; TYR-505; ARG-956 AND GLY-1018; VARIANT MLII LEU-348;
A novel intermediate mucolipidosis II/IIIalphabeta caused by GNPTAB mutation in the cytosolic N-terminal domain.
Leroy J.G.; Sillence D.; Wood T.; Barnes J.; Lebel R.R.; Friez M.J.; Stevenson R.E.; Steet R.; Cathey S.S.;
Eur. J. Hum. Genet. 22:594-601(2014)
Cited for: VARIANT MLIIIA GLN-4; CHARACTERIZATION OF VARIANT MLIIIA GLN-4;
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.