Variant position: 142 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 631 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 YLQQHNIPQREVVDTTGLNQ SHLSQHLNKGTPMKTQKRAAL
Mouse YLQQHNIPQREVVDTTGLNQ SHLSQHLNKGTPMKTQKRAAL
Rat YLQQHNIPQREVVDTTGLNQ SHLSQHLNKGTPMKTQKRAAL
Chicken YLQQHNIPQREVVDTTGLNQ SHLSQHLNKGTPMKTQKRAAL
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 – 631 Hepatocyte nuclear factor 1-alpha
120 – 631 Missing. In isoform 8.
127 – 127 N -> W. Abolishes transcription activation.
132 – 132 E -> K. Abolishes transcription activation.
141 – 149
Diabetes mutations delineate an atypical POU domain in HNF-1alpha.
Chi Y.I.; Frantz J.D.; Oh B.C.; Hansen L.; Dhe-Paganon S.; Shoelson S.E.;
Mol. Cell 10:1129-1137(2002)
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 85-278 IN COMPLEX WITH DNA; FUNCTION; DNA-BINDING; MUTAGENESIS OF ASN-127; GLU-132; PHE-177; ILE-186; THR-190; ASN-202; VAL-246 AND ASN-257; CHARACTERIZATION OF VARIANTS MODY3 PHE-142 AND GLN-205;
Identification of nine novel mutations in the hepatocyte nuclear factor 1 alpha gene associated with maturity-onset diabetes of the young (MODY3).
Vaxillaire M.; Rouard M.; Yamagata K.; Oda N.; Kaisaki P.J.; Boriraj V.V.; Chevre J.-C.; Boccio V.; Cox R.D.; Lathrop G.M.; Dussoix P.; Philippe J.; Timsit J.; Charpentier G.; Velho G.; Bell G.I.; Froguel P.;
Hum. Mol. Genet. 6:583-586(1997)
Cited for: VARIANTS MODY3 CYS-122; PHE-142 AND GLN-159;
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.