Variant position: 22 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 615 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 GLKAAQKTLFPLRSIDDVVR LFAAELGREEPDLVLLSLVLG
Mouse GLKAAQKTLFPLRSIDDVVR LFAAELGREEPDLVLLSLVLG
Rat GLKAAQKTLFPLRSIDDVVR LFAAELGREEPDLVLLSLVLG
Bovine GLKAAQKTLFPLRSIDDVVR LFAAELGREEPDLVLLSLVLG
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.
Positional cloning of the gene for multiple endocrine neoplasia-type 1.
Chandrasekharappa S.C.; Guru S.C.; Manickam P.; Olufemi S.-E.; Collins F.S.; Emmert-Buck M.R.; Debelenko L.V.; Zhuang Z.; Lubensky I.A.; Liotta L.A.; Crabtree J.S.; Wang Y.; Roe B.A.; Weisemann J.; Boguski M.S.; Agarwal S.K.; Kester M.B.; Kim Y.S.; Heppner C.; Dong Q.; Spiegel A.M.; Burns A.L.; Marx S.J.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2); VARIANTS MEN1 ARG-22; LYS-119 DEL; GLU-368 DEL AND ARG-441; VARIANTS GLN-176 AND ALA-546;
Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription.
Agarwal S.K.; Guru S.C.; Heppner C.; Erdos M.R.; Collins R.M.; Park S.Y.; Saggar S.; Chandrasekharappa S.C.; Collins F.S.; Spiegel A.M.; Marx S.J.; Burns A.L.;
Cited for: INTERACTION WITH JUND; VARIANTS MEN1 LEU-12; ARG-22; ASP-139; TYR-139; PRO-165; PRO-181; VAL-247; PRO-291; PRO-314; ARG-349 AND ARG-441;
Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus.
Hughes C.M.; Rozenblatt-Rosen O.; Milne T.A.; Copeland T.D.; Levine S.S.; Lee J.C.; Hayes D.N.; Shanmugam K.S.; Bhattacharjee A.; Biondi C.A.; Kay G.F.; Hayward N.K.; Hess J.L.; Meyerson M.;
Mol. Cell 13:587-597(2004)
Cited for: FUNCTION IN H3K4 METHYLATION; IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX; INTERACTION WITH POLR2A AND POLR2B; VARIANTS MEN1 LEU-12; ARG-22; ASP-139; VAL-247; PRO-314; ARG-349 AND ARG-441;
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.