Sequence information
Variant position: 247 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:
YLKGSYMRCDRKMEVAFMVC
A INPSIDLHTDSLELLQLQQK
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 YLKGSYMRCDRKMEVAFMVCA INPSIDLHTDSLELLQLQQK
Mouse YLKGSYMRCDRKMEVAFMVCA INPSIDLHTDSLELLQLQQK
Rat YLKGSYMRCDRKMEVAFMVCA INPSIDLHTDSLELLQLQQK
Bovine YLKGSYMRCDRKMEVAFMVCA INPSIDLHTDSLELLQLQQK
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
Chain
1 – 615
Menin
Region
219 – 395
Interaction with FANCD2
Literature citations
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.;
Cell 96:143-152(1999)
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;
The same pocket in menin binds both MLL and JUND but has opposite effects on transcription.
Huang J.; Gurung B.; Wan B.; Matkar S.; Veniaminova N.A.; Wan K.; Merchant J.L.; Hua X.; Lei M.;
Nature 482:542-546(2012)
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-615 IN COMPLEX WITH KMT2A; PSIP1 AND JUND; INTERACTION WITH KMT2A AND JUND; INTERACTION OF KMT2A-MEN1 COMPLEX WITH PSIP1; CHARACTERIZATION OF VARIANTS MEN1 ASP-139; PHE-246; VAL-247; ARG-286 AND ARG-349; CHARACTERIZATION OF VARIANT GLN-289; MUTAGENESIS OF ALA-187; MET-283; ASP-290; GLU-293; GLU-295; TYR-324; TYR-328; GLU-371 AND ASP-375; FUNCTION;
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.