Variant position: 268 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 530 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 GPMRLYVGSLHFNITEDMLR GIFEPFGRIESIQLMMDSETG
Mouse GPMRLYVGSLHFNITEDMLR GIFEPFGRIESIQLMMDSETG
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.
Selective degradation of splicing factor CAPERalpha by anticancer sulfonamides.
Uehara T.; Minoshima Y.; Sagane K.; Sugi N.H.; Mitsuhashi K.O.; Yamamoto N.; Kamiyama H.; Takahashi K.; Kotake Y.; Uesugi M.; Yokoi A.; Inoue A.; Yoshida T.; Mabuchi M.; Tanaka A.; Owa T.;
Nat. Chem. Biol. 13:675-680(2017)
Cited for: FUNCTION; UBIQUITINATION; VARIANT VAL-268; CHARACTERIZATION OF VARIANT VAL-268;
Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15.
Han T.; Goralski M.; Gaskill N.; Capota E.; Kim J.; Ting T.C.; Xie Y.; Williams N.S.; Nijhawan D.;
Cited for: FUNCTION; UBIQUITINATION; VARIANTS LEU-265; ARG-268; GLU-268; TRP-268; VAL-268; GLN-271; GLY-271 AND SER-272; CHARACTERIZATION OF VARIANTS LEU-265; ARG-268; TRP-268; VAL-268; GLN-271 AND SER-272;
Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex.
Bussiere D.E.; Xie L.; Srinivas H.; Shu W.; Burke A.; Be C.; Zhao J.; Godbole A.; King D.; Karki R.G.; Hornak V.; Xu F.; Cobb J.; Carte N.; Frank A.O.; Frommlet A.; Graff P.; Knapp M.; Fazal A.; Okram B.; Jiang S.; Michellys P.Y.; Beckwith R.; Voshol H.; Wiesmann C.; Solomon J.M.; Paulk J.;
Nat. Chem. Biol. 16:15-23(2020)
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 91-171 IN COMPLEX WITH DCAF15; STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) IN COMPLEX WITH DCAF15; IDENTIFICATION IN THE DCX(DCAF15) COMPLEX; VARIANTS LEU-265; TRP-268 AND VAL-268; CHARACTERIZATION OF VARIANTS LEU-265; TRP-268 AND VAL-268;
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.