Variant position: 53 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 245 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 GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Mouse GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Rat GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Bovine GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Sheep GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Chicken GAELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Xenopus laevis GGELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Xenopus tropicalis GGELSNEERNLLSVAYKNVV GARRSSWRVVSSIEQKTEGAE
Drosophila GVELSNEERNLLSVAYKNVV GARRSSWRVISSIEQKTEASA
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 – 245 14-3-3 protein zeta/delta
56 – 56 Interaction with phosphoserine on interacting protein
58 – 58 Phosphoserine; by PKA and PKB/AKT1
68 – 68 N6-acetyllysine
1 – 98 MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVL -> MSQPCRKLWRHNYETSSCIEFLK. In isoform 2.
49 – 49 K -> E. Loss of interaction with NOXA1.
58 – 58 S -> A. Loss of sphingosine-activated PKA phosphorylation. Promotes homodimerization and heterodimerization with YWHAE. Enhanced transcriptional activity of P53.
58 – 58 S -> E. Loss of homodimerization. Reduced dimerization with YWHAE. Significantly reduced interaction with P53. No enhancement of P53 transcriptional activity.
38 – 67
A YWHAZ variant associated with cardiofaciocutaneous syndrome activates the RAF-ERK pathway.
Popov I.K.; Hiatt S.M.; Whalen S.; Keren B.; Ruivenkamp C.; van Haeringen A.; Chen M.J.; Cooper G.M.; Korf B.R.; Chang C.;
Front. Physiol. 10:388-388(2019)
Cited for: VARIANTS 14-GLU--ASN-245 DEL; ARG-53; LEU-145 AND TRP-230; CHARACTERIZATION OF VARIANT TRP-230; FUNCTION; INTERACTION WITH BRAF AND RAF1; PHOSPHORYLATION AT THR-232 BY CK1; MUTAGENESIS OF THR-232;
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.