Variant position: 69 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 198 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 CRDMEEASQRKWNFDFQNHK PLEGKYEWQEVEKGSLPEFYY
Mouse CRDMEEASQRKWNFDFQNHK PLEGRYEWQEVERGSLPEFYY
Cat CRDMEEASQRKWNFDFQNHK PLEGKYEWQEVEKGSLPEFYY
Dog CIDMEEASQNKWNFDFQNHK PLEGKYEWQEVEKGSLPEFYY
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 – 198 Cyclin-dependent kinase inhibitor 1B
74 – 74 Phosphotyrosine; by SRC
88 – 88 Phosphotyrosine; by ABL, LYN, SRC and JAK2
89 – 89 Phosphotyrosine
74 – 74 Y -> F. No change in binding CDK4 and no inhibition of CDK4 activity. Translocates to nucleus. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7.
88 – 88 Y -> F. Abolishes LYN-mediated phosphorylation, reduceS CDK2-mediated phosphorylation on T-187, has greater cell cycle arrest into S-phase, no effect on binding CDK2 complexes, reduced CDK4 binding and inhibits CDK4 enzyme activity. No nuclear translocation. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-89.
89 – 89 Y -> F. No effect on binding CDK2 complexes, reduced CDK4 binding and greatly inhibits CDK4 enzyme activity. No nuclear translocation. Inhibits in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-88.
A novel germline CDKN1B mutation causing multiple endocrine tumors: clinical, genetic and functional characterization.
Molatore S.; Marinoni I.; Lee M.; Pulz E.; Ambrosio M.R.; degli Uberti E.C.; Zatelli M.C.; Pellegata N.S.;
Hum. Mutat. 31:E1825-E1835(2010)
Cited for: VARIANT LEU-69; CHARACTERIZATION OF VARIANT LEU-69;
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.