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UniProtKB/Swiss-Prot Q00532: Variant p.Gln275Glu

Cyclin-dependent kinase-like 1
Gene: CDKL1
Variant information

Variant position:  275
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glutamine (Q) to Glutamate (E) at position 275 (Q275E, p.Gln275Glu).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from medium size and polar (Q) to medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  275
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  358
The length of the canonical sequence.

Location on the sequence:   PNISYPALGLLKGCLHMDPT  Q RLTCEQLLHHPYFENIREIE
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                         PNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIE

Mouse                         PNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVG

Rat                           PNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIRDVG

Zebrafish                     PNLSYQALSLMKGCLRMDPAERLSCEQLLEQPYFDSLREES

Caenorhabditis elegans        PNASSAQLDFLQKCFEMSPDRRFSCSELMLHGIFSNW----

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.

TypePositionsDescription
Chain 1 – 358 Cyclin-dependent kinase-like 1
Domain 5 – 288 Protein kinase
Alternative sequence 248 – 358 EPLELKFPNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIEDLAKEHNKPTRKTLRKSRKHHCFTETSKLQYLPQLTGSSILPALDNKKYYCDTKKLNYRFPNI -> SLCLSVTLTEGGLLASGAVKRSQMGSSVSQATSWPHPDIVAETAELDDIAMARQTPVMLRFNRQKEQEKYLSYGA. In isoform 2.
Alternative sequence 268 – 276 CLHMDPTQR -> RVPIASRTE. In isoform 3.
Turn 273 – 275


Literature citations

A family of human cdc2-related protein kinases.
Meyerson M.; Enders G.H.; Wu C.-L.; Su L.-K.; Gorka C.; Nelson C.; Harlow E.; Tsai L.-H.;
EMBO J. 11:2909-2917(1992)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLU-275;

Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1); VARIANTS PRO-67; GLU-275; VAL-330 AND ASN-342;

CDKL Family Kinases Have Evolved Distinct Structural Features and Ciliary Function.
Canning P.; Park K.; Goncalves J.; Li C.; Howard C.J.; Sharpe T.D.; Holt L.J.; Pelletier L.; Bullock A.N.; Leroux M.R.;
Cell Rep. 22:885-894(2018)
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-300 OF VARIANT GLU-275 IN COMPLEX WITH SYNTHETIC INHIBITOR;

Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-275 AND VAL-330;

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.