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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13950: Variant p.Arg225Gln

Runt-related transcription factor 2
Gene: RUNX2
Variant information Variant position: help 225 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Arginine (R) to Glutamine (Q) at position 225 (R225Q, p.Arg225Gln). 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: help Change from large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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

Variant description: help In CLCD1; interferes with nuclear localization; abolishes DNA binding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.

Sequence information Variant position: help 225 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 521 The length of the canonical sequence.
Location on the sequence: help TNPPQVATYHRAIKVTVDGP R EPRRHRQKLDDSKPSLFSDR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.


Sequence annotation in neighborhood: help 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.
Chain 1 – 521 Runt-related transcription factor 2
Domain 101 – 229 Runt
Region 222 – 340 Disordered
Compositional bias 222 – 242 Basic and acidic residues
Cross 238 – 238 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Literature citations
Mutation analysis of core binding factor A1 in patients with cleidocranial dysplasia.
Quack I.; Vonderstrass B.; Stock M.; Aylsworth A.S.; Becker A.; Brueton L.; Lee P.J.; Majewski F.; Mulliken J.B.; Suri M.; Zenker M.; Mundlos S.; Otto F.;
Am. J. Hum. Genet. 65:1268-1278(1999)
Cited for: VARIANTS CLCD1 ARG-113; ARG-118; CYS-121; ARG-123; ARG-205; GLN-225 AND TRP-225; VARIANT SER-511; CBFA1 mutation analysis and functional correlation with phenotypic variability in cleidocranial dysplasia.
Zhou G.; Chen Y.; Zhou L.; Thirunavukkarasu K.; Hecht J.; Chitayat D.; Gelb B.D.; Pirinen S.; Berry S.A.; Greenberg C.R.; Karsenty G.; Lee B.;
Hum. Mol. Genet. 8:2311-2316(1999)
Cited for: VARIANTS CLCD1 ASN-133 DEL; GLN-169; ARG-175; GLN-190; ASN-191; CYS-193; PHE-199; ALA-200; ARG-209 AND GLN-225; Functional analysis of RUNX2 mutations in Japanese patients with cleidocranial dysplasia demonstrates novel genotype-phenotype correlations.
Yoshida T.; Kanegane H.; Osato M.; Yanagida M.; Miyawaki T.; Ito Y.; Shigesada K.;
Am. J. Hum. Genet. 71:724-738(2002)
Cited for: VARIANTS CLCD1 TRP-190; SER-197; ASN-218; ILE-220; TRP-225 AND GLN-225; CHARACTERIZATION OF VARIANTS CLCD1 TRP-190; SER-197; ASN-218; ILE-220; TRP-225 AND GLN-225; Mutations in the RUNX2 gene in patients with cleidocranial dysplasia.
Otto F.; Kanegane H.; Mundlos S.;
Hum. Mutat. 19:209-216(2002)
Cited for: VARIANTS CLCD1 GLY-156; PRO-169; TRP-190; LYS-201; TRP-225; GLN-225 AND VAL-362; Four novel RUNX2 mutations including a splice donor site result in the cleidocranial dysplasia phenotype.
Kim H.-J.; Nam S.-H.; Kim H.-J.; Park H.-S.; Ryoo H.-M.; Kim S.-Y.; Cho T.-J.; Kim S.-G.; Bae S.-C.; Kim I.-S.; Stein J.L.; van Wijnen A.J.; Stein G.S.; Lian J.B.; Choi J.-Y.;
J. Cell. Physiol. 207:114-122(2006)
Cited for: VARIANTS CLCD1 GLY-131 AND GLN-225; A novel RUNX2 mutation in exon 8, G462X, in a patient with Cleidocranial Dysplasia.
Jung Y.J.; Bae H.S.; Ryoo H.M.; Baek S.H.;
J. Cell. Biochem. 119:1152-1162(2018)
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.