UniProtKB/SwissProt variant VAR

Variant information

Variant position:

431

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 Threonine (T) to Asparagine (N) at position 431 (T431N, p.Thr431Asn).

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:

Similar physico-chemical property. Both residues are medium size and polar.

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

0

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.

Variant rs2230774 [ dbSNP | Ensembl ]

Sequence information

Variant position:

431

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

Protein sequence length:

1388

The length of the canonical sequence.

Location on the sequence:

IGFTYYRENLLLSDSPSCRE T DSIQSRKNEESQEIQKKLYT

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                         IGFTYYRENLLLSDSPSCRETDSIQSRKNEESQEIQKKLYT

Mouse                         IGFTYFRENLLLSDSPPCRENDAIQTRKSEESQEIQKKLYA

Rat                           IGFTYFRENLLLSDSPPCRENDAIQTRKSEESQEIQKKLYA

Pig                           IGFTYYRENLLLSDSPSCKENDSIQIRKNEESQEIQKKLYT

Bovine                        IGFTYYRENLLLSDSPSCKENDSIQSRKNEESQEIQKKLYT

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
Chain	1 – 1388	Rho-associated protein kinase 2
Region	363 – 784	Interaction with PPP1R12A
Coiled coil	429 – 1024
Modified residue	414 – 414	Phosphothreonine; by ROCK2

Literature citations

Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24.
Takahashi N.; Tuiki H.; Saya H.; Kaibuchi K.;
Genomics 55:235-237(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ASN-431;

Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.
Ishikawa K.; Nagase T.; Suyama M.; Miyajima N.; Tanaka A.; Kotani H.; Nomura N.; Ohara O.;
DNA Res. 5:169-176(1998)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT ASN-431;

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] ASN-431; VAL-601 AND PRO-1194;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75116: Variant p.Thr431Asn