UniProtKB/SwissProt variant VAR

DNA-binding protein SATB1
Gene: SATB1
Feedback?

Variant information Variant position:

407 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Glutamate (E) to Glutamine (Q) at position 407 (E407Q, p.Glu407Gln). 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 acidic (E) to medium size and polar (Q) 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
Variant description:

In DHDBV. Any additional useful information about the variant.

Sequence information Variant position:

407 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

763 The length of the canonical sequence.
Location on the sequence:

GISQAVFARVAFNRTQGLLS E ILRKEEDPKTASQSLLVNLR 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                         GISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLR

Mouse                         GISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLR

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 – 763	DNA-binding protein SATB1
DNA binding	361 – 448	CUT 1
Binding site	390 – 390
Binding site	400 – 410
Binding site	425 – 425
Mutagenesis	395 – 395	R -> N. Reduced MAR-DNA-binding.
Mutagenesis	402 – 402	Q -> A. Impaired MAR-DNA-binding.
Mutagenesis	403 – 403	G -> A. Impaired MAR-DNA-binding.
Mutagenesis	406 – 406	S -> A. Impaired MAR-DNA-binding.
Mutagenesis	410 – 410	R -> N. Impaired MAR-DNA-binding.
Mutagenesis	411 – 411	K -> R. Normal sumoylation.
Mutagenesis	416 – 416	K -> N. Impaired MAR-DNA-binding.
Mutagenesis	427 – 427	R -> N. Reduced MAR-DNA-binding.
Helix	402 – 411

Literature citations
Mutation-specific pathophysiological mechanisms define different neurodevelopmental disorders associated with SATB1 dysfunction.
den Hoed J.; de Boer E.; Voisin N.; Dingemans A.J.M.; Guex N.; Wiel L.; Nellaker C.; Amudhavalli S.M.; Banka S.; Bena F.S.; Ben-Zeev B.; Bonagura V.R.; Bruel A.L.; Brunet T.; Brunner H.G.; Chew H.B.; Chrast J.; Cimbalistiene L.; Coon H.; Delot E.C.; Demurger F.; Denomme-Pichon A.S.; Depienne C.; Donnai D.; Dyment D.A.; Elpeleg O.; Faivre L.; Gilissen C.; Granger L.; Haber B.; Hachiya Y.; Abedi Y.H.; Hanebeck J.; Hehir-Kwa J.Y.; Horist B.; Itai T.; Jackson A.; Jewell R.; Jones K.L.; Joss S.; Kashii H.; Kato M.; Kattentidt-Mouravieva A.A.; Kok F.; Kotzaeridou U.; Krishnamurthy V.; Kucinskas V.; Kuechler A.; Lavillaureix A.; Liu P.; Manwaring L.; Matsumoto N.; Mazel B.; McWalter K.; Meiner V.; Mikati M.A.; Miyatake S.; Mizuguchi T.; Moey L.H.; Mohammed S.; Mor-Shaked H.; Mountford H.; Newbury-Ecob R.; Odent S.; Orec L.; Osmond M.; Palculict T.B.; Parker M.; Petersen A.K.; Pfundt R.; Preiksaitiene E.; Radtke K.; Ranza E.; Rosenfeld J.A.; Santiago-Sim T.; Schwager C.; Sinnema M.; Snijders Blok L.; Spillmann R.C.; Stegmann A.P.A.; Thiffault I.; Tran L.; Vaknin-Dembinsky A.; Vedovato-Dos-Santos J.H.; Schrier Vergano S.A.; Vilain E.; Vitobello A.; Wagner M.; Waheeb A.; Willing M.; Zuccarelli B.; Kini U.; Newbury D.F.; Kleefstra T.; Reymond A.; Fisher S.E.; Vissers L.E.L.M.;
Am. J. Hum. Genet. 108:346-356(2021)
Cited for: VARIANTS DHDBV LEU-181; VAL-323; ARG-402; GLN-407; GLY-407; LYS-413; ARG-420; ARG-525; GLN-530; GLY-530; LYS-530; LYS-547; ARG-577; ARG-619 AND VAL-682; CHARACTERIZATION OF VARIANTS DHDBV GLY-407; ARG-420; GLN-530; LYS-530; LYS-547 AND VAL-682; VARIANTS DEFDA 410-ARG--ASP-763 DEL AND 694-GLN--ASP-763 DEL; VARIANTS LEU-366; LEU-519 AND THR-573; CHARACTERIZATION OF VARIANTS LEU-366; LEU-519 AND THR-573; CHARACTERIZATION OF VARIANTS DEFDA 410-GLN--ASP-763 DEL AND 694-GLN--ASP-763 DEL; SUBCELLULAR LOCATION; FUNCTION;

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.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q01826: Variant p.Glu407Gln