UniProtKB/Swiss-Prot Q96Q15: Variant p.Ala35Thr

Serine/threonine-protein kinase SMG1
Gene: SMG1
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Variant information Variant position:

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

LB/B 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 Alanine (A) to Threonine (T) at position 35 (A35T, p.Ala35Thr). 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 small size and hydrophobic (A) to medium size and polar (T) 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 rs12051350 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

3661 The length of the canonical sequence.
Location on the sequence:

GGGGTKYPRSWNDWQPRTDS A SADPDNLKYSSSRDRGGSSS 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                         GGGGTKYPRSWNDWQPRTDSASADPDNLKY--SSSRDRGGSSS

Mouse                         GGGGTKYPRSWNDWQPRTDSASADPDTLKY--SSSRDRGVS

Zebrafish                     ---AHKLQRNWNDWQPRSDSLSASQDGVKC--SVSRDRGSE

Caenorhabditis elegans        FRQRDTPQKERKAILARIEEILQTTKNVES-----------

Drosophila                    --GAGTEEEASSAFHAEIDRVLLNNNGNHGDSSNEGGGGNG

Slime mold                    -TENNTLTATKNSINNTTTTTTTPNNNVNCLKTSGSIKLSA

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 – 3661	Serine/threonine-protein kinase SMG1
Region	1 – 1977	Interaction with SMG8 and SMG9
Region	1 – 101	Disordered
Compositional bias	25 – 67	Polar residues
Alternative sequence	1 – 1269	Missing. In isoform 4.
Alternative sequence	1 – 630	Missing. In isoform 3.
Alternative sequence	1 – 140	Missing. In isoform 2.

Literature citations
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
Matsuoka S.; Ballif B.A.; Smogorzewska A.; McDonald E.R. III; Hurov K.E.; Luo J.; Bakalarski C.E.; Zhao Z.; Solimini N.; Lerenthal Y.; Shiloh Y.; Gygi S.P.; Elledge S.J.;
Science 316:1160-1166(2007)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550 AND SER-3556; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Olsen J.V.; Vermeulen M.; Santamaria A.; Kumar C.; Miller M.L.; Jensen L.J.; Gnad F.; Cox J.; Jensen T.S.; Nigg E.A.; Brunak S.; Mann M.;
Sci. Signal. 3:RA3-RA3(2010)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; Toward a comprehensive characterization of a human cancer cell phosphoproteome.
Zhou H.; Di Palma S.; Preisinger C.; Peng M.; Polat A.N.; Heck A.J.; Mohammed S.;
J. Proteome Res. 12:260-271(2013)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550; SER-3556; SER-3570 AND THR-3573; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
Bian Y.; Song C.; Cheng K.; Dong M.; Wang F.; Huang J.; Sun D.; Wang L.; Ye M.; Zou H.;
J. Proteomics 96:253-262(2014)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; 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] THR-35; CYS-126; CYS-144; TYR-151; ASN-160; VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612; CYS-753; CYS-809; CYS-812; ILE-829; ASP-832; GLY-952; SER-969; LEU-1016; GLN-1029; SER-1072; HIS-1103; ARG-1275; PRO-1292; VAL-1332; PRO-1358; THR-1418; CYS-2171; SER-2258; LYS-2345; GLU-2730; SER-2889; ALA-2899; THR-3239 AND GLN-3583;

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.